{"size":20580,"totalNumberOfResults":20580,"elements":[{"complexAC":"CPX-5966","complexName":"Mitochondrial calcium uniporter complex, MICUB variant","organismName":"Homo sapiens; 9606","description":"Highly selective, inward-rectifying Ca2+ channel located on the inner mitochondrial membrane. The uniporter is quiescent in resting cellular conditions and becomes activated only when local Ca2+ levels rise above approximately 1 microM with the MCU tetramer forming a calcium-conducting pore. Ca2+ uptake is driven by the large negative inner mitochondrial membrane potential generated by proton pumping into the intermembrane space by the electron transport chain. Under certain conditions MCUB integrates into the normal importer complex (CPX-5961/CPX-5963/CPX-5965), displacing at least some of the MCU and MCU-bound MICU1/MICU2/MICU3 subunits. This appears to be a stress-responsive mechanism to alter mtCU gating and limit cooperative activation of the channel. For example, MCUB is not normally present in the uniporter complex of the heart at baseline, but only after stress or ischemic injury, and thus limits mitochondrial Ca2+ overload during cardiac injury.","predictedComplex":false,"interactors":[{"ac":"EBI-11908005","identifier":"Q9H4I9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H4I9/entry","name":"SMDT1","description":"Essential MCU regulator, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR33904","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2371996","identifier":"Q9BPX6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BPX6/entry","name":"MICU1","description":"Calcium uptake protein 1, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3197790","identifier":"Q8IYU8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IYU8/entry","name":"MICU2","description":"Calcium uptake protein 2, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6552124","identifier":"Q8NE86","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NE86/entry","name":"MCU","description":"Calcium uniporter protein, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-719989","identifier":"Q9NWR8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NWR8/entry","name":"MCUB","description":"Calcium uniporter regulatory subunit MCUb, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5967","complexName":"L-ascorbate-specific enzyme II complex","organismName":"Escherichia coli (strain K12); 83333","description":"Involved in the transport of L-ascorbic acid across the cell membrane as part of the phosphoenolpyruvate:sugar phosphotransferase system (PTS).  A phosphoryl group is transferred from hpr (P0AA04) to ulaC (IIA), from ulaC to ulaB (IIB) and finally from ulaB onto the incoming sugar bound to membrane-embedded laA (IIC).","predictedComplex":false,"interactors":[{"ac":"EBI-1113922","identifier":"P69822","identifierLink":"https://www.uniprot.org/uniprotkb/P69822/entry","name":"ulaB","description":"Ascorbate-specific PTS system EIIB component","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-1134987","identifier":"P69820","identifierLink":"https://www.uniprot.org/uniprotkb/P69820/entry","name":"ulaC","description":"Ascorbate-specific PTS system EIIA component","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR36203","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-556234","identifier":"P39301","identifierLink":"https://www.uniprot.org/uniprotkb/P39301/entry","name":"ulaA","description":"Ascorbate-specific PTS system EIIC component","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33843","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5968","complexName":"D-mannose-specific enzyme II complex","organismName":"Escherichia coli (strain K12); 83333","description":"Involved in the transport of D-mannose across the cell membrane as part of the phosphoenolpyruvate:sugar phosphotransferase system (PTS).  A phosphoryl group is transferred from hpr (P0AA04) to manX (IIA), from manX to manY (IIBC) and finally from manY onto the incoming sugar bound to membrane-embedded manY/manZ (IID). The mannose transporter has a broad substrate specificity, including glucose, mannose, fructose, glucosamine, N-acetylglucosamine, and N-acetylmannosamine, and it is the only transporter for mannose.","predictedComplex":false,"interactors":[{"ac":"EBI-554089","identifier":"P69797","identifierLink":"https://www.uniprot.org/uniprotkb/P69797/entry","name":"manX","description":"PTS system mannose-specific EIIAB component","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-906752","identifier":"P69801","identifierLink":"https://www.uniprot.org/uniprotkb/P69801/entry","name":"manY","description":"PTS system mannose-specific EIIC component","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32502","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-906762","identifier":"P69805","identifierLink":"https://www.uniprot.org/uniprotkb/P69805/entry","name":"manZ","description":"PTS system mannose-specific EIID component","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32502","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5969","complexName":"Glucitol/sorbitol enzyme II complex","organismName":"Escherichia coli (strain K12); 83333","description":"Involved in the transport of glucitol/sorbitol across the cell membrane as part of the phosphoenolpyruvate:sugar phosphotransferase system (PTS). May also bind and transport and D-mannitol with low affinity. A phosphoryl group is transferred from hpr (P0AA04) to srlB (IIA), from srlB to srlE (IIB) and finally from srlE onto the incoming sugar bound to membrane-embedded srlA (IIC).","predictedComplex":false,"interactors":[{"ac":"EBI-1130001","identifier":"P05706","identifierLink":"https://www.uniprot.org/uniprotkb/P05706/entry","name":"srlB","description":"PTS system glucitol/sorbitol-specific EIIA component","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR40398","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25750986","identifier":"P56580","identifierLink":"https://www.uniprot.org/uniprotkb/P56580/entry","name":"srlE","description":"PTS system glucitol/sorbitol-specific EIIB component","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR39427","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9151063","identifier":"P56579","identifierLink":"https://www.uniprot.org/uniprotkb/P56579/entry","name":"srlA","description":"PTS system glucitol/sorbitol-specific EIIC component","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR40399","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5970","complexName":"Phosphatidylinositol 3-kinase complex class IA, p110alpha/p55alpha","organismName":"Homo sapiens; 9606","description":"Uses 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate/PI(4,5)P2 (CHEBI:18348) as a substrate to generate the product 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate/PI(3,4,5)P3 (CHEBI:16618) which initiates major signaling pathways downstream. Performs a central role in cellular signaling, mediating responses to growth factors and extracellular stimuli. This variant is found to be ubiquitously expressed in human cells.","predictedComplex":false,"interactors":[{"ac":"EBI-2116585","identifier":"P42336","identifierLink":"https://www.uniprot.org/uniprotkb/P42336/entry","name":"PIK3CA","description":"Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9090282","identifier":"P27986-2","identifierLink":"https://www.uniprot.org/uniprotkb/P27986-2/entry","name":"PIK3R1","description":"Phosphatidylinositol 3-kinase regulatory subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-5971","complexName":"Phosphatidylinositol 3-kinase complex class IA, p110alpha/p50alpha","organismName":"Homo sapiens; 9606","description":"Uses 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate/PI(4,5)P2 (CHEBI:18348) as a substrate to generate the product 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate/PI(3,4,5)P3 (CHEBI:16618) which initiates major signaling pathways downstream. Performs a central role in cellular signaling, mediating responses to growth factors and extracellular stimuli. This variant is found to be ubiquitously expressed in human cells.","predictedComplex":false,"interactors":[{"ac":"EBI-16747607","identifier":"P27986-3","identifierLink":"https://www.uniprot.org/uniprotkb/P27986-3/entry","name":"PIK3R1","description":"Phosphatidylinositol 3-kinase regulatory subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2116585","identifier":"P42336","identifierLink":"https://www.uniprot.org/uniprotkb/P42336/entry","name":"PIK3CA","description":"Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5972","complexName":"Phosphatidylinositol 3-kinase complex class IA, p110beta/p50alpha","organismName":"Homo sapiens; 9606","description":"Uses 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate/PI(4,5)P2 (CHEBI:18348) as a substrate to generate the product 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate/PI(3,4,5)P3 (CHEBI:16618) which initiates major signaling pathways downstream. Performs a central role in cellular signaling, mediating responses to growth factors and extracellular stimuli. This variant is found to be ubiquitously expressed in human cells.","predictedComplex":false,"interactors":[{"ac":"EBI-16747607","identifier":"P27986-3","identifierLink":"https://www.uniprot.org/uniprotkb/P27986-3/entry","name":"PIK3R1","description":"Phosphatidylinositol 3-kinase regulatory subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2609540","identifier":"P42338","identifierLink":"https://www.uniprot.org/uniprotkb/P42338/entry","name":"PIK3CB","description":"Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5974","complexName":"Phosphatidylinositol 3-kinase complex class IA, p110beta/p55alpha","organismName":"Homo sapiens; 9606","description":"Uses 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate/PI(4,5)P2 (CHEBI:18348) as a substrate to generate the product 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate/PI(3,4,5)P3 (CHEBI:16618) which initiates major signaling pathways downstream. Performs a central role in cellular signaling, mediating responses to growth factors and extracellular stimuli. This variant is found to be ubiquitously expressed in human cells.","predictedComplex":false,"interactors":[{"ac":"EBI-2609540","identifier":"P42338","identifierLink":"https://www.uniprot.org/uniprotkb/P42338/entry","name":"PIK3CB","description":"Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9090282","identifier":"P27986-2","identifierLink":"https://www.uniprot.org/uniprotkb/P27986-2/entry","name":"PIK3R1","description":"Phosphatidylinositol 3-kinase regulatory subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-5975","complexName":"Phosphatidylinositol 3-kinase complex class IA, p110beta/p85alpha","organismName":"Homo sapiens; 9606","description":"Uses 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate/PI(4,5)P2 (CHEBI:18348) as a substrate to generate the product 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate/PI(3,4,5)P3 (CHEBI:16618) which initiates major signaling pathways downstream. Performs a central role in cellular signaling, mediating responses to growth factors and extracellular stimuli. This variant is found to be ubiquitously expressed in human cells.","predictedComplex":false,"interactors":[{"ac":"EBI-2609540","identifier":"P42338","identifierLink":"https://www.uniprot.org/uniprotkb/P42338/entry","name":"PIK3CB","description":"Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-79464","identifier":"P27986","identifierLink":"https://www.uniprot.org/uniprotkb/P27986/entry","name":"PIK3R1","description":"Phosphatidylinositol 3-kinase regulatory subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10155","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5976","complexName":"Phosphatidylinositol 3-kinase complex class IA, p110beta/p85beta","organismName":"Homo sapiens; 9606","description":"Uses 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate/PI(4,5)P2 (CHEBI:18348) as a substrate to generate the product 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate/PI(3,4,5)P3 (CHEBI:16618) which initiates major signaling pathways downstream. Performs a central role in cellular signaling, mediating responses to growth factors and extracellular stimuli. This variant is found to be ubiquitously expressed in human cells.","predictedComplex":false,"interactors":[{"ac":"EBI-2609540","identifier":"P42338","identifierLink":"https://www.uniprot.org/uniprotkb/P42338/entry","name":"PIK3CB","description":"Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-346930","identifier":"O00459","identifierLink":"https://www.uniprot.org/uniprotkb/O00459/entry","name":"PIK3R2","description":"Phosphatidylinositol 3-kinase regulatory subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10155","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5977","complexName":"Phosphatidylinositol 3-kinase complex class IA, p110beta/p55gamma","organismName":"Homo sapiens; 9606","description":"Uses PI(4,5)P2 as a substrate to generate the product PI(3,4,5)P3 which initiates major signaling pathways downstream. Performs a central role in cellular signaling, mediating responses to growth factors and extracellular stimuli. This variant is found to be ubiquitously expressed in human cells.","predictedComplex":false,"interactors":[{"ac":"EBI-2609540","identifier":"P42338","identifierLink":"https://www.uniprot.org/uniprotkb/P42338/entry","name":"PIK3CB","description":"Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-79893","identifier":"Q92569","identifierLink":"https://www.uniprot.org/uniprotkb/Q92569/entry","name":"PIK3R3","description":"Phosphatidylinositol 3-kinase regulatory subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10155","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5978","complexName":"Phosphatidylinositol 3-kinase complex class IA, p110delta/p55gamma","organismName":"Homo sapiens; 9606","description":"Uses 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate/PI(4,5)P2 (CHEBI:18348) as a substrate to generate the product 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate/PI(3,4,5)P3 (CHEBI:16618) which initiates major signaling pathways downstream. Performs a central role in cellular signaling, mediating responses to growth factors and extracellular stimuli.\r\nExpressed predominantly in leukocytes, where it mediates immune responses.\r\n\r\nGain-of-function mutations in the phosphoinositide 3-kinase (PI3K) genes PIK3CD and PIK3R1 can cause a combined immunodeficiency syndrome, referred to as activated PI3Kdelta syndrome (APDS).","predictedComplex":false,"interactors":[{"ac":"EBI-718309","identifier":"O00329","identifierLink":"https://www.uniprot.org/uniprotkb/O00329/entry","name":"PIK3CD","description":"Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-79893","identifier":"Q92569","identifierLink":"https://www.uniprot.org/uniprotkb/Q92569/entry","name":"PIK3R3","description":"Phosphatidylinositol 3-kinase regulatory subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10155","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5979","complexName":"Frv fructose-like enzyme II complex","organismName":"Escherichia coli (strain K12); 83333","description":"Probably involved in the transport of fructose across the cell membrane as part of the phosphoenolpyruvate:sugar phosphotransferase system (PTS). The fructose-specific PTS has no requirement for hpr/ptsH (P0AA04), fvuB combines a IIA domain with a HPr domain. frvA contains a duplicated EIIB domain (EIIB' domain) in the N-terminal which lacks the active site and functions to facilitate phosphoryl transfer between the EIIA domain of diphosphoryl transfer protein and the EIIB domain.","predictedComplex":false,"interactors":[{"ac":"EBI-1133990","identifier":"P32155","identifierLink":"https://www.uniprot.org/uniprotkb/P32155/entry","name":"frvA","description":"PTS system fructose-like EIIA component","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR47738","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25751516","identifier":"P32154","identifierLink":"https://www.uniprot.org/uniprotkb/P32154/entry","name":"frvB","description":"Fructose-like PTS system EIIBC component","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30505","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5980","complexName":"Phosphatidylinositol 3-kinase complex class IA, p110delta/p85beta","organismName":"Homo sapiens; 9606","description":"Uses 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate/PI(4,5)P2 (CHEBI:18348) as a substrate to generate the product 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate/PI(3,4,5)P3 (CHEBI:16618) which initiates major signaling pathways downstream.  Performs a central role in cellular signaling, mediating responses to growth factors and extracellular stimuli.\r\nExpressed predominantly in leukocytes, where it mediates immune responses.\r\n\r\nGain-of-function mutations in the phosphoinositide 3-kinase (PI3K) genes PIK3CD and PIK3R1 can cause a combined immunodeficiency syndrome, referred to as activated PI3Kdelta syndrome (APDS).","predictedComplex":false,"interactors":[{"ac":"EBI-346930","identifier":"O00459","identifierLink":"https://www.uniprot.org/uniprotkb/O00459/entry","name":"PIK3R2","description":"Phosphatidylinositol 3-kinase regulatory subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10155","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-718309","identifier":"O00329","identifierLink":"https://www.uniprot.org/uniprotkb/O00329/entry","name":"PIK3CD","description":"Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5983","complexName":"Phosphatidylinositol 3-kinase complex class IA, p110delta/p85alpha","organismName":"Homo sapiens; 9606","description":"Uses 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate/PI(4,5)P2 (CHEBI:18348) as a substrate to generate the product 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate/PI(3,4,5)P3 (CHEBI:16618) which initiates major signaling pathways downstream. Performs a central role in cellular signaling, mediating responses to growth factors and extracellular stimuli.\r\nExpressed predominantly in leukocytes, where it mediates immune responses.\r\n\r\nGain-of-function mutations in the phosphoinositide 3-kinase (PI3K) genes PIK3CD and PIK3R1 can cause a combined immunodeficiency syndrome, referred to as activated PI3Kdelta syndrome (APDS).","predictedComplex":false,"interactors":[{"ac":"EBI-718309","identifier":"O00329","identifierLink":"https://www.uniprot.org/uniprotkb/O00329/entry","name":"PIK3CD","description":"Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-79464","identifier":"P27986","identifierLink":"https://www.uniprot.org/uniprotkb/P27986/entry","name":"PIK3R1","description":"Phosphatidylinositol 3-kinase regulatory subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10155","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5984","complexName":"Phosphatidylinositol 3-kinase complex class IA, p110delta/p55alpha","organismName":"Homo sapiens; 9606","description":"Uses PI(4,5)P2 as a substrate to generate the product PI(3,4,5)P3 which initiates major signaling pathways downstream. Performs a central role in cellular signaling, mediating responses to growth factors and extracellular stimuli.\r\nExpressed predominantly in leukocytes, where it mediates immune responses.\r\n\r\nGain-of-function mutations in the phosphoinositide 3-kinase (PI3K) genes PIK3CD and PIK3R1 can cause a combined immunodeficiency syndrome, referred to as activated PI3Kdelta syndrome (APDS).","predictedComplex":false,"interactors":[{"ac":"EBI-718309","identifier":"O00329","identifierLink":"https://www.uniprot.org/uniprotkb/O00329/entry","name":"PIK3CD","description":"Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-79464","identifier":"P27986","identifierLink":"https://www.uniprot.org/uniprotkb/P27986/entry","name":"PIK3R1","description":"Phosphatidylinositol 3-kinase regulatory subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10155","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5985","complexName":"Phosphatidylinositol 3-kinase complex class IA, p110delta/p50alpha","organismName":"Homo sapiens; 9606","description":"Uses 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate/PI(4,5)P2 (CHEBI:18348) as a substrate to generate the product 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate/PI(3,4,5)P3 (CHEBI:16618) which initiates major signaling pathways downstream. Performs a central role in cellular signaling, mediating responses to growth factors and extracellular stimuli.\r\nExpressed predominantly in leukocytes, where it mediates immune responses.\r\n\r\nGain-of-function mutations in the phosphoinositide 3-kinase (PI3K) genes PIK3CD and PIK3R1 can cause a combined immunodeficiency syndrome, referred to as activated PI3Kdelta syndrome (APDS).","predictedComplex":false,"interactors":[{"ac":"EBI-16747607","identifier":"P27986-3","identifierLink":"https://www.uniprot.org/uniprotkb/P27986-3/entry","name":"PIK3R1","description":"Phosphatidylinositol 3-kinase regulatory subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-718309","identifier":"O00329","identifierLink":"https://www.uniprot.org/uniprotkb/O00329/entry","name":"PIK3CD","description":"Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5986","complexName":"Phosphatidylinositol 3-kinase complex class IB, p110gamma/p101","organismName":"Homo sapiens; 9606","description":"Uses 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate/PI(4,5)P2 (CHEBI:18348) as a substrate to generate the product 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate/PI(3,4,5)P3 (CHEBI:16618) which initiates major signaling pathways downstream. Also has serine/threonine protein kinase activity. Performs a central role in cellular signaling, mediating responses to growth factors and extracellular stimuli.\r\nLinks G-protein coupled receptor activation to PIP3 production. Involved in immune, inflammatory and allergic responses.","predictedComplex":false,"interactors":[{"ac":"EBI-1030384","identifier":"P48736","identifierLink":"https://www.uniprot.org/uniprotkb/P48736/entry","name":"PIK3CG","description":"Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2114827","identifier":"Q8WYR1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WYR1/entry","name":"PIK3R5","description":"Phosphoinositide 3-kinase regulatory subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15593","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5987","complexName":"Phosphatidylinositol 3-kinase complex class IB, p110gamma/p87","organismName":"Homo sapiens; 9606","description":"Uses 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate/PI(4,5)P2 (CHEBI:18348) as a substrate to generate the product 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate/PI(3,4,5)P3 (CHEBI:16618) which initiates major signaling pathways downstream. Also has serine/threonine protein kinase activity. Performs a central role in cellular signaling, mediating responses to growth factors and extracellular stimuli.\r\nLinks G-protein coupled receptor activation to PIP3 production. Involved in immune, inflammatory and allergic responses.","predictedComplex":false,"interactors":[{"ac":"EBI-1030384","identifier":"P48736","identifierLink":"https://www.uniprot.org/uniprotkb/P48736/entry","name":"PIK3CG","description":"Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6172907","identifier":"Q5UE93","identifierLink":"https://www.uniprot.org/uniprotkb/Q5UE93/entry","name":"PIK3R6","description":"Phosphoinositide 3-kinase regulatory subunit 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15593","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5989","complexName":"Nuclear mitotic cohesin complex, STAG1 variant","organismName":"Homo sapiens; 9606","description":"Required for sister chromatid cohesion during mitotic cell division, which enables cells to attach sister kinetochores  to microtubules with opposing polarity (bi-orientation) and subsequently resists the tendency of these microtubules to pull chromatids toward opposite spindle poles.","predictedComplex":false,"interactors":[{"ac":"EBI-1175097","identifier":"Q8WVM7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WVM7/entry","name":"STAG1","description":"Cohesin subunit SA-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11199","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-80690","identifier":"Q14683","identifierLink":"https://www.uniprot.org/uniprotkb/Q14683/entry","name":"SMC1A","description":"Structural maintenance of chromosomes protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-80718","identifier":"Q9UQE7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UQE7/entry","name":"SMC3","description":"Structural maintenance of chromosomes protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43977","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-80739","identifier":"O60216","identifierLink":"https://www.uniprot.org/uniprotkb/O60216/entry","name":"RAD21","description":"Double-strand-break repair protein rad21 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12585","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5990","complexName":"sgcABC sugar permease enzyme II complex","organismName":"Escherichia coli (strain K12); 83333","description":"Involved in the transport of sugars across the cell membrane as part of the phosphoenolpyruvate:sugar phosphotransferase system (PTS). A phosphoryl group is transferred from hpr (P0AA04) to sgc (IIA), from sgcB to srlE (IIB) and finally from sgcB onto the incoming sugar bound to membrane-embedded sgcC (IIC).","predictedComplex":false,"interactors":[{"ac":"EBI-25752695","identifier":"P58035","identifierLink":"https://www.uniprot.org/uniprotkb/P58035/entry","name":"sgcB","description":"Putative phosphotransferase enzyme IIB component SgcB","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-25752711","identifier":"P39365","identifierLink":"https://www.uniprot.org/uniprotkb/P39365/entry","name":"sgcC","description":"Putative permease IIC component","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR37324","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9149709","identifier":"P39363","identifierLink":"https://www.uniprot.org/uniprotkb/P39363/entry","name":"sgcA","description":"Putative phosphotransferase IIA component SgcA","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR36203","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5991","complexName":"Nuclear mitotic cohesin complex, STAG2 variant","organismName":"Homo sapiens; 9606","description":"Required for sister chromatid cohesion during mitotic cell division, which enables cells to attach sister kinetochores  to microtubules with opposing polarity (bi-orientation) and subsequently resists the tendency of these microtubules to pull chromatids toward opposite spindle poles.","predictedComplex":false,"interactors":[{"ac":"EBI-1057252","identifier":"Q8N3U4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N3U4/entry","name":"STAG2","description":"Cohesin subunit SA-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11199","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-80690","identifier":"Q14683","identifierLink":"https://www.uniprot.org/uniprotkb/Q14683/entry","name":"SMC1A","description":"Structural maintenance of chromosomes protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-80718","identifier":"Q9UQE7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UQE7/entry","name":"SMC3","description":"Structural maintenance of chromosomes protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43977","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-80739","identifier":"O60216","identifierLink":"https://www.uniprot.org/uniprotkb/O60216/entry","name":"RAD21","description":"Double-strand-break repair protein rad21 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12585","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5992","complexName":"SMC5-SMC6 SUMO ligase complex, EID3 variant","organismName":"Homo sapiens; 9606","description":"SUMO ligase complex with a role in homologous recombination (HR) and replication. Required for chromosome segregation at repetitive sequences. Localizes to repetitive elements such as the rDNA and telomeres  where is is thought to promote and resolve HR-dependent intermediates using ATP hydrolysis to symmetrically reel DNA into loops.\r\nThe complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex (CPX-5989 and CPX-5991) to double-strand breaks. \r\n\r\nMutations within its subunits might result in chromosome breakage syndrome.\r\n\r\nThe EID3 variant complex appears to be largely present in the testis.","predictedComplex":false,"interactors":[{"ac":"EBI-10975834","identifier":"Q9BQI6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BQI6/entry","name":"SLF1","description":"SMC5-SMC6 complex localization factor protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46677","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2557356","identifier":"Q96MG7","identifierLink":"https://www.uniprot.org/uniprotkb/Q96MG7/entry","name":"NSMCE3","description":"Non-structural maintenance of chromosomes element 3 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11736","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2557372","identifier":"Q8WV22","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WV22/entry","name":"NSMCE1","description":"Non-structural maintenance of chromosomes element 1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20973","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2557388","identifier":"Q96MF7","identifierLink":"https://www.uniprot.org/uniprotkb/Q96MF7/entry","name":"NSMCE2","description":"E3 SUMO-protein ligase NSE2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21330","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2682240","identifier":"Q8IX21","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IX21/entry","name":"SLF2","description":"SMC5-SMC6 complex localization factor protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16046","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-605405","identifier":"Q8IY18","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IY18/entry","name":"SMC5","description":"Structural maintenance of chromosomes protein 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45916","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-605415","identifier":"Q96SB8","identifierLink":"https://www.uniprot.org/uniprotkb/Q96SB8/entry","name":"SMC6","description":"Structural maintenance of chromosomes protein 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19306","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744483","identifier":"Q8N140","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N140/entry","name":"EID3","description":"EP300-interacting inhibitor of differentiation 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16140","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5993","complexName":"26S proteasome complex","organismName":"Homo sapiens; 9606","description":"Multi-enzyme complex that functions as the primary degradation machinery for the selective turnover of surplus or damaged proteins within the cell. Proteins targeted for degradation are covalently labeled with polyubiquitin chains which are recognized and removed by the proteasome. The core contains the protease active sites (chymotrypsin-like, trypsin-like and peptidylglutamyl-peptide hydrolyzing) that perform the proteolysis reactions in an internal chamber. The regulatory particles act as a discriminating gateway for potential substrates. The base drives the mechanical substrate unfolding and translocation of the unstructured polypeptides into the degradation chamber of the core peptidase. The lid contains the deubiquitinating enzyme (DUB) PSMD14 that cleaves polyubiquitin chains from targeted substrates as an essential step in proteasomal substrate processing.","predictedComplex":false,"interactors":[{"ac":"EBI-348380","identifier":"P25788","identifierLink":"https://www.uniprot.org/uniprotkb/P25788/entry","name":"PSMA3","description":"Proteasome subunit alpha type-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355475","identifier":"P28066","identifierLink":"https://www.uniprot.org/uniprotkb/P28066/entry","name":"PSMA5","description":"Proteasome subunit alpha type-5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356070","identifier":"Q9UNM6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UNM6/entry","name":"PSMD13","description":"26S proteasome non-ATPase regulatory subunit 13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10539","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357598","identifier":"P62191","identifierLink":"https://www.uniprot.org/uniprotkb/P62191/entry","name":"PSMC1","description":"26S proteasome regulatory subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357622","identifier":"O43242","identifierLink":"https://www.uniprot.org/uniprotkb/O43242/entry","name":"PSMD3","description":"26S proteasome non-ATPase regulatory subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10758","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357648","identifier":"Q13200","identifierLink":"https://www.uniprot.org/uniprotkb/Q13200/entry","name":"PSMD2","description":"26S proteasome non-ATPase regulatory subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10943","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357659","identifier":"P51665","identifierLink":"https://www.uniprot.org/uniprotkb/P51665/entry","name":"PSMD7","description":"26S proteasome non-ATPase regulatory subunit 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10540","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357669","identifier":"P62333","identifierLink":"https://www.uniprot.org/uniprotkb/P62333/entry","name":"PSMC6","description":"26S proteasome regulatory subunit 10B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357745","identifier":"P62195","identifierLink":"https://www.uniprot.org/uniprotkb/P62195/entry","name":"PSMC5","description":"26S proteasome regulatory subunit 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357793","identifier":"P60900","identifierLink":"https://www.uniprot.org/uniprotkb/P60900/entry","name":"PSMA6","description":"Proteasome subunit alpha type-6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357816","identifier":"O00231","identifierLink":"https://www.uniprot.org/uniprotkb/O00231/entry","name":"PSMD11","description":"26S proteasome non-ATPase regulatory subunit 11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357828","identifier":"P28074","identifierLink":"https://www.uniprot.org/uniprotkb/P28074/entry","name":"PSMB5","description":"Proteasome subunit beta type-5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357874","identifier":"Q99460","identifierLink":"https://www.uniprot.org/uniprotkb/Q99460/entry","name":"PSMD1","description":"26S proteasome non-ATPase regulatory subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10943","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359288","identifier":"P28072","identifierLink":"https://www.uniprot.org/uniprotkb/P28072/entry","name":"PSMB6","description":"Proteasome subunit beta type-6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359304","identifier":"P48556","identifierLink":"https://www.uniprot.org/uniprotkb/P48556/entry","name":"PSMD8","description":"26S proteasome non-ATPase regulatory subunit 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12387","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359310","identifier":"P25789","identifierLink":"https://www.uniprot.org/uniprotkb/P25789/entry","name":"PSMA4","description":"Proteasome subunit alpha type-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359318","identifier":"P55036","identifierLink":"https://www.uniprot.org/uniprotkb/P55036/entry","name":"PSMD4","description":"26S proteasome non-ATPase regulatory subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10223","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359335","identifier":"P49721","identifierLink":"https://www.uniprot.org/uniprotkb/P49721/entry","name":"PSMB2","description":"Proteasome subunit beta type-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359352","identifier":"P25786","identifierLink":"https://www.uniprot.org/uniprotkb/P25786/entry","name":"PSMA1","description":"Proteasome subunit alpha type-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359701","identifier":"Q15008","identifierLink":"https://www.uniprot.org/uniprotkb/Q15008/entry","name":"PSMD6","description":"26S proteasome non-ATPase regulatory subunit 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14145","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359710","identifier":"P35998","identifierLink":"https://www.uniprot.org/uniprotkb/P35998/entry","name":"PSMC2","description":"26S proteasome regulatory subunit 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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The fructose-specific PTS has no requirement for hpr/ptsH (P0AA04), ptsA/fruA combines a IIA domain with a HPr domain. The frw operon contains two IIB encoding genes (frwB and frwD) rather than  duplicated domains on a single polypeptide chains","predictedComplex":false,"interactors":[{"ac":"EBI-1134271","identifier":"P69816","identifierLink":"https://www.uniprot.org/uniprotkb/P69816/entry","name":"frwB","description":"PTS system fructose-like EIIB component 2","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-25754531","identifier":"P32672","identifierLink":"https://www.uniprot.org/uniprotkb/P32672/entry","name":"frwC","description":"Fructose-like permease IIC component 2","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30505","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25754549","identifier":"P32670","identifierLink":"https://www.uniprot.org/uniprotkb/P32670/entry","name":"ptsA","description":"Multiphosphoryl transfer protein 2","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR46244","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9135026","identifier":"P32676","identifierLink":"https://www.uniprot.org/uniprotkb/P32676/entry","name":"frwD","description":"PTS system fructose-like EIIB component 3","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]}]},{"complexAC":"CPX-6016","complexName":"ISGF3 complex","organismName":"Homo sapiens; 9606","description":"Transcription factor complex that is activated in response to type I interferon. Binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell into an antiviral state. STAT1 and STAT2 are usually phosphorylated in this complex but a continuous exposure of cells to a low level of IFN-beta induces the expression of the related, unphosphorylated complex. This unphosphorylated complex maintains the expression of a subset of the initially IFN-beta‐stimulated genes whose protein products lead to extended resistance to virus infection and DNA damage.","predictedComplex":false,"interactors":[{"ac":"EBI-1057697","identifier":"P42224","identifierLink":"https://www.uniprot.org/uniprotkb/P42224/entry","name":"STAT1","description":"Signal transducer and activator of transcription 1-alpha/beta","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11801","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1546963","identifier":"P52630","identifierLink":"https://www.uniprot.org/uniprotkb/P52630/entry","name":"STAT2","description":"Signal transducer and activator of transcription 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11801","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-626526","identifier":"Q00978","identifierLink":"https://www.uniprot.org/uniprotkb/Q00978/entry","name":"IRF9","description":"Interferon regulatory factor 9","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11949","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6017","complexName":"RZZ complex","organismName":"Homo sapiens; 9606","description":"A kinetochore component required for mitotic spindle assembly checkpoints. Builds a fibrous corona that assembles on mitotic kinetochores before microtubule attachment to promote chromosome alignment and robust spindle assembly checkpoint signaling. Required for the assembly of the dynein-dynactin and MAD1-MAD2 (CPX-85) complexes onto kinetochores.","predictedComplex":false,"interactors":[{"ac":"EBI-1001217","identifier":"O43264","identifierLink":"https://www.uniprot.org/uniprotkb/O43264/entry","name":"ZW10","description":"Centromere/kinetochore protein zw10 homolog","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12205","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1001239","identifier":"Q9H900","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H900/entry","name":"ZWILCH","description":"Protein zwilch homolog","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15995","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1001245","identifier":"P50748","identifierLink":"https://www.uniprot.org/uniprotkb/P50748/entry","name":"KNTC1","description":"Kinetochore-associated protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15688","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6018","complexName":"STING-TRAF3-TBK1 complex","organismName":"Homo sapiens; 9606","description":"Serine/threonine-kinase complex that, in response to viral infection, phosphorylates IRF3 (Q14653) to activate type I IFN production.","predictedComplex":false,"interactors":[{"ac":"EBI-2800345","identifier":"Q86WV6","identifierLink":"https://www.uniprot.org/uniprotkb/Q86WV6/entry","name":"STING1","description":"Stimulator of interferon genes protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR34339","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356402","identifier":"Q9UHD2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UHD2/entry","name":"TBK1","description":"Serine/threonine-protein kinase TBK1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22969","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357631","identifier":"Q13114","identifierLink":"https://www.uniprot.org/uniprotkb/Q13114/entry","name":"TRAF3","description":"TNF receptor-associated factor 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6019","complexName":"Putative dimethyl sulfoxide reductase","organismName":"Escherichia coli (strain K12); 83333","description":"Probably required for the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS) and other S- and N-oxide compounds during anaerobic growth. Has also been suggested to be a selenate reductase. The operon is induced under anaerobic conditions but is repressed by nitrate ions.","predictedComplex":false,"interactors":[{"ac":"EBI-11426020","identifier":"CHEBI:60539","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60539","name":"mo(=o)-bis(molybdopterin guanine dinucleotide)(4-)","description":"Mo(=O)-bis(molybdopterin guanine dinucleotide)(4-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-25757927","identifier":"P76173","identifierLink":"https://www.uniprot.org/uniprotkb/P76173/entry","name":"ynfH","description":"Anaerobic dimethyl sulfoxide reductase chain YnfH","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR38095","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25757943","identifier":"P0AAJ1","identifierLink":"https://www.uniprot.org/uniprotkb/P0AAJ1/entry","name":"ynfG","description":"Probable anaerobic dimethyl sulfoxide reductase chain YnfG","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6406285","identifier":"P77783","identifierLink":"https://www.uniprot.org/uniprotkb/P77783/entry","name":"ynfF","description":"Probable dimethyl sulfoxide reductase chain YnfF","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6020","complexName":"MdtIJ spermidine export complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes spermidine:proton antiport activity where the proton motive force provides the driving force for spermidine efflux. May transport other, generally cationic, compounds.","predictedComplex":false,"interactors":[{"ac":"EBI-1131904","identifier":"P69210","identifierLink":"https://www.uniprot.org/uniprotkb/P69210/entry","name":"mdtI","description":"Spermidine export protein MdtI","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30561","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25758463","identifier":"P69212","identifierLink":"https://www.uniprot.org/uniprotkb/P69212/entry","name":"mdtJ","description":"Spermidine export protein MdtJ","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30561","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6021","complexName":"SdsRQP multidrug transport complex","organismName":"Escherichia coli (strain K12); 83333","description":"Potential sulfa drug efflux pump.","predictedComplex":false,"interactors":[{"ac":"EBI-1124272","identifier":"P32714","identifierLink":"https://www.uniprot.org/uniprotkb/P32714/entry","name":"mdtP","description":"Multidrug resistance outer membrane protein MdtP","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30203","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1134618","identifier":"P32716","identifierLink":"https://www.uniprot.org/uniprotkb/P32716/entry","name":"mdtN","description":"Multidrug resistance protein MdtN","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30367","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-555775","identifier":"P32715","identifierLink":"https://www.uniprot.org/uniprotkb/P32715/entry","name":"mdtO","description":"Multidrug resistance protein MdtO","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30509","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6022","complexName":"KbaYZ tagatose-1,6-bisphosphate aldolase complex","organismName":"Escherichia coli (strain K12); 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83333","xrefs":[{"identifier":"PTHR30304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-6023","complexName":"GatYZ tagatose-1,6-bisphosphate aldolase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the reversible aldol condensation of dihydroxyacetone phosphate (CHEBI:16108) with glyceraldehyde 3-phosphate (CHEBI:17138) to produce tagatose 1,6-bisphosphate (CHEBI:16743) as a step in the catabolism of galactitol (CHEBI:16813).","predictedComplex":false,"interactors":[{"ac":"EBI-549361","identifier":"P0C8J6","identifierLink":"https://www.uniprot.org/uniprotkb/P0C8J6/entry","name":"gatY","description":"D-tagatose-1,6-bisphosphate aldolase subunit GatY","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-550954","identifier":"P0C8J8","identifierLink":"https://www.uniprot.org/uniprotkb/P0C8J8/entry","name":"gatZ","description":"D-tagatose-1,6-bisphosphate aldolase subunit GatZ","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32502","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-6024","complexName":"Interferon gamma complex","organismName":"Homo sapiens; 9606","description":"Cytokine secreted in response to infectious agents. Coordinates a diverse array of cellular programs through transcriptional regulation of immunologically relevant genes. Type II interferons exert their function through triggering the formation of a Receptor complex (CPX-6015).","predictedComplex":false,"interactors":[{"ac":"EBI-1030767","identifier":"P01579","identifierLink":"https://www.uniprot.org/uniprotkb/P01579/entry","name":"IFNG","description":"Interferon gamma","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11419","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6026","complexName":"YafNO toxin-antitoxin complex","organismName":"Escherichia coli (strain K12); 83333","description":"Type II toxin-antitoxin (TA) system formed by the toxin (yafO), and the antitoxin (yafN). TA systems act as effectors of dormancy and persistence, with the toxin causing growth arrest by interfering with a vital cellular process, such as  transcription, translation or DNA replication, and the cognate antitoxin neutralizing the toxin activity during normal growth conditions. Under conditions of stress the antitoxins are selectively degraded by cellular proteases such as Lon (P0A9M0) and ClpXP (CPX-3176), leaving the toxins to exert their effects which result in growth arrest and cell dormancy. Both the antitoxin and, in most cases, the TA complex bind the TA promoter to repress transcription, with TA complexes repressing transcription more efficiently than the antitoxins alone by increasing the co-operativity of antitoxin binding to operators. The YafNO genes are up-regulated during the SOS DNA damage response.","predictedComplex":false,"interactors":[{"ac":"EBI-1114856","identifier":"Q47156","identifierLink":"https://www.uniprot.org/uniprotkb/Q47156/entry","name":"yafN","description":"Antitoxin YafN","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33713","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1119355","identifier":"Q47157","identifierLink":"https://www.uniprot.org/uniprotkb/Q47157/entry","name":"yafO","description":"mRNA interferase toxin YafO","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]}]},{"complexAC":"CPX-6028","complexName":"Formate hydrogenlyase-H/Hydrogenase-4 complex","organismName":"Escherichia coli (strain K12); 83333","description":"Role in the mixed-acid fermentation that takes place under anaerobic conditions, ultimately producing molecular hydrogen.","predictedComplex":false,"interactors":[{"ac":"EBI-1121603","identifier":"P07658","identifierLink":"https://www.uniprot.org/uniprotkb/P07658/entry","name":"fdhF","description":"Formate dehydrogenase H","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1131425","identifier":"P77437","identifierLink":"https://www.uniprot.org/uniprotkb/P77437/entry","name":"hyfF","description":"Hydrogenase-4 component F","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42682","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11426020","identifier":"CHEBI:60539","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60539","name":"mo(=o)-bis(molybdopterin guanine dinucleotide)(4-)","description":"Mo(=O)-bis(molybdopterin guanine dinucleotide)(4-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-25760026","identifier":"P77858","identifierLink":"https://www.uniprot.org/uniprotkb/P77858/entry","name":"hyfC","description":"Hydrogenase-4 component C","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43359","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25760048","identifier":"P77416","identifierLink":"https://www.uniprot.org/uniprotkb/P77416/entry","name":"hyfD","description":"Hydrogenase-4 component D","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-548413","identifier":"P77329","identifierLink":"https://www.uniprot.org/uniprotkb/P77329/entry","name":"hyfG","description":"Hydrogenase-4 component G","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43485","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-553274","identifier":"P0AEW1","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEW1/entry","name":"hyfE","description":"Hydrogenase-4 component E","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR38601","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-554793","identifier":"P23482","identifierLink":"https://www.uniprot.org/uniprotkb/P23482/entry","name":"hyfB","description":"Hydrogenase-4 component B","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42682","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6029","complexName":"Formate dehydrogenase Z complex","organismName":"Escherichia coli (strain K12); 83333","description":"Formate:quinone oxidoreductase involved in electron transport during both aerobic and anaerobic respiration. Constitutively expressed, potentially allowing the cell to rapidly take advantage of changing growth conditions.","predictedComplex":false,"interactors":[{"ac":"EBI-1113082","identifier":"P0AEL0","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEL0/entry","name":"fdoI","description":"Formate dehydrogenase, cytochrome b556(fdo) subunit","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30074","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11426020","identifier":"CHEBI:60539","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60539","name":"mo(=o)-bis(molybdopterin guanine dinucleotide)(4-)","description":"Mo(=O)-bis(molybdopterin guanine dinucleotide)(4-)","stochiometry":"minValue: 3, maxValue: 3","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-25760299","identifier":"CHEBI:16374","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16374","name":"menaquinone","description":"menaquinone","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-368676","identifier":"P32176","identifierLink":"https://www.uniprot.org/uniprotkb/P32176/entry","name":"fdoG","description":"Formate dehydrogenase-O major subunit","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43598","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 6, maxValue: 6","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-6880484","identifier":"CHEBI:33725","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:33725","name":"fe4-s4","description":"tetra-μ3-sulfido-tetrairon","stochiometry":"minValue: 15, maxValue: 15","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-906676","identifier":"P0AAJ5","identifierLink":"https://www.uniprot.org/uniprotkb/P0AAJ5/entry","name":"fdoH","description":"Formate dehydrogenase-O iron-sulfur subunit","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43545","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6030","complexName":"Chaperonin-containing T-complex","organismName":"Homo sapiens; 9606","description":"Group II Heat Shock Protein 60 chaperonins which catalyses the cytoplasmic ATP-dependent folding of a subset of newly synthesized cytosolic proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-355710","identifier":"P48643","identifierLink":"https://www.uniprot.org/uniprotkb/P48643/entry","name":"CCT5","description":"T-complex protein 1 subunit epsilon","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356507","identifier":"P50990","identifierLink":"https://www.uniprot.org/uniprotkb/P50990/entry","name":"CCT8","description":"T-complex protein 1 subunit theta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356553","identifier":"P17987","identifierLink":"https://www.uniprot.org/uniprotkb/P17987/entry","name":"TCP1","description":"T-complex protein 1 subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356673","identifier":"P49368","identifierLink":"https://www.uniprot.org/uniprotkb/P49368/entry","name":"CCT3","description":"T-complex protein 1 subunit gamma","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356687","identifier":"P40227","identifierLink":"https://www.uniprot.org/uniprotkb/P40227/entry","name":"CCT6A","description":"T-complex protein 1 subunit zeta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356876","identifier":"P50991","identifierLink":"https://www.uniprot.org/uniprotkb/P50991/entry","name":"CCT4","description":"T-complex protein 1 subunit delta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357046","identifier":"Q99832","identifierLink":"https://www.uniprot.org/uniprotkb/Q99832/entry","name":"CCT7","description":"T-complex protein 1 subunit eta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357407","identifier":"P78371","identifierLink":"https://www.uniprot.org/uniprotkb/P78371/entry","name":"CCT2","description":"T-complex protein 1 subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6031","complexName":"Survival motor neuron complex","organismName":"Homo sapiens; 9606","description":"Molecular chaperone that plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, thus playing an important role in the splicing of cellular pre-mRNAs. With the PRMT5 methylosome complex (CPX-696), mediates the ordered assembly of the Sm complex (CPX-6033).","predictedComplex":false,"interactors":[{"ac":"EBI-2626001","identifier":"Q9NWZ8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NWZ8/entry","name":"GEMIN8","description":"Gem-associated protein 8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16238","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347658","identifier":"Q9UHI6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UHI6/entry","name":"DDX20","description":"Probable ATP-dependent RNA helicase DDX20","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47958","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356700","identifier":"P57678","identifierLink":"https://www.uniprot.org/uniprotkb/P57678/entry","name":"GEMIN4","description":"Gem-associated protein 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15571","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395421","identifier":"Q16637","identifierLink":"https://www.uniprot.org/uniprotkb/Q16637/entry","name":"SMN1","description":"Survival motor neuron protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13681","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-443630","identifier":"Q8TEQ6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TEQ6/entry","name":"GEMIN5","description":"Gem-associated protein 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46362","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-443648","identifier":"O14893","identifierLink":"https://www.uniprot.org/uniprotkb/O14893/entry","name":"GEMIN2","description":"Gem-associated protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12794","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-715455","identifier":"Q9H840","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H840/entry","name":"GEMIN7","description":"Gem-associated protein 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14679","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727414","identifier":"Q9Y3F4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3F4/entry","name":"STRAP","description":"Serine-threonine kinase receptor-associated protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19877","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752301","identifier":"Q8WXD5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WXD5/entry","name":"GEMIN6","description":"Gem-associated protein 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14710","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6033","complexName":"Sm complex","organismName":"Homo sapiens; 9606","description":"Essential role in pre-mRNA splicing. 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U1, U2, U4 and U5 snRNAs are produced in the nucleus by RNA polymerase II and exported to the cytoplasm, where the Sm proteins bind to them and promote the hypermethylation of the N7-monomethyl guanosine cap at their 5'-ends, to produce the 2,2,7-trimethyl guanosine cap structure.","predictedComplex":false,"interactors":[{"ac":"EBI-297993","identifier":"P62316","identifierLink":"https://www.uniprot.org/uniprotkb/P62316/entry","name":"SNRPD2","description":"Small nuclear ribonucleoprotein Sm D2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12777","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348082","identifier":"P62304","identifierLink":"https://www.uniprot.org/uniprotkb/P62304/entry","name":"SNRPE","description":"Small nuclear ribonucleoprotein E","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11193","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356900","identifier":"P62306","identifierLink":"https://www.uniprot.org/uniprotkb/P62306/entry","name":"SNRPF","description":"Small nuclear ribonucleoprotein F","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372177","identifier":"P62314","identifierLink":"https://www.uniprot.org/uniprotkb/P62314/entry","name":"SNRPD1","description":"Small nuclear ribonucleoprotein Sm D1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372458","identifier":"P14678","identifierLink":"https://www.uniprot.org/uniprotkb/P14678/entry","name":"SNRPB","description":"Small nuclear ribonucleoprotein-associated proteins B and B'","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372789","identifier":"P62318","identifierLink":"https://www.uniprot.org/uniprotkb/P62318/entry","name":"SNRPD3","description":"Small nuclear ribonucleoprotein Sm D3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-624585","identifier":"P62308","identifierLink":"https://www.uniprot.org/uniprotkb/P62308/entry","name":"SNRPG","description":"Small nuclear ribonucleoprotein G","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6035","complexName":"Elongation Factor TU-TS, tufA variant","organismName":"Escherichia coli (strain K12); 83333","description":"Elongation factor guanine nucleotide exchange complex. tsf/EF-Ts serves as the guanine nucleotide exchange factor for tufA/EF-Tu, catalyzing the release of guanosine diphosphate from EF-Tu. This enables EF-Tu to bind to a new GTP molecule, release EF-Ts and promote the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-301077","identifier":"P0CE47","identifierLink":"https://www.uniprot.org/uniprotkb/P0CE47/entry","name":"tufA","description":"Elongation factor Tu 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43721","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301164","identifier":"P0A6P1","identifierLink":"https://www.uniprot.org/uniprotkb/P0A6P1/entry","name":"tsf","description":"Elongation factor Ts","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11741","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6036","complexName":"Eukaryotic translation initiation factor 3 complex","organismName":"Homo sapiens; 9606","description":"Required for several steps in the initiation of protein synthesis. It associates with the 40S ribosome and facilitates the recruitment of eIF subunits to form the 43S pre-initiation complex (43S PIC). It is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S (CPX-5223) and 60S (CPX-5183) ribosomal subunits prior to initiation.","predictedComplex":false,"interactors":[{"ac":"EBI-347740","identifier":"P60228","identifierLink":"https://www.uniprot.org/uniprotkb/P60228/entry","name":"EIF3E","description":"Eukaryotic translation initiation factor 3 subunit E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10317","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353741","identifier":"Q99613","identifierLink":"https://www.uniprot.org/uniprotkb/Q99613/entry","name":"EIF3C","description":"Eukaryotic translation initiation factor 3 subunit C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353818","identifier":"O15371","identifierLink":"https://www.uniprot.org/uniprotkb/O15371/entry","name":"EIF3D","description":"Eukaryotic translation initiation factor 3 subunit D","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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MAVS-TRAF3 complex initiates type I IFN signalling and leads to activation of TBK1-IKKepsilon kinase (CPX-6038) which in turn phosphorylates and activates transcription factors IRF3 (Q14653) and IRF7 (Q92985).","predictedComplex":false,"interactors":[{"ac":"EBI-357631","identifier":"Q13114","identifierLink":"https://www.uniprot.org/uniprotkb/Q13114/entry","name":"TRAF3","description":"TNF receptor-associated factor 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-995373","identifier":"Q7Z434","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z434/entry","name":"MAVS","description":"Mitochondrial antiviral-signaling protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21446","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6038","complexName":"TBK1-IKKepsilon-NAP1 complex","organismName":"Homo sapiens; 9606","description":"Serine/threonine-protein kinase complex activated by MAVS-TRAF3 complex (CPX-6037) upon RNA virus infection. 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It mediates the response to IL23 (CPX-3290).","predictedComplex":false,"interactors":[{"ac":"EBI-1186538","identifier":"Q14765","identifierLink":"https://www.uniprot.org/uniprotkb/Q14765/entry","name":"STAT4","description":"Signal transducer and activator of transcription 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11801","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-518675","identifier":"P40763","identifierLink":"https://www.uniprot.org/uniprotkb/P40763/entry","name":"STAT3","description":"Signal transducer and activator of transcription 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11801","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6047","complexName":"STAT2/STAT6 complex","organismName":"Homo sapiens; 9606","description":"Signal transducer and transcription activator that mediates cellular responses to interleukins and other growth factors. It mediates the response to IL4 (P05112) and type I interferon.","predictedComplex":false,"interactors":[{"ac":"EBI-1186478","identifier":"P42226","identifierLink":"https://www.uniprot.org/uniprotkb/P42226/entry","name":"STAT6","description":"Signal transducer and activator of transcription 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11801","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1546963","identifier":"P52630","identifierLink":"https://www.uniprot.org/uniprotkb/P52630/entry","name":"STAT2","description":"Signal transducer and activator of transcription 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11801","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6048","complexName":"STAT1 homodimer","organismName":"Homo sapiens; 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Regulates homeostatic control of organelle volume and function during stress.","predictedComplex":false,"interactors":[{"ac":"EBI-11926384","identifier":"Q96ER9","identifierLink":"https://www.uniprot.org/uniprotkb/Q96ER9/entry","name":"CCDC51","description":"Mitochondrial potassium channel","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28624","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-722515","identifier":"Q9NUT2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NUT2/entry","name":"ABCB8","description":"Mitochondrial potassium channel ATP-binding subunit","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24221","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6084","complexName":"MITOK-MITOSUR mitochondrial potassium channel complex","organismName":"Mus musculus; 10090","description":"Mitochondrial inner membrane ATP-sensitive potassium channel which couples cell excitability with energy availability. 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Generally believed that APC acts as a scaffold that brings E2 enzymes and substrates into close proximity. APC activity is required for metaphase-anaphase transition, mitotic exit, G1 phase and DNA replication. Targets securin for destruction, which is necessary for chromosome segregation. APC seems to have similar function in meiosis. Co-activators, CDC20 (Q12834) and FRZ1/CDH1 (Q9UM11), associate with APC core complex (CPX-1860) at specific stages of cell cycle, and are thought to be involved in substrate specificity. APC-CDC20 is active in presence of high cyclin-cdk activity in M phase but after metaphase when cyclin-cdk activity decreases, FRZ1 is dephosphorylated, CDC20 is degraded and APC-FRZ1 (CPX-6088) activated.","predictedComplex":false,"interactors":[{"ac":"EBI-2649409","identifier":"CPX-1860","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-1860","name":"Anaphase-promoting core complex","description":"Anaphase-Promoting Complex variant 1","stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-367462","identifier":"Q12834","identifierLink":"https://www.uniprot.org/uniprotkb/Q12834/entry","name":"CDC20","description":"Cell division cycle protein 20 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19918","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6088","complexName":"Anaphase-promoting complex, FRZ1 variant","organismName":"Homo sapiens; 9606","description":"APC, a key regulator of cell cycle progression, is a conserved cullin-RING E3 ubiqutin ligase which facilitates multiubiqutination of cell cycle proteins, including cyclins, so marking them for proteasomal destruction. Generally believed that APC acts as a scaffold that brings E2 enzymes and substrates into close proximity. APC activity is required for metaphase-anaphase transition, mitotic exit, G1 phase and DNA replication. Targets securin for destruction, which is necessary for chromosome segregation. APC seems to have similar function in meiosis. Co-activators, CDC20 (Q12834) and FRZ1/CDH1 (Q9UM11), associate with APC core complex (CPX-1860) at specific stages of cell cycle, and are thought to be involved in substrate specificity. APC-CDC20 (CPX-6087) is active in presence of high cyclin-cdk activity in M phase but after metaphase when cyclin-cdk activity decreases, FRZ1 is dephosphorylated, CDC20 is degraded and APC-FRZ1 activated.","predictedComplex":false,"interactors":[{"ac":"EBI-2649409","identifier":"CPX-1860","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-1860","name":"Anaphase-promoting core complex","description":"Anaphase-Promoting Complex variant 1","stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-724997","identifier":"Q9UM11","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UM11/entry","name":"FZR1","description":"Fizzy-related protein homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19918","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6089","complexName":"TBK1-IKKepsilon-TANK complex","organismName":"Homo sapiens; 9606","description":"Serine/threonine-protein kinase complex that plays a role in antiviral innate immunity.","predictedComplex":false,"interactors":[{"ac":"EBI-307369","identifier":"Q14164","identifierLink":"https://www.uniprot.org/uniprotkb/Q14164/entry","name":"IKBKE","description":"Inhibitor of nuclear factor kappa-B kinase subunit epsilon","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22969","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356349","identifier":"Q92844","identifierLink":"https://www.uniprot.org/uniprotkb/Q92844/entry","name":"TANK","description":"TRAF family member-associated NF-kappa-B activator","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15249","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356402","identifier":"Q9UHD2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UHD2/entry","name":"TBK1","description":"Serine/threonine-protein kinase TBK1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22969","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6090","complexName":"TBK1-IKKepsilon-SINTBAD complex","organismName":"Homo sapiens; 9606","description":"Serine/threonine-protein kinase complex that plays a role in antiviral innate immunity.","predictedComplex":false,"interactors":[{"ac":"EBI-307369","identifier":"Q14164","identifierLink":"https://www.uniprot.org/uniprotkb/Q14164/entry","name":"IKBKE","description":"Inhibitor of nuclear factor kappa-B kinase subunit epsilon","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22969","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356402","identifier":"Q9UHD2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UHD2/entry","name":"TBK1","description":"Serine/threonine-protein kinase TBK1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22969","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359969","identifier":"A7MCY6","identifierLink":"https://www.uniprot.org/uniprotkb/A7MCY6/entry","name":"TBKBP1","description":"TANK-binding kinase 1-binding protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14432","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6091","complexName":"LPL-GPIHBP1 triglyceride-rich lipoprotein processing complex","organismName":"Homo sapiens; 9606","description":"Lipoprotein processing complex required for the hydrolysis of triglycerides in the bloodstream and for the delivery of lipid nutrients to vital tissues. GPIHBP1 recruits LPL to the luminal surface of vascular endothelium, capturing it within the interstitial spaces and shuttling it across endothelial cells to the capillary lumen where it then catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins.","predictedComplex":false,"interactors":[{"ac":"EBI-715909","identifier":"P06858","identifierLink":"https://www.uniprot.org/uniprotkb/P06858/entry","name":"LPL","description":"Lipoprotein lipase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11610","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9080234","identifier":"Q8IV16","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IV16/entry","name":"GPIHBP1","description":"Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16983","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6092","complexName":"GRASP55-GM45 Golgi stacking complex","organismName":"Homo sapiens; 9606","description":"Peripheral membrane complex that plays a key role in Golgi stacking.  Each Golgi stack is formed by five to eight tightly aligned flattened cisternae, GRASP55-GM45 forms mitotically regulated trans-oligomers that act  to hold adjacent Golgi cisternae into a stack, in particular the medial-trans-cisternae-Golgi network, which contain glycosylation enzymes and process cargo proteins and lipids.","predictedComplex":false,"interactors":[{"ac":"EBI-2548012","identifier":"Q9H2G9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H2G9/entry","name":"BLZF1","description":"Golgin-45","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13066","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-739467","identifier":"Q9H8Y8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H8Y8/entry","name":"GORASP2","description":"Golgi reassembly-stacking protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12893","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6093","complexName":"TP53-MDM2-MDM4 transcription regulation complex","organismName":"Homo sapiens; 9606","description":"Transcriptional repressor complex, formation of which inhibits the ability of TP53/p53 to induce cell cycle arrest. The mechanism of action is primarily through the ubiquitinylation of p53, a critical step in mediating its degradation by nuclear and cytoplasmic proteasomes, and by directly inhibiting p53 transactivation capacity and by promoting the nuclear export of p53.","predictedComplex":false,"interactors":[{"ac":"EBI-366083","identifier":"P04637","identifierLink":"https://www.uniprot.org/uniprotkb/P04637/entry","name":"TP53","description":"Cellular tumor antigen p53","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11447","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-389668","identifier":"Q00987","identifierLink":"https://www.uniprot.org/uniprotkb/Q00987/entry","name":"MDM2","description":"E3 ubiquitin-protein ligase Mdm2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46858","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398437","identifier":"O15151","identifierLink":"https://www.uniprot.org/uniprotkb/O15151/entry","name":"MDM4","description":"Protein Mdm4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12183","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6094","complexName":"HOXD10-Geminin transcriptional repressor complex","organismName":"Homo sapiens; 9606","description":"Plays a role in preventing the HOXD10  transcription factor from binding to DNA, thus inhibiting Hox-dependent transcriptional activation of downstream target genes.May also play a role in cell cycle progression, inhibiting the formation of the Cdt1-Geminin complex (CPX-659), thus inhibiting the function of Geminin in DNA replication licensing regulation.","predictedComplex":false,"interactors":[{"ac":"EBI-12690664","identifier":"P28358","identifierLink":"https://www.uniprot.org/uniprotkb/P28358/entry","name":"HOXD10","description":"Homeobox protein Hox-D10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45874","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371669","identifier":"O75496","identifierLink":"https://www.uniprot.org/uniprotkb/O75496/entry","name":"GMNN","description":"Geminin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13372","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6095","complexName":"SARS-CoV 3a complex","organismName":"Severe acute respiratory syndrome coronavirus; 694009","description":"Outward rectifier potassium channel complex of SARS-CoV coronavirus that is also sensitive to calcium. May modulate virus release. Up-regulates expression of fibrinogen subunits FGA (P02671), FGB (P02675) and FGG (P02679) in host lung epithelial cells. Downregulates the type 1 interferon receptor by inducing serine phosphorylation within the IFN alpha-receptor subunit 1 (IFNAR1, P17181) degradation motif and increasing IFNAR1 ubiquitination. Induces NLRP3 inflammasome (CPX-4141) activation.","predictedComplex":false,"interactors":[{"ac":"EBI-15595051","identifier":"P59632","identifierLink":"https://www.uniprot.org/uniprotkb/P59632/entry","name":"ap3a","description":"ORF3a protein","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus; 694009","xrefs":[]}]},{"complexAC":"CPX-6096","complexName":"Thyroid-stimulating hormone complex","organismName":"Homo sapiens; 9606","description":"Glycoprotein hormone synthesized and secreted by thyrotrope cells in the anterior pituitary gland, which regulates the endocrine function of the thyroid. TSH stimulates the thyroid gland to produce thyroxine (T4, CHEBI:18332), which is subsequently converted to triiodothyronine (T3, CHEBI:18258) the active hormone that stimulates metabolism throughout the body. A member of the family of pituitary glycoprotein hormones that play key roles in human fertility.","predictedComplex":false,"interactors":[{"ac":"EBI-25816038","identifier":"P01222-PRO_0000011746","identifierLink":"https://www.uniprot.org/uniprotkb/P01222-PRO_0000011746/entry","name":"TSHB","description":"Thyrotropin subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-718913","identifier":"P01215","identifierLink":"https://www.uniprot.org/uniprotkb/P01215/entry","name":"CGA","description":"Glycoprotein hormones alpha chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11509","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6097","complexName":"Luteinizing hormone complex","organismName":"Homo sapiens; 9606","description":"Glycoprotein hormone synthesized and secreted by gonadotropic cells in the anterior pituitary gland. An acute rise in levels of LH triggers ovulation and development of the corpus luteum in females. In males, it stimulates Leydig cell production of testosterone. It acts synergistically with the follicle-stimulating hormone complex (CPX-665). A member of the family of pituitary glycoprotein hormones that play key roles in human fertility.","predictedComplex":false,"interactors":[{"ac":"EBI-11659791","identifier":"P01229","identifierLink":"https://www.uniprot.org/uniprotkb/P01229/entry","name":"LHB","description":"Lutropin subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11515","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-718913","identifier":"P01215","identifierLink":"https://www.uniprot.org/uniprotkb/P01215/entry","name":"CGA","description":"Glycoprotein hormones alpha chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11509","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6098","complexName":"SARS-CoV-2 3a complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","description":"Outward rectifier potassium channel complex of SARS-CoV-2 coronavirus that is also sensitive to calcium. May modulate virus release. Up-regulates expression of fibrinogen subunits FGA (P02671), FGB (P02675) and FGG (P02679) in host lung epithelial cells. Downregulates the type 1 interferon receptor by inducing serine phosphorylation within the IFN alpha-receptor subunit 1 (IFNAR1, P17181) degradation motif and increasing IFNAR1 ubiquitination. Induces NLRP3 inflammasome (CPX-4141) activation.","predictedComplex":false,"interactors":[{"ac":"EBI-25475894","identifier":"P0DTC3","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTC3/entry","name":"ap3a","description":"ORF3a protein","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]}]},{"complexAC":"CPX-6100","complexName":"SARS-CoV-2 9b complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","description":"Outer mitochondrial membrane-attached complex of SARS-CoV-2 coronavirus that triggers proteasome-mediated degradation of DNM1L (O00429) and the MAVS signalosome components MAVS, TRAF3, TRAF6 and TOM70. Although the precise mechanisms remain unknown, it leads to suppression of mitochondrial fission, triggers mitochondria elongation, decreases type I interferon signalling and triggers formation of autophagosomes.","predictedComplex":false,"interactors":[{"ac":"EBI-25475909","identifier":"P0DTD2","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTD2/entry","name":"orf9b","description":"ORF9b protein","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]}]},{"complexAC":"CPX-6101","complexName":"SARS-CoV 9b complex","organismName":"Severe acute respiratory syndrome coronavirus; 694009","description":"Outer mitochondrial membrane-attached complex of SARS-CoV coronavirus that triggers proteasome-mediated degradation of DNM1L (O00429) and the MAVS signalosome components MAVS, TRAF3, TRAF6 and TOM70. Although the precise mechanisms remain unknown, it leads to suppression of mitochondrial fission, triggers mitochondria elongation, decreases type I interferon signalling and triggers formation of autophagosomes.","predictedComplex":false,"interactors":[{"ac":"EBI-9021274","identifier":"P59636","identifierLink":"https://www.uniprot.org/uniprotkb/P59636/entry","name":"orf9b","description":"ORF9b protein","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus; 694009","xrefs":[]}]},{"complexAC":"CPX-6121","complexName":"TOM40 mitochondrial outer membrane translocase complex","organismName":"Homo sapiens; 9606","description":"Translocase in the outer mitochondrial membrane that mediates the import of precursor protein and mediates inset of some resident outer membrane proteins. Most mitochondrial proteins are synthesised in the cytosol, imported into mitochondria, sorted to one of the four sub-mitochondrial compartments, where they function, and attain their functional native conformation, which is often facilitated by assembly into the membrane or a multi-protein complex. When translocation is coupled with that by the TIM23 (CPX-6129) or TIM22 (CPX-6124) complex, the TOM channel can operate as a passive pore to allow passage of the polypeptide segment, which is `pulled' by the TIM complex with the aid of differential membrane potential and/or ATP. When translocation is uncoupled from the inner-membrane translocators, the TOM complex uses both the stop-transfer pathway, which consists of two steps, the first requiring a membrane potential and an ATP-dependent chaperone mHsp70, and a second mechanism involving the folding of an N-terminal domain that has already crossed the outer membrane and can function as a trap in the intermembrane space to drive translocation of the C-terminal part of the protein by a Brownian ratchet mechanism.","predictedComplex":false,"interactors":[{"ac":"EBI-1047508","identifier":"Q9NS69","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NS69/entry","name":"TOMM22","description":"Mitochondrial import receptor subunit TOM22 homolog","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12504","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1057581","identifier":"O96008","identifierLink":"https://www.uniprot.org/uniprotkb/O96008/entry","name":"TOMM40","description":"Mitochondrial import receptor subunit TOM40 homolog","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10826510","identifier":"Q96B49","identifierLink":"https://www.uniprot.org/uniprotkb/Q96B49/entry","name":"TOMM6","description":"Mitochondrial import receptor subunit TOM6 homolog","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11032284","identifier":"Q8N4H5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N4H5/entry","name":"TOMM5","description":"Mitochondrial import receptor subunit TOM5 homolog","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28436","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1180558","identifier":"Q9P0U1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P0U1/entry","name":"TOMM7","description":"Mitochondrial import receptor subunit TOM7 homolog","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46722","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2800236","identifier":"O94826","identifierLink":"https://www.uniprot.org/uniprotkb/O94826/entry","name":"TOMM70","description":"Mitochondrial import receptor subunit TOM70","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46208","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-711636","identifier":"Q15388","identifierLink":"https://www.uniprot.org/uniprotkb/Q15388/entry","name":"TOMM20","description":"Mitochondrial import receptor subunit TOM20 homolog","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12430","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6123","complexName":"Mitochondrial respiratory chain complex IV","organismName":"Homo sapiens; 9606","description":"Terminal oxidase of the electron transport chain in mitochondria. It accepts electrons from cytochrome c to reduce the oxygen to water and pumps two protons from the matrix side to the intermembrane space. Electrons originating from reduced cytochrome c in the intermembrane space  are transferred via the dinuclear copper center of mt:CoII and heme A of mt:CoI to the active site in mt:CoI, a binuclear center formed by heme A3  and a second copper atom.. The binuclear center  reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the intermembrane space and 4 protons from the mitochondrial matrix.","predictedComplex":false,"interactors":[{"ac":"EBI-1047480","identifier":"P14854","identifierLink":"https://www.uniprot.org/uniprotkb/P14854/entry","name":"COX6B1","description":"Cytochrome c oxidase subunit 6B1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11387","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1049381","identifier":"O00483","identifierLink":"https://www.uniprot.org/uniprotkb/O00483/entry","name":"NDUFA4","description":"Cytochrome c oxidase subunit NDUFA4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14256","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1053725","identifier":"P10606","identifierLink":"https://www.uniprot.org/uniprotkb/P10606/entry","name":"COX5B","description":"Cytochrome c oxidase subunit 5B, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10122","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1056574","identifier":"P13073","identifierLink":"https://www.uniprot.org/uniprotkb/P13073/entry","name":"COX4I1","description":"Cytochrome c oxidase subunit 4 isoform 1, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10707","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12592690","identifier":"CHEBI:23378","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:23378","name":"copper cation","description":"copper cation","stochiometry":"minValue: 3, maxValue: 3","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2105756","identifier":"P00403","identifierLink":"https://www.uniprot.org/uniprotkb/P00403/entry","name":"MT-CO2","description":"Cytochrome c oxidase subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2115950","identifier":"P12074","identifierLink":"https://www.uniprot.org/uniprotkb/P12074/entry","name":"COX6A1","description":"Cytochrome c oxidase subunit 6A1, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11504","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2117234","identifier":"P00395","identifierLink":"https://www.uniprot.org/uniprotkb/P00395/entry","name":"MT-CO1","description":"Cytochrome c oxidase subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10422","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2606666","identifier":"P14406","identifierLink":"https://www.uniprot.org/uniprotkb/P14406/entry","name":"COX7A2","description":"Cytochrome c oxidase subunit 7A2, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10510","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2606678","identifier":"P15954","identifierLink":"https://www.uniprot.org/uniprotkb/P15954/entry","name":"COX7C","description":"Cytochrome c oxidase subunit 7C, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13313","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2684371","identifier":"P24311","identifierLink":"https://www.uniprot.org/uniprotkb/P24311/entry","name":"COX7B","description":"Cytochrome c oxidase subunit 7B, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16716","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3904738","identifier":"P10176","identifierLink":"https://www.uniprot.org/uniprotkb/P10176/entry","name":"COX8A","description":"Cytochrome c oxidase subunit 8A, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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In most cases, the pre-sequence is proteolytically removed by the mitochondrial-processing peptidase (CPX-1630).","predictedComplex":false,"interactors":[{"ac":"EBI-26019","identifier":"P42949","identifierLink":"https://www.uniprot.org/uniprotkb/P42949/entry","name":"PAM16","description":"Mitochondrial import inner membrane translocase subunit TIM16","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12388","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26467","identifier":"P36147","identifierLink":"https://www.uniprot.org/uniprotkb/P36147/entry","name":"PAM17","description":"Presequence translocated-associated motor subunit PAM17, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30302","identifier":"Q02776","identifierLink":"https://www.uniprot.org/uniprotkb/Q02776/entry","name":"TIM50","description":"Mitochondrial import inner membrane translocase subunit TIM50","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31963","identifier":"Q07914","identifierLink":"https://www.uniprot.org/uniprotkb/Q07914/entry","name":"PAM18","description":"Mitochondrial import inner membrane translocase subunit TIM14","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12763","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7891","identifier":"P38523","identifierLink":"https://www.uniprot.org/uniprotkb/P38523/entry","name":"MGE1","description":"GrpE protein homolog, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21237","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8637","identifier":"P0CS90","identifierLink":"https://www.uniprot.org/uniprotkb/P0CS90/entry","name":"SSC1","description":"Import motor subunit, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9127","identifier":"P39515","identifierLink":"https://www.uniprot.org/uniprotkb/P39515/entry","name":"TIM17","description":"Mitochondrial import inner membrane translocase subunit TIM17","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10485","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9136","identifier":"P32897","identifierLink":"https://www.uniprot.org/uniprotkb/P32897/entry","name":"TIM23","description":"Mitochondrial import inner membrane translocase subunit TIM23","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15371","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9141","identifier":"Q01852","identifierLink":"https://www.uniprot.org/uniprotkb/Q01852/entry","name":"TIM44","description":"Mitochondrial import inner membrane translocase subunit TIM44","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10721","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6131","complexName":"TIM8A-TIM13 mitochondrial intermembrane space protein transporter complex","organismName":"Homo sapiens; 9606","description":"Facilitates transport of hydrophobic precursors of a distinct subgroup of inner membrane proteins through the aqueous intermembrane space as they exit the TOM40 channel complex (CPX-6121) in the outer membrane. Functions as a chaperone to maintain the hydrophobic membrane proteins in an import competent state and escort substrates to the TIM22 insertion complex (CPX-6124), which mediates protein insertion into the membrane.\r\nLoss-of-function mutations in the DDP1/TIMM8A gene can cause the Mohr-Tranebjaerg syndrome.","predictedComplex":false,"interactors":[{"ac":"EBI-1049822","identifier":"O60220","identifierLink":"https://www.uniprot.org/uniprotkb/O60220/entry","name":"TIMM8A","description":"Mitochondrial import inner membrane translocase subunit Tim8 A","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1057344","identifier":"Q9Y5L4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5L4/entry","name":"TIMM13","description":"Mitochondrial import inner membrane translocase subunit Tim13","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6132","complexName":"TIM8B-TIM13 mitochondrial intermembrane space protein transporter complex","organismName":"Homo sapiens; 9606","description":"Facilitates transport of hydrophobic precursors of a distinct subgroup of inner membrane proteins through the aqueous intermembrane space as they exit the TOM40 channel complex (CPX-6121) in the outer membrane. Functions as a chaperone to maintain the hydrophobic membrane proteins in an import competent state and escorts substrates to the TIM22 insertion complex (CPX-6124), which mediates protein insertion into the membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-1049085","identifier":"Q9Y5J9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5J9/entry","name":"TIMM8B","description":"Mitochondrial import inner membrane translocase subunit Tim8 B","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1057344","identifier":"Q9Y5L4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5L4/entry","name":"TIMM13","description":"Mitochondrial import inner membrane translocase subunit Tim13","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6133","complexName":"SAM mitochondrial sorting and assembly machinery complex","organismName":"Homo sapiens; 9606","description":"Mediates insertion of beta-barrel proteins into the mitochondrial outer membrane. These are synthesized on cytosolic ribosomes and recognized initially by the import receptors of the translocase of the mitochondrial outer membrane (TOM40 complex CPX-6121). They are then translocated across the outer membrane via the general-import pore of the TOM40 complex and relayed to the SAM complex.","predictedComplex":false,"interactors":[{"ac":"EBI-1052588","identifier":"Q13505","identifierLink":"https://www.uniprot.org/uniprotkb/Q13505/entry","name":"MTX1","description":"Metaxin-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12289","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7415268","identifier":"O75431","identifierLink":"https://www.uniprot.org/uniprotkb/O75431/entry","name":"MTX2","description":"Metaxin-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12289","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-748409","identifier":"Q9Y512","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y512/entry","name":"SAMM50","description":"Sorting and assembly machinery component 50 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12815","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6134","complexName":"Phagocyte NADPH oxidase complex, RAC2 variant","organismName":"Homo sapiens; 9606","description":"Plays a crucial role in host defense against microbial infections by generating reactive oxygen species. Transfers electrons across the wall of the phagocytic vacuole, forming superoxide in the lumen and promoting microbial killing through the generation of reactive oxygen species and through the activity of myeloperoxidase.","predictedComplex":false,"interactors":[{"ac":"EBI-1036870","identifier":"Q15080","identifierLink":"https://www.uniprot.org/uniprotkb/Q15080/entry","name":"NCF4","description":"Neutrophil cytosol factor 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15706","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25820308","identifier":"CHEBI:37565","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:37565","name":"gtp(4-)","description":"GTP(4-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-395044","identifier":"P14598","identifierLink":"https://www.uniprot.org/uniprotkb/P14598/entry","name":"NCF1","description":"Neutrophil cytosol factor 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15706","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-489611","identifier":"P19878","identifierLink":"https://www.uniprot.org/uniprotkb/P19878/entry","name":"NCF2","description":"Neutrophil cytosol factor 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15175","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-489652","identifier":"P15153","identifierLink":"https://www.uniprot.org/uniprotkb/P15153/entry","name":"RAC2","description":"Ras-related C3 botulinum toxin substrate 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24072","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6253630","identifier":"P04839","identifierLink":"https://www.uniprot.org/uniprotkb/P04839/entry","name":"CYBB","description":"NADPH oxidase 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11972","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-986058","identifier":"P13498","identifierLink":"https://www.uniprot.org/uniprotkb/P13498/entry","name":"CYBA","description":"Cytochrome b-245 light chain","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15168","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6135","complexName":"Phagocyte NADPH oxidase complex, RAC3 variant","organismName":"Homo sapiens; 9606","description":"Plays a crucial role in host defense against microbial infections by generating reactive oxygen species. Transfers electrons across the wall of the phagocytic vacuole, forming superoxide in the lumen and promoting microbial killing through the generation of reactive oxygen species and through the activity of myeloperoxidase.","predictedComplex":false,"interactors":[{"ac":"EBI-1036870","identifier":"Q15080","identifierLink":"https://www.uniprot.org/uniprotkb/Q15080/entry","name":"NCF4","description":"Neutrophil cytosol factor 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15706","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25820308","identifier":"CHEBI:37565","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:37565","name":"gtp(4-)","description":"GTP(4-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-395044","identifier":"P14598","identifierLink":"https://www.uniprot.org/uniprotkb/P14598/entry","name":"NCF1","description":"Neutrophil cytosol factor 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15706","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-489611","identifier":"P19878","identifierLink":"https://www.uniprot.org/uniprotkb/P19878/entry","name":"NCF2","description":"Neutrophil cytosol factor 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15175","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6253630","identifier":"P04839","identifierLink":"https://www.uniprot.org/uniprotkb/P04839/entry","name":"CYBB","description":"NADPH oxidase 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11972","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-767084","identifier":"P60763","identifierLink":"https://www.uniprot.org/uniprotkb/P60763/entry","name":"RAC3","description":"Ras-related C3 botulinum toxin substrate 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24072","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-986058","identifier":"P13498","identifierLink":"https://www.uniprot.org/uniprotkb/P13498/entry","name":"CYBA","description":"Cytochrome b-245 light chain","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15168","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6141","complexName":"MICOS mitochondrial contact site and cristae organizing system complex","organismName":"Homo sapiens; 9606","description":"Required to maintain the folding of the mitochondrial inner membrane into cristae, crista junctions, inner membrane architecture, and the formation of contact sites to the outer mitochondrial membrane. Part of the mitochondrial intermembrane space bridging (MIB) super-complex.","predictedComplex":false,"interactors":[{"ac":"EBI-1053887","identifier":"Q5XKP0","identifierLink":"https://www.uniprot.org/uniprotkb/Q5XKP0/entry","name":"MICOS13","description":"MICOS complex subunit MIC13","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31816","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10763408","identifier":"Q9BUR5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BUR5/entry","name":"APOO","description":"MICOS complex subunit MIC26","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14564","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12886442","identifier":"Q5TGZ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q5TGZ0/entry","name":"MICOS10","description":"MICOS complex subunit MIC10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2557895","identifier":"Q9BRQ6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BRQ6/entry","name":"CHCHD6","description":"MICOS complex subunit MIC25","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47609","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-473801","identifier":"Q16891","identifierLink":"https://www.uniprot.org/uniprotkb/Q16891/entry","name":"IMMT","description":"MICOS complex subunit MIC60","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15415","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743375","identifier":"Q9NX63","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NX63/entry","name":"CHCHD3","description":"MICOS complex subunit MIC19","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9641073","identifier":"Q6UXV4","identifierLink":"https://www.uniprot.org/uniprotkb/Q6UXV4/entry","name":"APOOL","description":"MICOS complex subunit MIC27","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14564","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6142","complexName":"TSC1-TSC2 complex","organismName":"Homo sapiens; 9606","description":"Acts as a GTPase-activating protein (GAP) for the small GTPase RHEB (Q15382) thus negatively regulating mTORC1 signaling.\r\n\r\nTSC1 and TSC2 are the tumor suppressor genes.","predictedComplex":false,"interactors":[{"ac":"EBI-1047085","identifier":"Q92574","identifierLink":"https://www.uniprot.org/uniprotkb/Q92574/entry","name":"TSC1","description":"Hamartin","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15154","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3258000","identifier":"Q9P0N9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P0N9/entry","name":"TBC1D7","description":"TBC1 domain family member 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13530","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-396587","identifier":"P49815","identifierLink":"https://www.uniprot.org/uniprotkb/P49815/entry","name":"TSC2","description":"Tuberin","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10063","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6143","complexName":"R2TP core co-chaperone complex","organismName":"Homo sapiens; 9606","description":"Co-chaperone that works together with HSP90 in the activation and assembly of several macromolecular complexes, including RNA polymerase II, TSC1-TSC2 (CPX-6142) and mTORC1 (CPX-503).\r\nTogether with URI1 prefoldin complex (CPX-6144), POLR2E (P19388), ASDURF (L0R819) and WDR92 (Q96MX6) it forms the PAQosome complex (CPX-6145), which also acts as co-chaperone, but with different target specificities.","predictedComplex":false,"interactors":[{"ac":"EBI-352939","identifier":"Q9Y230","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y230/entry","name":"RUVBL2","description":"RuvB-like 2","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353675","identifier":"Q9Y265","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y265/entry","name":"RUVBL1","description":"RuvB-like 1","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356928","identifier":"Q9H6T3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H6T3/entry","name":"RPAP3","description":"RNA polymerase II-associated protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46423","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357318","identifier":"Q9NWS0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NWS0/entry","name":"PIH1D1","description":"PIH1 domain-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22997","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6144","complexName":"Prefoldin co-chaperone complex, URI1 variant","organismName":"Homo sapiens; 9606","description":"Co-chaperone that works together with HSP90 in the activation and assembly of several macromolecular complexes.\r\nTogether with R2TP complex (CPX-6143), POLR2E (P19388), ASDURF (L0R819) and WDR92 (Q96MX6) it forms the PAQosome complex (CPX-6145), that acts as co-chaperone as well, but with different target specificity.","predictedComplex":false,"interactors":[{"ac":"EBI-307050","identifier":"Q9NUG6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NUG6/entry","name":"PDRG1","description":"p53 and DNA damage-regulated protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21162","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356973","identifier":"O15212","identifierLink":"https://www.uniprot.org/uniprotkb/O15212/entry","name":"PFDN6","description":"Prefoldin subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21431","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357067","identifier":"O94763","identifierLink":"https://www.uniprot.org/uniprotkb/O94763/entry","name":"URI1","description":"Unconventional prefoldin RPB5 interactor 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15111","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357355","identifier":"Q9UBK9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UBK9/entry","name":"UXT","description":"Protein UXT","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13345","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359873","identifier":"Q9UHV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UHV9/entry","name":"PFDN2","description":"Prefoldin subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13303","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6145","complexName":"PAQosome co-chaperone complex","organismName":"Homo sapiens; 9606","description":"Co-chaperone that works together with HSP90, HSP70 and CCT in the activation and assembly of several macromolecular complexes.","predictedComplex":false,"interactors":[{"ac":"EBI-2434101","identifier":"Q96MX6","identifierLink":"https://www.uniprot.org/uniprotkb/Q96MX6/entry","name":"DNAAF10","description":"Dynein axonemal assembly factor 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25824475","identifier":"CPX-6143","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-6143","name":"R2TP core co-chaperone complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25824594","identifier":"CPX-6144","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-6144","name":"Prefoldin co-chaperone complex, URI1 variant","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25824664","identifier":"L0R819","identifierLink":"https://www.uniprot.org/uniprotkb/L0R819/entry","name":"ASDURF","description":"ASNSD1 upstream open reading frame protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-395189","identifier":"P19388","identifierLink":"https://www.uniprot.org/uniprotkb/P19388/entry","name":"POLR2E","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10535","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6147","complexName":"SARS-CoV-2 ORF8 complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","description":"SARS-CoV-2 coronavirus complex that negatively regulates the innate immune response. Binds MHC-I molecules intracellularly at the endoplasmic reticulum and targets them for lysosomal degradation by an autophagy-dependent mechanism. This down-regulates MHC-I cell surface expression and reduces the recognition and elimination of virus-infected cells by cytotoxic T-cells. Also inhibits type I interferon (IFN-beta) activation and downstream innate immune responses. \r\n\r\nProduces antibodies that are one of the principal markers of SARS-CoV-2 infections.","predictedComplex":false,"interactors":[{"ac":"EBI-25475900","identifier":"P0DTC8","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTC8/entry","name":"ns8","description":"ORF8 protein","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]}]},{"complexAC":"CPX-6148","complexName":"TTT complex","organismName":"Homo sapiens; 9606","description":"Co-chaperone complex that acts as a regulator of the DNA damage response (DDR). It is required to stabilize protein levels of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family proteins. Newly synthesized PIKK interacts with TELO2 assisted by HSP90. Phosphorylated TELO2 then appears to mediate the interaction between PIKK and R2TP (CPX-6143) complex to eventually lead to the proper assembly of PIKK. Promotes assembly, stabilizes and maintains the activity of mTORC1 (CPX-503) and mTORC2 (CPX-4402) complexes, which regulate cell growth and survival in response to nutrient and hormonal signals.","predictedComplex":false,"interactors":[{"ac":"EBI-1043674","identifier":"Q9Y4R8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4R8/entry","name":"TELO2","description":"Telomere length regulation protein TEL2 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15830","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1055680","identifier":"O43156","identifierLink":"https://www.uniprot.org/uniprotkb/O43156/entry","name":"TTI1","description":"TELO2-interacting protein 1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18460","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4566107","identifier":"Q6NXR4","identifierLink":"https://www.uniprot.org/uniprotkb/Q6NXR4/entry","name":"TTI2","description":"TELO2-interacting protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32226","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6149","complexName":"Prefoldin co-chaperone complex","organismName":"Homo sapiens; 9606","description":"Co-chaperone that works together with HSP90 in the activation and assembly of several macromolecular complexes. It binds specifically to cytosolic CCT complex (CPX-6030) and transfers target proteins to it.","predictedComplex":false,"interactors":[{"ac":"EBI-356919","identifier":"O60925","identifierLink":"https://www.uniprot.org/uniprotkb/O60925/entry","name":"PFDN1","description":"Prefoldin subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20903","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356973","identifier":"O15212","identifierLink":"https://www.uniprot.org/uniprotkb/O15212/entry","name":"PFDN6","description":"Prefoldin subunit 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21431","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357021","identifier":"Q9NQP4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NQP4/entry","name":"PFDN4","description":"Prefoldin subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21100","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357275","identifier":"Q99471","identifierLink":"https://www.uniprot.org/uniprotkb/Q99471/entry","name":"PFDN5","description":"Prefoldin subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12674","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357430","identifier":"P61758","identifierLink":"https://www.uniprot.org/uniprotkb/P61758/entry","name":"VBP1","description":"Prefoldin subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12409","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359873","identifier":"Q9UHV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UHV9/entry","name":"PFDN2","description":"Prefoldin subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13303","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6150","complexName":"R2SP co-chaperone complex","organismName":"Homo sapiens; 9606","description":"Co-chaperone required for liprin-alpha2/PPFIA2 (O75334) expression and for the assembly of liprin-alpha2 complex. This co-chaperone is particularly expressed in testis.","predictedComplex":false,"interactors":[{"ac":"EBI-10232538","identifier":"Q8WWB5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WWB5/entry","name":"PIH1D2","description":"PIH1 domain-containing protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22997","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10965756","identifier":"Q07617","identifierLink":"https://www.uniprot.org/uniprotkb/Q07617/entry","name":"SPAG1","description":"Sperm-associated antigen 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45984","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352939","identifier":"Q9Y230","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y230/entry","name":"RUVBL2","description":"RuvB-like 2","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353675","identifier":"Q9Y265","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y265/entry","name":"RUVBL1","description":"RuvB-like 1","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6151","complexName":"Mitochondrial proton-transporting ATP synthase complex","organismName":"Homo sapiens; 9606","description":"Acts to convert the energy of oxidation-reduction reactions of the electron transport chain (respiration) to the phosphorylation of ADP. The synthesis of ATP is coupled to the respiratory chain via the proton potential. The ATP synthase is a molecular motor composed of two separable parts: F1 and Fo. The F1 portion contains the catalytic sites for ATP synthesis and protrudes into the mitochondrial matrix. Fo forms a proton turbine that is embedded in the inner membrane and connected to the rotor of F1. The flux of protons flowing down a potential gradient powers the rotation of the rotor driving the synthesis of ATP. Thus, the flow of protons though Fo is coupled to the synthesis of ATP.","predictedComplex":false,"interactors":[{"ac":"EBI-10194585","identifier":"P05496","identifierLink":"https://www.uniprot.org/uniprotkb/P05496/entry","name":"ATP5MC1","description":"ATP synthase F(0) complex subunit C1, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1044001","identifier":"O75964","identifierLink":"https://www.uniprot.org/uniprotkb/O75964/entry","name":"ATP5MG","description":"ATP synthase F(0) complex subunit g, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12386","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1044810","identifier":"P24539","identifierLink":"https://www.uniprot.org/uniprotkb/P24539/entry","name":"ATP5PB","description":"ATP synthase peripheral stalk subunit b, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12733","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1049505","identifier":"P30049","identifierLink":"https://www.uniprot.org/uniprotkb/P30049/entry","name":"ATP5F1D","description":"ATP synthase F(1) complex subunit delta, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13822","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1389380","identifier":"P00846","identifierLink":"https://www.uniprot.org/uniprotkb/P00846/entry","name":"MT-ATP6","description":"ATP synthase F(0) complex subunit a","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11410","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22217047","identifier":"P56378","identifierLink":"https://www.uniprot.org/uniprotkb/P56378/entry","name":"ATP5MJ","description":"ATP synthase F(0) complex subunit j, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15233","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2270000","identifier":"P56385","identifierLink":"https://www.uniprot.org/uniprotkb/P56385/entry","name":"ATP5ME","description":"ATP synthase F(0) complex subunit e, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12427","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25825606","identifier":"Q7Z4Y8","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z4Y8/entry","name":"ATP5MGL","description":"ATP synthase subunit g 2, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12386","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2606700","identifier":"P18859","identifierLink":"https://www.uniprot.org/uniprotkb/P18859/entry","name":"ATP5PF","description":"ATP synthase peripheral stalk subunit F6, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12441","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3439833","identifier":"P03928","identifierLink":"https://www.uniprot.org/uniprotkb/P03928/entry","name":"MT-ATP8","description":"ATP synthase F(0) complex subunit 8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13722","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347797","identifier":"P48201","identifierLink":"https://www.uniprot.org/uniprotkb/P48201/entry","name":"ATP5MC3","description":"ATP synthase F(0) complex subunit C3, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-351437","identifier":"P25705","identifierLink":"https://www.uniprot.org/uniprotkb/P25705/entry","name":"ATP5F1A","description":"ATP synthase F(1) complex subunit alpha, mitochondrial","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355815","identifier":"P48047","identifierLink":"https://www.uniprot.org/uniprotkb/P48047/entry","name":"ATP5PO","description":"ATP synthase peripheral stalk subunit OSCP, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11910","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356231","identifier":"P06576","identifierLink":"https://www.uniprot.org/uniprotkb/P06576/entry","name":"ATP5F1B","description":"ATP synthase F(1) complex subunit beta, mitochondrial","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15184","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3904845","identifier":"P56381","identifierLink":"https://www.uniprot.org/uniprotkb/P56381/entry","name":"ATP5F1E","description":"ATP synthase F(1) complex subunit epsilon, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12448","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3912136","identifier":"Q06055","identifierLink":"https://www.uniprot.org/uniprotkb/Q06055/entry","name":"ATP5MC2","description":"ATP synthase F(0) complex subunit C2, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-711768","identifier":"P36542","identifierLink":"https://www.uniprot.org/uniprotkb/P36542/entry","name":"ATP5F1C","description":"ATP synthase F(1) complex subunit gamma, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11693","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712794","identifier":"P56134","identifierLink":"https://www.uniprot.org/uniprotkb/P56134/entry","name":"ATP5MF","description":"ATP synthase F(0) complex subunit f, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13080","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724024","identifier":"O75947","identifierLink":"https://www.uniprot.org/uniprotkb/O75947/entry","name":"ATP5PD","description":"ATP synthase peripheral stalk subunit d, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12700","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-954033","identifier":"Q96IX5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96IX5/entry","name":"ATP5MK","description":"ATP synthase F(0) complex subunit k, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR34038","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9978245","identifier":"Q5VTU8","identifierLink":"https://www.uniprot.org/uniprotkb/Q5VTU8/entry","name":"ATP5F1EP2","description":"ATP synthase subunit epsilon-like protein, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12448","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6152","complexName":"R2SD co-chaperone complex","organismName":"Homo sapiens; 9606","description":"Putative co-chaperone required for the assembly of macromolecular complexes.","predictedComplex":false,"interactors":[{"ac":"EBI-10965756","identifier":"Q07617","identifierLink":"https://www.uniprot.org/uniprotkb/Q07617/entry","name":"SPAG1","description":"Sperm-associated antigen 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45984","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352939","identifier":"Q9Y230","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y230/entry","name":"RUVBL2","description":"RuvB-like 2","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353675","identifier":"Q9Y265","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y265/entry","name":"RUVBL1","description":"RuvB-like 1","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9392930","identifier":"Q9NVR5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NVR5/entry","name":"DNAAF2","description":"Protein kintoun","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22997","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6153","complexName":"R2T co-chaperone complex","organismName":"Homo sapiens; 9606","description":"Putative co-chaperone required for the expression and for the assembly of other macromolecular complexes. This co-chaperone is particularly expressed in testis.","predictedComplex":false,"interactors":[{"ac":"EBI-21564289","identifier":"Q9H6T3-2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H6T3-2/entry","name":"RPAP3","description":"Isoform 2 of RNA polymerase II-associated protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-352939","identifier":"Q9Y230","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y230/entry","name":"RUVBL2","description":"RuvB-like 2","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353675","identifier":"Q9Y265","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y265/entry","name":"RUVBL1","description":"RuvB-like 1","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6154","complexName":"Mitochondrial pyruvate carrier complex","organismName":"Homo sapiens; 9606","description":"Regulates the uptake of pyruvate from the mitochondrial intermembrane space into the mitochondrial matrix.","predictedComplex":false,"interactors":[{"ac":"EBI-719403","identifier":"O95563","identifierLink":"https://www.uniprot.org/uniprotkb/O95563/entry","name":"MPC2","description":"Mitochondrial pyruvate carrier 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14154","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-721137","identifier":"Q9Y5U8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5U8/entry","name":"MPC1","description":"Mitochondrial pyruvate carrier 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14154","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6595","complexName":"bZIP transcription factor complex, ATF6-ATF6B","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.\r\n\r\nATF6 is a master regulator of one of the three main branches of the endoplasmic reticulum (ER) unfolded protein response, regulating numerous genes that restore ER protein-folding capacity, after which it is rapidly degraded. ATF6B can bind to and transcriptionally induce many of the same genes as ATF6, but is a much weaker transcriptional activator and may primarily act as a modulator of ATF6.","predictedComplex":false,"interactors":[{"ac":"EBI-2841031","identifier":"Q99941","identifierLink":"https://www.uniprot.org/uniprotkb/Q99941/entry","name":"ATF6B","description":"Cyclic AMP-dependent transcription factor ATF-6 beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46164","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-852157","identifier":"P18850","identifierLink":"https://www.uniprot.org/uniprotkb/P18850/entry","name":"ATF6","description":"Cyclic AMP-dependent transcription factor ATF-6 alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46164","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6596","complexName":"bZIP transcription factor complex, ATF6B-ATF6B","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. \r\n\r\nATF6 is a master regulator of one of the three main branches of the endoplasmic reticulum (ER) unfolded protein response, regulating numerous genes that restore ER protein-folding capacity, after which it is rapidly degraded. ATF6B can bind to and transcriptionally induce many of the same genes as ATF6 (P18850-PRO_0000296200), but is a much weaker transcriptional activator and may primarily act as a modulator of ATF6.","predictedComplex":false,"interactors":[{"ac":"EBI-2841031","identifier":"Q99941","identifierLink":"https://www.uniprot.org/uniprotkb/Q99941/entry","name":"ATF6B","description":"Cyclic AMP-dependent transcription factor ATF-6 beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46164","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6597","complexName":"bZIP transcription factor complex, ATF6-XBP1","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.\r\n\r\nATF6 is a master regulator of one of the three main branches of the endoplasmic reticulum (ER) unfolded protein response, regulating numerous genes that restore ER protein-folding capacity, after which it is rapidly degraded. ATF6 heterodimerization with XBP1 results in the induction of major ER-associated degradation (ERAD) components in response to ER stress.","predictedComplex":false,"interactors":[{"ac":"EBI-6942961","identifier":"P17861","identifierLink":"https://www.uniprot.org/uniprotkb/P17861/entry","name":"XBP1","description":"X-box-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46542","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-852157","identifier":"P18850","identifierLink":"https://www.uniprot.org/uniprotkb/P18850/entry","name":"ATF6","description":"Cyclic AMP-dependent transcription factor ATF-6 alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46164","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6598","complexName":"L-lactate dehydrogenase complex, A1B3 variant","organismName":"Homo sapiens; 9606","description":"Catalyzes the NAD(H)-dependent interconversion of lactate and pyruvate. Mainly expressed in reticular endothelial system.","predictedComplex":false,"interactors":[{"ac":"EBI-358748","identifier":"P07195","identifierLink":"https://www.uniprot.org/uniprotkb/P07195/entry","name":"LDHB","description":"L-lactate dehydrogenase B chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43128","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372327","identifier":"P00338","identifierLink":"https://www.uniprot.org/uniprotkb/P00338/entry","name":"LDHA","description":"L-lactate dehydrogenase A chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43128","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6599","complexName":"L-lactate dehydrogenase B complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the NAD(H)-dependent interconversion of lactate and pyruvate. Mainly expressed in cardiac muscles, erythrocytes and brain and preferentially converts lactate to pyruvate.","predictedComplex":false,"interactors":[{"ac":"EBI-358748","identifier":"P07195","identifierLink":"https://www.uniprot.org/uniprotkb/P07195/entry","name":"LDHB","description":"L-lactate dehydrogenase B chain","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43128","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6600","complexName":"bZIP transcription factor complex, ATF6B-XBP1","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.\r\n\r\nATF6 is a master regulator of one of the three main branches of the endoplasmic reticulum (ER) unfolded protein response, regulating numerous genes that restore ER protein-folding capacity, after which it is rapidly degraded. ATF6B can bind to and transcriptionally induce many of the same genes as ATF6, but is a much weaker transcriptional activator and may primarily act as a modulator of ATF6.","predictedComplex":false,"interactors":[{"ac":"EBI-2841031","identifier":"Q99941","identifierLink":"https://www.uniprot.org/uniprotkb/Q99941/entry","name":"ATF6B","description":"Cyclic AMP-dependent transcription factor ATF-6 beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46164","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6942961","identifier":"P17861","identifierLink":"https://www.uniprot.org/uniprotkb/P17861/entry","name":"XBP1","description":"X-box-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46542","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6601","complexName":"bZIP transcription factor complex, ATF6B-CREBZF","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.\r\n\r\nATF6 is a master regulator of one of the three main branches of the endoplasmic reticulum (ER) unfolded protein response, regulating numerous genes that restore ER protein-folding capacity, after which it is rapidly degraded. ATF6B can bind to and transcriptionally induce many of the same genes as ATF6, but is a much weaker transcriptional activator and may primarily act as a modulator of ATF6. CREBZF has also been shown to play a role in modulating the unfolded protein response.","predictedComplex":false,"interactors":[{"ac":"EBI-2841031","identifier":"Q99941","identifierLink":"https://www.uniprot.org/uniprotkb/Q99941/entry","name":"ATF6B","description":"Cyclic AMP-dependent transcription factor ATF-6 beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46164","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-632965","identifier":"Q9NS37","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NS37/entry","name":"CREBZF","description":"CREB/ATF bZIP transcription factor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6602","complexName":"L-lactate dehydrogenase C complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the NAD(H)-dependent interconversion of lactate and pyruvate. Mainly expressed in testes where it is possibly involved in sperm mobility and preferentially converts pyruvate to lactate.","predictedComplex":false,"interactors":[{"ac":"EBI-21716174","identifier":"P07864","identifierLink":"https://www.uniprot.org/uniprotkb/P07864/entry","name":"LDHC","description":"L-lactate dehydrogenase C chain","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43128","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6603","complexName":"Gamma-delta T cell receptor complex, TRGC2 variant","organismName":"Homo sapiens; 9606","description":"Antigen-specific receptor on the cell surface of T lymphocytes essential to the immune response. While alpha-beta TCR (CPX-6482, CPX-6581) expressing T cells are more commonly found in peripheral blood, gamma-delta TCR-expressing T cells constitute the major subset of resident T cells in tissues bordering the external environment such as the dermis, the intestine, the lung and the uterus. \r\n\r\nGamma-delta TCRs do not absolutely require classic antigen priming and clonal expansion in the thymus and appear to recognise microorganism-derived proteins and self-proteins (such as heat-shock proteins) without a requirement for antigen pre-processing or major-histocompatibility-complex (MHC) presentation of peptide epitopes. Some gamma-delta T-cell receptors recognise MHC class Ib molecules or structurally diverse and biologically unrelated compounds such as lipopeptides on cell surfaces. \r\n\r\nActivated cells produce cytokines (IFN-gamma, TNF-alpha, IL-17) and chemokines (RANTES, IP-10, lymphotactin), contributing to a rapid, innate-like immune response to a broad spectrum of pathogens during the initiation phase of the immune response. This rapid response bridges the transition from the innate to adaptive immune response. \r\n\r\nEach TCR possesses unique antigen specificity, determined by the antigen binding site created by the variable regions of the gamma and delta subunits (TRGC2, TRDC). Downstream signalling is activate by LCK (P06239) and FYN (P06241) kinases which phosphorylate the cytoplasmic immunoreceptor tyrosine-based activation motifs (ITAMs) of subunits CD3G, CD3E and CD247. As antigens only bind to the extracellular domains of the gamma and delta subunits and they do not possess ITAMs, information is probably relayed via the ITAMs of the cytoplasmic tails of the CD3 subunits. Gamma-delta TCRs appear to be more efficient in signalling than alpha-beta TCRs. \r\n\r\nThis rapid and un-primed response by T cells expressing gamma-delta TCRs and IL-17 can also induce inflammatory diseases, autoimmunity (in particular psoriasis), and metastasis.","predictedComplex":false,"interactors":[{"ac":"EBI-1165705","identifier":"P20963","identifierLink":"https://www.uniprot.org/uniprotkb/P20963/entry","name":"CD247","description":"T-cell surface glycoprotein CD3 zeta chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10035","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1211297","identifier":"P07766","identifierLink":"https://www.uniprot.org/uniprotkb/P07766/entry","name":"CD3E","description":"T-cell surface glycoprotein CD3 epsilon chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10570","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26902242","identifier":"B7Z8K6","identifierLink":"https://www.uniprot.org/uniprotkb/B7Z8K6/entry","name":"TRDC","description":"T cell receptor delta constant","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-26907233","identifier":"P03986","identifierLink":"https://www.uniprot.org/uniprotkb/P03986/entry","name":"TRGC2","description":"T cell receptor gamma constant 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19256","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3862428","identifier":"P09693","identifierLink":"https://www.uniprot.org/uniprotkb/P09693/entry","name":"CD3G","description":"T-cell surface glycoprotein CD3 gamma chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10570","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6622","complexName":"L-lactate dehydrogenase complex, LDHAL6B variant","organismName":"Homo sapiens; 9606","description":"Catalyzes the NAD(H)-dependent interconversion of lactate and pyruvate. Exclusively expressed in testes and preferentially converts pyruvate to lactate.","predictedComplex":false,"interactors":[{"ac":"EBI-1108377","identifier":"Q9BYZ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BYZ2/entry","name":"LDHAL6B","description":"L-lactate dehydrogenase A-like 6B","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43128","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6641","complexName":"ASCC DNA alkylation repair complex","organismName":"Homo sapiens; 9606","description":"Plays a role in ALKBH3 (Q96Q83)-mediated demethylation of  N-alkyl lesions in DNA. ASCC3 is a DNA helicase that unwinds DNA by translocating on one strand in 3'-to-5' direction, thus potentially providing single-stranded DNA as a substrate for de-alkylation repair by ALKBH3.  Recruitment of the ASCC complex requires recognition of Lys-64-linked poly-ubiquitin chains by the CUE (IPR003892) domain of ASCC2 whilst ASCC1 appears to modulate the localization of the complex during alkylation damage.","predictedComplex":false,"interactors":[{"ac":"EBI-10268317","identifier":"Q8N9N2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N9N2/entry","name":"ASCC1","description":"Activating signal cointegrator 1 complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13360","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1210710","identifier":"Q8N3C0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N3C0/entry","name":"ASCC3","description":"Activating signal cointegrator 1 complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24075","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-711197","identifier":"Q9H1I8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H1I8/entry","name":"ASCC2","description":"Activating signal cointegrator 1 complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21494","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6642","complexName":"RQT ribosome-associated quality control trigger complex","organismName":"Homo sapiens; 9606","description":"Recognizes ubiquitinated stalled ribosomes and induces subunit dissociation to facilitate the ribosome-associated quality control (RQC) pathway.The abnormal stalled ribosome is recognized and ubiquitinated at one or more specific residues by the E3 ubiquitin ligase ZNF598 (Q86UK7). Ubiquitinated 80S ribosomes appear to be dissociated into 40S and 60S subunits by the ATP-dependent helicase ASCC3. TRIP4 may promote complex binding to the ribosome via its zinc-finger domain. ACSS1 (Q8N9N2) may also be a component of the RQT complex, although the complex appears to retain activity in its absence.","predictedComplex":false,"interactors":[{"ac":"EBI-1210710","identifier":"Q8N3C0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N3C0/entry","name":"ASCC3","description":"Activating signal cointegrator 1 complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24075","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2800143","identifier":"Q15650","identifierLink":"https://www.uniprot.org/uniprotkb/Q15650/entry","name":"TRIP4","description":"Activating signal cointegrator 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12963","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-711197","identifier":"Q9H1I8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H1I8/entry","name":"ASCC2","description":"Activating signal cointegrator 1 complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21494","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6643","complexName":"RQT ribosome-associated quality control trigger complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Recognizes ubiquitinated stalled ribosomes and induces subunit dissociation to facilitate the ribosome-associated quality control (RQC) pathway. The complex associates with E3 ubiquitin-ligase HEL2 (Q05580)-ribosome complexes and required for the primary steps of RQC. The ubiquitin-binding activity of RQT3 and ATPase activity of CUE3 were crucial to trigger RQC.by the RQC complex (CPX-3265).","predictedComplex":false,"interactors":[{"ac":"EBI-23623","identifier":"P53327","identifierLink":"https://www.uniprot.org/uniprotkb/P53327/entry","name":"SLH1","description":"RQC trigger complex helicase SLH1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47961","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23916","identifier":"P53137","identifierLink":"https://www.uniprot.org/uniprotkb/P53137/entry","name":"CUE3","description":"RQC trigger complex subunit CUE3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21494","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26366","identifier":"P36119","identifierLink":"https://www.uniprot.org/uniprotkb/P36119/entry","name":"RQT4","description":"RQC trigger complex subunit RQT4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12963","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6661","complexName":"HOP2-MND1 recombination assembly factor complex","organismName":"Homo sapiens; 9606","description":"Recombinase cofactor complex that activates both RAD51 (Q06609)- and DMC1 (Q14565)-mediated homologous pairing during homologous recombination. Acts to stabilize the presynaptic filament, a right-handed helical nucleoprotein strand generated  by RAD51 and DMC1 from single-stranded DNA derived from the nucleolytic processing of a primary lesion. The HOP2-MND1 complex synergizes with the filament to assemble the synaptic complex, and promotes DMC1-/RAD51-mediated strand exchange between the presynaptic filament and recombining double-stranded DNA to form a D-loop, acting with RAD54L (Q92698), a nucleosome remodeler, to promote homologous pairing with the nucleosomal double-stranded DNA.","predictedComplex":false,"interactors":[{"ac":"EBI-11137441","identifier":"Q9BWT6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BWT6/entry","name":"MND1","description":"Meiotic nuclear division protein 1 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31398","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9057595","identifier":"Q9P2W1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P2W1/entry","name":"PSMC3IP","description":"Homologous-pairing protein 2 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15938","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6662","complexName":"tRNA-guanine transglycosylase complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GUN anticodons (tRNA-Asp, -Asn, -His and Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). Q34 appears to enhance the speed of translation of C-ending codons but reduced that of U-ending codons. In human cytoplasm, tRNAs for His and Asn have queuosine, whilst in mitochondria, queuosine occurs at the wobble positions of tRNAs for Tyr, His, Asn and Asp.","predictedComplex":false,"interactors":[{"ac":"EBI-1221028","identifier":"Q9H974","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H974/entry","name":"QTRT2","description":"Queuine tRNA-ribosyltransferase accessory subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46064","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-716832","identifier":"Q9BXR0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BXR0/entry","name":"QTRT1","description":"Queuine tRNA-ribosyltransferase catalytic subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43530","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-6663","complexName":"Serine palmitoyltransferase complex, SPTLC1-SPTLC2-SPTSSA variant","organismName":"Homo sapiens; 9606","description":"Catalyzes the first, rate-limiting step of the sphingolipid synthesis pathway, driving the condensation of L-serine and acyl-CoA thioester substrates to form 3-dehydrosphinganinium (CHEBI:58299). The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for a C16-CoA substrate, typically palmitoyl-CoA.","predictedComplex":false,"interactors":[{"ac":"EBI-1044323","identifier":"O15269","identifierLink":"https://www.uniprot.org/uniprotkb/O15269/entry","name":"SPTLC1","description":"Serine palmitoyltransferase 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13693","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-723396","identifier":"Q969W0","identifierLink":"https://www.uniprot.org/uniprotkb/Q969W0/entry","name":"SPTSSA","description":"Serine palmitoyltransferase small subunit A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47084","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-766136","identifier":"O15270","identifierLink":"https://www.uniprot.org/uniprotkb/O15270/entry","name":"SPTLC2","description":"Serine palmitoyltransferase 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13693","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8852014","identifier":"CHEBI:597326","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:597326","name":"pyridoxal 5'-phosphate(2-)","description":"pyridoxal 5'-phosphate(2-)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-4747","complexName":"E3 ligase (RANBP2) complex","organismName":"Homo sapiens; 9606","description":"SUMOylated E3 ligase complex that takes part in the termination of CRM1-mediated export by facilitating the hydrolysis of GTP by RAN (P62826), resulting in export complex disassembly.\r\n\r\nThe subunit RANBP2/NUP358 links the E3 ligase complex to the Nuclear Pore Complex (CPX-873). SUMOylation, mediated by the enzymatic activity of RANBP2, might play a role in the directionality of nucleo-cytoplasmic transport through the nuclear pore.","predictedComplex":false,"interactors":[{"ac":"EBI-396091","identifier":"P46060","identifierLink":"https://www.uniprot.org/uniprotkb/P46060/entry","name":"RANGAP1","description":"Ran GTPase-activating protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24113","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-80168","identifier":"P63279","identifierLink":"https://www.uniprot.org/uniprotkb/P63279/entry","name":"UBE2I","description":"SUMO-conjugating enzyme UBC9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-973138","identifier":"P49792","identifierLink":"https://www.uniprot.org/uniprotkb/P49792/entry","name":"RANBP2","description":"E3 SUMO-protein ligase RanBP2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23138","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4921","complexName":"E3 ligase (RANBP2) complex","organismName":"Mus musculus; 10090","description":"SUMOylated E3 ligase complex that takes part in the termination of CRM1-mediated export by facilitating the hydrolysis of GTP by Ran (P62827), resulting in export complex disassembly.\r\n\r\nThe subunit Ranbp2/Nup358 links the E3 ligase complex to the Nuclear Pore Complex (CPX-4474). SUMOylation, mediated by the enzymatic activity of Ranbp2, might play a role in the directionality of nucleo-cytoplasmic transport through the nuclear pore.","predictedComplex":false,"interactors":[{"ac":"EBI-1033051","identifier":"P46061","identifierLink":"https://www.uniprot.org/uniprotkb/P46061/entry","name":"Rangap1","description":"Ran GTPase-activating protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24113","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-643756","identifier":"Q9ERU9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ERU9/entry","name":"Ranbp2","description":"E3 SUMO-protein ligase RanBP2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23138","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-80180","identifier":"P63280","identifierLink":"https://www.uniprot.org/uniprotkb/P63280/entry","name":"Ube2i","description":"SUMO-conjugating enzyme UBC9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6664","complexName":"Serine palmitoyltransferase complex, SPTLC1-SPTLC2-SPTSSB variant","organismName":"Homo sapiens; 9606","description":"Catalyzes the first, rate-limiting step of the sphingolipid synthesis pathway, driving the condensation of L-serine and acyl-CoA thioester substrates to form 3-dehydrosphinganinium (CHEBI:58299). The SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for a C16-CoA and C18-CoA substrates or longer, such as stearoyl-CoA.","predictedComplex":false,"interactors":[{"ac":"EBI-1044323","identifier":"O15269","identifierLink":"https://www.uniprot.org/uniprotkb/O15269/entry","name":"SPTLC1","description":"Serine palmitoyltransferase 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13693","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15778024","identifier":"Q8NFR3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NFR3/entry","name":"SPTSSB","description":"Serine palmitoyltransferase small subunit B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28612","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-766136","identifier":"O15270","identifierLink":"https://www.uniprot.org/uniprotkb/O15270/entry","name":"SPTLC2","description":"Serine palmitoyltransferase 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13693","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8852014","identifier":"CHEBI:597326","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:597326","name":"pyridoxal 5'-phosphate(2-)","description":"pyridoxal 5'-phosphate(2-)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-6665","complexName":"Serine palmitoyltransferase complex, SPTLC1-SPTLC3-SPTSSA variant","organismName":"Homo sapiens; 9606","description":"Catalyzes the first, rate-limiting step of the sphingolipid synthesis pathway, driving the condensation of L-serine and acyl-CoA thioester substrates to form 3-dehydrosphinganinium (CHEBI:58299).  The SPTLC1-SPTLC3-SPTSSA complex uses C12-CoA, C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA.","predictedComplex":false,"interactors":[{"ac":"EBI-1044323","identifier":"O15269","identifierLink":"https://www.uniprot.org/uniprotkb/O15269/entry","name":"SPTLC1","description":"Serine palmitoyltransferase 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13693","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11614219","identifier":"Q9NUV7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NUV7/entry","name":"SPTLC3","description":"Serine palmitoyltransferase 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13693","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-723396","identifier":"Q969W0","identifierLink":"https://www.uniprot.org/uniprotkb/Q969W0/entry","name":"SPTSSA","description":"Serine palmitoyltransferase small subunit A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47084","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8852014","identifier":"CHEBI:597326","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:597326","name":"pyridoxal 5'-phosphate(2-)","description":"pyridoxal 5'-phosphate(2-)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-6681","complexName":"Serine palmitoyltransferase complex, SPTLC1-SPTLC3-SPTSSB variant","organismName":"Homo sapiens; 9606","description":"Catalyzes the first, rate-limiting step of the sphingolipid synthesis pathway, driving the condensation of L-serine and acyl-CoA thioester substrates to form 3-dehydrosphinganinium (CHEBI:58299). The SPTLC1-SPTLC3-SPTSSB complex appears to be able to bind to a range of acyl-CoA chain length substrates.","predictedComplex":false,"interactors":[{"ac":"EBI-1044323","identifier":"O15269","identifierLink":"https://www.uniprot.org/uniprotkb/O15269/entry","name":"SPTLC1","description":"Serine palmitoyltransferase 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13693","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11614219","identifier":"Q9NUV7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NUV7/entry","name":"SPTLC3","description":"Serine palmitoyltransferase 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13693","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15778024","identifier":"Q8NFR3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NFR3/entry","name":"SPTSSB","description":"Serine palmitoyltransferase small subunit B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28612","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8852014","identifier":"CHEBI:597326","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:597326","name":"pyridoxal 5'-phosphate(2-)","description":"pyridoxal 5'-phosphate(2-)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-6701","complexName":"Dehydrodolichyl diphosphate synthase complex","organismName":"Homo sapiens; 9606","description":"A cis-prenyltransferase which catalyzes the rate-limiting step in the synthesis of glycosyl carrier lipids required for protein glycosylation in the lumen of endoplasmic reticulum. Essential for the synthesis of dolichol phosphate (CHEBI:23875), an indispensable lipid carrier for protein N-glycosylation, O-mannosylation, C-mannosylation, and GPI-anchor formation, catalyzing the formation of its precursor dehydrodolichyl diphosphate (ditrans,polycis-polyprenyl diphosphate(3-), CHEBI:136960), a long-chain isoprenoid, by chain elongation of farnesyl diphosphate (CHEBI:175763) via multiple condensations with isopentenyl pyrophosphate (CHEBI:128769).","predictedComplex":false,"interactors":[{"ac":"EBI-26942900","identifier":"Q86SQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q86SQ9/entry","name":"DHDDS","description":"Dehydrodolichyl diphosphate synthase complex subunit DHDDS","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10291","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6949352","identifier":"Q96E22","identifierLink":"https://www.uniprot.org/uniprotkb/Q96E22/entry","name":"NUS1","description":"Dehydrodolichyl diphosphate synthase complex subunit NUS1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21528","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-6702","complexName":"CD8alpha-beta complex","organismName":"Mus musculus; 10090","description":"Integral membrane glycoprotein coreceptor complex that plays an essential role in the immune response and serves multiple functions in responses against both external and internal attacks. In T-cells, functions primarily as a T-cell receptor (TCR) coreceptor for the peptide-bound MHC (pMHC) class I complex. Interacts with the pMHC class I complex via its extracellular immunoglobulin domains, and potentially enhances TCR-pMHC binding of low-affinity TCRs. In turn, recruits the intracellular Src kinase Lck (P06240) to the vicinity of the TCR complex. Lck then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of cytotoxic T-lymphocytes (CTLs). This mechanism enables CTLs to recognize and eliminate infected cells and tumour cells. Additionally, plays a critical role in thymic selection of CD8+ T-cells. \r\n\r\nA palmitoylation site in the cytoplasmic tail of CD8B subunit contributes to partitioning of CD8 into the plasma membrane lipid rafts where signaling proteins are enriched. \r\n\r\nCD8ab complex is a stronger co-receptor than the related CD8aa (CPX-6742) complex. Both may occur on the same cells.","predictedComplex":false,"interactors":[{"ac":"EBI-1433","identifier":"P01731","identifierLink":"https://www.uniprot.org/uniprotkb/P01731/entry","name":"Cd8a","description":"T-cell surface glycoprotein CD8 alpha chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10441","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7541406","identifier":"P10300","identifierLink":"https://www.uniprot.org/uniprotkb/P10300/entry","name":"Cd8b","description":"T-cell surface glycoprotein CD8 beta chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11292","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6721","complexName":"bZIP transcription factor complex, ATF7-ATF7","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. Required to maintain epithelial regenerative capacity and protect against cell death during intestinal epithelial damage and repair.","predictedComplex":false,"interactors":[{"ac":"EBI-765623","identifier":"P17544","identifierLink":"https://www.uniprot.org/uniprotkb/P17544/entry","name":"ATF7","description":"Cyclic AMP-dependent transcription factor ATF-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6741","complexName":"CD8alpha-beta complex","organismName":"Homo sapiens; 9606","description":"Integral membrane glycoprotein coreceptor complex that plays an essential role in the immune response and serves multiple functions in responses against both external and internal attacks. In T-cells, functions primarily as a T-cell receptor (TCR, CPX-6581, CPX-6482, CPX-6582, CPX-6603) coreceptor for the peptide-bound MHC (pMHC) class I complex. Interacts with the pMHC class I complex via its extracellular immunoglobulin domains, and potentially enhances TCR-pMHC binding of low-affinity TCRs. In turn, recruits the intracellular Src kinase LCK (P06239) to the vicinity of the TCR complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of cytotoxic T-lymphocytes (CTLs). This mechanism enables CTLs to recognize and eliminate infected cells and tumour cells. Additionally, plays a critical role in thymic selection of CD8+ T-cells. \r\n\r\nA palmitoylation site in the cytoplasmic tail of CD8B subunit contributes to partitioning of CD8 into the plasma membrane lipid rafts where signaling proteins are enriched. \r\n\r\nCD8ab complex is a stronger co-receptor than the related CD8aa (CPX-6743) complex. Both may occur on the same cells.","predictedComplex":false,"interactors":[{"ac":"EBI-26971942","identifier":"P10966","identifierLink":"https://www.uniprot.org/uniprotkb/P10966/entry","name":"CD8B","description":"T-cell surface glycoprotein CD8 beta chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11292","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2873704","identifier":"P01732","identifierLink":"https://www.uniprot.org/uniprotkb/P01732/entry","name":"CD8A","description":"T-cell surface glycoprotein CD8 alpha chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10441","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6742","complexName":"CD8alpha-alpha complex","organismName":"Mus musculus; 10090","description":"Integral membrane glycoprotein coreceptor complex that plays an essential role in the immune response and serves multiple functions in responses against both external and internal attacks. In T-cells, functions primarily as a T-cell receptor (TCR) coreceptor for the peptide-bound MHC (pMHC) class I complex. Interacts with the pMHC class I complex via its extracellular immunoglobulin domains, and potentially enhances TCR-pMHC binding of low-affinity TCRs. In turn, recruits the intracellular Src kinase Lck (P06240) to the vicinity of the TCR complex. Lck then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of cytotoxic T-lymphocytes (CTLs). This mechanism enables CTLs to recognize and eliminate infected cells and tumour cells. Additionally, plays a critical role in thymic selection of CD8+ T-cells. \r\n\r\nCD8aa complex is a weaker co-receptor than the related CD8ab (CPX-6702) complex. Both may occur on the same cells.","predictedComplex":false,"interactors":[{"ac":"EBI-1433","identifier":"P01731","identifierLink":"https://www.uniprot.org/uniprotkb/P01731/entry","name":"Cd8a","description":"T-cell surface glycoprotein CD8 alpha chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10441","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6743","complexName":"CD8alpha-alpha complex","organismName":"Homo sapiens; 9606","description":"Integral membrane glycoprotein coreceptor complex that plays an essential role in the immune response and serves multiple functions in responses against both external and internal attacks. In T-cells, functions primarily as a T-cell receptor (TCR, CPX-6581, CPX-6482, CPX-6582, CPX-6603) coreceptor for the peptide-bound MHC (pMHC) class I complex. Interacts with the pMHC class I complex via its extracellular immunoglobulin domains, and potentially enhances TCR-pMHC binding of low-affinity TCRs. In turn, recruits the intracellular Src kinase LCK (P06239) to the vicinity of the TCR complex. LCK then initiates different intracellular signaling pathways by phosphorylating various substrates ultimately leading to lymphokine production, motility, adhesion and activation of cytotoxic T-lymphocytes (CTLs). This mechanism enables CTLs to recognize and eliminate infected cells and tumour cells. Additionally, plays a critical role in thymic selection of CD8+ T-cells. \r\n\r\nCD8aa complex is a weaker co-receptor than the related CD8ab (CPX-6741) complex. Both may occur on the same cells.","predictedComplex":false,"interactors":[{"ac":"EBI-2873704","identifier":"P01732","identifierLink":"https://www.uniprot.org/uniprotkb/P01732/entry","name":"CD8A","description":"T-cell surface glycoprotein CD8 alpha chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10441","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6744","complexName":"IgD - Ig kappa immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgD is the major antigen receptor isotype on the surface of most peripheral B-cells, where it is coexpressed with IgM. IgM and IgD molecules present on B cells have identical V regions and antigen-binding sites.","predictedComplex":false,"interactors":[{"ac":"EBI-1054530","identifier":"P01834","identifierLink":"https://www.uniprot.org/uniprotkb/P01834/entry","name":"IGKC","description":"Immunoglobulin kappa constant","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10683716","identifier":"P01880","identifierLink":"https://www.uniprot.org/uniprotkb/P01880/entry","name":"IGHD","description":"Immunoglobulin heavy constant delta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5690","complexName":"SARS-CoV-2 primase complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","description":"Primase complex of the SARS-CoV-2 coronavirus which binds dsRNA molecules and extends partially double-stranded RNA templates.","predictedComplex":false,"interactors":[{"ac":"EBI-25475871","identifier":"P0DTD1-PRO_0000449625","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTD1-PRO_0000449625/entry","name":"rep","description":"Non-structural protein 7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]},{"ac":"EBI-25475874","identifier":"P0DTD1-PRO_0000449626","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTD1-PRO_0000449626/entry","name":"rep","description":"Non-structural protein 8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]}]},{"complexAC":"CPX-6761","complexName":"SARS-CoV-2 Spike - human CLEC4M lectin complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","description":"Binding of SARS-CoV-2 coronavirus Spike protein to human lectin CLEC4M expressed on innate immune cells and subsequent internalisation may lead to virus clearance or, on the contrary, result in spread of the virus to susceptible cells, or even other hosts.","predictedComplex":false,"interactors":[{"ac":"EBI-1391211","identifier":"Q9H2X3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H2X3/entry","name":"CLEC4M","description":"C-type lectin domain family 4 member M","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25490330","identifier":"CPX-5682","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-5682","name":"SARS-CoV-2 cleaved Spike protein complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]}]},{"complexAC":"CPX-608","complexName":"ADA complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Chromatin remodelling complex that primarily acetylates nucleosomal  histones H3 and H2B. May not participate directly in transcription. ADA2 is thought to potentiate GCN5 catalytic activity and ADA3 to facilitate nucleosomal acetylation and an expanded lysine specificity. Shares the HAT module of ADA2-GCN5-NGG1-SGF29 with the related SAGA complex (CPX-656).","predictedComplex":false,"interactors":[{"ac":"EBI-21678","identifier":"P25554","identifierLink":"https://www.uniprot.org/uniprotkb/P25554/entry","name":"SGF29","description":"SAGA complex subunit SGF29","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21539","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2186","identifier":"Q02336","identifierLink":"https://www.uniprot.org/uniprotkb/Q02336/entry","name":"ADA2","description":"SAGA complex subunit ADA2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12374","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2192","identifier":"P32494","identifierLink":"https://www.uniprot.org/uniprotkb/P32494/entry","name":"NGG1","description":"SAGA complex subunit NGG1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13556","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21993","identifier":"P25649","identifierLink":"https://www.uniprot.org/uniprotkb/P25649/entry","name":"AHC2","description":"ADA histone acetyltransferase complex component 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-33947","identifier":"Q12433","identifierLink":"https://www.uniprot.org/uniprotkb/Q12433/entry","name":"AHC1","description":"Protein AHC1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13585","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7458","identifier":"Q03330","identifierLink":"https://www.uniprot.org/uniprotkb/Q03330/entry","name":"GCN5","description":"Histone acetyltransferase GCN5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45750","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-900","complexName":"SAGA complex, KAT2A variant","organismName":"Homo sapiens; 9606","description":"A histone acetyltransferase transcriptional co-activator complex that preferably acetylates histone H3 and possibly H4. Acetyl-CoA-dependent and appears to require the presence of ATP-dependent chromatin remodeling factors to enable its coactivator activity. Recruited to the promoter region by co-operatively binding to factors such as MYC (P01106) and TP53 (P04637). Also has histone H2A and H2B deubiquitinase activity which counteracts heterochromatin silencing. Interacts with the UV-damaged DNA binding proteins DDB1 (Q16531) and DDB2 (Q92466), suggesting possible roles in transcription-coupled pre-mRNA splicing and DNA damage repair. \r\nSAGA complex has also been called STAGA  complex, it is considered as the same complex in later publications (PMID:19114550, 25111486, 18206972, 15115762). The subunit composition also largely overlaps with TFTC complex (CPX-903) which has been separately described but may prove to be a different form of the same complex.","predictedComplex":false,"interactors":[{"ac":"EBI-1034238","identifier":"Q16514","identifierLink":"https://www.uniprot.org/uniprotkb/Q16514/entry","name":"TAF12","description":"Transcription initiation factor TFIID subunit 12","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12603476","identifier":"CHEBI:27363","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:27363","name":"zinc atom","description":"zinc atom","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1785876","identifier":"O75529","identifierLink":"https://www.uniprot.org/uniprotkb/O75529/entry","name":"TAF5L","description":"TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 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559292","xrefs":[]},{"ac":"EBI-35097","identifier":"Q03761","identifierLink":"https://www.uniprot.org/uniprotkb/Q03761/entry","name":"TAF12","description":"SAGA complex/transcription factor TFIID complex subunit TAF12","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4574","identifier":"P32657","identifierLink":"https://www.uniprot.org/uniprotkb/P32657/entry","name":"CHD1","description":"Chromo domain-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45623","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7458","identifier":"Q03330","identifierLink":"https://www.uniprot.org/uniprotkb/Q03330/entry","name":"GCN5","description":"Histone acetyltransferase GCN5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45750","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8287","identifier":"Q12060","identifierLink":"https://www.uniprot.org/uniprotkb/Q12060/entry","name":"HFI1","description":"SAGA complex subunit HFI1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21277","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3321","complexName":"SIN3A histone deacetylase complex","organismName":"Homo sapiens; 9606","description":"A histone deacetylation complex (HDAC) that promotes viability in normal and neoplastic cells by negatively regulating gene expression especially of genes regulating G1/S and G2/M cell cycle transitions as well as cell differentiation. Probably does not directly bind to DNA but is recruited to gene promoters by specific transcription factor such as REST (Q13127), RB (P06400), HBP1 (O60381), the Myc-inhibitors MXI1 (P50539) and MAD1 (Q9Y6D9), Klf13 (Q9Y2Y9), FOXK1 (P85037) and FOXK2 (Q01167) as well as with the nuclear hormone repressors, N-CoR (O75376) and SMRT (Q9Y618) and/or SWI/SNF chromatin remodelling complexes. \r\n\r\nBinds H3K4me2 and H3K4me3 histones via subunits ING1 and ING2 and hypoacetylated histones via subunits RBBP4 and RBBP7. \r\n\r\nUnlike the SIN3B complex (CPX-3322) it is found in differentiated cells as well as in embryonic stem cells. \r\n\r\nMay include several accessory proteins such as BAHCC1 (Q9P281), BBX (Q8WY36), IRS4 (O14654), PHF23 (Q9BUL5), SAP18 (O00422) and TNRC18 (O15417).","predictedComplex":false,"interactors":[{"ac":"EBI-1199878","identifier":"P29374","identifierLink":"https://www.uniprot.org/uniprotkb/P29374/entry","name":"ARID4A","description":"AT-rich interactive domain-containing protein 4A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2340040","identifier":"Q9HAJ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HAJ7/entry","name":"SAP30L","description":"Histone deacetylase complex subunit SAP30L","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13286","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2680990","identifier":"Q4LE39","identifierLink":"https://www.uniprot.org/uniprotkb/Q4LE39/entry","name":"ARID4B","description":"AT-rich interactive domain-containing protein 4B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301821","identifier":"Q92769","identifierLink":"https://www.uniprot.org/uniprotkb/Q92769/entry","name":"HDAC2","description":"Histone deacetylase 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301834","identifier":"Q13547","identifierLink":"https://www.uniprot.org/uniprotkb/Q13547/entry","name":"HDAC1","description":"Histone deacetylase 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347218","identifier":"Q96ST3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96ST3/entry","name":"SIN3A","description":"Paired amphipathic helix protein Sin3a","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352227","identifier":"Q16576","identifierLink":"https://www.uniprot.org/uniprotkb/Q16576/entry","name":"RBBP7","description":"Histone-binding protein RBBP7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-389787","identifier":"Q9H160","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H160/entry","name":"ING2","description":"Inhibitor of growth protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-399198","identifier":"Q9UK53","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK53/entry","name":"ING1","description":"Inhibitor of growth protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-540496","identifier":"Q9H7L9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H7L9/entry","name":"SUDS3","description":"Sin3 histone deacetylase corepressor complex component SDS3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5666615","identifier":"Q5PSV4","identifierLink":"https://www.uniprot.org/uniprotkb/Q5PSV4/entry","name":"BRMS1L","description":"Breast cancer metastasis-suppressor 1-like protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-620823","identifier":"Q09028","identifierLink":"https://www.uniprot.org/uniprotkb/Q09028/entry","name":"RBBP4","description":"Histone-binding protein RBBP4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-632609","identifier":"O75446","identifierLink":"https://www.uniprot.org/uniprotkb/O75446/entry","name":"SAP30","description":"Histone deacetylase complex subunit SAP30","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13286","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714781","identifier":"Q9HCU9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HCU9/entry","name":"BRMS1","description":"Breast cancer metastasis-suppressor 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-922886","identifier":"Q9H0E3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H0E3/entry","name":"SAP130","description":"Histone deacetylase complex subunit SAP130","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13497","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3323","complexName":"SIN3A histone deacetylase complex, ES cell-specific variant","organismName":"Homo sapiens; 9606","description":"A embryonic stem cell-specific histone deacetylation complex (HDAC) that is distinguished from the common SIN3A complex (CPX-3321) by the additional core subunits FAM60A, OCT, TET1. Negatively regulates gene expression of genes regulating G1/S and G2/M cell cycle transitions and required to promote rapid proliferation while preventing unscheduled differentiation. May bind to DNA directly via subunit FAM60A and is recruited to gene promoters by specific transcription factor such as REST (Q13127), RB (P06400), HBP1 (O60381), the Myc-inhibitors MXI1 (P50539) and MAD1L1/MAD1 (Q9Y6D9), KlF13 (Q9Y2Y9), FOXK1 (P85037) and FOXK2 (Q01167) as well as with the nuclear hormone repressors, NCOR1 (O75376) and NCOR2/SMRT (Q9Y618) and/or SWI/SNF chromatin remodelling complexes. \r\n\r\nBinds H3K4me2 and H3K4me3 histones via subunits ING1 and ING2 and hypoacetylated histones via subunits RBBP4 and RBBP7. \r\n\r\nMutations that abrogate its repressor activity may activate the TGF-beta signaling pathway leading to changes in cell morphology and increase in cell migration related to cancer progression. Cancer cell lines appear to express canonical and mutated versions of SIN3A complexes. \r\n\r\nMay include several accessory proteins such as BAHCC1 (Q9P281), BBX (Q8WY36), IRS4 (O14654), PHF23 (Q9BUL5), SAP18 (O00422) and TNRC18 (O15417).","predictedComplex":false,"interactors":[{"ac":"EBI-1199878","identifier":"P29374","identifierLink":"https://www.uniprot.org/uniprotkb/P29374/entry","name":"ARID4A","description":"AT-rich interactive domain-containing protein 4A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2340040","identifier":"Q9HAJ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HAJ7/entry","name":"SAP30L","description":"Histone deacetylase complex subunit SAP30L","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13286","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2680990","identifier":"Q4LE39","identifierLink":"https://www.uniprot.org/uniprotkb/Q4LE39/entry","name":"ARID4B","description":"AT-rich interactive domain-containing protein 4B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301821","identifier":"Q92769","identifierLink":"https://www.uniprot.org/uniprotkb/Q92769/entry","name":"HDAC2","description":"Histone deacetylase 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301834","identifier":"Q13547","identifierLink":"https://www.uniprot.org/uniprotkb/Q13547/entry","name":"HDAC1","description":"Histone deacetylase 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347218","identifier":"Q96ST3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96ST3/entry","name":"SIN3A","description":"Paired amphipathic helix protein Sin3a","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352227","identifier":"Q16576","identifierLink":"https://www.uniprot.org/uniprotkb/Q16576/entry","name":"RBBP7","description":"Histone-binding protein RBBP7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-389787","identifier":"Q9H160","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H160/entry","name":"ING2","description":"Inhibitor of growth protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-399198","identifier":"Q9UK53","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK53/entry","name":"ING1","description":"Inhibitor of growth protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-539828","identifier":"O15294","identifierLink":"https://www.uniprot.org/uniprotkb/O15294/entry","name":"OGT","description":"UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44366","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-540496","identifier":"Q9H7L9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H7L9/entry","name":"SUDS3","description":"Sin3 histone deacetylase corepressor complex component SDS3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5666615","identifier":"Q5PSV4","identifierLink":"https://www.uniprot.org/uniprotkb/Q5PSV4/entry","name":"BRMS1L","description":"Breast cancer metastasis-suppressor 1-like protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-620823","identifier":"Q09028","identifierLink":"https://www.uniprot.org/uniprotkb/Q09028/entry","name":"RBBP4","description":"Histone-binding protein RBBP4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-632609","identifier":"O75446","identifierLink":"https://www.uniprot.org/uniprotkb/O75446/entry","name":"SAP30","description":"Histone deacetylase complex subunit SAP30","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13286","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714781","identifier":"Q9HCU9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HCU9/entry","name":"BRMS1","description":"Breast cancer metastasis-suppressor 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-741906","identifier":"Q9NP50","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NP50/entry","name":"SINHCAF","description":"SIN3-HDAC complex-associated factor","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13422","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8833805","identifier":"Q8NFU7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NFU7/entry","name":"TET1","description":"Methylcytosine dioxygenase TET1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23358","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-922886","identifier":"Q9H0E3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H0E3/entry","name":"SAP130","description":"Histone deacetylase complex subunit SAP130","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13497","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3322","complexName":"SIN3B histone deacetylase complex","organismName":"Homo sapiens; 9606","description":"A histone deacetylation complex (HDAC) that negatively regulates gene expression especially of genes regulating G1/S and G2/M cell cycle transitions as well as cell differentiation. Interacts with the Rb family of proteins (RB [P06400], RBL1/p107 [P28749], and RBL2/p130 [Q08999]) and E2F4 (Q16254) downstream of the transcription start sites to repress the transcription of E2F target genes during cell cycle withdrawal. Probably does not directly bind to DNA but is recruited to gene promoters by specific transcription factor such as REST (Q13127), RB (P06400), HBP1 (O60381), the Myc-inhibitors MXI1 (P50539) and MAD1 (Q9Y6D9), Klf13 (Q9Y2Y9), FOXK1 (P85037) and FOXK2 (Q01167) as well as with the nuclear hormone repressors, N-CoR (O75376) and SMRT (Q9Y618) and/or SWI/SNF chromatin remodelling complexes.\r\n\r\nBinds H3K4me2 and H3K4me3 histones via subunits ING1 and ING2 and hypoacetylated histones via subunits RBBP4 and RBBP7. \r\n\r\nUnlike the SIN3A complex (CPX-3321) it is only found in differentiated cells. \r\n\r\nMay include several accessory proteins such as BAHCC1 (Q9P281), BBX (Q8WY36), IRS4 (O14654), PHF23 (Q9BUL5), SAP18 (O00422) and TNRC18 (O15417).","predictedComplex":false,"interactors":[{"ac":"EBI-1199878","identifier":"P29374","identifierLink":"https://www.uniprot.org/uniprotkb/P29374/entry","name":"ARID4A","description":"AT-rich interactive domain-containing protein 4A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2340040","identifier":"Q9HAJ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HAJ7/entry","name":"SAP30L","description":"Histone deacetylase complex subunit SAP30L","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13286","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2680990","identifier":"Q4LE39","identifierLink":"https://www.uniprot.org/uniprotkb/Q4LE39/entry","name":"ARID4B","description":"AT-rich interactive domain-containing protein 4B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301821","identifier":"Q92769","identifierLink":"https://www.uniprot.org/uniprotkb/Q92769/entry","name":"HDAC2","description":"Histone deacetylase 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301834","identifier":"Q13547","identifierLink":"https://www.uniprot.org/uniprotkb/Q13547/entry","name":"HDAC1","description":"Histone deacetylase 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352227","identifier":"Q16576","identifierLink":"https://www.uniprot.org/uniprotkb/Q16576/entry","name":"RBBP7","description":"Histone-binding protein RBBP7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-389787","identifier":"Q9H160","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H160/entry","name":"ING2","description":"Inhibitor of growth protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-399198","identifier":"Q9UK53","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK53/entry","name":"ING1","description":"Inhibitor of growth protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-540462","identifier":"O75182","identifierLink":"https://www.uniprot.org/uniprotkb/O75182/entry","name":"SIN3B","description":"Paired amphipathic helix protein Sin3b","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-540496","identifier":"Q9H7L9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H7L9/entry","name":"SUDS3","description":"Sin3 histone deacetylase corepressor complex component SDS3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5666615","identifier":"Q5PSV4","identifierLink":"https://www.uniprot.org/uniprotkb/Q5PSV4/entry","name":"BRMS1L","description":"Breast cancer metastasis-suppressor 1-like protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-620823","identifier":"Q09028","identifierLink":"https://www.uniprot.org/uniprotkb/Q09028/entry","name":"RBBP4","description":"Histone-binding protein RBBP4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-632609","identifier":"O75446","identifierLink":"https://www.uniprot.org/uniprotkb/O75446/entry","name":"SAP30","description":"Histone deacetylase complex subunit SAP30","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13286","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714781","identifier":"Q9HCU9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HCU9/entry","name":"BRMS1","description":"Breast cancer metastasis-suppressor 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-922886","identifier":"Q9H0E3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H0E3/entry","name":"SAP130","description":"Histone deacetylase complex subunit SAP130","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13497","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3441","complexName":"SIN3A histone deacetylase complex, ES cell-specific variant","organismName":"Mus musculus; 10090","description":"A embryonic stem cell-specific histone deacetylation complex (HDAC) that is distinguished from the common SIN3A complex (CPX-3443) by the additional core subunits FAM60A, OCT, TET1. Negatively regulates gene expression of genes regulating G1/S and G2/M cell cycle transitions and required to promote rapid proliferation while preventing unscheduled differentiation. May bind to DNA directly via subunit FAM60A and is recruited to gene promoters by specific transcription factor such as Rest (Q8VIG1), Rb (P13405), Hbp1 (Q8R316), the Myc‐inhibitors Mxi1 (P50540) and Mad1l1/MAD1 (Q9WTX8), Klf13 (Q9JJZ6), Foxk1 (P42128) and Foxk2 (Q3UCQ1) as well as with the nuclear hormone repressors, Ncor1 (Q60974) and Ncor2/SMRT (Q9WU42) and/or SWI/SNF chromatin remodelling complexes. \r\n\r\nBinds H3K4me2 and H3K4me3 histones via subunits Ing1 and Ing2 and hypoacetylated histones via subunits Rbbp4 and Rbbp7. \r\n\r\nMutations that abrogate its repressor activity may activate the TGF-beta signaling pathway leading to changes in cell morphology and increase in cell migration related to cancer progression. Cancer cell lines appear to express canonical and mutated versions of SIN3A complexes. \r\n\r\nMay include several accessory proteins such as Bahcc1 (Q3UHR0), Bbx (Q8VBW5), Irs4 (Q9Z0Y7), Phf23 (Q8BSN5), Sap18 (O55128) and Tnrc18 (Q80WC3).","predictedComplex":false,"interactors":[{"ac":"EBI-11149704","identifier":"Q8C8M1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C8M1/entry","name":"Sinhcaf","description":"SIN3-HDAC complex-associated factor","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13422","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1561388","identifier":"Q9ESK4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ESK4/entry","name":"Ing2","description":"Inhibitor of growth protein 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17168047","identifier":"Q3U1T3","identifierLink":"https://www.uniprot.org/uniprotkb/Q3U1T3/entry","name":"Brms1l","description":"Breast cancer metastasis-suppressor 1-like protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17168074","identifier":"F8VPQ2","identifierLink":"https://www.uniprot.org/uniprotkb/F8VPQ2/entry","name":"Arid4a","description":"AT-rich interactive domain-containing protein 4A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17168105","identifier":"Q9QXV3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9QXV3/entry","name":"Ing1","description":"Inhibitor of growth protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301912","identifier":"O09106","identifierLink":"https://www.uniprot.org/uniprotkb/O09106/entry","name":"Hdac1","description":"Histone deacetylase 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302251","identifier":"P70288","identifierLink":"https://www.uniprot.org/uniprotkb/P70288/entry","name":"Hdac2","description":"Histone deacetylase 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302291","identifier":"Q60972","identifierLink":"https://www.uniprot.org/uniprotkb/Q60972/entry","name":"Rbbp4","description":"Histone-binding protein RBBP4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302297","identifier":"Q60973","identifierLink":"https://www.uniprot.org/uniprotkb/Q60973/entry","name":"Rbbp7","description":"Histone-binding protein RBBP7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-349034","identifier":"Q60520","identifierLink":"https://www.uniprot.org/uniprotkb/Q60520/entry","name":"Sin3a","description":"Paired amphipathic helix protein Sin3a","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4291699","identifier":"Q3URK3","identifierLink":"https://www.uniprot.org/uniprotkb/Q3URK3/entry","name":"Tet1","description":"Methylcytosine dioxygenase TET1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23358","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-591431","identifier":"Q8BR65","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BR65/entry","name":"Suds3","description":"Sin3 histone deacetylase corepressor complex component SDS3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-593511","identifier":"O88574","identifierLink":"https://www.uniprot.org/uniprotkb/O88574/entry","name":"Sap30","description":"Histone deacetylase complex subunit SAP30","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13286","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6394082","identifier":"A2CG63","identifierLink":"https://www.uniprot.org/uniprotkb/A2CG63/entry","name":"Arid4b","description":"AT-rich interactive domain-containing protein 4B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8337929","identifier":"Q5SQF8","identifierLink":"https://www.uniprot.org/uniprotkb/Q5SQF8/entry","name":"Sap30l","description":"Histone deacetylase complex subunit SAP30L","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13286","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8340347","identifier":"Q8BIH0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BIH0/entry","name":"Sap130","description":"Histone deacetylase complex subunit SAP130","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13497","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8821356","identifier":"Q99N20","identifierLink":"https://www.uniprot.org/uniprotkb/Q99N20/entry","name":"Brms1","description":"Breast cancer metastasis-suppressor 1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-928496","identifier":"Q8CGY8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CGY8/entry","name":"Ogt","description":"UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR44366","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3443","complexName":"SIN3A histone deacetylase complex","organismName":"Mus musculus; 10090","description":"A histone deacetylation complex (HDAC) that promotes viability in normal and neoplastic cells by negatively regulating gene expression especially of genes regulating G1/S and G2/M cell cycle transitions as well as cell differentiation. Probably does not directly bind to DNA but is recruited to gene promoters by specific transcription factor such as Rest (Q8VIG1), Rb (P13405), Hbp1 (Q8R316), the Myc‐inhibitors Mxi1 (P50540) and Mad1l1/MAD1 (Q9WTX8), Klf13 (Q9JJZ6), Foxk1 (P42128) and Foxk2 (Q3UCQ1) as well as with the nuclear hormone repressors, Ncor1 (Q60974) and Ncor2/SMRT (Q9WU42) and/or SWI/SNF chromatin remodelling complexes. \r\n\r\nBinds H3K4me2 and H3K4me3 histones via subunits Ing1 and Ing2 and hypoacetylated histones via subunits Rbbp4 and Rbbp7. \r\n\r\nUnlike the SIN3B complex (CPX-3444) it is found in differentiated cells as well as in embryonic stem cells. \r\n\r\nMay include several accessory proteins such as Bahcc1 (Q3UHR0), Bbx (Q8VBW5), Irs4 (Q9Z0Y7), Phf23 (Q8BSN5), Sap18 (O55128) and Tnrc18 (Q80WC3).","predictedComplex":false,"interactors":[{"ac":"EBI-1561388","identifier":"Q9ESK4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ESK4/entry","name":"Ing2","description":"Inhibitor of growth protein 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17168047","identifier":"Q3U1T3","identifierLink":"https://www.uniprot.org/uniprotkb/Q3U1T3/entry","name":"Brms1l","description":"Breast cancer metastasis-suppressor 1-like protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17168074","identifier":"F8VPQ2","identifierLink":"https://www.uniprot.org/uniprotkb/F8VPQ2/entry","name":"Arid4a","description":"AT-rich interactive domain-containing protein 4A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17168105","identifier":"Q9QXV3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9QXV3/entry","name":"Ing1","description":"Inhibitor of growth protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301912","identifier":"O09106","identifierLink":"https://www.uniprot.org/uniprotkb/O09106/entry","name":"Hdac1","description":"Histone deacetylase 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302251","identifier":"P70288","identifierLink":"https://www.uniprot.org/uniprotkb/P70288/entry","name":"Hdac2","description":"Histone deacetylase 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302291","identifier":"Q60972","identifierLink":"https://www.uniprot.org/uniprotkb/Q60972/entry","name":"Rbbp4","description":"Histone-binding protein RBBP4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302297","identifier":"Q60973","identifierLink":"https://www.uniprot.org/uniprotkb/Q60973/entry","name":"Rbbp7","description":"Histone-binding protein RBBP7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-349034","identifier":"Q60520","identifierLink":"https://www.uniprot.org/uniprotkb/Q60520/entry","name":"Sin3a","description":"Paired amphipathic helix protein Sin3a","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-591431","identifier":"Q8BR65","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BR65/entry","name":"Suds3","description":"Sin3 histone deacetylase corepressor complex component SDS3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-593511","identifier":"O88574","identifierLink":"https://www.uniprot.org/uniprotkb/O88574/entry","name":"Sap30","description":"Histone deacetylase complex subunit SAP30","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13286","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6394082","identifier":"A2CG63","identifierLink":"https://www.uniprot.org/uniprotkb/A2CG63/entry","name":"Arid4b","description":"AT-rich interactive domain-containing protein 4B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8337929","identifier":"Q5SQF8","identifierLink":"https://www.uniprot.org/uniprotkb/Q5SQF8/entry","name":"Sap30l","description":"Histone deacetylase complex subunit SAP30L","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13286","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8340347","identifier":"Q8BIH0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BIH0/entry","name":"Sap130","description":"Histone deacetylase complex subunit SAP130","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13497","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8821356","identifier":"Q99N20","identifierLink":"https://www.uniprot.org/uniprotkb/Q99N20/entry","name":"Brms1","description":"Breast cancer metastasis-suppressor 1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3444","complexName":"SIN3B histone deacetylase complex","organismName":"Mus musculus; 10090","description":"A histone deacetylation complex (HDAC) that negatively regulates gene expression especially of genes regulating G1/S and G2/M cell cycle transitions as well as cell differentiation. Interacts with the Rb family of proteins (Rb [P13405], Rbl1/p107 [Q64701], and Rbl2/p130 [Q64700]) and E2f4 (Q8R0K9) downstream of the transcription start sites to repress the transcription of E2F target genes during cell cycle withdrawal. Probably does not directly bind to DNA but is recruited to gene promoters by specific transcription factor such as Rest (Q8VIG1), Rb (P13405), Hbp1 (Q8R316), the Myc‐inhibitors Mxi1 (P50540) and Mad1l1/MAD1 (Q9WTX8), Klf13 (Q9JJZ6), Foxk1 (P42128) and Foxk2 (Q3UCQ1) as well as with the nuclear hormone repressors, Ncor1 (Q60974) and Ncor2/SMRT (Q9WU42) and/or SWI/SNF chromatin remodelling complexes. \r\n\r\nBinds H3K4me2 and H3K4me3 histones via subunits Ing1 and Ing2 and hypoacetylated histones via subunits Rbbp4 and Rbbp7. \r\n\r\nUnlike the SIN3A complex (CPX-3443) it is only found in differentiated cells. \r\n\r\nMay include several accessory proteins such as Bahcc1 (Q3UHR0), Bbx (Q8VBW5), Irs4 (Q9Z0Y7), Phf23 (Q8BSN5), Sap18 (O55128) and Tnrc18 (Q80WC3).","predictedComplex":false,"interactors":[{"ac":"EBI-1561388","identifier":"Q9ESK4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ESK4/entry","name":"Ing2","description":"Inhibitor of growth protein 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17168047","identifier":"Q3U1T3","identifierLink":"https://www.uniprot.org/uniprotkb/Q3U1T3/entry","name":"Brms1l","description":"Breast cancer metastasis-suppressor 1-like protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17168074","identifier":"F8VPQ2","identifierLink":"https://www.uniprot.org/uniprotkb/F8VPQ2/entry","name":"Arid4a","description":"AT-rich interactive domain-containing protein 4A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17168105","identifier":"Q9QXV3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9QXV3/entry","name":"Ing1","description":"Inhibitor of growth protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301912","identifier":"O09106","identifierLink":"https://www.uniprot.org/uniprotkb/O09106/entry","name":"Hdac1","description":"Histone deacetylase 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302251","identifier":"P70288","identifierLink":"https://www.uniprot.org/uniprotkb/P70288/entry","name":"Hdac2","description":"Histone deacetylase 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302291","identifier":"Q60972","identifierLink":"https://www.uniprot.org/uniprotkb/Q60972/entry","name":"Rbbp4","description":"Histone-binding protein RBBP4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302297","identifier":"Q60973","identifierLink":"https://www.uniprot.org/uniprotkb/Q60973/entry","name":"Rbbp7","description":"Histone-binding protein RBBP7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-591431","identifier":"Q8BR65","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BR65/entry","name":"Suds3","description":"Sin3 histone deacetylase corepressor complex component SDS3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-591450","identifier":"Q62141","identifierLink":"https://www.uniprot.org/uniprotkb/Q62141/entry","name":"Sin3b","description":"Paired amphipathic helix protein Sin3b","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-593511","identifier":"O88574","identifierLink":"https://www.uniprot.org/uniprotkb/O88574/entry","name":"Sap30","description":"Histone deacetylase complex subunit SAP30","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13286","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6394082","identifier":"A2CG63","identifierLink":"https://www.uniprot.org/uniprotkb/A2CG63/entry","name":"Arid4b","description":"AT-rich interactive domain-containing protein 4B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8337929","identifier":"Q5SQF8","identifierLink":"https://www.uniprot.org/uniprotkb/Q5SQF8/entry","name":"Sap30l","description":"Histone deacetylase complex subunit SAP30L","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13286","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8340347","identifier":"Q8BIH0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BIH0/entry","name":"Sap130","description":"Histone deacetylase complex subunit SAP130","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13497","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8821356","identifier":"Q99N20","identifierLink":"https://www.uniprot.org/uniprotkb/Q99N20/entry","name":"Brms1","description":"Breast cancer metastasis-suppressor 1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-920","complexName":"SAGA complex, KAT2A variant","organismName":"Mus musculus; 10090","description":"A transcriptional co-activator complex that preferably acetylates histone H3 and possibly H4. 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The subunit composition also largely overlaps with TFTC complex (CPX-916) which has been separately described but may prove to be a different form of the same complex.","predictedComplex":false,"interactors":[{"ac":"EBI-12603476","identifier":"CHEBI:27363","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:27363","name":"zinc atom","description":"zinc atom","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-12667195","identifier":"B0QZW4","identifierLink":"https://www.uniprot.org/uniprotkb/B0QZW4/entry","name":"Supt3","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-12670606","identifier":"Q9CZV5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CZV5/entry","name":"Supt7l","description":"STAGA complex 65 subunit gamma","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR28598","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12671123","identifier":"D3Z4Z0","identifierLink":"https://www.uniprot.org/uniprotkb/D3Z4Z0/entry","name":"Tada2b","description":"Transcriptional adapter","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 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Glc3Man9GlcNAc2  is attached to nascent glycoproteins and presents various carbohydrate epitopes to lectins operating as molecular chaperones, cargo receptors, and degradation mediators. The D1 branch of the initial glycoform is capped by a triglucosyl moiety, Glc-alpha1,2-Glc-alpha1,3-Glc. Glucosidase I (Q13724) removes the outermost alpha1,2-linked glucose from the D1 branch and then glucosidase II trims the second and third alpha1,3-linked glucose residues by catalyzing hydrolyses at the Glc-alpha1,3-Glc and Glc-alpha1,3-Man glycosidic linkages. This triggers disengagement of glycoproteins from chaperone complexes for anterograde transport to the Golgi apparatus if they are successfully folded.","predictedComplex":false,"interactors":[{"ac":"EBI-348004","identifier":"Q14697","identifierLink":"https://www.uniprot.org/uniprotkb/Q14697/entry","name":"GANAB","description":"Neutral alpha-glucosidase AB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22762","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-716953","identifier":"P14314","identifierLink":"https://www.uniprot.org/uniprotkb/P14314/entry","name":"PRKCSH","description":"Glucosidase 2 subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6841","complexName":"N-acetylglucosamine-1-phosphotransferase complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the first step in the formation of mannose 6-phosphate (M6P) recognition marker on lysosomal enzymes required for their efficient M6P receptor-mediated transport to lysosomes. 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NFS1 provides sulfur for Fe-S cluster assembly by cleaving this atom from the side chain of the substrate L-cysteine and storing it in the form of a persulfide. The ISCU scaffold protein performs the transient assembly of the 2Fe-2S cluster using persulfide sulfur and Fe(II). Electrons are provided by a mitochondrial ferredoxin, FDX2.","predictedComplex":false,"interactors":[{"ac":"EBI-10252800","identifier":"Q6P4F2","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P4F2/entry","name":"FDX2","description":"Ferredoxin-2, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23426","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1047335","identifier":"Q9H1K1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H1K1/entry","name":"ISCU","description":"Iron-sulfur cluster assembly enzyme ISCU","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1246261","identifier":"O14561","identifierLink":"https://www.uniprot.org/uniprotkb/O14561/entry","name":"NDUFAB1","description":"Acyl carrier protein, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20863","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1751791","identifier":"Q9Y697","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y697/entry","name":"NFS1","description":"Cysteine desulfurase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11601","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3920810","identifier":"Q9HD34","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HD34/entry","name":"LYRM4","description":"LYR motif-containing protein 4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13166","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8852014","identifier":"CHEBI:597326","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:597326","name":"pyridoxal 5'-phosphate(2-)","description":"pyridoxal 5'-phosphate(2-)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-949340","identifier":"Q16595","identifierLink":"https://www.uniprot.org/uniprotkb/Q16595/entry","name":"FXN","description":"Frataxin, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16821","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-392","complexName":"Mitochondrial NIAUFX iron-sulfur cluster assembly complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for the de novo synthesis of iron-sulfur (Fe-S) clusters within mitochondria, which is required for maturation of both mitochondrial and cytoplasmic [2Fe-2S] and [4Fe-4S] proteins. 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Active in the nucleo-cytoplasmic compartments.","predictedComplex":false,"interactors":[{"ac":"EBI-10824516","identifier":"CHEBI:16856","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16856","name":"glutathione","description":"glutathione","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-22211","identifier":"P32642","identifierLink":"https://www.uniprot.org/uniprotkb/P32642/entry","name":"GRX4","description":"Monothiol glutaredoxin-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10293","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-24159","identifier":"P53082","identifierLink":"https://www.uniprot.org/uniprotkb/P53082/entry","name":"BOL2","description":"BolA-like protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12735","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25647592","identifier":"CHEBI:33737","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:33737","name":"di-mu-sulfido-diiron(2+)","description":"di-mu-sulfido-diiron(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1192","complexName":"Vacuolar proton translocating ATPase complex, Golgi variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Translocates protons across a lipid bilayer via an ATP-driven rotary mechanism, thus acidifing the lumen of its resident organelle. As newly synthesized proteins traverse the Golgi apparatus they undergo post-translational modifications, including glycosylation, sulfation, and phosphorylation, and are targeted to their appropriate destination in a pH-dependent manner. Membrane-bound ion transporters/proton exchangers use the pH gradient to sequester metal ions to the vacuole and other cellular organelles. The combined action of the V-ATPase and membrane transporters plays a key role in maintaining cellular homoeostasis. The variant of the complex containing the STV1 subunit results in the retention of the V-ATPase complex on Golgi and endosomal membranes. The N-terminal domain of STV1 contains the W83KY sequence, which is necessary and sufficient for targeting the complex to the Golgi apparatus. When yeast cells are deprived of glucose, the V1 and VO regions separate and are no longer able to hydrolyze ATP and transport protons.","predictedComplex":false,"interactors":[{"ac":"EBI-16210677","identifier":"Q3E7B6","identifierLink":"https://www.uniprot.org/uniprotkb/Q3E7B6/entry","name":"VMA9","description":"V-type proton ATPase subunit e","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12263","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18479","identifier":"P37296","identifierLink":"https://www.uniprot.org/uniprotkb/P37296/entry","name":"STV1","description":"V-type proton ATPase subunit a, Golgi isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11629","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20201","identifier":"P32366","identifierLink":"https://www.uniprot.org/uniprotkb/P32366/entry","name":"VMA6","description":"V-type proton ATPase subunit d","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 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559292","xrefs":[{"identifier":"PTHR10137","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20264","identifier":"P32610","identifierLink":"https://www.uniprot.org/uniprotkb/P32610/entry","name":"VMA8","description":"V-type proton ATPase subunit D","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11671","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20268","identifier":"P22203","identifierLink":"https://www.uniprot.org/uniprotkb/P22203/entry","name":"VMA4","description":"V-type proton ATPase subunit E","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45715","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20272","identifier":"P39111","identifierLink":"https://www.uniprot.org/uniprotkb/P39111/entry","name":"VMA7","description":"V-type proton ATPase subunit F","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 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559292","xrefs":[{"identifier":"PTHR10263","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20311","identifier":"P32842","identifierLink":"https://www.uniprot.org/uniprotkb/P32842/entry","name":"VMA11","description":"V-type proton ATPase subunit c'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10263","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2061527","identifier":"P53262","identifierLink":"https://www.uniprot.org/uniprotkb/P53262/entry","name":"VOA1","description":"V0 assembly protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-26597773","identifier":"P0C5R9","identifierLink":"https://www.uniprot.org/uniprotkb/P0C5R9/entry","name":"rnk","description":"V-type proton ATPase subunit f","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31733","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7739233","identifier":"P25515","identifierLink":"https://www.uniprot.org/uniprotkb/P25515/entry","name":"VMA3","description":"V-type proton ATPase subunit c","stochiometry":"minValue: 8, maxValue: 8","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10263","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1193","complexName":"Vacuolar proton translocating ATPase complex, vacuole variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Translocates protons across a lipid bilayer via an ATP-driven rotary mechanism, thus acidifing the lumen of its resident organelle. 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Reassembly is mediated by the RAVE complex (CPX-1627).","predictedComplex":false,"interactors":[{"ac":"EBI-16210677","identifier":"Q3E7B6","identifierLink":"https://www.uniprot.org/uniprotkb/Q3E7B6/entry","name":"VMA9","description":"V-type proton ATPase subunit e","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12263","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20201","identifier":"P32366","identifierLink":"https://www.uniprot.org/uniprotkb/P32366/entry","name":"VMA6","description":"V-type proton ATPase subunit d","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11028","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20245","identifier":"P17255","identifierLink":"https://www.uniprot.org/uniprotkb/P17255/entry","name":"VMA1","description":"V-type proton ATPase catalytic subunit A","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20254","identifier":"P16140","identifierLink":"https://www.uniprot.org/uniprotkb/P16140/entry","name":"VMA2","description":"V-type proton ATPase subunit B","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43389","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20260","identifier":"P31412","identifierLink":"https://www.uniprot.org/uniprotkb/P31412/entry","name":"VMA5","description":"V-type proton ATPase subunit C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10137","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20264","identifier":"P32610","identifierLink":"https://www.uniprot.org/uniprotkb/P32610/entry","name":"VMA8","description":"V-type proton ATPase subunit D","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11671","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20268","identifier":"P22203","identifierLink":"https://www.uniprot.org/uniprotkb/P22203/entry","name":"VMA4","description":"V-type proton ATPase subunit E","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45715","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20272","identifier":"P39111","identifierLink":"https://www.uniprot.org/uniprotkb/P39111/entry","name":"VMA7","description":"V-type proton ATPase subunit F","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13861","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20276","identifier":"P48836","identifierLink":"https://www.uniprot.org/uniprotkb/P48836/entry","name":"VMA10","description":"V-type proton ATPase subunit G","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12713","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20281","identifier":"P41807","identifierLink":"https://www.uniprot.org/uniprotkb/P41807/entry","name":"VMA13","description":"V-type proton ATPase subunit H","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10698","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20293","identifier":"P23968","identifierLink":"https://www.uniprot.org/uniprotkb/P23968/entry","name":"VMA16","description":"V-type proton ATPase subunit c''","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10263","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20311","identifier":"P32842","identifierLink":"https://www.uniprot.org/uniprotkb/P32842/entry","name":"VMA11","description":"V-type proton ATPase subunit c'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10263","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20455","identifier":"P32563","identifierLink":"https://www.uniprot.org/uniprotkb/P32563/entry","name":"VPH1","description":"V-type proton ATPase subunit a, vacuolar isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11629","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2061527","identifier":"P53262","identifierLink":"https://www.uniprot.org/uniprotkb/P53262/entry","name":"VOA1","description":"V0 assembly protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-26597773","identifier":"P0C5R9","identifierLink":"https://www.uniprot.org/uniprotkb/P0C5R9/entry","name":"rnk","description":"V-type proton ATPase subunit f","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31733","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7739233","identifier":"P25515","identifierLink":"https://www.uniprot.org/uniprotkb/P25515/entry","name":"VMA3","description":"V-type proton ATPase subunit c","stochiometry":"minValue: 8, maxValue: 8","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10263","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4764","complexName":"TRAPP II complex","organismName":"Mus musculus; 10090","description":"Multimeric vesicle tethering complex involved in vesicle transport between endoplasmic reticulum and Golgi compartments and in the regulation of COPI vesicle coating.\r\n\r\nActs as guanine exchange factors towards RAB1 (P62821) and RabE/Rab11 (P62492).","predictedComplex":false,"interactors":[{"ac":"EBI-1172213","identifier":"Q9CQA1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQA1/entry","name":"Trappc5","description":"Trafficking protein particle complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR20902","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1172223","identifier":"O55013","identifierLink":"https://www.uniprot.org/uniprotkb/O55013/entry","name":"Trappc3","description":"Trafficking protein particle complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1172267","identifier":"Q9CQP2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQP2/entry","name":"Trappc2","description":"Trafficking protein particle complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12403","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22051080","identifier":"Q3TIR1","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TIR1/entry","name":"Trappc13","description":"Trafficking protein particle complex subunit 13","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 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9606","description":"Translocates protons across a lipid bilayer via an ATP-driven rotary mechanism, thus acidifing the lumen of its resident organelle. Membrane-bound ion transporters/proton exchangers use the pH gradient to sequester metal ions to the vacuole and other cellular organelles. The combined action of the V-ATPase and membrane transporters plays a key role in maintaining cellular homoeostasis. The ATP6V0A2 variant localizes to the Golgi apparatus.","predictedComplex":false,"interactors":[{"ac":"EBI-1054757","identifier":"P38606","identifierLink":"https://www.uniprot.org/uniprotkb/P38606/entry","name":"ATP6V1A","description":"V-type proton ATPase catalytic subunit A","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18397230","identifier":"Q6P5S7","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P5S7/entry","name":"RNASEK","description":"Ribonuclease kappa","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31733","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2512037","identifier":"O75787","identifierLink":"https://www.uniprot.org/uniprotkb/O75787/entry","name":"ATP6AP2","description":"Renin receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2684998","identifier":"Q9Y5K8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5K8/entry","name":"ATP6V1D","description":"V-type proton ATPase subunit D","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11671","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27058934","identifier":"P15313","identifierLink":"https://www.uniprot.org/uniprotkb/P15313/entry","name":"atp6v1b_human","description":"V-type proton ATPase subunit B","stochiometry":"minValue: 3, maxValue: 3","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-27059051","identifier":"P21283","identifierLink":"https://www.uniprot.org/uniprotkb/P21283/entry","name":"atp6v1c_human","description":"V-type proton ATPase subunit C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-27061278","identifier":"Q96A05","identifierLink":"https://www.uniprot.org/uniprotkb/Q96A05/entry","name":"atp6v1e_human","description":"V-type proton ATPase subunit E","stochiometry":"minValue: 3, maxValue: 3","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-27061705","identifier":"O95670","identifierLink":"https://www.uniprot.org/uniprotkb/O95670/entry","name":"atp6v1g_human","description":"V-type proton ATPase subunit G","stochiometry":"minValue: 3, maxValue: 3","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-27062249","identifier":"Q8N8Y2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N8Y2/entry","name":"atp6v0d_human","description":"V-type proton ATPase V0 subunit d","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-27062250","identifier":"O15342","identifierLink":"https://www.uniprot.org/uniprotkb/O15342/entry","name":"atp6v0e_human","description":"V-type proton ATPase V0 subunit e","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-3904417","identifier":"Q99437","identifierLink":"https://www.uniprot.org/uniprotkb/Q99437/entry","name":"ATP6V0B","description":"V-type proton ATPase 21 kDa proteolipid subunit c''","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10263","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714667","identifier":"Q15904","identifierLink":"https://www.uniprot.org/uniprotkb/Q15904/entry","name":"ATP6AP1","description":"V-type proton ATPase subunit S1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12471","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714690","identifier":"Q16864","identifierLink":"https://www.uniprot.org/uniprotkb/Q16864/entry","name":"ATP6V1F","description":"V-type proton ATPase subunit F","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13861","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-721179","identifier":"P27449","identifierLink":"https://www.uniprot.org/uniprotkb/P27449/entry","name":"ATP6V0C","description":"V-type proton ATPase 16 kDa proteolipid subunit c","stochiometry":"minValue: 9, maxValue: 9","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10263","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724719","identifier":"Q9UI12","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UI12/entry","name":"ATP6V1H","description":"V-type proton ATPase subunit H","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10698","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-988630","identifier":"Q9Y487","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y487/entry","name":"ATP6V0A2","description":"V-type proton ATPase 116 kDa subunit a 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11629","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6905","complexName":"Vacuolar proton translocating ATPase complex, ATP6V0A3 variant","organismName":"Homo sapiens; 9606","description":"Translocates protons across a lipid bilayer via an ATP-driven rotary mechanism, thus acidifing the lumen of its resident organelle. Membrane-bound ion transporters/proton exchangers use the pH gradient to sequester metal ions to the vacuole and other cellular organelles. The combined action of the V-ATPase and membrane transporters plays a key role in maintaining cellular homoeostasis. The ATP6V0A3 variant localizes to endolysosomal compartments and can also be trafficked to the plasma membrane, being found at the ruffled border of osteoclasts.","predictedComplex":false,"interactors":[{"ac":"EBI-1054757","identifier":"P38606","identifierLink":"https://www.uniprot.org/uniprotkb/P38606/entry","name":"ATP6V1A","description":"V-type proton ATPase catalytic subunit A","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18397230","identifier":"Q6P5S7","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P5S7/entry","name":"RNASEK","description":"Ribonuclease kappa","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31733","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2512037","identifier":"O75787","identifierLink":"https://www.uniprot.org/uniprotkb/O75787/entry","name":"ATP6AP2","description":"Renin receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2684998","identifier":"Q9Y5K8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5K8/entry","name":"ATP6V1D","description":"V-type proton ATPase subunit D","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11671","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27058934","identifier":"P15313","identifierLink":"https://www.uniprot.org/uniprotkb/P15313/entry","name":"atp6v1b_human","description":"V-type proton ATPase subunit B","stochiometry":"minValue: 3, maxValue: 3","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-27059051","identifier":"P21283","identifierLink":"https://www.uniprot.org/uniprotkb/P21283/entry","name":"atp6v1c_human","description":"V-type proton ATPase subunit C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-27061278","identifier":"Q96A05","identifierLink":"https://www.uniprot.org/uniprotkb/Q96A05/entry","name":"atp6v1e_human","description":"V-type proton ATPase subunit E","stochiometry":"minValue: 3, maxValue: 3","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-27061705","identifier":"O95670","identifierLink":"https://www.uniprot.org/uniprotkb/O95670/entry","name":"atp6v1g_human","description":"V-type proton ATPase subunit G","stochiometry":"minValue: 3, maxValue: 3","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-27062249","identifier":"Q8N8Y2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N8Y2/entry","name":"atp6v0d_human","description":"V-type proton ATPase V0 subunit d","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-27062250","identifier":"O15342","identifierLink":"https://www.uniprot.org/uniprotkb/O15342/entry","name":"atp6v0e_human","description":"V-type proton ATPase V0 subunit e","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-3904417","identifier":"Q99437","identifierLink":"https://www.uniprot.org/uniprotkb/Q99437/entry","name":"ATP6V0B","description":"V-type proton ATPase 21 kDa proteolipid subunit c''","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10263","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3914669","identifier":"Q13488","identifierLink":"https://www.uniprot.org/uniprotkb/Q13488/entry","name":"TCIRG1","description":"V-type proton ATPase 116 kDa subunit a 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11629","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714667","identifier":"Q15904","identifierLink":"https://www.uniprot.org/uniprotkb/Q15904/entry","name":"ATP6AP1","description":"V-type proton ATPase subunit S1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12471","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714690","identifier":"Q16864","identifierLink":"https://www.uniprot.org/uniprotkb/Q16864/entry","name":"ATP6V1F","description":"V-type proton ATPase subunit F","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13861","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-721179","identifier":"P27449","identifierLink":"https://www.uniprot.org/uniprotkb/P27449/entry","name":"ATP6V0C","description":"V-type proton ATPase 16 kDa proteolipid subunit c","stochiometry":"minValue: 9, maxValue: 9","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10263","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724719","identifier":"Q9UI12","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UI12/entry","name":"ATP6V1H","description":"V-type proton ATPase subunit H","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10698","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6906","complexName":"IgD - Ig lambda 1 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgD is the major antigen receptor isotype on the surface of most peripheral B-cells, where it is coexpressed with IgM. IgM and IgD molecules present on B cells have identical V regions and antigen-binding sites.","predictedComplex":false,"interactors":[{"ac":"EBI-10683716","identifier":"P01880","identifierLink":"https://www.uniprot.org/uniprotkb/P01880/entry","name":"IGHD","description":"Immunoglobulin heavy constant delta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1221063","identifier":"P0CG04","identifierLink":"https://www.uniprot.org/uniprotkb/P0CG04/entry","name":"IGLC1","description":"Immunoglobulin lambda constant 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6907","complexName":"IgD - Ig lambda 2 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgD is the major antigen receptor isotype on the surface of most peripheral B-cells, where it is coexpressed with IgM. IgM and IgD molecules present on B cells have identical V regions and antigen-binding sites.","predictedComplex":false,"interactors":[{"ac":"EBI-10683716","identifier":"P01880","identifierLink":"https://www.uniprot.org/uniprotkb/P01880/entry","name":"IGHD","description":"Immunoglobulin heavy constant delta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6151637","identifier":"P0CG05","identifierLink":"https://www.uniprot.org/uniprotkb/P0CG05/entry","name":"IGLC2","description":"Immunoglobulin lambda constant 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6908","complexName":"IgD - Ig lambda 3 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgD is the major antigen receptor isotype on the surface of most peripheral B-cells, where it is coexpressed with IgM. IgM and IgD molecules present on B cells have identical V regions and antigen-binding sites.","predictedComplex":false,"interactors":[{"ac":"EBI-10683716","identifier":"P01880","identifierLink":"https://www.uniprot.org/uniprotkb/P01880/entry","name":"IGHD","description":"Immunoglobulin heavy constant delta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21503142","identifier":"P0DOY3","identifierLink":"https://www.uniprot.org/uniprotkb/P0DOY3/entry","name":"IGLC3","description":"Immunoglobulin lambda constant 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6909","complexName":"IgD - Ig lambda 6 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgD is the major antigen receptor isotype on the surface of most peripheral B-cells, where it is coexpressed with IgM. IgM and IgD molecules present on B cells have identical V regions and antigen-binding sites.","predictedComplex":false,"interactors":[{"ac":"EBI-10683716","identifier":"P01880","identifierLink":"https://www.uniprot.org/uniprotkb/P01880/entry","name":"IGHD","description":"Immunoglobulin heavy constant delta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6151653","identifier":"P0CF74","identifierLink":"https://www.uniprot.org/uniprotkb/P0CF74/entry","name":"IGLC6","description":"Immunoglobulin lambda constant 6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6910","complexName":"IgD - Ig lambda 7 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgD is the major antigen receptor isotype on the surface of most peripheral B-cells, where it is coexpressed with IgM. IgM and IgD molecules present on B cells have identical V regions and antigen-binding sites.","predictedComplex":false,"interactors":[{"ac":"EBI-10683716","identifier":"P01880","identifierLink":"https://www.uniprot.org/uniprotkb/P01880/entry","name":"IGHD","description":"Immunoglobulin heavy constant delta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6677450","identifier":"A0M8Q6","identifierLink":"https://www.uniprot.org/uniprotkb/A0M8Q6/entry","name":"IGLC7","description":"Immunoglobulin lambda constant 7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6911","complexName":"IgM - Ig kappa immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nThe membrane-bound form is found in the majority of normal B-cells alongside with IgD. The soluble form, which represents about 30% of the total serum immunoglobulins, is found almost exclusively as a homopentamer. IgM and IgD molecules present on B cells have identical V regions and antigen-binding sites. IgM antibodies are associated with a primary immune response.","predictedComplex":false,"interactors":[{"ac":"EBI-1054530","identifier":"P01834","identifierLink":"https://www.uniprot.org/uniprotkb/P01834/entry","name":"IGKC","description":"Immunoglobulin kappa constant","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-953797","identifier":"P01871","identifierLink":"https://www.uniprot.org/uniprotkb/P01871/entry","name":"IGHM","description":"Immunoglobulin heavy constant mu","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6912","complexName":"Vacuolar proton translocating ATPase complex, ATP6V0A4 variant","organismName":"Homo sapiens; 9606","description":"Translocates protons across a lipid bilayer via an ATP-driven rotary mechanism, thus acidifing the lumen of its resident organelle. Membrane-bound ion transporters/proton exchangers use the pH gradient to sequester metal ions to the vacuole and other cellular organelles. The combined action of the V-ATPase and membrane transporters plays a key role in maintaining cellular homoeostasis. The ATP6V0A4 variant is trafficked to the plasma membrane, being found at the apical membrane of type A intercalated cells.","predictedComplex":false,"interactors":[{"ac":"EBI-1054757","identifier":"P38606","identifierLink":"https://www.uniprot.org/uniprotkb/P38606/entry","name":"ATP6V1A","description":"V-type proton ATPase catalytic subunit A","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18397230","identifier":"Q6P5S7","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P5S7/entry","name":"RNASEK","description":"Ribonuclease kappa","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31733","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2512037","identifier":"O75787","identifierLink":"https://www.uniprot.org/uniprotkb/O75787/entry","name":"ATP6AP2","description":"Renin receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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9606","xrefs":[]},{"ac":"EBI-27059051","identifier":"P21283","identifierLink":"https://www.uniprot.org/uniprotkb/P21283/entry","name":"atp6v1c_human","description":"V-type proton ATPase subunit C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-27061278","identifier":"Q96A05","identifierLink":"https://www.uniprot.org/uniprotkb/Q96A05/entry","name":"atp6v1e_human","description":"V-type proton ATPase subunit E","stochiometry":"minValue: 3, maxValue: 3","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-27061705","identifier":"O95670","identifierLink":"https://www.uniprot.org/uniprotkb/O95670/entry","name":"atp6v1g_human","description":"V-type proton ATPase subunit G","stochiometry":"minValue: 3, maxValue: 3","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-27062249","identifier":"Q8N8Y2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N8Y2/entry","name":"atp6v0d_human","description":"V-type proton ATPase V0 subunit d","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-27062250","identifier":"O15342","identifierLink":"https://www.uniprot.org/uniprotkb/O15342/entry","name":"atp6v0e_human","description":"V-type proton ATPase V0 subunit e","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-3904417","identifier":"Q99437","identifierLink":"https://www.uniprot.org/uniprotkb/Q99437/entry","name":"ATP6V0B","description":"V-type proton ATPase 21 kDa proteolipid subunit c''","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10263","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714667","identifier":"Q15904","identifierLink":"https://www.uniprot.org/uniprotkb/Q15904/entry","name":"ATP6AP1","description":"V-type proton ATPase subunit S1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12471","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714690","identifier":"Q16864","identifierLink":"https://www.uniprot.org/uniprotkb/Q16864/entry","name":"ATP6V1F","description":"V-type proton ATPase subunit F","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13861","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-721179","identifier":"P27449","identifierLink":"https://www.uniprot.org/uniprotkb/P27449/entry","name":"ATP6V0C","description":"V-type proton ATPase 16 kDa proteolipid subunit c","stochiometry":"minValue: 9, maxValue: 9","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10263","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724719","identifier":"Q9UI12","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UI12/entry","name":"ATP6V1H","description":"V-type proton ATPase subunit H","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10698","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6921","complexName":"GRX4 iron-sulfur cluster assembly homodimer complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Reversibly binds [2Fe-2S] clusters and appears to play a role in Fe-S cluster assembly and trafficking, and in transferring an intact [2Fe-2S] cluster to an apo acceptor protein. Active in the nucleo-cytoplasmic compartments.","predictedComplex":false,"interactors":[{"ac":"EBI-10824516","identifier":"CHEBI:16856","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16856","name":"glutathione","description":"glutathione","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-22211","identifier":"P32642","identifierLink":"https://www.uniprot.org/uniprotkb/P32642/entry","name":"GRX4","description":"Monothiol glutaredoxin-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10293","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25647592","identifier":"CHEBI:33737","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:33737","name":"di-mu-sulfido-diiron(2+)","description":"di-mu-sulfido-diiron(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-6922","complexName":"IgM - Ig lambda 1 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nThe membrane-bound form is found in the majority of normal B-cells alongside with IgD. The soluble form, which represents about 30% of the total serum immunoglobulins, is found almost exclusively as a homopentamer. IgM and IgD molecules present on B cells have identical V regions and antigen-binding sites. IgM antibodies are associated with a primary immune response.","predictedComplex":false,"interactors":[{"ac":"EBI-1221063","identifier":"P0CG04","identifierLink":"https://www.uniprot.org/uniprotkb/P0CG04/entry","name":"IGLC1","description":"Immunoglobulin lambda constant 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-953797","identifier":"P01871","identifierLink":"https://www.uniprot.org/uniprotkb/P01871/entry","name":"IGHM","description":"Immunoglobulin heavy constant mu","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6923","complexName":"IgM - Ig lambda 2 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\n\r\nThe membrane-bound form is found in the majority of normal B-cells alongside with IgD. The soluble form, which represents about 30% of the total serum immunoglobulins, is found almost exclusively as a homopentamer. IgM and IgD molecules present on B cells have identical V regions and antigen-binding sites. IgM antibodies are associated with a primary immune response.","predictedComplex":false,"interactors":[{"ac":"EBI-6151637","identifier":"P0CG05","identifierLink":"https://www.uniprot.org/uniprotkb/P0CG05/entry","name":"IGLC2","description":"Immunoglobulin lambda constant 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-953797","identifier":"P01871","identifierLink":"https://www.uniprot.org/uniprotkb/P01871/entry","name":"IGHM","description":"Immunoglobulin heavy constant mu","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6924","complexName":"GRX3 iron-sulfur cluster assembly homodimer complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Reversibly binds [2Fe-2S] clusters and appears to play a role in Fe-S cluster assembly and trafficking, and in transferring an intact [2Fe-2S] cluster to an apo acceptor protein. Active in the nucleo-cytoplasmic compartments.","predictedComplex":false,"interactors":[{"ac":"EBI-10824516","identifier":"CHEBI:16856","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16856","name":"glutathione","description":"glutathione","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-22178","identifier":"Q03835","identifierLink":"https://www.uniprot.org/uniprotkb/Q03835/entry","name":"GRX3","description":"Monothiol glutaredoxin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10293","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25647592","identifier":"CHEBI:33737","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:33737","name":"di-mu-sulfido-diiron(2+)","description":"di-mu-sulfido-diiron(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-6925","complexName":"IgM - Ig lambda 3 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nThe membrane-bound form is found in the majority of normal B-cells alongside with IgD. The soluble form, which represents about 30% of the total serum immunoglobulins, is found almost exclusively as a homopentamer. IgM and IgD molecules present on B cells have identical V regions and antigen-binding sites. IgM antibodies are associated with a primary immune response.","predictedComplex":false,"interactors":[{"ac":"EBI-21503142","identifier":"P0DOY3","identifierLink":"https://www.uniprot.org/uniprotkb/P0DOY3/entry","name":"IGLC3","description":"Immunoglobulin lambda constant 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-953797","identifier":"P01871","identifierLink":"https://www.uniprot.org/uniprotkb/P01871/entry","name":"IGHM","description":"Immunoglobulin heavy constant mu","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6926","complexName":"IgM - Ig lambda 6 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nThe membrane-bound form is found in the majority of normal B-cells alongside with IgD. The soluble form, which represents about 30% of the total serum immunoglobulins, is found almost exclusively as a homopentamer. IgM and IgD molecules present on B cells have identical V regions and antigen-binding sites. IgM antibodies are associated with a primary immune response.","predictedComplex":false,"interactors":[{"ac":"EBI-6151653","identifier":"P0CF74","identifierLink":"https://www.uniprot.org/uniprotkb/P0CF74/entry","name":"IGLC6","description":"Immunoglobulin lambda constant 6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-953797","identifier":"P01871","identifierLink":"https://www.uniprot.org/uniprotkb/P01871/entry","name":"IGHM","description":"Immunoglobulin heavy constant mu","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6927","complexName":"IgM - Ig lambda 7 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nThe membrane-bound form is found in the majority of normal B-cells alongside with IgD. The soluble form, which represents about 30% of the total serum immunoglobulins, is found almost exclusively as a homopentamer. IgM and IgD molecules present on B cells have identical V regions and antigen-binding sites. IgM antibodies are associated with a primary immune response.","predictedComplex":false,"interactors":[{"ac":"EBI-6677450","identifier":"A0M8Q6","identifierLink":"https://www.uniprot.org/uniprotkb/A0M8Q6/entry","name":"IGLC7","description":"Immunoglobulin lambda constant 7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-953797","identifier":"P01871","identifierLink":"https://www.uniprot.org/uniprotkb/P01871/entry","name":"IGHM","description":"Immunoglobulin heavy constant mu","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6928","complexName":"BOL1-GRX5 iron-sulfur cluster assembly complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Reversibly binds [2Fe-2S] clusters and appears to play a role in Fe-S cluster assembly and trafficking, and in transferring an intact [2Fe-2S] cluster to an apo acceptor protein. Active in the nucleo-cytoplasmic compartments.","predictedComplex":false,"interactors":[{"ac":"EBI-10824516","identifier":"CHEBI:16856","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16856","name":"glutathione","description":"glutathione","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2344281","identifier":"Q3E793","identifierLink":"https://www.uniprot.org/uniprotkb/Q3E793/entry","name":"BOL1","description":"BolA-like protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46230","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25647592","identifier":"CHEBI:33737","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:33737","name":"di-mu-sulfido-diiron(2+)","description":"di-mu-sulfido-diiron(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-29427","identifier":"Q02784","identifierLink":"https://www.uniprot.org/uniprotkb/Q02784/entry","name":"GRX5","description":"Monothiol glutaredoxin-5, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10293","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6929","complexName":"IgG1 - Ig kappa immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. 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Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgG occurs predominantly in secreted form and is responsible for longlasting humoral immunity.","predictedComplex":false,"interactors":[{"ac":"EBI-1054530","identifier":"P01834","identifierLink":"https://www.uniprot.org/uniprotkb/P01834/entry","name":"IGKC","description":"Immunoglobulin kappa constant","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356114","identifier":"P01857","identifierLink":"https://www.uniprot.org/uniprotkb/P01857/entry","name":"IGHG1","description":"Immunoglobulin heavy constant gamma 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6930","complexName":"BOL3-GRX5 iron-sulfur cluster assembly complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Reversibly binds [2Fe-2S] clusters and appears to play a role in Fe-S cluster assembly and trafficking, and in transferring an intact [2Fe-2S] cluster to an apo acceptor protein. 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SYNE4 interacts with the motor protein kinesin and consequently, with the microtubule network.","predictedComplex":false,"interactors":[{"ac":"EBI-2796904","identifier":"O94901","identifierLink":"https://www.uniprot.org/uniprotkb/O94901/entry","name":"SUN1","description":"SUN domain-containing protein 1","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12911","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7131783","identifier":"Q8N205","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N205/entry","name":"SYNE4","description":"Nesprin-4","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21640","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 3, maxValue: 3","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-7681","complexName":"Kinetochore MIS12 complex, Nnf1a variant","organismName":"Drosophila melanogaster; 7227","description":"Required for normal chromosome alignment and segregation, kinetochore formation during mitosis, proper kinetochore microtubule attachments and for the spindle assembly checkpoint. 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The mediator complex lacking the CKM complex has a stimulatory effect on basal transcription. In contrast, the mediator complex containing the sub-complex represses basal transcription. This effect is independent of kinase activity but binding of the complex to the Mediator may interfere with RNAPII recruitment and repress transcription re-initiation.","predictedComplex":false,"interactors":[{"ac":"EBI-110730","identifier":"Q7KTX8","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KTX8/entry","name":"skd","description":"Mediator of RNA polymerase II transcription subunit 13","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR48249","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-139710","identifier":"Q9VW47","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VW47/entry","name":"kto","description":"Mediator of RNA polymerase II transcription subunit 12","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46007","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-163640","identifier":"Q9VT57","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VT57/entry","name":"Cdk8","description":"Cyclin-dependent kinase 8","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-195485","identifier":"P25008","identifierLink":"https://www.uniprot.org/uniprotkb/P25008/entry","name":"CycC","description":"Cyclin-C","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7722","complexName":"Fukutin-FKRP-TMEM5 multienzyme complex","organismName":"Homo sapiens; 9606","description":"Contributes to the biosynthesis of glycans required for dystroglycan function. O-mannosyl glycans essential for the ligand-binding activity of alpha-dystroglycan (PRO_0000021065) are connected to [- 3-xylosyl-alpha-1,3-glucuronic acid-beta-1-] repeats by a tandem ribitol-phosphate (Rbo-P). FKTN and FKRP encode Rbo-P transferases that synthesize the tandem Rbo-P structure and the ribitol xylosyltransferase, RXYL1, forms a Xylosyl-Rbo-P linkage","predictedComplex":false,"interactors":[{"ac":"EBI-21505709","identifier":"Q9H9S5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H9S5/entry","name":"FKRP","description":"Ribitol 5-phosphate transferase FKRP","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13627","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21511782","identifier":"O75072","identifierLink":"https://www.uniprot.org/uniprotkb/O75072/entry","name":"FKTN","description":"Ribitol-5-phosphate transferase FKTN","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15407","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3914763","identifier":"Q9Y2B1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2B1/entry","name":"RXYLT1","description":"Ribitol-5-phosphate xylosyltransferase 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15576","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7723","complexName":"BRAHMA SWI/SNF ATP-dependent chromatin remodeling complex","organismName":"Arabidopsis thaliana; 3702","description":"An ATP-dependent chromatin remodeling complex which is recruited to promoters and enhancers of target genes in cells and alters chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors. 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3702","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-40269257","identifier":"Q8L4Y5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8L4Y5/entry","name":"ARP7","description":"Actin-related protein 7","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-40269396","identifier":"Q9LM88","identifierLink":"https://www.uniprot.org/uniprotkb/Q9LM88/entry","name":"q9lm88","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR22881","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-40269411","identifier":"Q8GZ14","identifierLink":"https://www.uniprot.org/uniprotkb/Q8GZ14/entry","name":"q8gz14","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 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9606","description":"Plays a role in RHO‐driven actin polymerisation via the Rho guanine nucleotide exchange activity of ARHGEF12. This may affect endosome position and motility.","predictedComplex":false,"interactors":[{"ac":"EBI-1049513","identifier":"Q9P0V3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P0V3/entry","name":"SH3BP4","description":"SH3 domain-binding protein 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15603","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350606","identifier":"Q9UM54","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UM54/entry","name":"MYO6","description":"Unconventional myosin-VI","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13140","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373132","identifier":"O14908","identifierLink":"https://www.uniprot.org/uniprotkb/O14908/entry","name":"GIPC1","description":"PDZ domain-containing protein GIPC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12259","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-821440","identifier":"Q9NZN5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZN5/entry","name":"ARHGEF12","description":"Rho guanine nucleotide exchange factor 12","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45872","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7725","complexName":"DISP septin regulator complex","organismName":"Homo sapiens; 9606","description":"Promotes the formation of septin rings, indicative of septin displacement from actin, thus regulating the actin cytoskeleton, potentially via the  guanine nucleotide exchange factor activity of DOCK7 which activates RAC1 (P63000).","predictedComplex":false,"interactors":[{"ac":"EBI-2433703","identifier":"Q96N67","identifierLink":"https://www.uniprot.org/uniprotkb/Q96N67/entry","name":"DOCK7","description":"Dedicator of cytokinesis protein 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23317","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350606","identifier":"Q9UM54","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UM54/entry","name":"MYO6","description":"Unconventional myosin-VI","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13140","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8795942","identifier":"Q96II8","identifierLink":"https://www.uniprot.org/uniprotkb/Q96II8/entry","name":"LRCH3","description":"DISP complex protein LRCH3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7726","complexName":"SYD-associated SWI/SNF ATP-dependent chromatin remodeling complex","organismName":"Arabidopsis thaliana; 3702","description":"An ATP-dependent chromatin remodeling complex which is recruited to promoters and enhancers of target genes in cells and alters chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors. 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3702","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34613130","identifier":"Q9FLP2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9FLP2/entry","name":"MCO15.16","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR34572","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-40269222","identifier":"Q8GYJ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8GYJ0/entry","name":"q8gyj0","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR34572","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-40269231","identifier":"Q84M92","identifierLink":"https://www.uniprot.org/uniprotkb/Q84M92/entry","name":"ARP4","description":"Actin-related protein 4","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-40269257","identifier":"Q8L4Y5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8L4Y5/entry","name":"ARP7","description":"Actin-related protein 7","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-40270350","identifier":"Q9LS90","identifierLink":"https://www.uniprot.org/uniprotkb/Q9LS90/entry","name":"LFR","description":"Armadillo repeat-containing protein LFR","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-40270408","identifier":"F4I9P8","identifierLink":"https://www.uniprot.org/uniprotkb/F4I9P8/entry","name":"f4i9p8","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[]},{"ac":"EBI-40270422","identifier":"C0SV00","identifierLink":"https://www.uniprot.org/uniprotkb/C0SV00/entry","name":"c0sv00","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[]},{"ac":"EBI-40270432","identifier":"Q5PNS0","identifierLink":"https://www.uniprot.org/uniprotkb/Q5PNS0/entry","name":"y3228","description":"PHD finger protein At3g20280","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[]},{"ac":"EBI-40270449","identifier":"F4J9M5","identifierLink":"https://www.uniprot.org/uniprotkb/F4J9M5/entry","name":"CHR12","description":"Probable ATP-dependent DNA helicase CHR12","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-40270484","identifier":"Q8VY54","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VY54/entry","name":"q8vy54","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR48316","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-40270496","identifier":"F4J5R1","identifierLink":"https://www.uniprot.org/uniprotkb/F4J5R1/entry","name":"f4j5r1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-40270515","identifier":"Q9LPJ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9LPJ1/entry","name":"q9lpj1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR35696","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4436027","identifier":"Q8RWJ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8RWJ7/entry","name":"SHH2","description":"Protein SAWADEE HOMEODOMAIN HOMOLOG 2","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR33827","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7728","complexName":"RB1-E2F3-DP1 transcriptional repressor complex","organismName":"Homo sapiens; 9606","description":"Formation of this complex, by binding of RB1 to the E2F2-DP1 transcription factor complex (CPX-1973), negatively regulates the G1-S transition by blocking the transactivation domain of E2F1. RB1 dissociates from the complex following hyperphosphorylation by cyclin-dependent kinases.","predictedComplex":false,"interactors":[{"ac":"EBI-491274","identifier":"P06400","identifierLink":"https://www.uniprot.org/uniprotkb/P06400/entry","name":"RB1","description":"Retinoblastoma-associated protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749713","identifier":"Q14186","identifierLink":"https://www.uniprot.org/uniprotkb/Q14186/entry","name":"TFDP1","description":"Transcription factor Dp-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12548","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-765551","identifier":"O00716","identifierLink":"https://www.uniprot.org/uniprotkb/O00716/entry","name":"E2F3","description":"Transcription factor E2F3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12081","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7741","complexName":"LIN-10-LIN-2-LIN-7 complex, LIN7A variant","organismName":"Mus musculus; 10090","description":"Scaffolding complex which appears to act as a major organization hub for modulating cellular functions, such as neuronal synaptic transmission, and cell polarity establishment and maintenance, with four PDZ domains, an SH3-GK tandem, and a PTB domain not involved in complex formation and thus available for binding to various target proteins.  May associate with the motor protein Kif17 (Q99PW8) to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B (Q01097) along microtubules..","predictedComplex":false,"interactors":[{"ac":"EBI-770029","identifier":"Q8JZS0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8JZS0/entry","name":"Lin7a","description":"Protein lin-7 homolog A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14063","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-771402","identifier":"O70589","identifierLink":"https://www.uniprot.org/uniprotkb/O70589/entry","name":"Cask","description":"Peripheral plasma membrane protein CASK","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23122","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8840254","identifier":"B2RUJ5","identifierLink":"https://www.uniprot.org/uniprotkb/B2RUJ5/entry","name":"Apba1","description":"Amyloid-beta A4 precursor protein-binding family A member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12345","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7742","complexName":"LIN-10-LIN-2-LIN-7 complex, LIN7C variant","organismName":"Mus musculus; 10090","description":"Scaffolding complex which appears to act as a major organization hub for modulating cellular functions, such as neuronal synaptic transmission, and cell polarity establishment and maintenance, with four PDZ domains, an SH3-GK tandem, and a PTB domain not involved in complex formation and thus available for binding to various target proteins.  May associate with the motor protein Kif17 (Q99PW8) to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B (Q01097) along microtubules..","predictedComplex":false,"interactors":[{"ac":"EBI-771402","identifier":"O70589","identifierLink":"https://www.uniprot.org/uniprotkb/O70589/entry","name":"Cask","description":"Peripheral plasma membrane protein CASK","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23122","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-821316","identifier":"O88952","identifierLink":"https://www.uniprot.org/uniprotkb/O88952/entry","name":"Lin7c","description":"Protein lin-7 homolog C","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14063","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8840254","identifier":"B2RUJ5","identifierLink":"https://www.uniprot.org/uniprotkb/B2RUJ5/entry","name":"Apba1","description":"Amyloid-beta A4 precursor protein-binding family A member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12345","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7743","complexName":"LIN-10-LIN-2-LIN-7 complex, LIN7B variant","organismName":"Homo sapiens; 9606","description":"Scaffolding complex which appears to act as a major organization hub for modulating cellular functions, such as neuronal synaptic transmission, and cell polarity establishment and maintenance, with four PDZ domains, an SH3-GK tandem, and a PTB domain not involved in complex formation and thus available for binding to various target proteins.  May associate with the motor protein KIF17 (Q9P2E2) to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B (Q13224) along microtubules..","predictedComplex":false,"interactors":[{"ac":"EBI-1215506","identifier":"O14936","identifierLink":"https://www.uniprot.org/uniprotkb/O14936/entry","name":"CASK","description":"Peripheral plasma membrane protein CASK","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23122","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-368690","identifier":"Q02410","identifierLink":"https://www.uniprot.org/uniprotkb/Q02410/entry","name":"APBA1","description":"Amyloid-beta A4 precursor protein-binding family A member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12345","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-821335","identifier":"Q9HAP6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HAP6/entry","name":"LIN7B","description":"Protein lin-7 homolog B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14063","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7744","complexName":"LIN-10-LIN-2-LIN-7 complex, LIN7A variant","organismName":"Homo sapiens; 9606","description":"Scaffolding complex which appears to act as a major organization hub for modulating cellular functions, such as neuronal synaptic transmission, and cell polarity establishment and maintenance, with four PDZ domains, an SH3-GK tandem, and a PTB domain not involved in complex formation and thus available for binding to various target proteins.  May associate with the motor protein KIF17 (Q9P2E2) to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B (Q13224) along microtubules..","predictedComplex":false,"interactors":[{"ac":"EBI-1215506","identifier":"O14936","identifierLink":"https://www.uniprot.org/uniprotkb/O14936/entry","name":"CASK","description":"Peripheral plasma membrane protein CASK","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23122","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2513988","identifier":"O14910","identifierLink":"https://www.uniprot.org/uniprotkb/O14910/entry","name":"LIN7A","description":"Protein lin-7 homolog A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14063","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-368690","identifier":"Q02410","identifierLink":"https://www.uniprot.org/uniprotkb/Q02410/entry","name":"APBA1","description":"Amyloid-beta A4 precursor protein-binding family A member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12345","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7745","complexName":"LIN-10-LIN-2-LIN-7 complex, LIN7C variant","organismName":"Homo sapiens; 9606","description":"Scaffolding complex which appears to act as a major organization hub for modulating cellular functions, such as neuronal synaptic transmission, and cell polarity establishment and maintenance, with four PDZ domains, an SH3-GK tandem, and a PTB domain not involved in complex formation and thus available for binding to various target proteins.  May associate with the motor protein KIF17 (Q9P2E2) to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B (Q13224) along microtubules..","predictedComplex":false,"interactors":[{"ac":"EBI-1171517","identifier":"Q9NUP9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NUP9/entry","name":"LIN7C","description":"Protein lin-7 homolog C","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14063","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1215506","identifier":"O14936","identifierLink":"https://www.uniprot.org/uniprotkb/O14936/entry","name":"CASK","description":"Peripheral plasma membrane protein CASK","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23122","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-368690","identifier":"Q02410","identifierLink":"https://www.uniprot.org/uniprotkb/Q02410/entry","name":"APBA1","description":"Amyloid-beta A4 precursor protein-binding family A member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12345","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7747","complexName":"SCF E3 ubiquitin ligase complex, FBXW2 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXW2  target proteins include SKP2 (Q13309) and CTNNB1 (P35222). thus regulating cell cycle progression.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-914727","identifier":"Q9UKT8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UKT8/entry","name":"FBXW2","description":"F-box/WD repeat-containing protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44436","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7761","complexName":"SCF E3 ubiquitin ligase complex, FBXW4 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. FBXW4 variants have been associated with limb malformations suggesting SCF-FBXW4  plays a role in embryonic limb development.","predictedComplex":false,"interactors":[{"ac":"EBI-2372268","identifier":"P57775","identifierLink":"https://www.uniprot.org/uniprotkb/P57775/entry","name":"FBXW4","description":"F-box/WD repeat-containing protein 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14381","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7762","complexName":"SCF E3 ubiquitin ligase complex, FBXW5 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXW5  target proteins include the actin remodeller EPS8 (Q12929), the centrosomal scaffold protein SAS6 (Q6UVJ0) thus restricting centrosome re-duplication, the COPII component SEC23B (Q15437)  and apoptosis signal‐regulating kinase,MAP3K5 (Q99683). The complex targets KIF2C (Q99661) for proteasomal degradation predominantly during G2 suggesting a role in the regulation of ciliogenesis.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-741068","identifier":"Q969U6","identifierLink":"https://www.uniprot.org/uniprotkb/Q969U6/entry","name":"FBXW5","description":"F-box/WD repeat-containing protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20995","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7763","complexName":"SCF E3 ubiquitin ligase complex, FBXW7 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXW7 target proteins include WDR5 (P61964), a member of numerous histone-lysine N-methyltransferase complexes, thus promoting mitotic cell death and preventing mitotic slippage, escape from the spindle assembly checkpoint-induced mitotic arrest. The complex ubiquitinates the MYC (P01106) transcription factor when it is phosphorylated at Thr-73 and Ser-77.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359574","identifier":"Q969H0","identifierLink":"https://www.uniprot.org/uniprotkb/Q969H0/entry","name":"FBXW7","description":"F-box/WD repeat-containing protein 7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19849","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7764","complexName":"SFPQ-PSPC1 RNA-binding complex","organismName":"Homo sapiens; 9606","description":"RNA-binding complex which is a core component of paraspeckles, discrete subnuclear bodies in the interchromatin nucleoplasmic space, often located adjacent to nuclear specks. Biogenesis and structural integrity of paraspeckles mainly depend on the interaction of NONO, SFPQ, and PSPC1 homo/heterodimers with the long non-coding RNA nuclear-enriched autosomal non-coding transcripts (NEAT1). The complex plays a role in several nuclear processes, such as pre-mRNA splicing, DNA repair, and transcriptional regulation","predictedComplex":false,"interactors":[{"ac":"EBI-1392258","identifier":"Q8WXF1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WXF1/entry","name":"PSPC1","description":"Paraspeckle component 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23189","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355453","identifier":"P23246","identifierLink":"https://www.uniprot.org/uniprotkb/P23246/entry","name":"SFPQ","description":"Splicing factor, proline- and glutamine-rich","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23189","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7765","complexName":"SFPQ-NONO RNA-binding complex","organismName":"Homo sapiens; 9606","description":"RNA-binding complex which is a core component of paraspeckles, discrete subnuclear bodies in the interchromatin nucleoplasmic space, often located adjacent to nuclear specks. Biogenesis and structural integrity of paraspeckles mainly depend on the interaction of NONO, SFPQ, and PSPC1 homo/heterodimers with the long non-coding RNA nuclear-enriched autosomal non-coding transcripts (NEAT1). The complex plays a role in several nuclear processes, such as pre-mRNA splicing, DNA repair, and transcriptional regulation","predictedComplex":false,"interactors":[{"ac":"EBI-350527","identifier":"Q15233","identifierLink":"https://www.uniprot.org/uniprotkb/Q15233/entry","name":"NONO","description":"Non-POU domain-containing octamer-binding protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23189","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355453","identifier":"P23246","identifierLink":"https://www.uniprot.org/uniprotkb/P23246/entry","name":"SFPQ","description":"Splicing factor, proline- and glutamine-rich","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23189","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7781","complexName":"NONO RNA-binding homodimer","organismName":"Homo sapiens; 9606","description":"RNA-binding complex which is a core component of paraspeckles, discrete subnuclear bodies in the interchromatin nucleoplasmic space, often located adjacent to nuclear specks. Biogenesis and structural integrity of paraspeckles mainly depend on the interaction of NONO, SFPQ, and PSPC1 homo/heterodimers with the long non-coding RNA nuclear-enriched autosomal non-coding transcripts (NEAT1). The complex plays a role in several nuclear processes, such as pre-mRNA splicing, DNA repair, and transcriptional regulation","predictedComplex":false,"interactors":[{"ac":"EBI-350527","identifier":"Q15233","identifierLink":"https://www.uniprot.org/uniprotkb/Q15233/entry","name":"NONO","description":"Non-POU domain-containing octamer-binding protein","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23189","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7782","complexName":"SFPQ RNA-binding homodimer","organismName":"Homo sapiens; 9606","description":"RNA-binding complex which is a core component of paraspeckles, discrete subnuclear bodies in the interchromatin nucleoplasmic space, often located adjacent to nuclear specks. Biogenesis and structural integrity of paraspeckles mainly depend on the interaction of NONO, SFPQ, and PSPC1 homo/heterodimers with the long non-coding RNA nuclear-enriched autosomal non-coding transcripts (NEAT1). The complex plays a role in several nuclear processes, such as pre-mRNA splicing, DNA repair, and transcriptional regulation  An excess of Zion ions, in conditions such as Alzheimer Disease, results in SFPQ oligermerisation and misloaction to the cytoplasm.","predictedComplex":false,"interactors":[{"ac":"EBI-355453","identifier":"P23246","identifierLink":"https://www.uniprot.org/uniprotkb/P23246/entry","name":"SFPQ","description":"Splicing factor, proline- and glutamine-rich","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23189","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7783","complexName":"PSPC1 RNA-binding homodimer","organismName":"Homo sapiens; 9606","description":"RNA-binding complex which is a core component of paraspeckles, discrete subnuclear bodies in the interchromatin nucleoplasmic space, often located adjacent to nuclear specks. Biogenesis and structural integrity of paraspeckles mainly depend on the interaction of NONO, SFPQ, and PSPC1 homo/heterodimers with the long non-coding RNA nuclear-enriched autosomal non-coding transcripts (NEAT1). The complex plays a role in several nuclear processes, such as pre-mRNA splicing, DNA repair, and transcriptional regulation","predictedComplex":false,"interactors":[{"ac":"EBI-1392258","identifier":"Q8WXF1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WXF1/entry","name":"PSPC1","description":"Paraspeckle component 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23189","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7784","complexName":"SCF E3 ubiquitin ligase complex, FBXW8-CUL7 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXW8  target proteins include BTRC (Q9Y297) a component of the SCF E3 ubiquitin ligase complex, BTRC variant  (CPX-2365)","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-308606","identifier":"Q14999","identifierLink":"https://www.uniprot.org/uniprotkb/Q14999/entry","name":"CUL7","description":"Cullin-7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22771","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-914770","identifier":"Q8N3Y1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N3Y1/entry","name":"FBXW8","description":"F-box/WD repeat-containing protein 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7785","complexName":"SCF E3 ubiquitin ligase complex, FBXW9 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.","predictedComplex":false,"interactors":[{"ac":"EBI-2322729","identifier":"Q5XUX1","identifierLink":"https://www.uniprot.org/uniprotkb/Q5XUX1/entry","name":"FBXW9","description":"F-box/WD repeat-containing protein 9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19855","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7786","complexName":"SCF E3 ubiquitin ligase complex, FBXW10 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. The cellular levels and function of FBXW10 depend on the protein O-GlcNAcylation and overexpression of this protein results in the degradation of CBX5 (P45973) and CBX1 (P83916).","predictedComplex":false,"interactors":[{"ac":"EBI-11603405","identifier":"Q5XX13","identifierLink":"https://www.uniprot.org/uniprotkb/Q5XX13/entry","name":"FBXW10","description":"F-box/WD repeat-containing protein 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19872","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7801","complexName":"KPC E3 ubiquitin ligase complex","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which regulates degradation of the cyclin-dependent kinase inhibitor CDKN1B (P46527) at the G1 phase of the cell cycle. Ubiquitinates NFKB1 (P19838) which rsults in limited proteosomal processing and generation of the active NF-kappa-B p50 protein (PRO_0000030311).","predictedComplex":false,"interactors":[{"ac":"EBI-1057418","identifier":"Q5XPI4","identifierLink":"https://www.uniprot.org/uniprotkb/Q5XPI4/entry","name":"RNF123","description":"E3 ubiquitin-protein ligase RNF123","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13363","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749370","identifier":"Q9BSL1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BSL1/entry","name":"UBAC1","description":"Ubiquitin-associated domain-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46738","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7802","complexName":"Thyrostimulin thyroid-stimulating hormone complex","organismName":"Homo sapiens; 9606","description":"Glycoprotein hormone which binds and activates the thyroid-stimulating hormone receptor (P16473), leading to increased cAMP production. The lability of the complex has suggested an autocrine or paracrine role for the complex, rather than it acting as an endocrine factor.","predictedComplex":false,"interactors":[{"ac":"EBI-11659696","identifier":"Q96T91","identifierLink":"https://www.uniprot.org/uniprotkb/Q96T91/entry","name":"GPHA2","description":"Glycoprotein hormone alpha-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11659720","identifier":"Q86YW7","identifierLink":"https://www.uniprot.org/uniprotkb/Q86YW7/entry","name":"GPHB5","description":"Glycoprotein hormone beta-5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11515","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7803","complexName":"COPI vesicle coat complex, COPG1-COPZ1 variant","organismName":"Homo sapiens; 9606","description":"Coats vesicles which bud from the Golgi membrane and subsequently transport proteins from the cis end of the Golgi complex back to the rough endoplasmic reticulum (ER), where they were originally synthesized (retrograde transport), and between Golgi compartments. The complex binds to di-lysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi to the trans Golgi network. Cargo containing the sorting motifs KKXX and KXKXX interact with COPI to form carriers. The COPG1-COPZ1 variant is preferentially present in the early Golgi apparatus.","predictedComplex":false,"interactors":[{"ac":"EBI-1044491","identifier":"P48444","identifierLink":"https://www.uniprot.org/uniprotkb/P48444/entry","name":"ARCN1","description":"Coatomer subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10121","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1049127","identifier":"Q9Y678","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y678/entry","name":"COPG1","description":"Coatomer subunit gamma-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10261","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1049939","identifier":"P61923","identifierLink":"https://www.uniprot.org/uniprotkb/P61923/entry","name":"COPZ1","description":"Coatomer subunit zeta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11043","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1056534","identifier":"P35606","identifierLink":"https://www.uniprot.org/uniprotkb/P35606/entry","name":"COPB2","description":"Coatomer subunit beta'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19876","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356273","identifier":"P53621","identifierLink":"https://www.uniprot.org/uniprotkb/P53621/entry","name":"COPA","description":"Coatomer subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19876","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359063","identifier":"P53618","identifierLink":"https://www.uniprot.org/uniprotkb/P53618/entry","name":"COPB1","description":"Coatomer subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10635","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-711301","identifier":"O14579","identifierLink":"https://www.uniprot.org/uniprotkb/O14579/entry","name":"COPE","description":"Coatomer subunit epsilon","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10805","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7821","complexName":"SCF E3 ubiquitin ligase complex, FBXW11 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXW11 target proteins include phosphorylated CTNNB1 (P35222) thus participating in the regulation of Wnt signaling, and phosphorylated NFKBIA (P25963), degradation of which frees the associated NFKB1 (P19838) to translocate into the nucleus and to activate transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355189","identifier":"Q9UKB1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UKB1/entry","name":"FBXW11","description":"F-box/WD repeat-containing protein 11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7822","complexName":"SCF E3 ubiquitin ligase complex, FBXW12 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXW12 target proteins include the IL-22 receptor (Q8N6P7/Q969J5) thus mediating IL-22 signaling via JAK/STAT pathways.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-44433100","identifier":"Q6X9E4","identifierLink":"https://www.uniprot.org/uniprotkb/Q6X9E4/entry","name":"FBXW12","description":"F-box/WD repeat-containing protein 12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7841","complexName":"Glycine receptor complex, GLRA1-GLRB","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel, the activation of which results in a chloride ion flow across the membrane regulated by the chloride ion equilibrium potential. This induces membrane hyperpolarization which, in turn, inhibits neuronal activity. Adult glycine receptors are mainly of the heteromeric GLRA1-GLRB type.","predictedComplex":false,"interactors":[{"ac":"EBI-11733190","identifier":"P48167","identifierLink":"https://www.uniprot.org/uniprotkb/P48167/entry","name":"GLRB","description":"Glycine receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12020340","identifier":"P23415","identifierLink":"https://www.uniprot.org/uniprotkb/P23415/entry","name":"GLRA1","description":"Glycine receptor subunit alpha-1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7842","complexName":"Retromer complex, VPS26A variant","organismName":"Homo sapiens; 9606","description":"Mediates the recycling of transmembrane proteins from endosomes to the trans-Golgi network. Functions in endosomal membrane protein sorting and transport for endosome-to-Golgi retrieval.","predictedComplex":false,"interactors":[{"ac":"EBI-1043891","identifier":"O75436","identifierLink":"https://www.uniprot.org/uniprotkb/O75436/entry","name":"VPS26A","description":"Vacuolar protein sorting-associated protein 26A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12233","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1054634","identifier":"Q96QK1","identifierLink":"https://www.uniprot.org/uniprotkb/Q96QK1/entry","name":"VPS35","description":"Vacuolar protein sorting-associated protein 35","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11099","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-718596","identifier":"Q9UBQ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UBQ0/entry","name":"VPS29","description":"Vacuolar protein sorting-associated protein 29","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11124","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7843","complexName":"Retromer complex, VPS26B variant","organismName":"Homo sapiens; 9606","description":"Mediates the recycling of transmembrane proteins from endosomes to the trans-Golgi network. Functions in endosomal membrane protein sorting and transport for endosome-to-Golgi retrieval.","predictedComplex":false,"interactors":[{"ac":"EBI-1054634","identifier":"Q96QK1","identifierLink":"https://www.uniprot.org/uniprotkb/Q96QK1/entry","name":"VPS35","description":"Vacuolar protein sorting-associated protein 35","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11099","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6151831","identifier":"Q4G0F5","identifierLink":"https://www.uniprot.org/uniprotkb/Q4G0F5/entry","name":"VPS26B","description":"Vacuolar protein sorting-associated protein 26B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12233","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-718596","identifier":"Q9UBQ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UBQ0/entry","name":"VPS29","description":"Vacuolar protein sorting-associated protein 29","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11124","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7844","complexName":"Glycine receptor complex, GLRA2-GLRB","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel, the activation of which results in a chloride ion flow across the membrane regulated by the chloride ion equilibrium potential. This induces membrane hyperpolarization which, in turn, inhibits neuronal activity.","predictedComplex":false,"interactors":[{"ac":"EBI-11733190","identifier":"P48167","identifierLink":"https://www.uniprot.org/uniprotkb/P48167/entry","name":"GLRB","description":"Glycine receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-725038","identifier":"P23416","identifierLink":"https://www.uniprot.org/uniprotkb/P23416/entry","name":"GLRA2","description":"Glycine receptor subunit alpha-2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7845","complexName":"Glycine receptor complex, GLRA3-GLRB","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel, the activation of which results in a chloride ion flow across the membrane regulated by the chloride ion equilibrium potential. This induces membrane hyperpolarization which, in turn, inhibits neuronal activity.","predictedComplex":false,"interactors":[{"ac":"EBI-11733190","identifier":"P48167","identifierLink":"https://www.uniprot.org/uniprotkb/P48167/entry","name":"GLRB","description":"Glycine receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16357053","identifier":"O75311","identifierLink":"https://www.uniprot.org/uniprotkb/O75311/entry","name":"GLRA3","description":"Glycine receptor subunit alpha-3","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7846","complexName":"SCF E3 ubiquitin ligase complex, CCNF variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-CCNF target proteins include CP110 (O43303) during G2 phase, the complex thereby acts as an inhibitor of centrosome reduplication. It also ubiquitinylates E2F1 (Q01094) during the G2/M phase of the cell cycle, preventing DNA replication stress.","predictedComplex":false,"interactors":[{"ac":"EBI-1207574","identifier":"P41002","identifierLink":"https://www.uniprot.org/uniprotkb/P41002/entry","name":"CCNF","description":"Cyclin-F","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7847","complexName":"SCF E3 ubiquitin ligase complex, FBXO2 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXO2 target proteins include bacterial surface glycan, thus enabling xenophagy, and glycosylated SUN2 (Q9UH99) involved in the connection between the nuclear lamina and the cytoskeleton.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4287196","identifier":"Q9UK22","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK22/entry","name":"FBXO2","description":"F-box only protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12125","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7849","complexName":"2-(3-amino-3-carboxypropyl)histidine synthase complex","organismName":"Homo sapiens; 9606","description":"Essential for the first step of biosynthesis of diphthamide, a unique post-translationally modified histidine residue on EEF2 (P13639), a GTPase that is essential in the elongation step of translation. The complex catalyzes the addition of an aminocarboxypropyl (ACP) group to a specific histidine residue in EEF2 using S-adenosylmethionine as a substrate. A small iron-containing protein DPH3 (Q96FX2) donates one Fe atom to convert the [3Fe-4S] cluster in DPH1-DPH2 to a functional [4Fe-4S] cluster during the radical-SAM enzyme catalytic cycle. the [4Fe-4S]2+ cluster in DPH1-DPH2 is reduced to [4Fe-4S]+ using dithionite as the reductant. The [4Fe-4S]+ cluster donates two electrons to SAM, cleaving it, forming an organometallic complex and releasing methylthioadenosine.The organometallic intermediate serves as a stabilized ACP radical and reacts with EEF2 to form an intermediate which is converted to the ACP-modified EEF2 product after loss of a hydrogen atom","predictedComplex":false,"interactors":[{"ac":"EBI-10237931","identifier":"Q9BQC3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BQC3/entry","name":"DPH2","description":"2-(3-amino-3-carboxypropyl)histidine synthase subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10762","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10303200","identifier":"Q9BZG8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BZG8/entry","name":"DPH1","description":"2-(3-amino-3-carboxypropyl)histidine synthase subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10762","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-7850","complexName":"2-(3-amino-3-carboxypropyl)histidine synthase complex","organismName":"Drosophila melanogaster; 7227","description":"Essential for the first step of biosynthesis of diphthamide, a unique post-translationally modified histidine residue on EEF2 (P13060), a GTPase that is essential in the elongation step of translation. The complex catalyzes the addition of an aminocarboxypropyl (ACP) group to a specific histidine residue in EEF2 using S-adenosylmethionine as a substrate. A small iron-containing protein DPH3 (Q9VGQ9) donates one Fe atom to convert the [3Fe-4S] cluster in DPH1-DPH2 to a functional [4Fe-4S] cluster during the radical-SAM enzyme catalytic cycle. the [4Fe-4S]2+ cluster in DPH1-DPH2 is reduced to [4Fe-4S]+ using dithionite as the reductant. The [4Fe-4S]+ cluster donates two electrons to SAM, cleaving it, forming an organometallic complex and releasing methylthioadenosine.The organometallic intermediate serves as a stabilized ACP radical and reacts with EEF2 to form an intermediate which is converted to the ACP-modified EEF2 product after loss of a hydrogen atom","predictedComplex":false,"interactors":[{"ac":"EBI-116672","identifier":"Q9VTM2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VTM2/entry","name":"Dph1","description":"2-(3-amino-3-carboxypropyl)histidine synthase subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10762","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-183332","identifier":"Q9VFE9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VFE9/entry","name":"Dph2","description":"2-(3-amino-3-carboxypropyl)histidine synthase subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10762","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7861","complexName":"PHF2-ARID5B histone lysine demethylase complex","organismName":"Homo sapiens; 9606","description":"Histone lysine demethylase which acts as a signal-sensing epigenetic determinant through removal of a repressive histone methylation mark on transcriptionally responsive promoters. Complex formation results in the demethylation of ARID5B by PHF2 and the subsequent recruitment of the  complex to H3K9me2-marked promoters of specific genes regulated by transcription factor SOX9 (P48436) or the lipogenic transcription factor MLXIPL (Q9NP71).","predictedComplex":false,"interactors":[{"ac":"EBI-10972034","identifier":"O75151","identifierLink":"https://www.uniprot.org/uniprotkb/O75151/entry","name":"PHF2","description":"Lysine-specific demethylase PHF2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23123","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1210388","identifier":"Q14865","identifierLink":"https://www.uniprot.org/uniprotkb/Q14865/entry","name":"ARID5B","description":"AT-rich interactive domain-containing protein 5B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7881","complexName":"SCF E3 ubiquitin ligase complex, FBXO3 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXO3 target proteins include FBXL2 (Q9UKC9/CPX-3292), thus promoting TNF receptor-associated factor (TRAF) signal transduction and cytokine gene transcription. May also regulate autoimmunity by ubiquitylating the  transcriptional regulator AIRE (O43918).","predictedComplex":false,"interactors":[{"ac":"EBI-2509901","identifier":"Q9UK99","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK99/entry","name":"FBXO3","description":"F-box only protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46550","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7882","complexName":"SCF E3 ubiquitin ligase complex, FBXO4 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. 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SCF-FBXO6 target proteins include unfolded N-glycoproteins thus initiating their endoplasmic reticulum‐related protein degradation. May play a role in inhibiting ER stress-induced apoptosis through ubiquitination of the ERO1A (Q96HE7) oxidoreductase.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3938499","identifier":"Q9NRD1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NRD1/entry","name":"FBXO6","description":"F-box only protein 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12125","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7906","complexName":"SCF E3 ubiquitin ligase complex, FBXO7 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXO7 target proteins include the potential cell cycle regulator DLGAP5 (Q15398), the E3 ubiquitin-protein ligase BIRC2 (Q13490) and TRAF2 (Q12933) thus influencing NF-kappa-B signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-1161222","identifier":"Q9Y3I1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3I1/entry","name":"FBXO7","description":"F-box only protein 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15537","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7921","complexName":"SCF E3 ubiquitin ligase complex, FBXO8 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXO8 target proteins include the Pi class phase II metabolizing enzyme glutathione S-transferase P1 (P09211) and the ADP-ribosylation factor, ARF6 (P62330) which regulates membrane remodeling at cell peripheries.","predictedComplex":false,"interactors":[{"ac":"EBI-11615366","identifier":"Q9NRD0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NRD0/entry","name":"FBXO8","description":"F-box only protein 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10663","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7922","complexName":"SCF E3 ubiquitin ligase complex, FBXO9 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXO9 target proteins include TELO2 (Q9Y4R8) and TTI1 (O43156) found in TORC1 (CPX-503) and TTT (CPX-6148) complexes thus limiting cell growth and protein translation","predictedComplex":false,"interactors":[{"ac":"EBI-2869927","identifier":"Q9UK97","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK97/entry","name":"FBXO9","description":"F-box only protein 9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12874","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7923","complexName":"SCF E3 ubiquitin ligase complex, FBXO10 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXO10 target proteins include the receptor for advanced glycation end products, AGER (Q15109), a cell surface pattern recognition receptor that senses endogenous stress signals and plays a role in inflammation. Also targets the long-chain fatty-acid-CoA ligase ACSL4 (O60488), a key enzyme in arachidonic acid biosynthesis which has been shown to contribute to ferroptosis, a type of programmed cell death dependent on iron and characterized by the accumulation of lipid peroxides.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6425614","identifier":"Q9UK96","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK96/entry","name":"FBXO10","description":"F-box only protein 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22990","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7924","complexName":"SCF E3 ubiquitin ligase complex, FBXO11 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXO11 target proteins include DTL (Q9NZJ0), a substrate-specific adapter of DDB1-CUL4-DTL (CPX-2795/CPX-2777) E3 ubiquitin-protein ligase complex required for cell cycle control, DNA damage response and translesion DNA synthesis. NEDDylates TP53 (P04637) Lys-320, Lys-321 resulting in the selective inhibition of p53 transcriptional activity, and influencing nuclear export by preventing p53 monoubiquitination.","predictedComplex":false,"interactors":[{"ac":"EBI-1047804","identifier":"Q86XK2","identifierLink":"https://www.uniprot.org/uniprotkb/Q86XK2/entry","name":"FBXO11","description":"F-box only protein 11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22990","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7925","complexName":"SCF E3 ubiquitin ligase complex, FBXO15 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXO15 target proteins include cardiolipin synthase (Q9UJA2) thus regulating cardiolipin levels and mitochondrial integrity.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6660598","identifier":"Q8NCQ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NCQ5/entry","name":"FBXO15","description":"F-box only protein 15","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46731","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7926","complexName":"SCF E3 ubiquitin ligase complex, FBXO16 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.","predictedComplex":false,"interactors":[{"ac":"EBI-12063229","identifier":"Q8IX29","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IX29/entry","name":"FBXO16","description":"F-box only protein 16","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46857","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7927","complexName":"SCF E3 ubiquitin ligase complex, FBXO17 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXO17 target proteins include the constitutively active protein kinase GSK3B (P49841) thus regulating WNT/CTNNB1 signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-2510157","identifier":"Q96EF6","identifierLink":"https://www.uniprot.org/uniprotkb/Q96EF6/entry","name":"FBXO17","description":"F-box only protein 17","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12125","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7928","complexName":"SCF E3 ubiquitin ligase complex, FBH1 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBH1 target proteins include the constitutively active protein kinase GSK3B (P49841) thus regulating WNT/CTNNB1 signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724767","identifier":"Q8NFZ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NFZ0/entry","name":"FBH1","description":"F-box DNA helicase 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11070","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7929","complexName":"SCF E3 ubiquitin ligase complex, LMO7 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-LMO7 target proteins include STING (CPX-2127), the Lys-63-linked poly-ubiquitination of which controls steady-state STING degradation and thus the the innate immune response to nucleic acids, particularly cytosolic double-srranded DNA from bacteria and viruses and mitochondrial damage.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350367","identifier":"Q8WWI1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WWI1/entry","name":"LMO7","description":"LIM domain only protein 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7930","complexName":"SCF E3 ubiquitin ligase complex, FBXO21 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBX21 target proteins include the transcription corepressor EID1 (Q9Y6B2).","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-311435","identifier":"O94952","identifierLink":"https://www.uniprot.org/uniprotkb/O94952/entry","name":"FBXO21","description":"F-box only protein 21","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31350","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7931","complexName":"DNA replication factor C complex, RAD17 variant","organismName":"Homo sapiens; 9606","description":"DNA-dependent ATPase clamp-loader complex that uses the energy of ATP binding and hydrolysis to recruit the checkpoint clamp complex (CPX-1829) to the recessed 5' end of a dsDNA-ssDNA junction as part of a DNA damage checkpoint system..","predictedComplex":false,"interactors":[{"ac":"EBI-1055010","identifier":"P40938","identifierLink":"https://www.uniprot.org/uniprotkb/P40938/entry","name":"RFC3","description":"Replication factor C subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-476409","identifier":"P35250","identifierLink":"https://www.uniprot.org/uniprotkb/P35250/entry","name":"RFC2","description":"Replication factor C subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-476655","identifier":"P35249","identifierLink":"https://www.uniprot.org/uniprotkb/P35249/entry","name":"RFC4","description":"Replication factor C subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712376","identifier":"P40937","identifierLink":"https://www.uniprot.org/uniprotkb/P40937/entry","name":"RFC5","description":"Replication factor C subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968231","identifier":"O75943","identifierLink":"https://www.uniprot.org/uniprotkb/O75943/entry","name":"RAD17","description":"Cell cycle checkpoint protein RAD17","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12172","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7941","complexName":"PHO transcriptional repressor complex, PHO variant","organismName":"Drosophila melanogaster; 7227","description":"Polycomb group protein complex which binds Polycomb Response Elements (PREs) in the promoters of specific genes, for example HOX genes, and represses transcription. Recruits additional proteins to form higher-order polycomb repressive complexes.","predictedComplex":false,"interactors":[{"ac":"EBI-117801","identifier":"Q9VK33","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VK33/entry","name":"Sfmbt","description":"Polycomb protein Sfmbt","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12247","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-125201","identifier":"Q8ST83","identifierLink":"https://www.uniprot.org/uniprotkb/Q8ST83/entry","name":"pho","description":"Polycomb protein PHO","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14003","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7942","complexName":"PHO transcriptional repressor complex, PHOL variant","organismName":"Drosophila melanogaster; 7227","description":"Polycomb group protein complex which binds Polycomb Response Elements (PREs) in the promoters of specific genes, for example HOX genes, and represses transcription. Recruits additional proteins to form higher-order polycomb repressive complexes.","predictedComplex":false,"interactors":[{"ac":"EBI-117801","identifier":"Q9VK33","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VK33/entry","name":"Sfmbt","description":"Polycomb protein Sfmbt","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12247","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-176113","identifier":"Q9VSZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VSZ3/entry","name":"phol","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14003","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7943","complexName":"NatC N-alpha-acetyltransferase complex","organismName":"Drosophila melanogaster; 7227","description":"N(alpha)-acetyltransferases responsible for the covalent attachment of an acetyl group (CH3CO) to the free alpha-amino group (NH3+) at the N-terminal end of a polypeptide, one of the most common co-translational modifications. This changes the electrostatic properties of proteins and therefore protein function, stability and localization. NatC acetylates N-terminal methionine of proteins with hydrophobic/amphipathic N-termini (Met-Leu- Met-Ile-, Met-Phe-, Met-Trp-, Mat-Val-, Met-Met-, Met-His-, and Met-Lys-) to varying degrees","predictedComplex":false,"interactors":[{"ac":"EBI-15117977","identifier":"Q8IPZ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IPZ7/entry","name":"Sbat","description":"N-alpha-acetyltransferase 38, NatC auxiliary subunit","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-165029","identifier":"Q95RC0","identifierLink":"https://www.uniprot.org/uniprotkb/Q95RC0/entry","name":"Naa30A","description":"N-alpha-acetyltransferase 30A","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45896","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-178642","identifier":"Q9W1A2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W1A2/entry","name":"Naa35","description":"N-alpha-acetyltransferase 35, NatC auxiliary subunit homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21373","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7961","complexName":"NatC N-alpha-acetyltransferase complex, testis-specific variant","organismName":"Drosophila melanogaster; 7227","description":"N(alpha)-acetyltransferases responsible for the covalent attachment of an acetyl group (CH3CO) to the free alpha-amino group (NH3+) at the N-terminal end of a polypeptide, one of the most common co-translational modifications. This changes the electrostatic properties of proteins and therefore protein function, stability and localization. NatC acetylates N-terminal methionine of proteins with hydrophobic/amphipathic N-termini (Met-Leu- Met-Ile-, Met-Phe-, Met-Trp-, Mat-Val-, Met-Met-, Met-His-, and Met-Lys-) to varying degrees. This variant is highly expressed in the testis.","predictedComplex":false,"interactors":[{"ac":"EBI-15117977","identifier":"Q8IPZ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IPZ7/entry","name":"Sbat","description":"N-alpha-acetyltransferase 38, NatC auxiliary subunit","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-178642","identifier":"Q9W1A2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W1A2/entry","name":"Naa35","description":"N-alpha-acetyltransferase 35, NatC auxiliary subunit homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21373","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-44449254","identifier":"Q8IRH2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IRH2/entry","name":"Naa30B","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45896","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7962","complexName":"SCF E3 ubiquitin ligase complex, FBXO22 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.","predictedComplex":false,"interactors":[{"ac":"EBI-2510137","identifier":"Q8NEZ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NEZ5/entry","name":"FBXO22","description":"F-box only protein 22","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14939","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7963","complexName":"SCF E3 ubiquitin ligase complex, FBXO24 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXO24 target proteins include the arginine methyltransferase PRMT6 (Q96LA8) and the nucleoside diphosphate kinase A (P15531) thus regulating cell proliferation.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6425658","identifier":"O75426","identifierLink":"https://www.uniprot.org/uniprotkb/O75426/entry","name":"FBXO24","description":"F-box only protein 24","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47004","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7964","complexName":"COP9 signalosome complex, testis-specific variant","organismName":"Drosophila melanogaster; 7227","description":"Plays a central role in the regulation of the E3-cullin RING ubiquitin ligases, deNEDDylating the cullin subunit via the isopeptidase activity of the CNS5 subunit. CSN1a lacks a PCI domain (IPR000717) and is primarily expressed in the testis.","predictedComplex":false,"interactors":[{"ac":"EBI-107823","identifier":"Q8SYG2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8SYG2/entry","name":"CSN3","description":"COP9 signalosome complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10758","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-141466","identifier":"Q9V345","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V345/entry","name":"CSN4","description":"COP9 signalosome complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10855","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-155199","identifier":"Q9V4S8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V4S8/entry","name":"CSN7","description":"COP9 signalosome complex subunit 7","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15350","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-163377","identifier":"Q9VJR9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VJR9/entry","name":"CSN1a","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14145","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-183494","identifier":"Q9VCY3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VCY3/entry","name":"CSN6","description":"COP9 signalosome complex subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10540","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26824078","identifier":"Q7KTH8","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KTH8/entry","name":"CSN8","description":"COP9 signalosome complex subunit 8","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13339","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-87133","identifier":"Q94899","identifierLink":"https://www.uniprot.org/uniprotkb/Q94899/entry","name":"alien","description":"COP9 signalosome complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-97187","identifier":"Q9XZ58","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XZ58/entry","name":"CSN5","description":"COP9 signalosome complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10410","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7965","complexName":"SCF E3 ubiquitin ligase complex, FBXO25 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXO25 target proteins include the histone H2A monoubiquitinating the protein at lysine 120 (H2BK120), promoting trimethylation of histone 3 trimethylated at lysine 4 (H3K4).","predictedComplex":false,"interactors":[{"ac":"EBI-1161114","identifier":"Q8TCJ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TCJ0/entry","name":"FBXO25","description":"F-box only protein 25","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13123","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7966","complexName":"SCF E3 ubiquitin ligase complex, FBXO27 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXO27 target proteins include the luminal part of the lysosome-associated membrane glycoprotein LAMP2 (P13473), following membrane permeabilization, thus acting as a sensor of lysosomal damage.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6425694","identifier":"Q8NI29","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NI29/entry","name":"FBXO27","description":"F-box only protein 27","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12125","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7967","complexName":"SCF E3 ubiquitin ligase complex, FBXO28 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXO28 target proteins include the master transcriptional regulator of the adaptive response to hypoxia HIF1A (Q16665) and also the MYC (P01106) transcription factor, ubuiqination of which by the complex stimulates MYC-p300 interactions at target promoters rather than degradation. SCF-FBXO28 activity and stability are regulated during the cell cycle by CDK1/2-mediated phosphorylation of FBXO28","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-740282","identifier":"Q9NVF7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NVF7/entry","name":"FBXO28","description":"F-box only protein 28","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13252","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7968","complexName":"SCF E3 ubiquitin ligase complex, FBXO30 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXO30 target proteins include the master transcriptional regulator of the adaptive response to hypoxia HIF1A (Q16665).","predictedComplex":false,"interactors":[{"ac":"EBI-2556210","identifier":"Q8TB52","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TB52/entry","name":"FBXO30","description":"F-box only protein 30","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15933","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7969","complexName":"COPI vesicle coat complex, COPG2-COPZ1 variant","organismName":"Homo sapiens; 9606","description":"Coats vesicles which bud from the Golgi membrane and subsequently transport proteins from the cis end of the Golgi complex back to the rough endoplasmic reticulum (ER), where they were originally synthesized (retrograde transport), and between Golgi compartments. The complex binds to di-lysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi to the trans Golgi network. Cargo containing the sorting motifs KKXX and KXKXX interact with COPI to form carriers. The COPG2-COPZ1 variant is preferentially present in the early Golgi apparatus.","predictedComplex":false,"interactors":[{"ac":"EBI-1044491","identifier":"P48444","identifierLink":"https://www.uniprot.org/uniprotkb/P48444/entry","name":"ARCN1","description":"Coatomer subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10121","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1045840","identifier":"Q9UBF2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UBF2/entry","name":"COPG2","description":"Coatomer subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10261","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1049939","identifier":"P61923","identifierLink":"https://www.uniprot.org/uniprotkb/P61923/entry","name":"COPZ1","description":"Coatomer subunit zeta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11043","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1056534","identifier":"P35606","identifierLink":"https://www.uniprot.org/uniprotkb/P35606/entry","name":"COPB2","description":"Coatomer subunit beta'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19876","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356273","identifier":"P53621","identifierLink":"https://www.uniprot.org/uniprotkb/P53621/entry","name":"COPA","description":"Coatomer subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19876","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359063","identifier":"P53618","identifierLink":"https://www.uniprot.org/uniprotkb/P53618/entry","name":"COPB1","description":"Coatomer subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10635","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-711301","identifier":"O14579","identifierLink":"https://www.uniprot.org/uniprotkb/O14579/entry","name":"COPE","description":"Coatomer subunit epsilon","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10805","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7970","complexName":"COPI vesicle coat complex, COPG1-COPZ2 variant","organismName":"Homo sapiens; 9606","description":"Coats vesicles which bud from the Golgi membrane and subsequently transport proteins from the cis end of the Golgi complex back to the rough endoplasmic reticulum (ER), where they were originally synthesized (retrograde transport), and between Golgi compartments. The complex binds to di-lysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi to the trans Golgi network. Cargo containing the sorting motifs KKXX and KXKXX interact with COPI to form carriers. The COPG1-COPZ2 variant is preferentially present in the late Golgi apparatus.","predictedComplex":false,"interactors":[{"ac":"EBI-1044491","identifier":"P48444","identifierLink":"https://www.uniprot.org/uniprotkb/P48444/entry","name":"ARCN1","description":"Coatomer subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10121","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1049127","identifier":"Q9Y678","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y678/entry","name":"COPG1","description":"Coatomer subunit gamma-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10261","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1056534","identifier":"P35606","identifierLink":"https://www.uniprot.org/uniprotkb/P35606/entry","name":"COPB2","description":"Coatomer subunit beta'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19876","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34576422","identifier":"Q9P299","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P299/entry","name":"COPZ2","description":"Coatomer subunit zeta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11043","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356273","identifier":"P53621","identifierLink":"https://www.uniprot.org/uniprotkb/P53621/entry","name":"COPA","description":"Coatomer subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19876","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359063","identifier":"P53618","identifierLink":"https://www.uniprot.org/uniprotkb/P53618/entry","name":"COPB1","description":"Coatomer subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10635","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-711301","identifier":"O14579","identifierLink":"https://www.uniprot.org/uniprotkb/O14579/entry","name":"COPE","description":"Coatomer subunit epsilon","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10805","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7971","complexName":"SCF E3 ubiquitin ligase complex, FBXO31 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXO31 target proteins include the phospholipid hydroperoxide glutathione peroxidase (P36969) thus regulating ferroptosis and the retinal cell surface receptor CD147 (P35613), resulting in repression of lipid synthesis. Acts as a dedicated DNA damage checkpoint protein causing cell cycle arrest at G1 and G2/M phases through two independent pathways, either via the degradation of MDM2 (Q00987) in p53-positive cells which results in increased levels of p53, leading to growth arrest and senescence through transcriptional activation of CDKN1A  (P38936) or in p53-deficient cells, the complex mediates the degradation of CCND1 (P24385) resulting in G1 arrest.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6162477","identifier":"Q5XUX0","identifierLink":"https://www.uniprot.org/uniprotkb/Q5XUX0/entry","name":"FBXO31","description":"F-box only protein 31","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10706","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7972","complexName":"SCF E3 ubiquitin ligase complex, FBXO32 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXO32 target proteins include the initiation factor,EIF3F (O00303), the myogenic transcription factor, MYOD1 (P15172) and the growth-related transcription factor, MYC.(P01106).","predictedComplex":false,"interactors":[{"ac":"EBI-2932534","identifier":"Q969P5","identifierLink":"https://www.uniprot.org/uniprotkb/Q969P5/entry","name":"FBXO32","description":"F-box only protein 32","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13123","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7973","complexName":"SCF E3 ubiquitin ligase complex, FBXO33 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXO33 target proteins include the nucleic acid Y-box-binding protein YBX1 (P67809).","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8555452","identifier":"Q7Z6M2","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z6M2/entry","name":"FBXO33","description":"F-box only protein 33","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20933","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7974","complexName":"COP9 signalosome complex","organismName":"Drosophila melanogaster; 7227","description":"Plays a central role in the regulation of the E3-cullin RING ubiquitin ligases, deNEDDylating the cullin subunit via the isopeptidase activity of the CNS5 subunit. CSN1a lacks a PCI domain and is primarily expressed in the testis.","predictedComplex":false,"interactors":[{"ac":"EBI-107823","identifier":"Q8SYG2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8SYG2/entry","name":"CSN3","description":"COP9 signalosome complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10758","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-141466","identifier":"Q9V345","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V345/entry","name":"CSN4","description":"COP9 signalosome complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10855","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-155199","identifier":"Q9V4S8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V4S8/entry","name":"CSN7","description":"COP9 signalosome complex subunit 7","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15350","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-183494","identifier":"Q9VCY3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VCY3/entry","name":"CSN6","description":"COP9 signalosome complex subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10540","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26824078","identifier":"Q7KTH8","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KTH8/entry","name":"CSN8","description":"COP9 signalosome complex subunit 8","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13339","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3406597","identifier":"Q9VVU5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVU5/entry","name":"CSN1b","description":"COP9 signalosome complex subunit 1b","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14145","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-87133","identifier":"Q94899","identifierLink":"https://www.uniprot.org/uniprotkb/Q94899/entry","name":"alien","description":"COP9 signalosome complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-97187","identifier":"Q9XZ58","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XZ58/entry","name":"CSN5","description":"COP9 signalosome complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10410","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7975","complexName":"SCF E3 ubiquitin ligase complex, FBXO34 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXO34 target proteins include the cyclin CCNB1 (P14635), a component of the maturation promoting factor (CPX-2007), thus regulating both the G2/M transition and anaphase entry in meiotic oocytes.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-719816","identifier":"Q9NWN3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NWN3/entry","name":"FBXO34","description":"F-box only protein 34","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16271","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7976","complexName":"SCF E3 ubiquitin ligase complex, FBXO36 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-44452119","identifier":"Q8NEA4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NEA4/entry","name":"FBXO36","description":"F-box only protein 36","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-7977","complexName":"SCF E3 ubiquitin ligase complex, FBXO38 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXO38 target proteins include the zinc finger proteins ZXDA/B (P98168/P98169) which are responsible for CENP-B protein stabilization at centromeres.","predictedComplex":false,"interactors":[{"ac":"EBI-2513135","identifier":"Q6PIJ6","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PIJ6/entry","name":"FBXO38","description":"F-box only protein 38","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7978","complexName":"RNA polymerase I selectivity factor 1 complex","organismName":"Homo sapiens; 9606","description":"Triggers pre-initiation complex (PIC) formation through recruitment of RNA polymerase 1 (CPX-2386) at the rDNA promoter by associating with the core promoter of 47S pre-rRNA cooperatively with the nucleolar transcription factor UBTF1 (P17480).","predictedComplex":false,"interactors":[{"ac":"EBI-1560239","identifier":"Q53T94","identifierLink":"https://www.uniprot.org/uniprotkb/Q53T94/entry","name":"TAF1B","description":"TATA box-binding protein-associated factor RNA polymerase I subunit B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31576","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2510647","identifier":"Q15573","identifierLink":"https://www.uniprot.org/uniprotkb/Q15573/entry","name":"TAF1A","description":"TATA box-binding protein-associated factor RNA polymerase I subunit A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32122","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2510659","identifier":"Q15572","identifierLink":"https://www.uniprot.org/uniprotkb/Q15572/entry","name":"TAF1C","description":"TATA box-binding protein-associated factor RNA polymerase I subunit C","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15319","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355371","identifier":"P20226","identifierLink":"https://www.uniprot.org/uniprotkb/P20226/entry","name":"TBP","description":"TATA-box-binding protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10126","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-716128","identifier":"Q9H5J8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H5J8/entry","name":"TAF1D","description":"TATA box-binding protein-associated factor RNA polymerase I subunit D","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14562","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7979","complexName":"SCF E3 ubiquitin ligase complex, FBXO39 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.","predictedComplex":false,"interactors":[{"ac":"EBI-12383478","identifier":"Q8N4B4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N4B4/entry","name":"FBXO39","description":"F-box only protein 39","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10706","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7981","complexName":"SCF E3 ubiquitin ligase complex, FBXO40 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. May play a role in muscle atrophy","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6425769","identifier":"Q9UH90","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UH90/entry","name":"FBXO40","description":"F-box only protein 40","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15933","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6305","complexName":"ATP8B4-CDC50A P4-ATPase complex","organismName":"Homo sapiens; 9606","description":"A membrane pump which actively translocates, or flips, phospholipids across cell membranes from the exoplasmic to the cytoplasmic leaflet of the lipid bilayer. This generates and maintains membrane lipid asymmetry, a property essential for a wide variety of cellular processes such as vesicle budding and intracellular vesicle trafficking. Transport is accomplished by cyclic changes between two main enzyme conformations, during which the ATP8B4 ATPase is phosphorylated by ATP at a conserved aspartate residue (Asp-392) and subsequently dephosphorylated. CDC50 proteins are required for transport of P4‐ATPases from the endoplasmic reticulum to their final destinations and may also affect the catalytic cycle of the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-2836942","identifier":"Q9NV96","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NV96/entry","name":"TMEM30A","description":"Cell cycle control protein 50A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10926","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9527207","identifier":"Q8TF62","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TF62/entry","name":"ATP8B4","description":"Probable phospholipid-transporting ATPase IM","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6306","complexName":"ATP8B4-CDC50B P4-ATPase complex","organismName":"Homo sapiens; 9606","description":"A membrane pump which actively translocates, or flips, phospholipids across cell membranes from the exoplasmic to the cytoplasmic leaflet of the lipid bilayer. This generates and maintains membrane lipid asymmetry, a property essential for a wide variety of cellular processes such as vesicle budding and intracellular vesicle trafficking. Transport is accomplished by cyclic changes between two main enzyme conformations, during which the ATP8B4 ATPase is phosphorylated by ATP at a conserved aspartate residue (Asp-392) and subsequently dephosphorylated. CDC50 proteins are required for transport of P4‐ATPases from the endoplasmic reticulum to their final destinations and may also affect the catalytic cycle of the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-9527107","identifier":"Q3MIR4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3MIR4/entry","name":"TMEM30B","description":"Cell cycle control protein 50B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10926","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9527207","identifier":"Q8TF62","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TF62/entry","name":"ATP8B4","description":"Probable phospholipid-transporting ATPase IM","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6307","complexName":"ATP10A-CDC50A P4-ATPase complex","organismName":"Homo sapiens; 9606","description":"A membrane pump which actively translocates, or flips, phospholipids across cell membranes from the exoplasmic to the cytoplasmic leaflet of the lipid bilayer. This generates and maintains membrane lipid asymmetry, a property essential for a wide variety of cellular processes such as vesicle budding and intracellular vesicle trafficking. Transport is accomplished by cyclic changes between two main enzyme conformations, during which the AT10A ATPase is phosphorylated by ATP at a conserved aspartate residue (Asp-427) and subsequently dephosphorylated. CDC50 proteins are required for transport of P4‐ATPases from the endoplasmic reticulum to their final destinations and may also affect the catalytic cycle of the complex. Preferentially transports phosphatidylcholine and glucosylceramide in the plasma membrane. Plays a role in determining cell shape and size and cell adhesion.","predictedComplex":false,"interactors":[{"ac":"EBI-26444318","identifier":"O60312","identifierLink":"https://www.uniprot.org/uniprotkb/O60312/entry","name":"ATP10A","description":"Phospholipid-transporting ATPase VA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2836942","identifier":"Q9NV96","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NV96/entry","name":"TMEM30A","description":"Cell cycle control protein 50A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10926","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6308","complexName":"ATP10B-CDC50A P4-ATPase complex","organismName":"Homo sapiens; 9606","description":"A membrane pump which actively translocates, or flips, phospholipids across cell membranes from the exoplasmic to the cytoplasmic leaflet of the lipid bilayer. This generates and maintains membrane lipid asymmetry, a property essential for a wide variety of cellular processes such as vesicle budding and intracellular vesicle trafficking. Transport is accomplished by cyclic changes between two main enzyme conformations, during which the AT10B ATPase is phosphorylated by ATP at a conserved aspartate residue (Asp-433) and subsequently dephosphorylated. CDC50 proteins are required for transport of P4‐ATPases from the endoplasmic reticulum to their final destinations and may also affect the catalytic cycle of the complex. Expressed in the cytosolic membrane leaflet of the late endosome and lysosome membranes and preferentially translocates glucosylceramide and phosphatidylcholine towards the cytosolic membrane leaflet.","predictedComplex":false,"interactors":[{"ac":"EBI-14012818","identifier":"O94823","identifierLink":"https://www.uniprot.org/uniprotkb/O94823/entry","name":"ATP10B","description":"Phospholipid-transporting ATPase VB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2836942","identifier":"Q9NV96","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NV96/entry","name":"TMEM30A","description":"Cell cycle control protein 50A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10926","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6309","complexName":"ATP10D-CDC50A P4-ATPase complex","organismName":"Homo sapiens; 9606","description":"A membrane pump which actively translocates, or flips, phospholipids across cell membranes from the exoplasmic to the cytoplasmic leaflet of the lipid bilayer. This generates and maintains membrane lipid asymmetry, a property essential for a wide variety of cellular processes such as vesicle budding and intracellular vesicle trafficking. Transport is accomplished by cyclic changes between two main enzyme conformations, during which the AT10D ATPase is phosphorylated by ATP at a conserved aspartate residue (Asp-438) and subsequently dephosphorylated. CDC50 proteins are required for transport of P4‐ATPases from the endoplasmic reticulum to their final destinations and may also affect the catalytic cycle of the complex. Preferentially transports glucosylceramide in the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-26444531","identifier":"Q9P241","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P241/entry","name":"ATP10D","description":"Phospholipid-transporting ATPase VD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2836942","identifier":"Q9NV96","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NV96/entry","name":"TMEM30A","description":"Cell cycle control protein 50A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10926","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6310","complexName":"ATP11A-CDC50A P4-ATPase complex","organismName":"Homo sapiens; 9606","description":"A membrane pump which actively translocates, or flips, phospholipids across cell membranes from the exoplasmic to the cytoplasmic leaflet of the lipid bilayer. This generates and maintains membrane lipid asymmetry, a property essential for a wide variety of cellular processes such as vesicle budding and intracellular vesicle trafficking. Transport is accomplished by cyclic changes between two main enzyme conformations, during which the ATP11A ATPase is phosphorylated by ATP at a conserved aspartate residue (Asp-414) and subsequently dephosphorylated. CDC50 proteins are required for transport of P4‐ATPases from the endoplasmic reticulum to their final destinations and may also affect the catalytic cycle of the complex. Preferentially translocates phosphatidylethanolamine and phosphatidylserine in the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-21519640","identifier":"P98196","identifierLink":"https://www.uniprot.org/uniprotkb/P98196/entry","name":"ATP11A","description":"Phospholipid-transporting ATPase IH","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2836942","identifier":"Q9NV96","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NV96/entry","name":"TMEM30A","description":"Cell cycle control protein 50A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10926","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6311","complexName":"ATP11B-CDC50A P4-ATPase complex","organismName":"Homo sapiens; 9606","description":"A membrane pump which actively translocates, or flips, phospholipids across cell membranes from the exoplasmic to the cytoplasmic leaflet of the lipid bilayer. This generates and maintains membrane lipid asymmetry, a property essential for a wide variety of cellular processes such as vesicle budding and intracellular vesicle trafficking. Transport is accomplished by cyclic changes between two main enzyme conformations, during which the ATP11B ATPase is phosphorylated by ATP at a conserved aspartate residue (Asp-407) and subsequently dephosphorylated. CDC50 proteins are required for transport of P4‐ATPases from the endoplasmic reticulum to their final destinations and may also affect the catalytic cycle of the complex. May preferentially translocate phosphatidylethanolamine and phosphatidylserine.","predictedComplex":false,"interactors":[{"ac":"EBI-20857228","identifier":"Q9Y2G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2G3/entry","name":"ATP11B","description":"Phospholipid-transporting ATPase IF","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2836942","identifier":"Q9NV96","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NV96/entry","name":"TMEM30A","description":"Cell cycle control protein 50A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10926","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6312","complexName":"ATP11C-CDC50A P4-ATPase complex","organismName":"Homo sapiens; 9606","description":"A membrane pump which actively translocates, or flips, phospholipids across cell membranes from the exoplasmic to the cytoplasmic leaflet of the lipid bilayer. This generates and maintains membrane lipid asymmetry, a property essential for a wide variety of cellular processes such as vesicle budding and intracellular vesicle trafficking. Transport is accomplished by cyclic changes between two main enzyme conformations, during which the ATP11C ATPase is phosphorylated by ATP at a conserved aspartate residue (Asp-412) and subsequently dephosphorylated. CDC50 proteins are required for transport of P4‐ATPases from the endoplasmic reticulum to their final destinations and may also affect the catalytic cycle of the complex. Preferentially translocates phosphatidylethanolamine and phosphatidylserine in the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-11279131","identifier":"Q8NB49","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NB49/entry","name":"ATP11C","description":"Phospholipid-transporting ATPase IG","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2836942","identifier":"Q9NV96","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NV96/entry","name":"TMEM30A","description":"Cell cycle control protein 50A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10926","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6321","complexName":"CLCN7-OSTM1 chloride channel complex","organismName":"Homo sapiens; 9606","description":"Electrogenic chloride ion/proton antiporter that translocates chloride ions across cell membranes to maintain the membrane potential, regulate trans-epithelial chloride transport, and control intravesicular pH. Displays slow voltage-dependent activation and deactivation in comparison to other chloride channels, resulting in strongly outwardly rectifying currents. Mainly present in lysosomes and osteoclast ruffled membranes.","predictedComplex":false,"interactors":[{"ac":"EBI-11037160","identifier":"Q86WC4","identifierLink":"https://www.uniprot.org/uniprotkb/Q86WC4/entry","name":"OSTM1","description":"Osteopetrosis-associated transmembrane protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4402346","identifier":"P51798","identifierLink":"https://www.uniprot.org/uniprotkb/P51798/entry","name":"CLCN7","description":"H(+)/Cl(-) exchange transporter 7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11689","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5223","complexName":"40S cytosolic small ribosomal subunit","organismName":"Homo sapiens; 9606","description":"Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). 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9606","xrefs":[{"identifier":"PTHR11710","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-354515","identifier":"P62847","identifierLink":"https://www.uniprot.org/uniprotkb/P62847/entry","name":"RPS24","description":"Small ribosomal subunit protein eS24","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10496","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-354542","identifier":"P25398","identifierLink":"https://www.uniprot.org/uniprotkb/P25398/entry","name":"RPS12","description":"Small ribosomal subunit protein eS12","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11843","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356625","identifier":"P62753","identifierLink":"https://www.uniprot.org/uniprotkb/P62753/entry","name":"RPS6","description":"Small ribosomal subunit protein eS6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11502","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357375","identifier":"P62979","identifierLink":"https://www.uniprot.org/uniprotkb/P62979/entry","name":"RPS27A","description":"Ubiquitin-ribosomal protein eS31 fusion protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10666","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358093","identifier":"P62861","identifierLink":"https://www.uniprot.org/uniprotkb/P62861/entry","name":"FAU","description":"Ubiquitin-like FUBI-ribosomal protein eS30 fusion protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10666","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358255","identifier":"P08708","identifierLink":"https://www.uniprot.org/uniprotkb/P08708/entry","name":"RPS17","description":"Small ribosomal subunit protein eS17","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 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The assembly factor TIMMDC1 (Q9NPL8) has also been identified in association with the MCIA complex and stalled complex I intermediates.","predictedComplex":false,"interactors":[{"ac":"EBI-2510719","identifier":"Q9H845","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H845/entry","name":"ACAD9","description":"Complex I assembly factor ACAD9, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2800657","identifier":"Q8IUX1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IUX1/entry","name":"TMEM126B","description":"Complex I assembly factor TMEM126B, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16296","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6570735","identifier":"Q9GZY4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9GZY4/entry","name":"COA1","description":"Cytochrome c oxidase assembly factor 1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47148","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712452","identifier":"Q9BQ95","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BQ95/entry","name":"ECSIT","description":"Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13113","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-741874","identifier":"Q9Y375","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y375/entry","name":"NDUFAF1","description":"Complex I intermediate-associated protein 30, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13194","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9089409","identifier":"Q96B77","identifierLink":"https://www.uniprot.org/uniprotkb/Q96B77/entry","name":"TMEM186","description":"Transmembrane protein 186","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13603","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6341","complexName":"Molybdopterin synthase complex","organismName":"Homo sapiens; 9606","description":"Involved in molybdopterin cofactor (Moco) biosynthesis under anaerobic conditions converting molybdopterin precursor Z (CHEBI:52994) to molybdopterin (CHEBI:44074). This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group.","predictedComplex":false,"interactors":[{"ac":"EBI-723640","identifier":"O96007","identifierLink":"https://www.uniprot.org/uniprotkb/O96007/entry","name":"MOCS2","description":"Molybdopterin synthase catalytic subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23404","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9056334","identifier":"O96033","identifierLink":"https://www.uniprot.org/uniprotkb/O96033/entry","name":"MOCS2","description":"Molybdopterin synthase sulfur carrier subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6362","complexName":"SWI/SNF chromatin remodelling complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"An ATP-dependent chromatin remodelling complex which disrupts the nucleosome structure, increases the binding of transcription factors to nucleosomes, mobilizes histone octamers along DNA in cis, transfers histone octamers to different DNA fragments, displaces histone H2A/H2B dimers and generates superhelical torsion in DNA. Binds preferentially to four-way DNA and promotes resection initiation at a DNA double-strand break. 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The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-1170906","identifier":"P15336","identifierLink":"https://www.uniprot.org/uniprotkb/P15336/entry","name":"ATF2","description":"Cyclic AMP-dependent transcription factor ATF-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712767","identifier":"P18847","identifierLink":"https://www.uniprot.org/uniprotkb/P18847/entry","name":"ATF3","description":"Cyclic AMP-dependent transcription factor ATF-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6408","complexName":"bZIP transcription factor complex, ATF2-ATF4","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-1170906","identifier":"P15336","identifierLink":"https://www.uniprot.org/uniprotkb/P15336/entry","name":"ATF2","description":"Cyclic AMP-dependent transcription factor ATF-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-492498","identifier":"P18848","identifierLink":"https://www.uniprot.org/uniprotkb/P18848/entry","name":"ATF4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6409","complexName":"bZIP transcription factor complex, ATF2-ATF7","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-1170906","identifier":"P15336","identifierLink":"https://www.uniprot.org/uniprotkb/P15336/entry","name":"ATF2","description":"Cyclic AMP-dependent transcription factor ATF-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-765623","identifier":"P17544","identifierLink":"https://www.uniprot.org/uniprotkb/P17544/entry","name":"ATF7","description":"Cyclic AMP-dependent transcription factor ATF-7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6411","complexName":"tRNA-splicing ligase complex","organismName":"Homo sapiens; 9606","description":"tRNA ligase required for  tRNA splicing, thus regulating tRNA maturation. Joins the resulting exon halves once introns have been removed from pre-tRNAs, acting upon the 2',3' cyclic phosphate of the 5' exon to ligate the second exon  This complex, or a sub-complex of it, may also shuttle between the nucleus and the cytoplasm.","predictedComplex":false,"interactors":[{"ac":"EBI-1043130","identifier":"Q52LJ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q52LJ0/entry","name":"FAM98B","description":"Protein FAM98B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1104547","identifier":"Q9Y224","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y224/entry","name":"RTRAF","description":"RNA transcription, translation and transport factor protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15924","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1210765","identifier":"Q8NCA5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NCA5/entry","name":"FAM98A","description":"Protein FAM98A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2107208","identifier":"Q9Y3I0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3I0/entry","name":"RTCB","description":"RNA-splicing ligase RtcB homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11118","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2808825","identifier":"Q8IWT0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IWT0/entry","name":"ZBTB8OS","description":"Protein archease","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12682","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358474","identifier":"Q92499","identifierLink":"https://www.uniprot.org/uniprotkb/Q92499/entry","name":"DDX1","description":"ATP-dependent RNA helicase DDX1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5458641","identifier":"Q9BVC5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BVC5/entry","name":"C2orf49","description":"Ashwin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28359","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6412","complexName":"bZIP transcription factor complex, ATF2-BACH1","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-1170906","identifier":"P15336","identifierLink":"https://www.uniprot.org/uniprotkb/P15336/entry","name":"ATF2","description":"Cyclic AMP-dependent transcription factor ATF-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1263541","identifier":"O14867","identifierLink":"https://www.uniprot.org/uniprotkb/O14867/entry","name":"BACH1","description":"Transcription regulator protein BACH1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6413","complexName":"bZIP transcription factor complex, ATF2-BATF","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-1170906","identifier":"P15336","identifierLink":"https://www.uniprot.org/uniprotkb/P15336/entry","name":"ATF2","description":"Cyclic AMP-dependent transcription factor ATF-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749503","identifier":"Q16520","identifierLink":"https://www.uniprot.org/uniprotkb/Q16520/entry","name":"BATF","description":"Basic leucine zipper transcriptional factor ATF-like","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6414","complexName":"bZIP transcription factor complex, ATF2-BATF3","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-10312707","identifier":"Q9NR55","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NR55/entry","name":"BATF3","description":"Basic leucine zipper transcriptional factor ATF-like 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1170906","identifier":"P15336","identifierLink":"https://www.uniprot.org/uniprotkb/P15336/entry","name":"ATF2","description":"Cyclic AMP-dependent transcription factor ATF-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6415","complexName":"bZIP transcription factor complex, ATF2-DDIT3","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-1170906","identifier":"P15336","identifierLink":"https://www.uniprot.org/uniprotkb/P15336/entry","name":"ATF2","description":"Cyclic AMP-dependent transcription factor ATF-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742651","identifier":"P35638","identifierLink":"https://www.uniprot.org/uniprotkb/P35638/entry","name":"DDIT3","description":"DNA damage-inducible transcript 3 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16833","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6416","complexName":"bZIP transcription factor complex, ATF2-FOS","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-1170906","identifier":"P15336","identifierLink":"https://www.uniprot.org/uniprotkb/P15336/entry","name":"ATF2","description":"Cyclic AMP-dependent transcription factor ATF-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-852851","identifier":"P01100","identifierLink":"https://www.uniprot.org/uniprotkb/P01100/entry","name":"FOS","description":"Protein c-Fos","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6417","complexName":"bZIP transcription factor complex, ATF2-FOSL1","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-1170906","identifier":"P15336","identifierLink":"https://www.uniprot.org/uniprotkb/P15336/entry","name":"ATF2","description":"Cyclic AMP-dependent transcription factor ATF-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744510","identifier":"P15407","identifierLink":"https://www.uniprot.org/uniprotkb/P15407/entry","name":"FOSL1","description":"Fos-related antigen 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6418","complexName":"bZIP transcription factor complex, ATF2-FOSL2","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-1170906","identifier":"P15336","identifierLink":"https://www.uniprot.org/uniprotkb/P15336/entry","name":"ATF2","description":"Cyclic AMP-dependent transcription factor ATF-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3893419","identifier":"P15408","identifierLink":"https://www.uniprot.org/uniprotkb/P15408/entry","name":"FOSL2","description":"Fos-related antigen 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6419","complexName":"bZIP transcription factor complex, ATF2-JDP2","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-1170906","identifier":"P15336","identifierLink":"https://www.uniprot.org/uniprotkb/P15336/entry","name":"ATF2","description":"Cyclic AMP-dependent transcription factor ATF-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1248415","identifier":"Q8WYK2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WYK2/entry","name":"JDP2","description":"Jun dimerization protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6420","complexName":"bZIP transcription factor complex, ATF2-JUN","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-1170906","identifier":"P15336","identifierLink":"https://www.uniprot.org/uniprotkb/P15336/entry","name":"ATF2","description":"Cyclic AMP-dependent transcription factor ATF-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-852823","identifier":"P05412","identifierLink":"https://www.uniprot.org/uniprotkb/P05412/entry","name":"JUN","description":"Transcription factor Jun","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6421","complexName":"bZIP transcription factor complex, ATF2-JUNB","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-1170906","identifier":"P15336","identifierLink":"https://www.uniprot.org/uniprotkb/P15336/entry","name":"ATF2","description":"Cyclic AMP-dependent transcription factor ATF-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-748062","identifier":"P17275","identifierLink":"https://www.uniprot.org/uniprotkb/P17275/entry","name":"JUNB","description":"Transcription factor JunB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6422","complexName":"bZIP transcription factor complex, ATF2-JUND","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-1170906","identifier":"P15336","identifierLink":"https://www.uniprot.org/uniprotkb/P15336/entry","name":"ATF2","description":"Cyclic AMP-dependent transcription factor ATF-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2682803","identifier":"P17535","identifierLink":"https://www.uniprot.org/uniprotkb/P17535/entry","name":"JUND","description":"Transcription factor JunD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6423","complexName":"Trehalose-6-phosphate synthase/phosphatase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Catalyzes the production of trehalose from glucose-6-phosphate and UDP-glucose in a two step process. The Tps1 subunit is a trehalose-6-phosphate synthase (TPS) and catalyses the production of alpha,alpha-trehalose 6-phosphate from UDP-glucose and D-glucose 6-phosphate. Tpp1 acts as a trehalose-6-phosphate phosphatase (TPP) to release trehalose as a final product. The role of ntp1 in the  complex is unclear. Depending on the subunit stoichiometries it is either neutral or gives the complex neutral trehalase activity, converting trehalose to glucose.","predictedComplex":false,"interactors":[{"ac":"EBI-26616855","identifier":"O42893","identifierLink":"https://www.uniprot.org/uniprotkb/O42893/entry","name":"ntp1","description":"Cytosolic neutral trehalase","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23403","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26616873","identifier":"P40387","identifierLink":"https://www.uniprot.org/uniprotkb/P40387/entry","name":"tps1","description":"Alpha,alpha-trehalose-phosphate synthase [UDP-forming]","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10788","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26616958","identifier":"P78875","identifierLink":"https://www.uniprot.org/uniprotkb/P78875/entry","name":"tpp1","description":"Trehalose-phosphatase","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10788","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6442","complexName":"SARS-CoV-2 replication and transcription complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","description":"Replication and transcription complex (RTC) of the SARS-CoV-2 coronavirus which consists of the polymerase complex (CPX-5742) and 2 helicase molecules (nsp13). Although coronavirus nsp13s have been proposed to unwind RNA in the 5' to 3' direction, the 5' extension of template RNA is fed into the active site of SARS-CoV-2 nsp13 in the 3' to 5' direction. RNA polymerase has been known to possess a “backtrack” feature, in which the productive elongation and translocation complexes are in the same conformation to facilitate reversible backward motion during RNA synthesis. The SARS-CoV-2 RTC structure suggests it has the same function here. \r\n\r\nThe nsp12 nucleotidyltransferase (NiRAN) domain possesses guanylyltransferase activity, catalyzing the formation of the cap core structure (GpppA) on the nascent mRNA. ADP-Mg2+ binds in the catalytic site of this domain.","predictedComplex":false,"interactors":[{"ac":"EBI-25475871","identifier":"P0DTD1-PRO_0000449625","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTD1-PRO_0000449625/entry","name":"rep","description":"Non-structural protein 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]},{"ac":"EBI-25475874","identifier":"P0DTD1-PRO_0000449626","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTD1-PRO_0000449626/entry","name":"rep","description":"Non-structural protein 8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]},{"ac":"EBI-25475885","identifier":"P0DTD1-PRO_0000449629","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTD1-PRO_0000449629/entry","name":"rep","description":"RNA-directed RNA polymerase nsp12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]},{"ac":"EBI-25475888","identifier":"P0DTD1-PRO_0000449630","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTD1-PRO_0000449630/entry","name":"rep","description":"Helicase nsp13","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]}]},{"complexAC":"CPX-6461","complexName":"RFX gene regulatory complex","organismName":"Homo sapiens; 9606","description":"Regulates the transcription of major histocompatibility complex class II (MHC II) molecules, nucleating the assembly of cell-specific multi-protein complexes on the MHC II promoters. Specifically recognizes and binds to the X-box regulatory element present at the enhancer region of MHC II genes.","predictedComplex":false,"interactors":[{"ac":"EBI-1057665","identifier":"O14593","identifierLink":"https://www.uniprot.org/uniprotkb/O14593/entry","name":"RFXANK","description":"DNA-binding protein RFXANK","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24124","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3929296","identifier":"O00287","identifierLink":"https://www.uniprot.org/uniprotkb/O00287/entry","name":"RFXAP","description":"Regulatory factor X-associated protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15110","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-923266","identifier":"P48382","identifierLink":"https://www.uniprot.org/uniprotkb/P48382/entry","name":"RFX5","description":"DNA-binding protein RFX5","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6462","complexName":"SARS-CoV replication and transcription complex","organismName":"Severe acute respiratory syndrome coronavirus; 694009","description":"Replication and transcription complex (RTC) of the SARS-CoV coronavirus which consists of the polymerase complex (CPX-5717) and 2 helicase molecules (nsp13). Although coronavirus nsp13s have been proposed to unwind RNA in the 5' to 3' direction, the 5' extension of template RNA is fed into the active site of SARS-CoV-2 nsp13 in the 3' to 5' direction. RNA polymerase has been known to possess a 'backtrack' feature, in which the productive elongation and translocation complexes are in the same conformation to facilitate reversible backward motion during RNA synthesis. The SARS-CoV-2 RTC structure suggests it has the same function here. \r\n\r\nThe nsp12 nucleotidyltransferase (NiRAN) domain possesses guanylyltransferase activity, catalyzing the formation of the cap core structure (GpppA) on the nascent mRNA. ADP-Mg2+ binds in the catalytic site of this domain.","predictedComplex":false,"interactors":[{"ac":"EBI-25487672","identifier":"P0C6X7-PRO_0000037314","identifierLink":"https://www.uniprot.org/uniprotkb/P0C6X7-PRO_0000037314/entry","name":"rep","description":"Non-structural protein 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus; 694009","xrefs":[]},{"ac":"EBI-25487684","identifier":"P0C6X7-PRO_0000037318","identifierLink":"https://www.uniprot.org/uniprotkb/P0C6X7-PRO_0000037318/entry","name":"rep","description":"RNA-directed RNA polymerase nsp12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus; 694009","xrefs":[]},{"ac":"EBI-25487926","identifier":"P0C6X7-PRO_0000037319","identifierLink":"https://www.uniprot.org/uniprotkb/P0C6X7-PRO_0000037319/entry","name":"rep","description":"Helicase nsp13","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus; 694009","xrefs":[]},{"ac":"EBI-25487941","identifier":"P0C6X7-PRO_0000037315","identifierLink":"https://www.uniprot.org/uniprotkb/P0C6X7-PRO_0000037315/entry","name":"rep","description":"Non-structural protein 8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus; 694009","xrefs":[]}]},{"complexAC":"CPX-6463","complexName":"MERS-CoV replication and transcription complex","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","description":"Replication and transcription complex (RTC) of the MERS-CoV coronavirus which consists of the polymerase complex (CPX-5717) and 2 helicase molecules (nsp13). Although coronavirus nsp13s have been proposed to unwind RNA in the 5' to 3' direction, the 5' extension of template RNA is fed into the active site of SARS-CoV-2 nsp13 in the 3' to 5' direction. RNA polymerase has been known to possess a “backtrack” feature, in which the productive elongation and translocation complexes are in the same conformation to facilitate reversible backward motion during RNA synthesis. The SARS-CoV-2 RTC structure suggests it has the same function here. \r\n\r\nThe nsp12 nucleotidyltransferase (NiRAN) domain possesses guanylyltransferase activity, catalyzing the formation of the cap core structure (GpppA) on the nascent mRNA. ADP-Mg2+ binds in the catalytic site of this domain.","predictedComplex":false,"interactors":[{"ac":"EBI-25592074","identifier":"K9N7C7-PRO_0000422445","identifierLink":"https://www.uniprot.org/uniprotkb/K9N7C7-PRO_0000422445/entry","name":"rep","description":"Non-structural protein 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","xrefs":[]},{"ac":"EBI-25592080","identifier":"K9N7C7-PRO_0000422446","identifierLink":"https://www.uniprot.org/uniprotkb/K9N7C7-PRO_0000422446/entry","name":"rep","description":"Non-structural protein 8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","xrefs":[]},{"ac":"EBI-25592936","identifier":"K9N7C7-PRO_0000422449","identifierLink":"https://www.uniprot.org/uniprotkb/K9N7C7-PRO_0000422449/entry","name":"rep","description":"RNA-directed RNA polymerase nsp12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","xrefs":[]},{"ac":"EBI-26429470","identifier":"K9N7C7-PRO_0000422450","identifierLink":"https://www.uniprot.org/uniprotkb/K9N7C7-PRO_0000422450/entry","name":"rep","description":"Helicase nsp13","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","xrefs":[]}]},{"complexAC":"CPX-6464","complexName":"GET complex","organismName":"Homo sapiens; 9606","description":"Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. GET1 and CAMLG (GET2) act as a membrane receptor for soluble GET3, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol, delivered to it by the BAT3 transmembrane domain recognition complex (CPX-132).","predictedComplex":false,"interactors":[{"ac":"EBI-1748958","identifier":"P49069","identifierLink":"https://www.uniprot.org/uniprotkb/P49069/entry","name":"CAMLG","description":"Guided entry of tail-anchored proteins factor CAMLG","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18908258","identifier":"O00258","identifierLink":"https://www.uniprot.org/uniprotkb/O00258/entry","name":"GET1","description":"Guided entry of tail-anchored proteins factor 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR42650","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2515857","identifier":"O43681","identifierLink":"https://www.uniprot.org/uniprotkb/O43681/entry","name":"GET3","description":"ATPase GET3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10803","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-6465","complexName":"bZIP transcription factor complex, ATF3-ATF3","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The homodimer appears to act as a transcriptional repressor, modulating the immune response, atherogenesis, cell cycle, apoptosis, and glucose homeostasis. ATF3 is an adaptive-response gene, expressed at low levels in normal and quiescent cells but its expression is increased by cytokines, cell death-inducing agents, and physiological stresses. The ATF3 gene also includes a number of isoforms lacking the bzip domain, expression of which antagonize the transcriptional activity of ATF3.","predictedComplex":false,"interactors":[{"ac":"EBI-712767","identifier":"P18847","identifierLink":"https://www.uniprot.org/uniprotkb/P18847/entry","name":"ATF3","description":"Cyclic AMP-dependent transcription factor ATF-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6466","complexName":"bZIP transcription factor complex, ATF3-ATF7","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-712767","identifier":"P18847","identifierLink":"https://www.uniprot.org/uniprotkb/P18847/entry","name":"ATF3","description":"Cyclic AMP-dependent transcription factor ATF-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-765623","identifier":"P17544","identifierLink":"https://www.uniprot.org/uniprotkb/P17544/entry","name":"ATF7","description":"Cyclic AMP-dependent transcription factor ATF-7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6467","complexName":"bZIP transcription factor complex, ATF3-BATF","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-712767","identifier":"P18847","identifierLink":"https://www.uniprot.org/uniprotkb/P18847/entry","name":"ATF3","description":"Cyclic AMP-dependent transcription factor ATF-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749503","identifier":"Q16520","identifierLink":"https://www.uniprot.org/uniprotkb/Q16520/entry","name":"BATF","description":"Basic leucine zipper transcriptional factor ATF-like","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6468","complexName":"bZIP transcription factor complex, ATF3-BATF3","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-10312707","identifier":"Q9NR55","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NR55/entry","name":"BATF3","description":"Basic leucine zipper transcriptional factor ATF-like 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712767","identifier":"P18847","identifierLink":"https://www.uniprot.org/uniprotkb/P18847/entry","name":"ATF3","description":"Cyclic AMP-dependent transcription factor ATF-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6469","complexName":"bZIP transcription factor complex, ATF3-CEBPA","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-1172054","identifier":"P49715","identifierLink":"https://www.uniprot.org/uniprotkb/P49715/entry","name":"CEBPA","description":"CCAAT/enhancer-binding protein alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712767","identifier":"P18847","identifierLink":"https://www.uniprot.org/uniprotkb/P18847/entry","name":"ATF3","description":"Cyclic AMP-dependent transcription factor ATF-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6470","complexName":"bZIP transcription factor complex, ATF3-CEBPB","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-712767","identifier":"P18847","identifierLink":"https://www.uniprot.org/uniprotkb/P18847/entry","name":"ATF3","description":"Cyclic AMP-dependent transcription factor ATF-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-969696","identifier":"P17676","identifierLink":"https://www.uniprot.org/uniprotkb/P17676/entry","name":"CEBPB","description":"CCAAT/enhancer-binding protein beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6471","complexName":"bZIP transcription factor complex, ATF3-CEBPG","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-712767","identifier":"P18847","identifierLink":"https://www.uniprot.org/uniprotkb/P18847/entry","name":"ATF3","description":"Cyclic AMP-dependent transcription factor ATF-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-969696","identifier":"P17676","identifierLink":"https://www.uniprot.org/uniprotkb/P17676/entry","name":"CEBPB","description":"CCAAT/enhancer-binding protein beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6472","complexName":"bZIP transcription factor complex, ATF3-CEBPE","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-3907048","identifier":"Q15744","identifierLink":"https://www.uniprot.org/uniprotkb/Q15744/entry","name":"CEBPE","description":"CCAAT/enhancer-binding protein epsilon","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712767","identifier":"P18847","identifierLink":"https://www.uniprot.org/uniprotkb/P18847/entry","name":"ATF3","description":"Cyclic AMP-dependent transcription factor ATF-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6473","complexName":"bZIP transcription factor complex, ATF3-DDIT3","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site. Formation of this heterodimer prevents the ATF3 homodimer (CPX-6465) from binding to the ATF/cyclicAMP response element consensus site and thus overcomes its transcription repression activity.","predictedComplex":false,"interactors":[{"ac":"EBI-712767","identifier":"P18847","identifierLink":"https://www.uniprot.org/uniprotkb/P18847/entry","name":"ATF3","description":"Cyclic AMP-dependent transcription factor ATF-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742651","identifier":"P35638","identifierLink":"https://www.uniprot.org/uniprotkb/P35638/entry","name":"DDIT3","description":"DNA damage-inducible transcript 3 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16833","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6474","complexName":"bZIP transcription factor complex, ATF3-JUN","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-712767","identifier":"P18847","identifierLink":"https://www.uniprot.org/uniprotkb/P18847/entry","name":"ATF3","description":"Cyclic AMP-dependent transcription factor ATF-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-852823","identifier":"P05412","identifierLink":"https://www.uniprot.org/uniprotkb/P05412/entry","name":"JUN","description":"Transcription factor Jun","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6476","complexName":"bZIP transcription factor complex, ATF3-JUNB","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-712767","identifier":"P18847","identifierLink":"https://www.uniprot.org/uniprotkb/P18847/entry","name":"ATF3","description":"Cyclic AMP-dependent transcription factor ATF-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-748062","identifier":"P17275","identifierLink":"https://www.uniprot.org/uniprotkb/P17275/entry","name":"JUNB","description":"Transcription factor JunB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6477","complexName":"bZIP transcription factor complex, ATF3-FOS","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-712767","identifier":"P18847","identifierLink":"https://www.uniprot.org/uniprotkb/P18847/entry","name":"ATF3","description":"Cyclic AMP-dependent transcription factor ATF-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-852851","identifier":"P01100","identifierLink":"https://www.uniprot.org/uniprotkb/P01100/entry","name":"FOS","description":"Protein c-Fos","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6478","complexName":"bZIP transcription factor complex, ATF3-FOSL1","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-712767","identifier":"P18847","identifierLink":"https://www.uniprot.org/uniprotkb/P18847/entry","name":"ATF3","description":"Cyclic AMP-dependent transcription factor ATF-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744510","identifier":"P15407","identifierLink":"https://www.uniprot.org/uniprotkb/P15407/entry","name":"FOSL1","description":"Fos-related antigen 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6479","complexName":"bZIP transcription factor complex, ATF3-FOSL2","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-3893419","identifier":"P15408","identifierLink":"https://www.uniprot.org/uniprotkb/P15408/entry","name":"FOSL2","description":"Fos-related antigen 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712767","identifier":"P18847","identifierLink":"https://www.uniprot.org/uniprotkb/P18847/entry","name":"ATF3","description":"Cyclic AMP-dependent transcription factor ATF-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6480","complexName":"bZIP transcription factor complex, ATF3-MAFF","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-712767","identifier":"P18847","identifierLink":"https://www.uniprot.org/uniprotkb/P18847/entry","name":"ATF3","description":"Cyclic AMP-dependent transcription factor ATF-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-721128","identifier":"Q9ULX9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ULX9/entry","name":"MAFF","description":"Transcription factor MafF","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6481","complexName":"bZIP transcription factor complex, ATF3-MAFG","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-712767","identifier":"P18847","identifierLink":"https://www.uniprot.org/uniprotkb/P18847/entry","name":"ATF3","description":"Cyclic AMP-dependent transcription factor ATF-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-713514","identifier":"O15525","identifierLink":"https://www.uniprot.org/uniprotkb/O15525/entry","name":"MAFG","description":"Transcription factor MafG","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2140","complexName":"iscS-thiI sulfurtransferase complex","organismName":"Escherichia coli (strain K12); 83333","description":"tRNA sulfurtransferase which catalyzes the ATP-dependent transfer of a persulfide sulfur formed at the active site of iscS to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein thiS, forming thiS-thiocarboxylate, a step in the synthesis of thiazole, in the thiamine biosynthesis pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-1114380","identifier":"P77718","identifierLink":"https://www.uniprot.org/uniprotkb/P77718/entry","name":"thiI","description":"tRNA sulfurtransferase","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43209","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-550055","identifier":"P0A6B7","identifierLink":"https://www.uniprot.org/uniprotkb/P0A6B7/entry","name":"iscS","description":"Cysteine desulfurase IscS","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11601","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8852014","identifier":"CHEBI:597326","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:597326","name":"pyridoxal 5'-phosphate(2-)","description":"pyridoxal 5'-phosphate(2-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-6482","complexName":"Alpha-beta T cell receptor complex, TRBC2 variant","organismName":"Homo sapiens; 9606","description":"Antigen-specific receptor on the cell surface of T lymphocytes essential to the immune response. Recognises peptide-major histocompatibility complexes (pMHC) that are displayed by antigen presenting cells, a prerequisite for efficient T cell adaptive immunity against pathogens. Each TCR possesses unique antigen specificity, determined by the antigen binding site created by the variable regions of the alpha and beta subunits (TRAC, TRBC2). Binding of alpha-beta subunits to the antigen bound to MHC initiates TCR clustering on the cell surface. Downstream signalling is activate by LCK (P06239) which phosphorylates the cytoplasmic immunoreceptor tyrosine-based activation motifs (ITAMs) of subunits CD3G, CD3D, CD3E and CD247. As antigens only bind to the extracellular domains of the alpha and beta subunits and they do not possess ITAMs the TCR-pMHC-binding information is probably relayed via the ITAMs of the cytoplasmic tails of the CD3 subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-1034847","identifier":"P01848","identifierLink":"https://www.uniprot.org/uniprotkb/P01848/entry","name":"TRAC","description":"T cell receptor alpha chain constant","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19433","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1165705","identifier":"P20963","identifierLink":"https://www.uniprot.org/uniprotkb/P20963/entry","name":"CD247","description":"T-cell surface glycoprotein CD3 zeta chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10035","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1211297","identifier":"P07766","identifierLink":"https://www.uniprot.org/uniprotkb/P07766/entry","name":"CD3E","description":"T-cell surface glycoprotein CD3 epsilon chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10570","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3862416","identifier":"P04234","identifierLink":"https://www.uniprot.org/uniprotkb/P04234/entry","name":"CD3D","description":"T-cell surface glycoprotein CD3 delta chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10570","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3862428","identifier":"P09693","identifierLink":"https://www.uniprot.org/uniprotkb/P09693/entry","name":"CD3G","description":"T-cell surface glycoprotein CD3 gamma chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10570","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9010220","identifier":"A0A5B9","identifierLink":"https://www.uniprot.org/uniprotkb/A0A5B9/entry","name":"TRBC2","description":"T cell receptor beta constant 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6502","complexName":"Glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex","organismName":"Homo sapiens; 9606","description":"Monoglycosyltransferase complex that catalyses the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to the 6-position of phosphatidylinositol, the first, and committed, step of glycosylphosphatidylinositol (GPI) biosynthesis. GPI is a complex glycolipid with a core structure, phosphoethanolamine-6-mannose-alpha1,2-mannose-alpha1,6-mannose-alpha1,4-glucosamine-alpha1,6-inositol-phospholipid that functions as a membrane anchor for many cell surface proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-17630288","identifier":"P57054","identifierLink":"https://www.uniprot.org/uniprotkb/P57054/entry","name":"PIGP","description":"Phosphatidylinositol N-acetylglucosaminyltransferase subunit P","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2339260","identifier":"Q9BRB3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BRB3/entry","name":"PIGQ","description":"Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21329","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26643054","identifier":"P37287","identifierLink":"https://www.uniprot.org/uniprotkb/P37287/entry","name":"PIGA","description":"Phosphatidylinositol N-acetylglucosaminyltransferase subunit A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45871","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2803676","identifier":"Q14442","identifierLink":"https://www.uniprot.org/uniprotkb/Q14442/entry","name":"PIGH","description":"Phosphatidylinositol N-acetylglucosaminyltransferase subunit H","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15231","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3920125","identifier":"Q3MUY2","identifierLink":"https://www.uniprot.org/uniprotkb/Q3MUY2/entry","name":"PIGY","description":"Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR39235","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-721918","identifier":"Q92535","identifierLink":"https://www.uniprot.org/uniprotkb/Q92535/entry","name":"PIGC","description":"Phosphatidylinositol N-acetylglucosaminyltransferase subunit C","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12982","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9097061","identifier":"O94777","identifierLink":"https://www.uniprot.org/uniprotkb/O94777/entry","name":"DPM2","description":"Dolichol phosphate-mannose biosynthesis regulatory protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15039","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6503","complexName":"GPI-anchor transamidase complex","organismName":"Homo sapiens; 9606","description":"Transamidase enzyme complex that transfers the glycosylphosphatidylinositol (GPI) lipid to the newly made GPI protein in the endoplasmic reticulum, replacing the C-terminal GPI attachment signal peptide of a protein with the lipid. GPI is a complex glycolipid with a core structure (phosphoethanolamine-6-mannose-alpha1,2-mannose-alpha1,6-mannose-alpha1,4-glucosamine-alpha1,6-inositol-phospholipid) that functions as a membrane anchor for many cell surface proteins. The complex cleaves the GPI attachment signal peptide between the omega and omega + 1 amino acids, generating a substrate-enzyme intermediate linked by a thioester bond between the omega amino acid carboxyl group and a catalytic cysteine side chain of the enzyme. The thioester bond is attacked by an amino group of the terminal ethanolamine of GPI, completing the transfer of GPI by transamidation","predictedComplex":false,"interactors":[{"ac":"EBI-11290294","identifier":"Q9H490","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H490/entry","name":"PIGU","description":"GPI-anchor transamidase component PIGU","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13121","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2908273","identifier":"Q96S52","identifierLink":"https://www.uniprot.org/uniprotkb/Q96S52/entry","name":"PIGS","description":"GPI-anchor transamidase component PIGS","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21072","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-720225","identifier":"O43292","identifierLink":"https://www.uniprot.org/uniprotkb/O43292/entry","name":"GPAA1","description":"GPI-anchor transamidase component GPAA1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-726383","identifier":"Q969N2","identifierLink":"https://www.uniprot.org/uniprotkb/Q969N2/entry","name":"PIGT","description":"GPI-anchor transamidase component PIGT","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12959","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8617711","identifier":"Q92643","identifierLink":"https://www.uniprot.org/uniprotkb/Q92643/entry","name":"PIGK","description":"GPI-anchor transamidase","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6521","complexName":"bZIP transcription factor complex, ATF4-ATF4","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. \r\n\r\nATF4 coordinates the general retrograde response to stress, acting downstream of the integrated stress response signaling pathways to decrease global translation.","predictedComplex":false,"interactors":[{"ac":"EBI-492498","identifier":"P18848","identifierLink":"https://www.uniprot.org/uniprotkb/P18848/entry","name":"ATF4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6522","complexName":"bZIP transcription factor complex, ATF4-BATF","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.\r\n\r\nATF4 acts both as a regulator of normal cellular processes and also coordinates the general retrograde response to stress, acting downstream of the integrated stress response signaling pathways to decrease global translation.","predictedComplex":false,"interactors":[{"ac":"EBI-492498","identifier":"P18848","identifierLink":"https://www.uniprot.org/uniprotkb/P18848/entry","name":"ATF4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749503","identifier":"Q16520","identifierLink":"https://www.uniprot.org/uniprotkb/Q16520/entry","name":"BATF","description":"Basic leucine zipper transcriptional factor ATF-like","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6523","complexName":"bZIP transcription factor complex, ATF4-BATF2","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.\r\n\r\nATF4 acts both as a regulator of normal cellular processes and also coordinates the general retrograde response to stress, acting downstream of the integrated stress response signaling pathways to decrease global translation.","predictedComplex":false,"interactors":[{"ac":"EBI-492498","identifier":"P18848","identifierLink":"https://www.uniprot.org/uniprotkb/P18848/entry","name":"ATF4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742695","identifier":"Q8N1L9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N1L9/entry","name":"BATF2","description":"Basic leucine zipper transcriptional factor ATF-like 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6524","complexName":"bZIP transcription factor complex, ATF4-BATF3","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.\r\n\r\nATF4 acts both as a regulator of normal cellular processes and also coordinates the general retrograde response to stress, acting downstream of the integrated stress response signaling pathways to decrease global translation.","predictedComplex":false,"interactors":[{"ac":"EBI-10312707","identifier":"Q9NR55","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NR55/entry","name":"BATF3","description":"Basic leucine zipper transcriptional factor ATF-like 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-492498","identifier":"P18848","identifierLink":"https://www.uniprot.org/uniprotkb/P18848/entry","name":"ATF4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6525","complexName":"bZIP transcription factor complex, ATF4-CEBPA","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.\r\n\r\nATF4 acts both as a regulator of normal cellular processes and also coordinates the general retrograde response to stress, acting downstream of the integrated stress response signaling pathways to decrease global translation.","predictedComplex":false,"interactors":[{"ac":"EBI-1172054","identifier":"P49715","identifierLink":"https://www.uniprot.org/uniprotkb/P49715/entry","name":"CEBPA","description":"CCAAT/enhancer-binding protein alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-492498","identifier":"P18848","identifierLink":"https://www.uniprot.org/uniprotkb/P18848/entry","name":"ATF4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6526","complexName":"bZIP transcription factor complex, ATF4-CEBPB","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.\r\n\r\nATF4 acts both as a regulator of normal cellular processes and also coordinates the general retrograde response to stress, acting downstream of the integrated stress response signaling pathways to decrease global translation.","predictedComplex":false,"interactors":[{"ac":"EBI-492498","identifier":"P18848","identifierLink":"https://www.uniprot.org/uniprotkb/P18848/entry","name":"ATF4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-969696","identifier":"P17676","identifierLink":"https://www.uniprot.org/uniprotkb/P17676/entry","name":"CEBPB","description":"CCAAT/enhancer-binding protein beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6527","complexName":"bZIP transcription factor complex, ATF4-CEBPG","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.\r\n\r\nATF4 acts both as a regulator of normal cellular processes and also coordinates the general retrograde response to stress, acting downstream of the integrated stress response signaling pathways to decrease global translation.","predictedComplex":false,"interactors":[{"ac":"EBI-492498","identifier":"P18848","identifierLink":"https://www.uniprot.org/uniprotkb/P18848/entry","name":"ATF4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-740209","identifier":"P53567","identifierLink":"https://www.uniprot.org/uniprotkb/P53567/entry","name":"CEBPG","description":"CCAAT/enhancer-binding protein gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6528","complexName":"bZIP transcription factor complex, ATF4-CEBPD","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.\r\n\r\nATF4 acts both as a regulator of normal cellular processes and also coordinates the general retrograde response to stress, acting downstream of the integrated stress response signaling pathways to decrease global translation.","predictedComplex":false,"interactors":[{"ac":"EBI-492498","identifier":"P18848","identifierLink":"https://www.uniprot.org/uniprotkb/P18848/entry","name":"ATF4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7962058","identifier":"P49716","identifierLink":"https://www.uniprot.org/uniprotkb/P49716/entry","name":"CEBPD","description":"CCAAT/enhancer-binding protein delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6529","complexName":"bZIP transcription factor complex, ATF4-CEBPE","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.\r\n\r\nATF4 acts both as a regulator of normal cellular processes and also coordinates the general retrograde response to stress, acting downstream of the integrated stress response signaling pathways to decrease global translation.","predictedComplex":false,"interactors":[{"ac":"EBI-3907048","identifier":"Q15744","identifierLink":"https://www.uniprot.org/uniprotkb/Q15744/entry","name":"CEBPE","description":"CCAAT/enhancer-binding protein epsilon","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-492498","identifier":"P18848","identifierLink":"https://www.uniprot.org/uniprotkb/P18848/entry","name":"ATF4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6541","complexName":"bZIP transcription factor complex, ATF4-CREB3","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.\r\n\r\nATF4 acts both as a regulator of normal cellular processes and also coordinates the general retrograde response to stress, acting downstream of the integrated stress response signaling pathways to decrease global translation.","predictedComplex":false,"interactors":[{"ac":"EBI-492498","identifier":"P18848","identifierLink":"https://www.uniprot.org/uniprotkb/P18848/entry","name":"ATF4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-625002","identifier":"O43889","identifierLink":"https://www.uniprot.org/uniprotkb/O43889/entry","name":"CREB3","description":"Cyclic AMP-responsive element-binding protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45996","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6542","complexName":"bZIP transcription factor complex, ATF4-CREBZF","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.\r\n\r\nATF4 acts both as a regulator of normal cellular processes and also coordinates the general retrograde response to stress, acting downstream of the integrated stress response signaling pathways to decrease global translation.","predictedComplex":false,"interactors":[{"ac":"EBI-492498","identifier":"P18848","identifierLink":"https://www.uniprot.org/uniprotkb/P18848/entry","name":"ATF4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-632965","identifier":"Q9NS37","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NS37/entry","name":"CREBZF","description":"CREB/ATF bZIP transcription factor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6543","complexName":"bZIP transcription factor complex, ATF4-DDIT3","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.\r\n\r\nATF4 acts both as a regulator of normal cellular processes and also coordinates the general retrograde response to stress, acting downstream of the integrated stress response signaling pathways to decrease global translation.","predictedComplex":false,"interactors":[{"ac":"EBI-492498","identifier":"P18848","identifierLink":"https://www.uniprot.org/uniprotkb/P18848/entry","name":"ATF4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742651","identifier":"P35638","identifierLink":"https://www.uniprot.org/uniprotkb/P35638/entry","name":"DDIT3","description":"DNA damage-inducible transcript 3 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16833","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6562","complexName":"bZIP transcription factor complex, ATF4-JUN","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.\r\n\r\nATF4 acts both as a regulator of normal cellular processes and also coordinates the general retrograde response to stress, acting downstream of the integrated stress response signaling pathways to decrease global translation.","predictedComplex":false,"interactors":[{"ac":"EBI-492498","identifier":"P18848","identifierLink":"https://www.uniprot.org/uniprotkb/P18848/entry","name":"ATF4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-852823","identifier":"P05412","identifierLink":"https://www.uniprot.org/uniprotkb/P05412/entry","name":"JUN","description":"Transcription factor Jun","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6563","complexName":"bZIP transcription factor complex, ATF4-JUNB","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.\r\n\r\nATF4 acts both as a regulator of normal cellular processes and also coordinates the general retrograde response to stress, acting downstream of the integrated stress response signaling pathways to decrease global translation.","predictedComplex":false,"interactors":[{"ac":"EBI-492498","identifier":"P18848","identifierLink":"https://www.uniprot.org/uniprotkb/P18848/entry","name":"ATF4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-748062","identifier":"P17275","identifierLink":"https://www.uniprot.org/uniprotkb/P17275/entry","name":"JUNB","description":"Transcription factor JunB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6564","complexName":"bZIP transcription factor complex, ATF4-FOS","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.\r\n\r\nATF4 acts both as a regulator of normal cellular processes and also coordinates the general retrograde response to stress, acting downstream of the integrated stress response signaling pathways to decrease global translation.","predictedComplex":false,"interactors":[{"ac":"EBI-492498","identifier":"P18848","identifierLink":"https://www.uniprot.org/uniprotkb/P18848/entry","name":"ATF4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-852851","identifier":"P01100","identifierLink":"https://www.uniprot.org/uniprotkb/P01100/entry","name":"FOS","description":"Protein c-Fos","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6565","complexName":"bZIP transcription factor complex, ATF4-FOSL1","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.\r\n\r\nATF4 acts both as a regulator of normal cellular processes and also coordinates the general retrograde response to stress, acting downstream of the integrated stress response signaling pathways to decrease global translation.","predictedComplex":false,"interactors":[{"ac":"EBI-492498","identifier":"P18848","identifierLink":"https://www.uniprot.org/uniprotkb/P18848/entry","name":"ATF4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744510","identifier":"P15407","identifierLink":"https://www.uniprot.org/uniprotkb/P15407/entry","name":"FOSL1","description":"Fos-related antigen 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6566","complexName":"bZIP transcription factor complex, ATF4-MAF","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.\r\n\r\nATF4 acts both as a regulator of normal cellular processes and also coordinates the general retrograde response to stress, acting downstream of the integrated stress response signaling pathways to decrease global translation.","predictedComplex":false,"interactors":[{"ac":"EBI-2805091","identifier":"O75444","identifierLink":"https://www.uniprot.org/uniprotkb/O75444/entry","name":"MAF","description":"Transcription factor Maf","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-492498","identifier":"P18848","identifierLink":"https://www.uniprot.org/uniprotkb/P18848/entry","name":"ATF4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6567","complexName":"bZIP transcription factor complex, ATF4-MAFB","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.\r\n\r\nATF4 acts both as a regulator of normal cellular processes and also coordinates the general retrograde response to stress, acting downstream of the integrated stress response signaling pathways to decrease global translation.","predictedComplex":false,"interactors":[{"ac":"EBI-3649340","identifier":"Q9Y5Q3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5Q3/entry","name":"MAFB","description":"Transcription factor MafB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-492498","identifier":"P18848","identifierLink":"https://www.uniprot.org/uniprotkb/P18848/entry","name":"ATF4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6568","complexName":"bZIP transcription factor complex, ATF4-NFE2","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.\r\n\r\nATF4 acts both as a regulator of normal cellular processes and also coordinates the general retrograde response to stress, acting downstream of the integrated stress response signaling pathways to decrease global translation.","predictedComplex":false,"interactors":[{"ac":"EBI-492498","identifier":"P18848","identifierLink":"https://www.uniprot.org/uniprotkb/P18848/entry","name":"ATF4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-726369","identifier":"Q16621","identifierLink":"https://www.uniprot.org/uniprotkb/Q16621/entry","name":"NFE2","description":"Transcription factor NF-E2 45 kDa subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6569","complexName":"bZIP transcription factor complex, ATF4-NFE2L1","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.\r\n\r\nATF4 acts both as a regulator of normal cellular processes and also coordinates the general retrograde response to stress, acting downstream of the integrated stress response signaling pathways to decrease global translation.","predictedComplex":false,"interactors":[{"ac":"EBI-28952014","identifier":"Q14494-PRO_0000443103","identifierLink":"https://www.uniprot.org/uniprotkb/Q14494-PRO_0000443103/entry","name":"NFE2L1","description":"Transcription factor NRF1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-492498","identifier":"P18848","identifierLink":"https://www.uniprot.org/uniprotkb/P18848/entry","name":"ATF4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6570","complexName":"bZIP transcription factor complex, ATF4-NFE2L2","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.\r\n\r\nATF4 acts both as a regulator of normal cellular processes and also coordinates the general retrograde response to stress, acting downstream of the integrated stress response signaling pathways to decrease global translation.","predictedComplex":false,"interactors":[{"ac":"EBI-2007911","identifier":"Q16236","identifierLink":"https://www.uniprot.org/uniprotkb/Q16236/entry","name":"NFE2L2","description":"Nuclear factor erythroid 2-related factor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-492498","identifier":"P18848","identifierLink":"https://www.uniprot.org/uniprotkb/P18848/entry","name":"ATF4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6572","complexName":"bZIP transcription factor complex, ATF4-NFE2L3","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.\r\n\r\nATF4 acts both as a regulator of normal cellular processes and also coordinates the general retrograde response to stress, acting downstream of the integrated stress response signaling pathways to decrease global translation.","predictedComplex":false,"interactors":[{"ac":"EBI-10890629","identifier":"Q9Y4A8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4A8/entry","name":"NFE2L3","description":"Nuclear factor erythroid 2-related factor 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-492498","identifier":"P18848","identifierLink":"https://www.uniprot.org/uniprotkb/P18848/entry","name":"ATF4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6573","complexName":"L-lactate dehydrogenase A complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the NAD(H)-dependent interconversion of lactate and pyruvate. Mainly expressed in skeletal muscles and preferentially converts pyruvate to lactate.","predictedComplex":false,"interactors":[{"ac":"EBI-372327","identifier":"P00338","identifierLink":"https://www.uniprot.org/uniprotkb/P00338/entry","name":"LDHA","description":"L-lactate dehydrogenase A chain","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43128","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6581","complexName":"Alpha-beta T cell receptor complex, TRBC1 variant","organismName":"Homo sapiens; 9606","description":"Antigen-specific receptor on the cell surface of T lymphocytes essential to the immune response. Recognises peptide-major histocompatibility complexes (pMHC) that are displayed by antigen presenting cells, a prerequisite for efficient T cell adaptive immunity against pathogens. Each TCR possesses unique antigen specificity, determined by the antigen binding site created by the variable regions of the alpha and beta subunits (TRAC, TRBC1). Binding of alpha-beta subunits to the antigen bound to MHC initiates TCR clustering on the cell surface. Downstream signalling is activate by LCK (P06239) which phosphorylates the cytoplasmic immunoreceptor tyrosine-based activation motifs (ITAMs) of subunits CD3G, CD3D, CD3E and CD247. As antigens only bind to the extracellular domains of the alpha and beta subunits and they do not possess ITAMs the TCR-pMHC-binding information is probably relayed via the ITAMs of the cytoplasmic tails of the CD3 subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-1034839","identifier":"P01850","identifierLink":"https://www.uniprot.org/uniprotkb/P01850/entry","name":"TRBC1","description":"T cell receptor beta constant 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1034847","identifier":"P01848","identifierLink":"https://www.uniprot.org/uniprotkb/P01848/entry","name":"TRAC","description":"T cell receptor alpha chain constant","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19433","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1165705","identifier":"P20963","identifierLink":"https://www.uniprot.org/uniprotkb/P20963/entry","name":"CD247","description":"T-cell surface glycoprotein CD3 zeta chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10035","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1211297","identifier":"P07766","identifierLink":"https://www.uniprot.org/uniprotkb/P07766/entry","name":"CD3E","description":"T-cell surface glycoprotein CD3 epsilon chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10570","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3862416","identifier":"P04234","identifierLink":"https://www.uniprot.org/uniprotkb/P04234/entry","name":"CD3D","description":"T-cell surface glycoprotein CD3 delta chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10570","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3862428","identifier":"P09693","identifierLink":"https://www.uniprot.org/uniprotkb/P09693/entry","name":"CD3G","description":"T-cell surface glycoprotein CD3 gamma chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10570","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6582","complexName":"Gamma-delta T cell receptor complex, TRGC1 variant","organismName":"Homo sapiens; 9606","description":"Antigen-specific receptor on the cell surface of T lymphocytes essential to the immune response. While alpha-beta TCR (CPX-6482, CPX-6581) expressing T cells are more commonly found in peripheral blood, gamma-delta TCR-expressing T cells constitute the major subset of resident T cells in tissues bordering the external environment such as the dermis, the intestine, the lung and the uterus. \r\n\r\nGamma-delta TCRs do not absolutely require classic antigen priming and clonal expansion in the thymus and appear to recognise microorganism-derived proteins and self-proteins (such as heat-shock proteins) without a requirement for antigen pre-processing or major-histocompatibility-complex (MHC) presentation of peptide epitopes. Some gamma-delta T-cell receptors recognise MHC class Ib molecules or structurally diverse and biologically unrelated compounds such as lipopeptides on cell surfaces. \r\n\r\nActivated cells produce cytokines (IFN-gamma, TNF-alpha, IL-17) and chemokines (RANTES, IP-10, lymphotactin), contributing to a rapid, innate-like immune response to a broad spectrum of pathogens during the initiation phase of the immune response. This rapid response bridges the transition from the innate to adaptive immune response. \r\n\r\nEach TCR possesses unique antigen specificity, determined by the antigen binding site created by the variable regions of the gamma and delta subunits (TRGC1, TRDC). Downstream signalling is activate by LCK (P06239) and FYN (P06241) kinases which phosphorylate the cytoplasmic immunoreceptor tyrosine-based activation motifs (ITAMs) of subunits CD3G, CD3E and CD247. As antigens only bind to the extracellular domains of the gamma and delta subunits and they do not possess ITAMs, information is probably relayed via the ITAMs of the cytoplasmic tails of the CD3 subunits. Gamma-delta TCRs appear to be more efficient in signalling than alpha-beta TCRs. \r\n\r\nThis rapid and un-primed response by T cells expressing gamma-delta TCRs and IL-17 can also induce inflammatory diseases, autoimmunity (in particular psoriasis), and metastasis.","predictedComplex":false,"interactors":[{"ac":"EBI-1165705","identifier":"P20963","identifierLink":"https://www.uniprot.org/uniprotkb/P20963/entry","name":"CD247","description":"T-cell surface glycoprotein CD3 zeta chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10035","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1211297","identifier":"P07766","identifierLink":"https://www.uniprot.org/uniprotkb/P07766/entry","name":"CD3E","description":"T-cell surface glycoprotein CD3 epsilon chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10570","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26902226","identifier":"P0CF51","identifierLink":"https://www.uniprot.org/uniprotkb/P0CF51/entry","name":"TRGC1","description":"T cell receptor gamma constant 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-26902242","identifier":"B7Z8K6","identifierLink":"https://www.uniprot.org/uniprotkb/B7Z8K6/entry","name":"TRDC","description":"T cell receptor delta constant","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-3862428","identifier":"P09693","identifierLink":"https://www.uniprot.org/uniprotkb/P09693/entry","name":"CD3G","description":"T-cell surface glycoprotein CD3 gamma chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10570","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6585","complexName":"bZIP transcription factor complex, ATF5-BATF","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-492509","identifier":"Q9Y2D1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2D1/entry","name":"ATF5","description":"Cyclic AMP-dependent transcription factor ATF-5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749503","identifier":"Q16520","identifierLink":"https://www.uniprot.org/uniprotkb/Q16520/entry","name":"BATF","description":"Basic leucine zipper transcriptional factor ATF-like","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6586","complexName":"bZIP transcription factor complex, ATF5-CEBPA","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-1172054","identifier":"P49715","identifierLink":"https://www.uniprot.org/uniprotkb/P49715/entry","name":"CEBPA","description":"CCAAT/enhancer-binding protein alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-492509","identifier":"Q9Y2D1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2D1/entry","name":"ATF5","description":"Cyclic AMP-dependent transcription factor ATF-5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6588","complexName":"bZIP transcription factor complex, ATF5-CEBPG","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-492509","identifier":"Q9Y2D1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2D1/entry","name":"ATF5","description":"Cyclic AMP-dependent transcription factor ATF-5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-740209","identifier":"P53567","identifierLink":"https://www.uniprot.org/uniprotkb/P53567/entry","name":"CEBPG","description":"CCAAT/enhancer-binding protein gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6589","complexName":"bZIP transcription factor complex, ATF5-CEBPE","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-3907048","identifier":"Q15744","identifierLink":"https://www.uniprot.org/uniprotkb/Q15744/entry","name":"CEBPE","description":"CCAAT/enhancer-binding protein epsilon","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-492509","identifier":"Q9Y2D1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2D1/entry","name":"ATF5","description":"Cyclic AMP-dependent transcription factor ATF-5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6591","complexName":"Platelet-derived growth factor AB complex","organismName":"Rattus norvegicus; 10116","description":"A- and B-chain of the platelet-derived growth factor (PDGF). Binds to and activates PDGF receptor alpha (PDGFRalpha, P20786) and beta (PDGFRbeta, Q05030) subunits by inducing receptor dimerisation and tyrosine phosphorylation. Is a potent mitogen for cells of mesenchymal origin. Plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Plays an important role in wound healing.","predictedComplex":false,"interactors":[{"ac":"EBI-26905402","identifier":"P28576","identifierLink":"https://www.uniprot.org/uniprotkb/P28576/entry","name":"Pdgfa","description":"Platelet-derived growth factor subunit A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26905475","identifier":"Q05028","identifierLink":"https://www.uniprot.org/uniprotkb/Q05028/entry","name":"Pdgfb","description":"Platelet-derived growth factor subunit B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6592","complexName":"L-lactate dehydrogenase complex, A3B1 variant","organismName":"Homo sapiens; 9606","description":"Catalyzes the NAD(H)-dependent interconversion of lactate and pyruvate. Mainly expressed in kidney, placenta and pancreas.","predictedComplex":false,"interactors":[{"ac":"EBI-358748","identifier":"P07195","identifierLink":"https://www.uniprot.org/uniprotkb/P07195/entry","name":"LDHB","description":"L-lactate dehydrogenase B chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43128","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372327","identifier":"P00338","identifierLink":"https://www.uniprot.org/uniprotkb/P00338/entry","name":"LDHA","description":"L-lactate dehydrogenase A chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43128","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6593","complexName":"bZIP transcription factor complex, ATF6-ATF6","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. \r\n\r\nATF6 is a master regulator of one of the three main branches of the endoplasmic reticulum (ER) unfolded protein response, regulating numerous genes that restore ER protein-folding capacity, after which it is rapidly degraded.","predictedComplex":false,"interactors":[{"ac":"EBI-852157","identifier":"P18850","identifierLink":"https://www.uniprot.org/uniprotkb/P18850/entry","name":"ATF6","description":"Cyclic AMP-dependent transcription factor ATF-6 alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46164","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6594","complexName":"L-lactate dehydrogenase complex, A2B2 variant","organismName":"Homo sapiens; 9606","description":"Catalyzes the NAD(H)-dependent interconversion of lactate and pyruvate. Mainly expressed in lungs.","predictedComplex":false,"interactors":[{"ac":"EBI-358748","identifier":"P07195","identifierLink":"https://www.uniprot.org/uniprotkb/P07195/entry","name":"LDHB","description":"L-lactate dehydrogenase B chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43128","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372327","identifier":"P00338","identifierLink":"https://www.uniprot.org/uniprotkb/P00338/entry","name":"LDHA","description":"L-lactate dehydrogenase A chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43128","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3984","complexName":"Hsp90-Cdc37 chaperone complex","organismName":"Caenorhabditis elegans; 6239","description":"A chaperone complex required for the proper folding, maturation and stabilization of target proteins (mostly signalling protein kinases, some steroid hormone receptors), usually during or immediately after completion of translation. Complex binding also prevents rapid ubiquitin-dependent proteosomal degradation of target proteins. The complex exhibits little ATP hydrolysis activity due to the binding of cdc-37 to daf-21/Hsp90, which inhibits the ATPase of daf-21/Hsp90. However, inhibition may be relieved by the binding of aha-1 to the complex; aha-1 eventually displaces cdc-37 from the complex. The highly conserved, phosphorylated cdc-37 Ser-14 is essential for complex assembly and binding to its target protein. cdc-37-Ser14 is phosphorylated by Casein kinase II/kin-3 (P18334), which in turn is a target of cdc-37 creating a positive feedback loop. cdc-37-Ser14 is de-phosphorylated by pph-5 (Q9NES8) within the serine/threonine phosphatase Hsp90-cdc-37-pph-5 complex (CPX-3983). HSP90/daf-21 does not bind any particular motif but rather associates with intrinsically unstable kinases.","predictedComplex":false,"interactors":[{"ac":"EBI-313329","identifier":"Q18688","identifierLink":"https://www.uniprot.org/uniprotkb/Q18688/entry","name":"hsp-90","description":"Heat shock protein 90","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11528","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-329675","identifier":"O02108","identifierLink":"https://www.uniprot.org/uniprotkb/O02108/entry","name":"cdc-37","description":"Probable Hsp90 co-chaperone cdc37","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4001","complexName":"PKD1-PKD2 Polycystin complex","organismName":"Homo sapiens; 9606","description":"Appears to form a calcium-permeable ion channel in the primary cilia with a role in fluid-flow mechano-sensation in the renal epithelium. May act as a regulator of cilium length. Recent results suggest that PKD2 may function independently as a monovalent cation-selective channel  and that PDK1 serves as the receptor to sense chemical and mechanical force stimuli.","predictedComplex":false,"interactors":[{"ac":"EBI-1752013","identifier":"P98161","identifierLink":"https://www.uniprot.org/uniprotkb/P98161/entry","name":"PKD1","description":"Polycystin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46730","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7813714","identifier":"Q13563","identifierLink":"https://www.uniprot.org/uniprotkb/Q13563/entry","name":"PKD2","description":"Polycystin-2","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10877","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4002","complexName":"Hsp90-cdc-37-aha-1 complex","organismName":"Caenorhabditis elegans; 6239","description":"A chaperone complex that may be required for the proper folding, maturation and stabilization of target protein. Most likely plays a role in the maturation of protein kinases. Aha-1 has a strong affinity for Hsp90/daf-21, and aha-1 binding to the Hsp90-cdc37 complex relieves ATPase hydrolysis inhibition and eventually displaces cdc-37.","predictedComplex":false,"interactors":[{"ac":"EBI-2408984","identifier":"O02219","identifierLink":"https://www.uniprot.org/uniprotkb/O02219/entry","name":"aha-1","description":"Aryl hydrocarbon receptor nuclear translocator homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR23042","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-313329","identifier":"Q18688","identifierLink":"https://www.uniprot.org/uniprotkb/Q18688/entry","name":"hsp-90","description":"Heat shock protein 90","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11528","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-329675","identifier":"O02108","identifierLink":"https://www.uniprot.org/uniprotkb/O02108/entry","name":"cdc-37","description":"Probable Hsp90 co-chaperone cdc37","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4003","complexName":"Hsp90-sti-1 chaperone complex","organismName":"Caenorhabditis elegans; 6239","description":"A chaperone complex that may be required for the proper folding, maturation and stabilization of target proteins. As in yeast (but not in human), the complex in C.elegans exhibits little ATP hydrolysis activity due to the binding of sti-1 to daf-21/Hsp90, which inhibits the ATPase of daf-21/Hsp90.","predictedComplex":false,"interactors":[{"ac":"EBI-313329","identifier":"Q18688","identifierLink":"https://www.uniprot.org/uniprotkb/Q18688/entry","name":"hsp-90","description":"Heat shock protein 90","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11528","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6514174","identifier":"O16259","identifierLink":"https://www.uniprot.org/uniprotkb/O16259/entry","name":"sti-1","description":"Stress-induced-phosphoprotein 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR22904","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4004","complexName":"Hsp90-daf-41 chaperone complex","organismName":"Caenorhabditis elegans; 6239","description":"A chaperone complex that may be required for the proper folding, maturation and stabilization of target proteins. As in human (but not in yeast), the complex in C.elegans exhibits little ATP hydrolysis activity due to the binding of p23/daf-41 to daf-21/Hsp90, which inhibits the ATPase of daf-21/Hsp90. Within the complex, p23/daf-41 controls the ATP hydrolysis rate to regulate the formation of stable complexes between Hsp90/daf-21 and its target proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-21004599","identifier":"Q23280","identifierLink":"https://www.uniprot.org/uniprotkb/Q23280/entry","name":"daf-41","description":"Co-chaperone protein daf-41","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR22932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-313329","identifier":"Q18688","identifierLink":"https://www.uniprot.org/uniprotkb/Q18688/entry","name":"hsp-90","description":"Heat shock protein 90","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11528","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4005","complexName":"Exodeoxyribonuclease VII complex","organismName":"Escherichia coli (strain K12); 83333","description":"Single-strand DNA-specific exodeoxyribonuclease which possesses dual polarity, degrading both 3-prime and 5-prime ends, in a processive reaction. The products of the reaction are oligonucleotides, 4-12 nucleotides in length, which are then degraded further into small acid-soluble oligonucleotides. \r\nThe complex can digest into the duplex region, probably the result of the 'breathing' of the duplex to form single-stranded termini. \r\nMediates mismatch repair by aborting frameshift and template-switch mutations in a manner partially redundant with 3-prime exonuclease, sbcB (P04995).","predictedComplex":false,"interactors":[{"ac":"EBI-1116872","identifier":"P0A8G9","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8G9/entry","name":"xseB","description":"Exodeoxyribonuclease 7 small subunit","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34137","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-559703","identifier":"P04994","identifierLink":"https://www.uniprot.org/uniprotkb/P04994/entry","name":"xseA","description":"Exodeoxyribonuclease 7 large subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30008","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4021","complexName":"sbcCD DNA exo/endonuclease complex","organismName":"Escherichia coli (strain K12); 83333","description":"Combined ATPase/endo/ 3-prime exonuclease complex which both senses and removes blocked DNA ends. The hydrolysis of ATP enables the complex to cleave DNA 15–25 base pairs away from diverse blocks through endonuclease activity. Displays a preference for hairpin secondary structures in DNA which it cleaves close to the unpaired tip. SbcCD can also cleave 4-strand cruciforms and can open hairpin-capped ends. Cleaves at secondary structures formed by inverted repeats, or palindromic DNA sequences, producing double-strand breaks. \r\nThe complex is also required to repair breaks made by restriction endonuclease activity and its exonuclease activity may process the ends of broken chromosomes. May bind and coordinate the two ends of broken DNA molecules to assist in their repair and may remove covalently attached or tightly bound proteins that interfere with end processing.","predictedComplex":false,"interactors":[{"ac":"EBI-1116543","identifier":"P0AG76","identifierLink":"https://www.uniprot.org/uniprotkb/P0AG76/entry","name":"sbcD","description":"Nuclease SbcCD subunit D","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30337","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-546919","identifier":"P13458","identifierLink":"https://www.uniprot.org/uniprotkb/P13458/entry","name":"sbcC","description":"Nuclease SbcCD subunit C","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32114","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4022","complexName":"ATP synthase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Acts to convert the energy of oxidation-reduction reactions of the electron transport chain (respiration) to the phosphorylation of ADP. The synthesis of ATP is coupled to the respiratory chain via the proton potential. The ATP synthase is a molecular motor composed of two separable parts: F1 and F0. The F0 motor spans the membrane converting the potential energy of the proton motive force (pmf) into rotation of the central stalk that in turn drives conformational changes in the F1 catalytic sites. Bacterial F-ATPase can also function in reverse, employing ATP hydrolysis to generate a proton gradient across the membrane when needed","predictedComplex":false,"interactors":[{"ac":"EBI-1121219","identifier":"P68699","identifierLink":"https://www.uniprot.org/uniprotkb/P68699/entry","name":"atpE","description":"ATP synthase subunit c","stochiometry":"minValue: 10, maxValue: 10","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1131012","identifier":"P0ABA0","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABA0/entry","name":"atpF","description":"ATP synthase subunit b","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33445","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1133640","identifier":"P0ABA4","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABA4/entry","name":"atpH","description":"ATP synthase subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11910","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-368707","identifier":"P0ABB0","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABB0/entry","name":"atpA","description":"ATP synthase subunit alpha","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR48082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-368783","identifier":"P0ABB4","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABB4/entry","name":"atpD","description":"ATP synthase subunit beta","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR15184","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544306","identifier":"P0ABA6","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABA6/entry","name":"atpG","description":"ATP synthase gamma chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11693","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544362","identifier":"P0A6E6","identifierLink":"https://www.uniprot.org/uniprotkb/P0A6E6/entry","name":"atpC","description":"ATP synthase epsilon chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR13822","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549592","identifier":"P0AB98","identifierLink":"https://www.uniprot.org/uniprotkb/P0AB98/entry","name":"atpB","description":"ATP synthase subunit a","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42823","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4024","complexName":"MTM6-MTM9 myotubularin lipid phosphatase complex","organismName":"Caenorhabditis elegans; 6239","description":"A protein phosphatase complex that dephosphorylates the 3'-phosphate of phosphatidylinositol-3-phosphate (PI3P) (CHEBI:26034) to regulate phosphoinositide (PI)-phosphate levels. PIs control processes such as membrane trafficking through their ability to bind effector proteins containing PI-binding domains to the membrane. The complex functions in an arf-6- and rme-1-mediated endocytic pathway in coelomocytes. Plays a role in endosome trafficking probably by regulating PI3P levels. In addition, the complex regulates neuronal function by promoting synapse formation of DA9 motor neurons.","predictedComplex":false,"interactors":[{"ac":"EBI-21004803","identifier":"Q965W9","identifierLink":"https://www.uniprot.org/uniprotkb/Q965W9/entry","name":"mtm-9","description":"Myotubularin-related protein 9","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10807","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21004827","identifier":"G5ED68","identifierLink":"https://www.uniprot.org/uniprotkb/G5ED68/entry","name":"mtm-6","description":"Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR6","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10807","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4025","complexName":"pph-6-saps-1 phosphatase complex","organismName":"Caenorhabditis elegans; 6239","description":"A protein phosphatase complex that dephosphorylates targets to modulate processes such as cytokinesis during cell division. Specifically, the complex is required for the organisation of cortical non-muscle myosin II (nmy-2) (G5EBY3) and spindle positioning in one-cell stage embryos. Plays a role in nmy-1 distribution during anaphase and cytokinesis. Required for proper pulling forces that drive mitotic spindle movement during anaphase, by promoting the cortical localization of components of the gpr-1-gpr-2-lin-5 complex (CPX-4027).","predictedComplex":false,"interactors":[{"ac":"EBI-2002622","identifier":"Q09496","identifierLink":"https://www.uniprot.org/uniprotkb/Q09496/entry","name":"pph-6","description":"Serine/threonine-protein phosphatase 6 catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-324363","identifier":"B2D6K9","identifierLink":"https://www.uniprot.org/uniprotkb/B2D6K9/entry","name":"saps-1","description":"Serine/threonine-protein phosphatase 6 regulatory subunit","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12634","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4027","complexName":"gpr-1-gpr-2-lin-5 complex","organismName":"Caenorhabditis elegans; 6239","description":"Controls nuclear rotation and spindle elongation during mitosis in early embryonic divisions, activating G-protein signaling to affect mitotic spindle forces that drive spindle movement. Within the complex, gpr-1 binds to G protein goa-1 (P51875; ADP-bound form), which plays a role in the cortical localization of gpr-1 and gpr-2.","predictedComplex":false,"interactors":[{"ac":"EBI-21005023","identifier":"Q03569","identifierLink":"https://www.uniprot.org/uniprotkb/Q03569/entry","name":"gpr-2","description":"G-protein regulator 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-316069","identifier":"Q95QJ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q95QJ7/entry","name":"gpr-1","description":"G-protein regulator 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-320134","identifier":"P45970","identifierLink":"https://www.uniprot.org/uniprotkb/P45970/entry","name":"lin-5","description":"Spindle apparatus protein lin-5","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR43939","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4041","complexName":"PKD1-PKD2 Polycystin complex","organismName":"Mus musculus; 10090","description":"Appears to form a calcium-permeable ion channel in the primary cilia with a role in fluid-flow mechano-sensation in the renal epithelium. May act as a regulator of cilium length. Recent results suggest that Pkd2 may function independently as a monovalent cation-selective channel and that Pkd1 serves as the receptor to sense chemical and mechanical force stimuli.","predictedComplex":false,"interactors":[{"ac":"EBI-6666305","identifier":"O08852","identifierLink":"https://www.uniprot.org/uniprotkb/O08852/entry","name":"Pkd1","description":"Polycystin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46730","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9823400","identifier":"O35245","identifierLink":"https://www.uniprot.org/uniprotkb/O35245/entry","name":"Pkd2","description":"Polycystin-2","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10877","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4061","complexName":"NLGN1(-SSA-SSB) - NRXN1-beta(-SS4) complex","organismName":"Rattus norvegicus; 10116","description":"A cell adhesion complex that forms at synaptic clefts and mediates trans-synaptic signaling. Composed by binding of the extracellular domains of two presynaptic neurexin proteins and two postsynaptic neuroligin proteins. \r\n\r\nExpression of both subunits is regulated by neuronal activity. \r\n\r\nRequired for synaptic differentiation, maturation and maintenance, dendritic spine remodelling and axon arborisation. Possibly required for synapse formation. Mediates bidirectional synaptic signalling and coupling of presynaptic, Ca2+-dependent synaptic vesicle exocytosis (= neurotransmitter release) with postsynaptic neurotransmitter receptor recruitment. \r\n\r\nActs as a molecular switch between excitatory and inhibitory synapses: this complex acts primarily, but not exclusively, on GABAergic, inhibitory synapses that mainly release neurotransmitters GABA and glycine. \r\n\r\nMainly found in synaptic clefts of the central nervous system but also at neuromuscular junctions (particularly alpha neurexin-containing complexes).","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-20994039","identifier":"Q62765-2","identifierLink":"https://www.uniprot.org/uniprotkb/Q62765-2/entry","name":"Nlgn1","description":"Neuroligin-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-20994045","identifier":"Q63373-3","identifierLink":"https://www.uniprot.org/uniprotkb/Q63373-3/entry","name":"Nrxn1","description":"Neurexin-1-beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-4063","complexName":"ChpBS toxin-antitoxin complex","organismName":"Escherichia coli (strain K12); 83333","description":"Type II toxin-antitoxin (TA) system formed by the toxin (chpB), and the antitoxin (chpS). TA systems act as effectors of dormancy and persistence, with the toxin causing growth arrest by interfering with a vital cellular process, such as  transcription, translation or DNA replication,  and the cognate antitoxin neutralizing the toxin activity during normal growth conditions. chpB acts as an endoribonuclease able to cleave RNA in the absence of ribosomes, thus inhibiting protein synthesis. Under conditions of stress the antitoxins are selectively degraded by cellular proteases such as Lon (P0A9M0) and ClpXP (CPX-3176), leaving the toxins to exert their effects which result in growth arrest and cell dormancy. Both the antitoxin and, in most cases, the TA complex bind the TA promoter to repress transcription, with TA complexes repressing transcription more efficiently than the antitoxins alone by increasing the co-operativity of antitoxin binding to operators.","predictedComplex":false,"interactors":[{"ac":"EBI-21016815","identifier":"P33647","identifierLink":"https://www.uniprot.org/uniprotkb/P33647/entry","name":"chpB","description":"Endoribonuclease toxin ChpB","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33988","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-556499","identifier":"P08365","identifierLink":"https://www.uniprot.org/uniprotkb/P08365/entry","name":"chpS","description":"Antitoxin ChpS","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR40516","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4082","complexName":"NLRP1 inflammasome","organismName":"Homo sapiens; 9606","description":"A pro-inflammatory thiol protease complex that is activated in response to pathogen infections and toxins (e.g. Anthrax lethal toxin). Primarily acts in monocytes and macrophages. \r\n\r\nActivating platform for Caspase-1 (CPX-952) through proximity-induced self-cleavage in an ATP-dependent reaction.\r\n\r\nActivated Caspase-1 cleaves interleukins 1beta (IL1B, P01584) and IL18 (Q14116) releasing the mature cytokines which are involved in a variety of inflammatory processes and is also involved in pyroptosis of macrophages, a special case of cell death, associated with infection by intracellular pathogens where it cleaves GSDMD (P57764). \r\n\r\nBelongs to the family of Inflammasomes that includes NLRP3 inflammasome (CPX-4141), NLRC4 inflammasome (CPX-4144), AIM2 inflammasome (CPX-4142) and Pyrin inflammasome (CPX-4143).\r\n\r\nSingle-nucleotide polymorphisms in the NLRP1 gene are associated with vitiligo.","predictedComplex":false,"interactors":[{"ac":"EBI-1220518","identifier":"Q9C000","identifierLink":"https://www.uniprot.org/uniprotkb/Q9C000/entry","name":"NLRP1","description":"NACHT, LRR and PYD domains-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46985","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-516667","identifier":"P29466","identifierLink":"https://www.uniprot.org/uniprotkb/P29466/entry","name":"CASP1","description":"Caspase-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47901","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-751215","identifier":"Q9ULZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ULZ3/entry","name":"PYCARD","description":"Apoptosis-associated speck-like protein containing a CARD","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46985","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4083","complexName":"NLGN1(-SSA-SSB) - NRXN1-beta(-SS4) complex","organismName":"Mus musculus; 10090","description":"A cell adhesion complex that forms at synaptic clefts and mediates trans-synaptic signaling. Composed by binding of the extracellular domains of two presynaptic neurexin proteins and two postsynaptic neuroligin proteins. \r\n\r\nExpression of both subunits is regulated by neuronal activity. \r\n\r\nRequired for synaptic differentiation, maturation and maintenance, dendritic spine remodelling and axon arborisation. Possibly required for synapse formation. Mediates bidirectional synaptic signalling and coupling of presynaptic, Ca2+-dependent synaptic vesicle exocytosis (= neurotransmitter release) with postsynaptic neurotransmitter receptor recruitment. \r\n\r\nActs as a molecular switch between excitatory and inhibitory synapses: this complex acts primarily, but not exclusively, on GABAergic, inhibitory synapses that mainly release neurotransmitters GABA and glycine. \r\n\r\nMainly found in synaptic clefts of the central nervous system but also at neuromuscular junctions (particularly alpha neurexin-containing complexes).","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-16735905","identifier":"E9QK34","identifierLink":"https://www.uniprot.org/uniprotkb/E9QK34/entry","name":"Nlgn1","description":null,"stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-2794440","identifier":"P0DI97","identifierLink":"https://www.uniprot.org/uniprotkb/P0DI97/entry","name":"Nrxn1","description":"Neurexin-1-beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-4084","complexName":"GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA2 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex that is predominately recruited to CTCF (P49711), KLF4 (O43474) and Sp5-dependent targets sites, promoters and enhancers, depending on cell type. Targeted to chromatin, especially to H3K27ac, H3K4me1 and H3K4me3 markers, via by the bromo domain of its BRD9 subunit. Recruitment may be aided by BRD4 (O60885), especially in embryonic stem cells (ESC). \r\n\r\nActs predominantly as a transcriptional activator that regulates tissue development, cell differentiation and cell proliferation and maintains naive pluripotency in ESC. \r\n\r\nMutation is several subunits are linked to various cancers. SS18-SSX fusion gene is a hallmark for synovial sarcoma and malignant rhabdoid tumour.","predictedComplex":false,"interactors":[{"ac":"EBI-10258305","identifier":"Q9H8M2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H8M2/entry","name":"BRD9","description":"Bromodomain-containing protein 9","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22881","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1754943","identifier":"Q9NZM4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZM4/entry","name":"BICRA","description":"BRD4-interacting chromatin-remodeling complex-associated protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15572","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2560588","identifier":"Q9BQE9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BQE9/entry","name":"BCL7B","description":"B-cell CLL/lymphoma 7 protein family member B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2560599","identifier":"Q15532","identifierLink":"https://www.uniprot.org/uniprotkb/Q15532/entry","name":"SS18","description":"Protein SSXT","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23107","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355018","identifier":"O96019","identifierLink":"https://www.uniprot.org/uniprotkb/O96019/entry","name":"ACTL6A","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359917","identifier":"Q4VC05","identifierLink":"https://www.uniprot.org/uniprotkb/Q4VC05/entry","name":"BCL7A","description":"B-cell CLL/lymphoma 7 protein family member A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679562","identifier":"P51531","identifierLink":"https://www.uniprot.org/uniprotkb/P51531/entry","name":"SMARCA2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7850114","identifier":"Q8WUZ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WUZ0/entry","name":"BCL7C","description":"B-cell CLL/lymphoma 7 protein family member C","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4101","complexName":"NLGN1(+SSA+SSB) - NRXN1-beta(-SS4) complex","organismName":"Homo sapiens; 9606","description":"A cell adhesion complex that forms at synaptic clefts and mediates trans-synaptic signaling. Composed by binding of the extracellular domains of two presynaptic neurexin proteins and two postsynaptic neuroligin proteins. \r\n\r\nExpression of both subunits is regulated by neuronal activity. \r\n\r\nRequired for synaptic differentiation, maturation and maintenance, dendritic spine remodelling and axon arborisation. Possibly required for synapse formation. Mediates bidirectional synaptic signalling and coupling of presynaptic, Ca2+-dependent synaptic vesicle exocytosis (= neurotransmitter release) with postsynaptic neurotransmitter receptor recruitment. \r\n\r\nActs as a molecular switch between excitatory and inhibitory synapses: this complex acts primarily, but not exclusively, on glutamatergic, excitatory synapses that mainly release neurotransmitters glutamate and aspartate. \r\n\r\nMainly found in synaptic clefts of the central nervous system but also at neuromuscular junctions. \r\n\r\nMutations in the neuroligin dimer interface as well as allosteric affects of mutation in both subunits affect spacial and fear-associated memory and result in autism-related disorders, mental retardation disorders and schizophrenia.","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-16513622","identifier":"P58400-1","identifierLink":"https://www.uniprot.org/uniprotkb/P58400-1/entry","name":"NRXN1","description":"Neurexin-1-beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-8287193","identifier":"Q8N2Q7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N2Q7/entry","name":"NLGN1","description":"Neuroligin-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43903","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4102","complexName":"PrlF-YhaV toxin-antitoxin complex","organismName":"Escherichia coli (strain K12); 83333","description":"Type II toxin-antitoxin (TA) system formed by the toxin (yhaV), and the antitoxin (prlF). TA systems act as effectors of dormancy and persistence, with the toxin causing growth arrest by interfering with a vital cellular process, such as  transcription, translation or DNA replication,  and the cognate antitoxin neutralizing the toxin activity during normal growth conditions. yhaV acts as an endoribonuclease able to cleave RNA in the absence of ribosomes, thus inhibiting protein synthesis. Under conditions of stress the antitoxins are selectively degraded by cellular proteases such as Lon (P0A9M0) and ClpXP (CPX-3176), leaving the toxins to exert their effects which result in growth arrest and cell dormancy. Both the antitoxin and, in most cases, the TA complex bind the TA promoter to repress transcription, with TA complexes repressing transcription more efficiently than the antitoxins alone by increasing the co-operativity of antitoxin binding to operators.","predictedComplex":false,"interactors":[{"ac":"EBI-1122597","identifier":"P15373","identifierLink":"https://www.uniprot.org/uniprotkb/P15373/entry","name":"prlF","description":"Antitoxin PrlF","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-21170040","identifier":"P64594","identifierLink":"https://www.uniprot.org/uniprotkb/P64594/entry","name":"yhaV","description":"Ribonuclease toxin YhaV","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]}]},{"complexAC":"CPX-4103","complexName":"Collagen type IX trimer","organismName":"Rattus norvegicus; 10116","description":"Nonfibrillar collagen (FACIT) that associate to form a structure that links glycosaminoglycans to type II collagen fibrils. The molecules contain three functional regions. One region comprises one or two triple helical domains and serves for the interaction and adhesion of these molecules to the fibrils. A second region, comprising another triple helical domain, serves as a rigid arm that projects out of the fibril and a third region, which does not include triple helices and may serve for interaction with other matrix elements or with cells. The various triple helical domains are separated by short nontriple helical domains (NC domains). Type IX collagen is found in ECMs containing type II collagen as their main fibril-forming structure, such as hyaline cartilage  and the vitreous body of the eye.","predictedComplex":false,"interactors":[{"ac":"EBI-21174420","identifier":"P20850","identifierLink":"https://www.uniprot.org/uniprotkb/P20850/entry","name":"Col9a1","description":"Collagen alpha-1(IX) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-21174432","identifier":"D3ZNT5","identifierLink":"https://www.uniprot.org/uniprotkb/D3ZNT5/entry","name":"Col9a2","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21174457","identifier":"D3ZX71","identifierLink":"https://www.uniprot.org/uniprotkb/D3ZX71/entry","name":"Col9a3","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4104","complexName":"Collagen type IX trimer","organismName":"Gallus gallus; 9031","description":"Nonfibrillar collagen (FACIT) that associate to form a structure that links glycosaminoglycans to type II collagen fibrils. The molecules contain three functional regions. One region comprises one or two triple helical domains and serves for the interaction and adhesion of these molecules to the fibrils. A second region, comprising another triple helical domain, serves as a rigid arm that projects out of the fibril and a third region, which does not include triple helices and may serve for interaction with other matrix elements or with cells. The various triple helical domains are separated by short nontriple helical domains (NC domains). Type IX collagen is found in ECMs containing type II collagen as their main fibril-forming structure, such as hyaline cartilage  and the vitreous body of the eye.","predictedComplex":false,"interactors":[{"ac":"EBI-21174513","identifier":"P12106","identifierLink":"https://www.uniprot.org/uniprotkb/P12106/entry","name":"COL9A1","description":"Collagen alpha-1(IX) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21174526","identifier":"P12108","identifierLink":"https://www.uniprot.org/uniprotkb/P12108/entry","name":"COL9A2","description":"Collagen alpha-2(IX) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21174538","identifier":"P32017","identifierLink":"https://www.uniprot.org/uniprotkb/P32017/entry","name":"COL9A3","description":"Collagen alpha-3(IX) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4105","complexName":"Collagen type IX trimer","organismName":"Bos taurus; 9913","description":"Nonfibrillar collagen (FACIT) that associate to form a structure that links glycosaminoglycans to type II collagen fibrils. The molecules contain three functional regions. One region comprises one or two triple helical domains and serves for the interaction and adhesion of these molecules to the fibrils. A second region, comprising another triple helical domain, serves as a rigid arm that projects out of the fibril and a third region, which does not include triple helices and may serve for interaction with other matrix elements or with cells. The various triple helical domains are separated by short nontriple helical domains (NC domains). Type IX collagen is found in ECMs containing type II collagen as their main fibril-forming structure, such as hyaline cartilage  and the vitreous body of the eye.","predictedComplex":false,"interactors":[{"ac":"EBI-21174573","identifier":"C0HLN2","identifierLink":"https://www.uniprot.org/uniprotkb/C0HLN2/entry","name":"COL9A2","description":"Collagen alpha-2(IX) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5281339","identifier":"F1MND9","identifierLink":"https://www.uniprot.org/uniprotkb/F1MND9/entry","name":"COL9A1","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[]},{"ac":"EBI-70789136","identifier":"A0AAA9S8K3","identifierLink":"https://www.uniprot.org/uniprotkb/A0AAA9S8K3/entry","name":"COL9A3","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[]}]},{"complexAC":"CPX-4106","complexName":"Thrombospondin 4 complex","organismName":"Rattus norvegicus; 10116","description":"Secreted glycoprotein that functions during the tissue remodeling that is associated with development, wound healing, synaptogenesis, angiogenesis, and cancer. Through its interactions with proteins and proteoglycans, such as glycosaminoglycans, low density lipoprotein receptor-related protein-1, various integrins, calreticulin, and fibrinogen, TSP-4 functions at the interface of the cell membrane and the extracellular matrix to regulate matrix structure and cellular behaviour.","predictedComplex":false,"interactors":[{"ac":"EBI-2465782","identifier":"P49744","identifierLink":"https://www.uniprot.org/uniprotkb/P49744/entry","name":"Thbs4","description":"Thrombospondin-4","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR10199","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4107","complexName":"Thrombospondin 1 complex","organismName":"Bos taurus; 9913","description":"Secreted glycoprotein that functions during the tissue remodeling that is associated with development, wound healing, synaptogenesis, angiogenesis, and cancer. Through its interactions with proteins and proteoglycans, such as glycosaminoglycans, low density lipoprotein receptor-related protein-1, various integrins, calreticulin, and fibrinogen, TSP-1 functions at the interface of the cell membrane and the extracellular matrix to regulate matrix structure and cellular behaviour.","predictedComplex":false,"interactors":[{"ac":"EBI-5281283","identifier":"Q28178","identifierLink":"https://www.uniprot.org/uniprotkb/Q28178/entry","name":"THBS1","description":"Thrombospondin-1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR10199","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4108","complexName":"Collagen type I homotrimer","organismName":"Homo sapiens; 9606","description":"A collagen fibrils type only found in foetal tissue, fibrosis and cancer tissue. Resistant to mammalian collagenases.","predictedComplex":false,"interactors":[{"ac":"EBI-982999","identifier":"P02452","identifierLink":"https://www.uniprot.org/uniprotkb/P02452/entry","name":"COL1A1","description":"Collagen alpha-1(I) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4111","complexName":"Collagen type I trimer","organismName":"Ovis aries; 9940","description":"Form the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite.","predictedComplex":false,"interactors":[{"ac":"EBI-21180993","identifier":"Q9MZW3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9MZW3/entry","name":"COL1A1","description":null,"stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Ovis aries; 9940","xrefs":[]},{"ac":"EBI-21181000","identifier":"W5NTT7","identifierLink":"https://www.uniprot.org/uniprotkb/W5NTT7/entry","name":"COL1A2","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Ovis aries; 9940","xrefs":[]}]},{"complexAC":"CPX-4112","complexName":"Collagen type I trimer","organismName":"Sus scrofa; 9823","description":"Forms the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite.","predictedComplex":false,"interactors":[{"ac":"EBI-21181053","identifier":"F1SFA7","identifierLink":"https://www.uniprot.org/uniprotkb/F1SFA7/entry","name":"COL1A2","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Sus scrofa; 9823","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21181100","identifier":"A0A287A1S6","identifierLink":"https://www.uniprot.org/uniprotkb/A0A287A1S6/entry","name":"COL1A1","description":null,"stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Sus scrofa; 9823","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4113","complexName":"Collagen type III trimer","organismName":"Canis lupus familiaris; 9615","description":"Occurs in most soft connective tissues. Bonded to type I collagen (CPX-3103) by covalent lysine-derived cross-links.","predictedComplex":false,"interactors":[{"ac":"EBI-34579438","identifier":"A0A8C0MYN9","identifierLink":"https://www.uniprot.org/uniprotkb/A0A8C0MYN9/entry","name":"COL3A1","description":null,"stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Canis lupus familiaris; 9615","xrefs":[]}]},{"complexAC":"CPX-4114","complexName":"Prohibitin complex","organismName":"Caenorhabditis elegans; 6239","description":"Chaperone which is essential for mitochondrial biogenesis and degradation, and for the mitochondrial stress response. Functions to protect the cell from imbalances in the production of mitochondrial proteins by stabilizing newly synthesised mitochondrial-encoded proteins . Also acts as a scaffold that recruits membrane proteins to a specific lipid environment. Plays a role in longevity.","predictedComplex":false,"interactors":[{"ac":"EBI-2005861","identifier":"Q9BKU4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BKU4/entry","name":"phb-1","description":"Mitochondrial prohibitin complex protein 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR23222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-328169","identifier":"P50093","identifierLink":"https://www.uniprot.org/uniprotkb/P50093/entry","name":"phb-2","description":"Mitochondrial prohibitin complex protein 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR23222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4115","complexName":"RnlAB toxin-antitoxin complex","organismName":"Escherichia coli (strain K12); 83333","description":"Type II toxin-antitoxin (TA) system formed by the toxin (rnlA), and the antitoxin (rnlB). TA systems act as effectors of dormancy and persistence, with the toxin causing growth arrest by interfering with a vital cellular process, such as  transcription, translation or DNA replication, and the cognate antitoxin neutralizing the toxin activity during normal growth conditions. \r\n\r\nrnlA acts as an endoribonucleases able to cleave RNA in the absence of ribosomes, thus inhibiting protein synthesis. Binding of rnlB antitoxin inhibits rnlA endoribonuclease activity. Under conditions of stress the antitoxins are selectively degraded by cellular proteases such as Lon (P0A9M0) and ClpXP (CPX-3176), leaving the toxins to exert their effects which result in growth arrest and cell dormancy. Both the antitoxin and, in most cases, the TA complex bind the TA promoter to repress transcription, with TA complexes repressing transcription more efficiently than the antitoxins alone by increasing the co-operativity of antitoxin binding to operators.","predictedComplex":false,"interactors":[{"ac":"EBI-21183386","identifier":"P52130","identifierLink":"https://www.uniprot.org/uniprotkb/P52130/entry","name":"rnlB","description":"Antitoxin RnlB","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-560462","identifier":"P52129","identifierLink":"https://www.uniprot.org/uniprotkb/P52129/entry","name":"rnlA","description":"mRNA endoribonuclease toxin LS","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]}]},{"complexAC":"CPX-4116","complexName":"Collagen type V trimer variant 1","organismName":"Canis lupus familiaris; 9615","description":"Form the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite.","predictedComplex":false,"interactors":[{"ac":"EBI-34579416","identifier":"A0A8C0N620","identifierLink":"https://www.uniprot.org/uniprotkb/A0A8C0N620/entry","name":"COL5A2","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Canis lupus familiaris; 9615","xrefs":[]},{"ac":"EBI-34579430","identifier":"A0A8I3NPQ5","identifierLink":"https://www.uniprot.org/uniprotkb/A0A8I3NPQ5/entry","name":"COL5A1","description":null,"stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Canis lupus familiaris; 9615","xrefs":[]}]},{"complexAC":"CPX-4117","complexName":"Collagen type V trimer variant 2","organismName":"Canis lupus familiaris; 9615","description":"Form the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite.","predictedComplex":false,"interactors":[{"ac":"EBI-21183398","identifier":"A0A8C0TGY8","identifierLink":"https://www.uniprot.org/uniprotkb/A0A8C0TGY8/entry","name":"COL5A3","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Canis lupus familiaris; 9615","xrefs":[]},{"ac":"EBI-34579416","identifier":"A0A8C0N620","identifierLink":"https://www.uniprot.org/uniprotkb/A0A8C0N620/entry","name":"COL5A2","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Canis lupus familiaris; 9615","xrefs":[]},{"ac":"EBI-34579430","identifier":"A0A8I3NPQ5","identifierLink":"https://www.uniprot.org/uniprotkb/A0A8I3NPQ5/entry","name":"COL5A1","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Canis lupus familiaris; 9615","xrefs":[]}]},{"complexAC":"CPX-4118","complexName":"Collagen type V trimer variant 3","organismName":"Canis lupus familiaris; 9615","description":"Form the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite.","predictedComplex":false,"interactors":[{"ac":"EBI-34579430","identifier":"A0A8I3NPQ5","identifierLink":"https://www.uniprot.org/uniprotkb/A0A8I3NPQ5/entry","name":"COL5A1","description":null,"stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Canis lupus familiaris; 9615","xrefs":[]}]},{"complexAC":"CPX-4119","complexName":"HicAB toxin-antitoxin complex","organismName":"Escherichia coli (strain K12); 83333","description":"Type II toxin-antitoxin (TA) system formed by the toxin (hicA), and the antitoxin (hicB). TA systems act as effectors of dormancy and persistence, with the toxin causing growth arrest by interfering with a vital cellular process, such as  transcription, translation or DNA replication, and the cognate antitoxin neutralizing the toxin activity during normal growth conditions. \r\n\r\nhicA is a probable translation-independent mRNA interferase. Under conditions of stress the antitoxins are selectively degraded by cellular proteases such as Lon (P0A9M0) and ClpXP (CPX-3176), leaving the toxins to exert their effects which result in growth arrest and cell dormancy. Both the antitoxin and, in most cases, the TA complex bind the TA promoter to repress transcription, with TA complexes repressing transcription more efficiently than the antitoxins alone by increasing the co-operativity of antitoxin binding to operators.","predictedComplex":false,"interactors":[{"ac":"EBI-9154018","identifier":"P67697","identifierLink":"https://www.uniprot.org/uniprotkb/P67697/entry","name":"hicB","description":"Antitoxin HicB","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34504","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9154027","identifier":"P76106","identifierLink":"https://www.uniprot.org/uniprotkb/P76106/entry","name":"hicA","description":"Probable mRNA interferase toxin HicA","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]}]},{"complexAC":"CPX-4121","complexName":"HigAB toxin-antitoxin complex","organismName":"Escherichia coli (strain K12); 83333","description":"Type II toxin-antitoxin (TA) system formed by the toxin (higB), and the antitoxin (higA). TA systems act as effectors of dormancy and persistence, with the toxin causing growth arrest by interfering with a vital cellular process, such as  transcription, translation or DNA replication, and the cognate antitoxin neutralizing the toxin activity during normal growth conditions. higB is a probable translation-dependent mRNA interferase. Under conditions of stress the antitoxins are selectively degraded by cellular proteases such as Lon (P0A9M0) and ClpXP (CPX-3176), leaving the toxins to exert their effects which result in growth arrest and cell dormancy. Both the antitoxin and, in most cases, the TA complex bind the TA promoter to repress transcription, with TA complexes repressing transcription more efficiently than the antitoxins alone by increasing the co-operativity of antitoxin binding to operators.","predictedComplex":false,"interactors":[{"ac":"EBI-1131548","identifier":"P67701","identifierLink":"https://www.uniprot.org/uniprotkb/P67701/entry","name":"higA","description":"Antitoxin HigA","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR40455","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1135071","identifier":"P64578","identifierLink":"https://www.uniprot.org/uniprotkb/P64578/entry","name":"higB","description":"mRNA interferase toxin HigB","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]}]},{"complexAC":"CPX-4122","complexName":"NLGN1(+SSA+SSB) - NRXN1-beta(-SS4) complex","organismName":"Mus musculus; 10090","description":"A cell adhesion complex that forms at synaptic clefts and mediates trans-synaptic signaling. Composed by binding of the extracellular domains of two presynaptic neurexin proteins and two postsynaptic neuroligin proteins. \r\n\r\nExpression of both subunits is regulated by neuronal activity. \r\n\r\nRequired for synaptic differentiation, maturation and maintenance, dendritic spine remodelling and axon arborisation. Possibly required for synapse formation. Mediates bidirectional synaptic signalling and coupling of presynaptic, Ca2+-dependent synaptic vesicle exocytosis (= neurotransmitter release) with postsynaptic neurotransmitter receptor recruitment. \r\n\r\nActs as a molecular switch between excitatory and inhibitory synapses: this complex acts primarily, but not exclusively, on glutamatergic, excitatory synapses that mainly release neurotransmitters glutamate and aspartate. \r\n\r\nMainly found in synaptic clefts of the central nervous system but also at neuromuscular junctions.","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2794440","identifier":"P0DI97","identifierLink":"https://www.uniprot.org/uniprotkb/P0DI97/entry","name":"Nrxn1","description":"Neurexin-1-beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-775037","identifier":"Q99K10","identifierLink":"https://www.uniprot.org/uniprotkb/Q99K10/entry","name":"Nlgn1","description":"Neuroligin-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR43903","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4123","complexName":"NLGN1(+SSA+SSB) - NRXN1-beta(-SS4) complex","organismName":"Rattus norvegicus; 10116","description":"A cell adhesion complex that forms at synaptic clefts and mediates trans-synaptic signaling. Composed by binding of the extracellular domains of two presynaptic neurexin proteins and two postsynaptic neuroligin proteins. \r\n\r\nExpression of both subunits is regulated by neuronal activity. \r\n\r\nRequired for synaptic differentiation, maturation and maintenance, dendritic spine remodelling and axon arborisation. Possibly required for synapse formation. Mediates bidirectional synaptic signalling and coupling of presynaptic, Ca2+-dependent synaptic vesicle exocytosis (= neurotransmitter release) with postsynaptic neurotransmitter receptor recruitment. \r\n\r\nActs as a molecular switch between excitatory and inhibitory synapses: this complex acts primarily, but not exclusively, on glutamatergic, excitatory synapses that mainly release neurotransmitters glutamate and aspartate. \r\n\r\nMainly found in synaptic clefts of the central nervous system but also at neuromuscular junctions.","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-20994045","identifier":"Q63373-3","identifierLink":"https://www.uniprot.org/uniprotkb/Q63373-3/entry","name":"Nrxn1","description":"Neurexin-1-beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-7281118","identifier":"Q62765","identifierLink":"https://www.uniprot.org/uniprotkb/Q62765/entry","name":"Nlgn1","description":"Neuroligin-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR43903","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4124","complexName":"Collagen type VI trimer","organismName":"Bos taurus; 9913","description":"May play a role as an interface between the main collagen fibril network and the cells.","predictedComplex":false,"interactors":[{"ac":"EBI-21194229","identifier":"E1BI98","identifierLink":"https://www.uniprot.org/uniprotkb/E1BI98/entry","name":"COL6A1","description":"Collagen alpha-1(VI) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21194252","identifier":"F1MKG2","identifierLink":"https://www.uniprot.org/uniprotkb/F1MKG2/entry","name":"COL6A2","description":"Collagen alpha-2(VI) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21194278","identifier":"E1BB91","identifierLink":"https://www.uniprot.org/uniprotkb/E1BB91/entry","name":"COL6A3","description":"Collagen alpha-3(VI) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4126","complexName":"Integrin alphav-beta3 complex","organismName":"Bos taurus; 9913","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and von Willebrand factor which its binds via the sequence R-G-D in the ligand.","predictedComplex":false,"interactors":[{"ac":"EBI-6446031","identifier":"F1MTN1","identifierLink":"https://www.uniprot.org/uniprotkb/F1MTN1/entry","name":"ITGB3","description":"Integrin beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6446072","identifier":"P80746","identifierLink":"https://www.uniprot.org/uniprotkb/P80746/entry","name":"ITGAV","description":"Integrin alpha-V","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4127","complexName":"ZFP-1(AF10)/DOT-1 complex","organismName":"Caenorhabditis elegans; 6239","description":"Histone methylation complex which preferentially methylates 'Lys-79' of histone H3 to modulate transcription. Part of a negative feedback mechanism opposing H2B ubiquitination and contributing to the pausing of transcription elongation by RNA polymerase II that occurs on essential genes widely expressed during development.","predictedComplex":false,"interactors":[{"ac":"EBI-21195283","identifier":"Q6AW06","identifierLink":"https://www.uniprot.org/uniprotkb/Q6AW06/entry","name":"dot-1.1","description":"Histone-lysine N-methyltransferase, H3 lysine-79 specific","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR21451","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6740300","identifier":"P34447","identifierLink":"https://www.uniprot.org/uniprotkb/P34447/entry","name":"zfp-1","description":"Zinc finger protein zfp-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13793","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4141","complexName":"NLRP3 inflammasome","organismName":"Homo sapiens; 9606","description":"A pro-inflammatory thiol protease complex that is activated by Gram-positive bacteria such as Staphylococcus aureus and Group B Streptococcus, viruses such as influenza virus, pore-forming toxins such as hemolysin and pneumolysin, as well as by endogenous ligands and crystalline substances such as ATP, silica, and alum. Primarily acts in monocytes and macrophages. \r\n\r\nNLRP3 activation is triggered by two sequential signals. The basal level of NLRP3 in macrophages is quite low. Before activation, NLRP3 needs to be “primed” by Toll-like receptor (TLR) agonists such as lipopolysaccharide (LPS). Activation of TLR signaling not only transcriptionally up-regulates NLRP3 expression, but also post-transcriptionally activates NLRP3 by phosphorylation and deubiquitination. The second step, defined as “activation,” can be induced by several potent stimuli such as pore-forming toxins, leading to the oligomerization of NLRP3 and the subsequent assembly of inflammasome.\r\n\r\nActivating platform for Caspase-1 (CPX-952) through proximity-induced self-cleavage in an ATP-dependent reaction.\r\n\r\nActivated Caspase-1 cleaves interleukins 1beta (IL1B, P01584) and IL18 (Q14116) releasing the mature cytokines which are involved in a variety of inflammatory processes and is also involved in pyroptosis of macrophages, a special case of cell death, associated with infection by intracellular pathogens where it cleaves GSDMD (P57764). \r\n\r\nActivation of NLRP3 inflammasome is also required for HMGB1 (P09429) secretion which stimulate inflammatory responses. \r\n\r\nIt belongs to the family of Inflammasomes that includes NLRP1 inflammasome (CPX-4082), NLRC4 inflammasome (CPX-4144), AIM2 inflammasome (CPX-4142) and Pyrin inflammasome (CPX-4143).\r\n\r\nThe expression of NLRP3 and PYCARD is up-regulated in adipocytes from obese patients. Elevation of NLRP3 inflammasome activity has been observed in myeloid cells of patients affected by type 2 diabetes. Moreover, animal models support a role of this complex in multiple sclerosis, Alzheimer's disease, Parkinson's disease, gout, Cryopyrin-associated periodic syndromes and atherosclerosis.","predictedComplex":false,"interactors":[{"ac":"EBI-516667","identifier":"P29466","identifierLink":"https://www.uniprot.org/uniprotkb/P29466/entry","name":"CASP1","description":"Caspase-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47901","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6253230","identifier":"Q96P20","identifierLink":"https://www.uniprot.org/uniprotkb/Q96P20/entry","name":"NLRP3","description":"NACHT, LRR and PYD domains-containing protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45690","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-751215","identifier":"Q9ULZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ULZ3/entry","name":"PYCARD","description":"Apoptosis-associated speck-like protein containing a CARD","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46985","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4142","complexName":"AIM2 inflammasome","organismName":"Homo sapiens; 9606","description":"A pro-inflammatory thiol protease complex that is activated by direct binding to cytosolic dsDNA, which may be encountered during pathogenic and viral infection or can be released upon loss of nuclear envelope integrity. It requires a dsDNA of at least 80base pairs for optimal activation. Primarily acts in monocytes and macrophages. \r\n\r\nActivating platform for Caspase-1 (CPX-952) through proximity-induced self-cleavage in an ATP-dependent reaction.\r\n\r\nActivated Caspase-1 cleaves interleukins 1beta (IL1B, P01584) and IL18 (Q14116) releasing the mature cytokines which are involved in a variety of inflammatory processes and is also involved in pyroptosis of macrophages, a special case of cell death, associated with infection by intracellular pathogens where it cleaves GSDMD (P57764). \r\n\r\nIt belongs to the family of Inflammasomes that includes NLRP1 inflammasome (CPX-4082), NLRP3 inflammasome (CPX-4141), NLRC4 inflammasome (CPX-4144) and Pyrin inflammasome (CPX-4143).\r\n\r\nAIM2 acts as a tumor suppressor.","predictedComplex":false,"interactors":[{"ac":"EBI-516667","identifier":"P29466","identifierLink":"https://www.uniprot.org/uniprotkb/P29466/entry","name":"CASP1","description":"Caspase-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47901","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6253193","identifier":"O14862","identifierLink":"https://www.uniprot.org/uniprotkb/O14862/entry","name":"AIM2","description":"Interferon-inducible protein AIM2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12200","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-751215","identifier":"Q9ULZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ULZ3/entry","name":"PYCARD","description":"Apoptosis-associated speck-like protein containing a CARD","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46985","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4143","complexName":"Pyrin inflammasome","organismName":"Homo sapiens; 9606","description":"A pro-inflammatory thiol protease complex that is up-regulated in response to inactivating modifications of Rho GTPases by various bacterial species (Clostridium difficile, Vibrio parahemolyticus, Clostridium botulinum, Burkholderia cenocepacia and Bordetella pertussis). Primarily acts in myeloid cells. \r\n\r\nActivating platform for Caspase-1 (CPX-952) through proximity-induced self-cleavage in an ATP-dependent reaction.\r\n\r\nActivated Caspase-1 cleaves interleukins 1beta (IL1B, P01584) and IL18 (Q14116) releasing the mature cytokines which are involved in a variety of inflammatory processes and is also involved in pyroptosis of macrophages, a special case of cell death, associated with infection by intracellular pathogens where it cleaves GSDMD (P57764). \r\n\r\nIt belongs to the family of Inflammasomes that includes NLRP1 inflammasome (CPX-4082), NLRP3 inflammasome (CPX-4141), NLRC4 inflammasome (CPX-4144) and AIM2 inflammasome (CPX-4142). \r\n\r\nMEFV/pyrin protein is associated to the Familial Mediterranean fever.","predictedComplex":false,"interactors":[{"ac":"EBI-516667","identifier":"P29466","identifierLink":"https://www.uniprot.org/uniprotkb/P29466/entry","name":"CASP1","description":"Caspase-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47901","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-751215","identifier":"Q9ULZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ULZ3/entry","name":"PYCARD","description":"Apoptosis-associated speck-like protein containing a CARD","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46985","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7644532","identifier":"O15553","identifierLink":"https://www.uniprot.org/uniprotkb/O15553/entry","name":"MEFV","description":"Pyrin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24103","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4144","complexName":"NLRC4 inflammasome","organismName":"Homo sapiens; 9606","description":"A pro-inflammatory thiol protease complex that acts as effective cytosolic surveillance to detect bacteria that bears flagella or/and a T3SS. Primarily acts in macrophages, monocytes and dendritic cells. \r\n\r\nActivating platform for Caspase-1 (CPX-952) through proximity-induced self-cleavage in an ATP-dependent reaction.\r\n\r\nActivated Caspase-1 cleaves interleukins 1beta (IL1B, P01584) and IL18 (Q14116) releasing the mature cytokines which are involved in a variety of inflammatory processes and is also involved in pyroptosis of macrophages, a special case of cell death, associated with infection by intracellular pathogens where it cleaves GSDMD (P57764). NLRC4 inflammasome also induces eicosanoid production. \r\n\r\nIt belongs to the family of Inflammasomes that includes NLRP1 inflammasome (CPX-4082), NLRP3 inflammasome (CPX-4141), pyrin inflammasome (CPX-4143) and AIM2 inflammasome (CPX-4142). \r\n\r\nGain-of-function mutations in NLRC4 as the cause of a syndrome of infantile enterocolitis and recurrent macrophage activation syndrome.","predictedComplex":false,"interactors":[{"ac":"EBI-1222527","identifier":"Q9NPP4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPP4/entry","name":"NLRC4","description":"NLR family CARD domain-containing protein 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47688","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2874875","identifier":"Q13075","identifierLink":"https://www.uniprot.org/uniprotkb/Q13075/entry","name":"NAIP","description":"Baculoviral IAP repeat-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46914","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-516667","identifier":"P29466","identifierLink":"https://www.uniprot.org/uniprotkb/P29466/entry","name":"CASP1","description":"Caspase-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47901","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-751215","identifier":"Q9ULZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ULZ3/entry","name":"PYCARD","description":"Apoptosis-associated speck-like protein containing a CARD","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46985","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4202","complexName":"GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA2 variant","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex that is predominately recruited to Ctcf (Q61164), Klf4 (Q60793) and Sp5-dependent targets sites, promoters and enhancers, depending on cell type. Targeted to chromatin, especially to H3K27ac, H3K4me1 and H3K4me3 markers, via by the bromo domain of its BRD9 subunit. Recruitment may be aided by Brd4 (Q9ESU6), especially in embryonic stem cells (ESC). \r\n\r\nActs predominantly as a transcriptional activator that regulates tissue development, cell differentiation and cell proliferation and maintains naive pluripotency in ESC.","predictedComplex":false,"interactors":[{"ac":"EBI-10765904","identifier":"Q6DIC0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6DIC0/entry","name":"Smarca2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16371163","identifier":"Q9CXE2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CXE2/entry","name":"Bcl7a","description":"B-cell CLL/lymphoma 7 protein family member A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21349117","identifier":"F8VPZ9","identifierLink":"https://www.uniprot.org/uniprotkb/F8VPZ9/entry","name":"Bicra","description":"BRD4-interacting chromatin-remodeling complex-associated protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15572","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2552901","identifier":"Q921K9","identifierLink":"https://www.uniprot.org/uniprotkb/Q921K9/entry","name":"Bcl7b","description":"B-cell CLL/lymphoma 7 protein family member B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942759","identifier":"Q9Z2N8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z2N8/entry","name":"Actl6a","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-309327","identifier":"Q62280","identifierLink":"https://www.uniprot.org/uniprotkb/Q62280/entry","name":"Ss18","description":"Protein SSXT","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23107","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371529","identifier":"Q61466","identifierLink":"https://www.uniprot.org/uniprotkb/Q61466/entry","name":"Smarcd1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-648047","identifier":"P97496","identifierLink":"https://www.uniprot.org/uniprotkb/P97496/entry","name":"Smarcc1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8459301","identifier":"O08664","identifierLink":"https://www.uniprot.org/uniprotkb/O08664/entry","name":"Bcl7c","description":"B-cell CLL/lymphoma 7 protein family member C","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9988701","identifier":"Q3UQU0","identifierLink":"https://www.uniprot.org/uniprotkb/Q3UQU0/entry","name":"Brd9","description":"Bromodomain-containing protein 9","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22881","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4203","complexName":"GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA2 variant","organismName":"Homo sapiens; 9606","description":"The SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, SMARCA2/BRM and SMARCA4/BRG1, do not co-occur in the same complex. It is unclear if the 3 BCL7 protein occur in the same complex or form further variants. \r\n\r\nMay contain 2 instances of subunit SMARCC1. \r\n\r\nClosely related to BICRA (GLTSCR1) variant (CPX-4084). Distinguished from the canonical SWI/SNF complexes by the inclusion of BCL7A/B/C, BICRAL, BRD9 and SS18 and lack of canonical core subunits ARID1A/B (O14497/Q8NFD5), DPF2 (Q92785), SMARCB1 (Q12824), or SMARCE1 (Q969G3).","predictedComplex":false,"interactors":[{"ac":"EBI-1012434","identifier":"Q6AI39","identifierLink":"https://www.uniprot.org/uniprotkb/Q6AI39/entry","name":"BICRAL","description":"BRD4-interacting chromatin-remodeling complex-associated protein-like","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15572","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10258305","identifier":"Q9H8M2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H8M2/entry","name":"BRD9","description":"Bromodomain-containing protein 9","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22881","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2560588","identifier":"Q9BQE9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BQE9/entry","name":"BCL7B","description":"B-cell CLL/lymphoma 7 protein family member B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2560599","identifier":"Q15532","identifierLink":"https://www.uniprot.org/uniprotkb/Q15532/entry","name":"SS18","description":"Protein SSXT","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23107","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355018","identifier":"O96019","identifierLink":"https://www.uniprot.org/uniprotkb/O96019/entry","name":"ACTL6A","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359917","identifier":"Q4VC05","identifierLink":"https://www.uniprot.org/uniprotkb/Q4VC05/entry","name":"BCL7A","description":"B-cell CLL/lymphoma 7 protein family member A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679562","identifier":"P51531","identifierLink":"https://www.uniprot.org/uniprotkb/P51531/entry","name":"SMARCA2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7850114","identifier":"Q8WUZ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WUZ0/entry","name":"BCL7C","description":"B-cell CLL/lymphoma 7 protein family member C","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4204","complexName":"GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA2 variant","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex that is predominately recruited to Ctcf (Q61164), Klf4 (Q60793) and Sp5-dependent targets sites, promoters and enhancers, depending on cell type. Targeted to chromatin, especially to H3K27ac, H3K4me1 and H3K4me3 markers, via by the bromo domain of its BRD9 subunit. Recruitment may be aided by Brd4 (Q9ESU6), especially in embryonic stem cells (ESC). \r\n\r\nActs predominantly as a transcriptional activator that regulates tissue development, cell differentiation and cell proliferation and maintains naive pluripotency in ESC.","predictedComplex":false,"interactors":[{"ac":"EBI-10765904","identifier":"Q6DIC0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6DIC0/entry","name":"Smarca2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16371163","identifier":"Q9CXE2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CXE2/entry","name":"Bcl7a","description":"B-cell CLL/lymphoma 7 protein family member A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21349600","identifier":"Q8CHH5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CHH5/entry","name":"Bicral","description":"BRD4-interacting chromatin-remodeling complex-associated protein-like","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15572","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2552901","identifier":"Q921K9","identifierLink":"https://www.uniprot.org/uniprotkb/Q921K9/entry","name":"Bcl7b","description":"B-cell CLL/lymphoma 7 protein family member B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942759","identifier":"Q9Z2N8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z2N8/entry","name":"Actl6a","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-309327","identifier":"Q62280","identifierLink":"https://www.uniprot.org/uniprotkb/Q62280/entry","name":"Ss18","description":"Protein SSXT","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23107","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371529","identifier":"Q61466","identifierLink":"https://www.uniprot.org/uniprotkb/Q61466/entry","name":"Smarcd1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-648047","identifier":"P97496","identifierLink":"https://www.uniprot.org/uniprotkb/P97496/entry","name":"Smarcc1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8459301","identifier":"O08664","identifierLink":"https://www.uniprot.org/uniprotkb/O08664/entry","name":"Bcl7c","description":"B-cell CLL/lymphoma 7 protein family member C","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9988701","identifier":"Q3UQU0","identifierLink":"https://www.uniprot.org/uniprotkb/Q3UQU0/entry","name":"Brd9","description":"Bromodomain-containing protein 9","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22881","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4206","complexName":"GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA4 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex that is predominately recruited to CTCF (P49711), KLF4 (O43474) and Sp5-dependent targets sites, promoters and enhancers, depending on cell type. Targeted to chromatin, especially to H3K27ac, H3K4me1 and H3K4me3 markers, via by the bromo domain of its BRD9 subunit. Recruitment may be aided by BRD4 (O60885), especially in embryonic stem cells (ESC). \r\n\r\nActs predominantly as a transcriptional activator that regulates tissue development, cell differentiation and cell proliferation and maintains naive pluripotency in ESC. \r\n\r\nMutation is several subunits are linked to various cancers. SS18-SSX fusion gene is a hallmark for synovial sarcoma and malignant rhabdoid tumour.","predictedComplex":false,"interactors":[{"ac":"EBI-10258305","identifier":"Q9H8M2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H8M2/entry","name":"BRD9","description":"Bromodomain-containing protein 9","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22881","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1754943","identifier":"Q9NZM4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZM4/entry","name":"BICRA","description":"BRD4-interacting chromatin-remodeling complex-associated protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15572","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2560588","identifier":"Q9BQE9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BQE9/entry","name":"BCL7B","description":"B-cell CLL/lymphoma 7 protein family member B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2560599","identifier":"Q15532","identifierLink":"https://www.uniprot.org/uniprotkb/Q15532/entry","name":"SS18","description":"Protein SSXT","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23107","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302489","identifier":"P51532","identifierLink":"https://www.uniprot.org/uniprotkb/P51532/entry","name":"SMARCA4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355018","identifier":"O96019","identifierLink":"https://www.uniprot.org/uniprotkb/O96019/entry","name":"ACTL6A","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359917","identifier":"Q4VC05","identifierLink":"https://www.uniprot.org/uniprotkb/Q4VC05/entry","name":"BCL7A","description":"B-cell CLL/lymphoma 7 protein family member A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7850114","identifier":"Q8WUZ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WUZ0/entry","name":"BCL7C","description":"B-cell CLL/lymphoma 7 protein family member C","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4207","complexName":"GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA4 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex that is predominately recruited to CTCF (P49711), KLF4 (O43474) and Sp5-dependent targets sites, promoters and enhancers, depending on cell type. Targeted to chromatin, especially to H3K27ac, H3K4me1 and H3K4me3 markers, via by the bromo domain of its BRD9 subunit. Recruitment may be aided by BRD4 (O60885), especially in embryonic stem cells (ESC). \r\n\r\nActs predominantly as a transcriptional activator that regulates tissue development, cell differentiation and cell proliferation and maintains naive pluripotency in ESC. \r\n\r\nMutation is several subunits are linked to various cancers. 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Responsible for generating the carboxyl terminus of the amyloid beta-protein (Abeta) from the amyloid protein precursor, APP (P05067).","predictedComplex":false,"interactors":[{"ac":"EBI-21396145","identifier":"P49810-PRO_0000025604","identifierLink":"https://www.uniprot.org/uniprotkb/P49810-PRO_0000025604/entry","name":"PSEN2","description":"Presenilin-2 CTF subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2606342","identifier":"P49810-PRO_0000025603","identifierLink":"https://www.uniprot.org/uniprotkb/P49810-PRO_0000025603/entry","name":"PSEN2","description":"Presenilin-2 NTF subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2606935","identifier":"Q96BI3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96BI3/entry","name":"APH1A","description":"Gamma-secretase subunit APH-1A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12889","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-998440","identifier":"Q92542","identifierLink":"https://www.uniprot.org/uniprotkb/Q92542/entry","name":"NCSTN","description":"Nicastrin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-998468","identifier":"Q9NZ42","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZ42/entry","name":"PSENEN","description":"Gamma-secretase subunit PEN-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16318","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4232","complexName":"Gamma-secretase complex, APH1B-PSEN2 variant","organismName":"Homo sapiens; 9606","description":"Integral membrane aspartyl protease which performs the intramembrane cleavage of integral membrane proteins such as Notch receptors, clearing the anchors of type-I membrane proteins left in the membrane after shedding of their ectodomain. 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Responsible for generating the carboxyl terminus of the amyloid beta-protein (Abeta) from the amyloid protein precursor, APP (P05067).","predictedComplex":false,"interactors":[{"ac":"EBI-21395953","identifier":"P49768-PRO_0000236055","identifierLink":"https://www.uniprot.org/uniprotkb/P49768-PRO_0000236055/entry","name":"PSEN1","description":"Presenilin-1 CTF12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2606326","identifier":"P49768-PRO_0000025591","identifierLink":"https://www.uniprot.org/uniprotkb/P49768-PRO_0000025591/entry","name":"PSEN1","description":"Presenilin-1 NTF subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2606497","identifier":"Q8WW43","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WW43/entry","name":"APH1B","description":"Gamma-secretase subunit APH-1B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12889","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-998440","identifier":"Q92542","identifierLink":"https://www.uniprot.org/uniprotkb/Q92542/entry","name":"NCSTN","description":"Nicastrin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-998468","identifier":"Q9NZ42","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZ42/entry","name":"PSENEN","description":"Gamma-secretase subunit PEN-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16318","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4234","complexName":"Gamma-secretase complex, Aph1a-Psen1 variant","organismName":"Mus musculus; 10090","description":"Integral membrane aspartyl protease which performs the intramembrane cleavage of integral membrane proteins such as Notch receptors, clearing the anchors of type-I membrane proteins left in the membrane after shedding of their ectodomain. 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Responsible for generating the carboxyl terminus of the amyloid beta-protein (Abeta) from the amyloid protein precursor, App (P12023).","predictedComplex":false,"interactors":[{"ac":"EBI-5260983","identifier":"P49769-PRO_0000025597","identifierLink":"https://www.uniprot.org/uniprotkb/P49769-PRO_0000025597/entry","name":"Psen1","description":"Presenilin-1 NTF subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-5260997","identifier":"P49769-PRO_0000025598","identifierLink":"https://www.uniprot.org/uniprotkb/P49769-PRO_0000025598/entry","name":"Psen1","description":"Presenilin-1 CTF subunit","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-7188432","identifier":"Q8BVF7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BVF7/entry","name":"Aph1a","description":"Gamma-secretase subunit APH-1A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12889","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-998934","identifier":"P57716","identifierLink":"https://www.uniprot.org/uniprotkb/P57716/entry","name":"Ncstn","description":"Nicastrin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-998974","identifier":"Q9CQR7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQR7/entry","name":"Psenen","description":"Gamma-secretase subunit PEN-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16318","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4235","complexName":"Gamma-secretase complex, Aph1b-Psen1 variant","organismName":"Mus musculus; 10090","description":"Integral membrane aspartyl protease which performs the intramembrane cleavage of integral membrane proteins such as Notch receptors, clearing the anchors of type-I membrane proteins left in the membrane after shedding of their ectodomain. Cleaves proteins consisting of a single hydrophobic transmembrane helix and with a remaining ectodomain of limited length. Responsible for generating the carboxyl terminus of the amyloid beta-protein (Abeta) from the amyloid protein precursor, App (P12023).","predictedComplex":false,"interactors":[{"ac":"EBI-21396320","identifier":"Q8C7N7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C7N7/entry","name":"Aph1b","description":"Gamma-secretase subunit APH-1B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12889","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5260983","identifier":"P49769-PRO_0000025597","identifierLink":"https://www.uniprot.org/uniprotkb/P49769-PRO_0000025597/entry","name":"Psen1","description":"Presenilin-1 NTF subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-5260997","identifier":"P49769-PRO_0000025598","identifierLink":"https://www.uniprot.org/uniprotkb/P49769-PRO_0000025598/entry","name":"Psen1","description":"Presenilin-1 CTF subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-998934","identifier":"P57716","identifierLink":"https://www.uniprot.org/uniprotkb/P57716/entry","name":"Ncstn","description":"Nicastrin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-998974","identifier":"Q9CQR7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQR7/entry","name":"Psenen","description":"Gamma-secretase subunit PEN-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16318","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4236","complexName":"Gamma-secretase complex, Aph1a-Psen2 variant","organismName":"Mus musculus; 10090","description":"Integral membrane aspartyl protease which performs the intramembrane cleavage of integral membrane proteins such as Notch receptors, clearing the anchors of type-I membrane proteins left in the membrane after shedding of their ectodomain. Cleaves proteins consisting of a single hydrophobic transmembrane helix and with a remaining ectodomain of limited length. Responsible for generating the carboxyl terminus of the amyloid beta-protein (Abeta) from the amyloid protein precursor, App (P12023).","predictedComplex":false,"interactors":[{"ac":"EBI-21396381","identifier":"Q61144-PRO_0000025607","identifierLink":"https://www.uniprot.org/uniprotkb/Q61144-PRO_0000025607/entry","name":"Psen2","description":"Presenilin-2 NTF subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-21396390","identifier":"Q61144-PRO_0000025608","identifierLink":"https://www.uniprot.org/uniprotkb/Q61144-PRO_0000025608/entry","name":"Psen2","description":"Presenilin-2 CTF subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-7188432","identifier":"Q8BVF7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BVF7/entry","name":"Aph1a","description":"Gamma-secretase subunit APH-1A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12889","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-998934","identifier":"P57716","identifierLink":"https://www.uniprot.org/uniprotkb/P57716/entry","name":"Ncstn","description":"Nicastrin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-998974","identifier":"Q9CQR7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQR7/entry","name":"Psenen","description":"Gamma-secretase subunit PEN-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16318","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4237","complexName":"Gamma-secretase complex, Aph1b-Psen2 variant","organismName":"Mus musculus; 10090","description":"Integral membrane aspartyl protease which performs the intramembrane cleavage of integral membrane proteins such as Notch receptors, clearing the anchors of type-I membrane proteins left in the membrane after shedding of their ectodomain. Cleaves proteins consisting of a single hydrophobic transmembrane helix and with a remaining ectodomain of limited length. Responsible for generating the carboxyl terminus of the amyloid beta-protein (Abeta) from the amyloid protein precursor, App (P12023).","predictedComplex":false,"interactors":[{"ac":"EBI-21396320","identifier":"Q8C7N7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C7N7/entry","name":"Aph1b","description":"Gamma-secretase subunit APH-1B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12889","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21396381","identifier":"Q61144-PRO_0000025607","identifierLink":"https://www.uniprot.org/uniprotkb/Q61144-PRO_0000025607/entry","name":"Psen2","description":"Presenilin-2 NTF subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-21396390","identifier":"Q61144-PRO_0000025608","identifierLink":"https://www.uniprot.org/uniprotkb/Q61144-PRO_0000025608/entry","name":"Psen2","description":"Presenilin-2 CTF subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-998934","identifier":"P57716","identifierLink":"https://www.uniprot.org/uniprotkb/P57716/entry","name":"Ncstn","description":"Nicastrin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-998974","identifier":"Q9CQR7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQR7/entry","name":"Psenen","description":"Gamma-secretase subunit PEN-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16318","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4241","complexName":"NLRP3 inflammasome","organismName":"Mus musculus; 10090","description":"A pro-inflammatory thiol protease complex that is activated by Gram-positive bacteria such as Staphylococcus aureus and Group B Streptococcus, viruses such as influenza virus, pore-forming toxins such as hemolysin and pneumolysin, as well as by endogenous ligands and crystalline substances such as ATP, silica, and alum. Primarily acts in monocytes and macrophages. \r\n\r\nNlrp3 activation is triggered by two sequential signals. The basal level of Nlrp3 in macrophages is quite low. Before activation, Nlrp3 needs to be “primed” by Toll-like receptor (TLR) agonists such as lipopolysaccharide (LPS). Activation of TLR signaling not only transcriptionally up-regulates Nlrp3 expression, but also post-transcriptionally activates Nlrp3 by phosphorylation and deubiquitination. The second step, defined as “activation,” can be induced by several potent stimuli such as pore-forming toxins, leading to the oligomerization of Nlrp3 and the subsequent assembly of inflammasome.\r\n\r\nActivating platform for Caspase-1 (CPX-4242) through proximity-induced self-cleavage in an ATP-dependent reaction.\r\n\r\nActivated Caspase-1 cleaves interleukins 1beta (Il1b, P10749) and Il18 (P70380) releasing the mature cytokines which are involved in a variety of inflammatory processes and is also involved in pyroptosis of macrophages, a special case of cell death, associated with infection by intracellular pathogens where it cleaves Gsdmdc1 (Q9D8T2). \r\n\r\nActivation of NLRP3 inflammasome is also required for Hmgb1 (P63158) secretion which stimulate inflammatory responses. \r\n\r\nIt belongs to the family of Inflammasomes that includes NLRP1 inflammasome (CPX-4261, CPX-4266, CPX-4269, CPX-4270 and CPX-4271), NLRC4 inflammasome, AIM2 inflammasome (CPX-4243) and Pyrin inflammasome (CPX-4244).","predictedComplex":false,"interactors":[{"ac":"EBI-489700","identifier":"P29452","identifierLink":"https://www.uniprot.org/uniprotkb/P29452/entry","name":"Casp1","description":"Caspase-1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR47901","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6253348","identifier":"Q9EPB4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9EPB4/entry","name":"Pycard","description":"Apoptosis-associated speck-like protein containing a CARD","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46985","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6910832","identifier":"Q8R4B8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R4B8/entry","name":"Nlrp3","description":"NACHT, LRR and PYD domains-containing protein 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45690","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4242","complexName":"Caspase-1 complex","organismName":"Mus musculus; 10090","description":"A pro-inflammatory thiol protease complex that is activated in response to pathogen infections and toxins. Primarily acts in monocytes and macrophages. \r\n\r\nActivation by autocatalytic cleavage is an ATP-dependent reaction and occurs within an activation platform, the Inflammasome (CPX-4241, CPX-4243, CPX-4244, CPX-4261, CPX-4266, CPX-4269, CPX-4270 and CPX-4271). \r\n\r\nOnce activated, it has a strict requirement for an Asp residue at position P1 and preferred cleavage sequence of Asp-Glu-Val-Asp-|-. It cleaves interleukins 1beta (Il1b, P10749) and Il18 (P70380) between an Asp and an Ala, releasing the mature cytokines which are involved in a variety of inflammatory processes. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Related to, but independent of, Il1b activation it is also involved in pyroptosis of macrophages, a special case of cell death, associated with infection by intracellular pathogens where it cleaves Gsdmdc1 (Q9D8T2). However, as a side effect of pyroptosis active Il1b is often released form the dead cells and therefore some link exists between both activities. While primarily a pro-inflammatory caspase it can also promote apoptosis in non-immune cells, especially in response to brain, kidney and renal cell injury.\r\n\r\nCaspase-1-deficient mice are protected from several acute and chronic inflammatory diseases, including sepsis and colitis.","predictedComplex":false,"interactors":[{"ac":"EBI-21399534","identifier":"P29452-PRO_0000004526","identifierLink":"https://www.uniprot.org/uniprotkb/P29452-PRO_0000004526/entry","name":"Casp1","description":"Caspase-1 subunit p20","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-21399550","identifier":"P29452-PRO_0000004528","identifierLink":"https://www.uniprot.org/uniprotkb/P29452-PRO_0000004528/entry","name":"Casp1","description":"Caspase-1 subunit p10","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-4243","complexName":"AIM2 inflammasome","organismName":"Mus musculus; 10090","description":"A pro-inflammatory thiol protease complex that is activated by direct binding to cytosolic dsDNA, which may be encountered during pathogenic and viral infection or can be released upon loss of nuclear envelope integrity. It requires a dsDNA of at least 80base pairs for optimal activation. Primarily acts in monocytes and macrophages. \r\n\r\nActivating platform for Caspase-1 (CPX-4242) through proximity-induced self-cleavage in an ATP-dependent reaction.\r\n\r\nActivated Caspase-1 cleaves interleukins 1beta (Il1b, P10749) and Il18 (P70380) releasing the mature cytokines which are involved in a variety of inflammatory processes and is also involved in pyroptosis of macrophages, a special case of cell death, associated with infection by intracellular pathogens where it cleaves Gsdmdc1 (Q9D8T2). \r\n\r\nIt belongs to the family of Inflammasomes that includes NLRP1 inflammasome (CPX-4261, CPX-4266, CPX-4269, CPX-4270 and CPX-4271), NLRP3 inflammasome (CPX-4241), NLRC4 inflammasome and Pyrin inflammasome (CPX-4244).","predictedComplex":false,"interactors":[{"ac":"EBI-489700","identifier":"P29452","identifierLink":"https://www.uniprot.org/uniprotkb/P29452/entry","name":"Casp1","description":"Caspase-1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR47901","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6253348","identifier":"Q9EPB4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9EPB4/entry","name":"Pycard","description":"Apoptosis-associated speck-like protein containing a CARD","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46985","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6253384","identifier":"Q91VJ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q91VJ1/entry","name":"Aim2","description":"Interferon-inducible protein AIM2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12200","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4244","complexName":"Pyrin inflammasome","organismName":"Mus musculus; 10090","description":"A pro-inflammatory thiol protease complex that is up-regulated in response to inactivating modifications of Rho GTPases by various bacterial species (Clostridium difficile, Vibrio parahemolyticus, Clostridium botulinum, Burkholderia cenocepacia and Bordetella pertussis). Primarily acts in myeloid cells. \r\n\r\nActivating platform for Caspase-1 (CPX-4242) through proximity-induced self-cleavage in an ATP-dependent reaction.\r\n\r\nActivated Caspase-1 cleaves interleukins 1beta (Il1b, P10749) and Il18 (P70380) releasing the mature cytokines which are involved in a variety of inflammatory processes and is also involved in pyroptosis of macrophages, a special case of cell death, associated with infection by intracellular pathogens where it cleaves Gsdmdc1 (Q9D8T2). \r\n\r\nIt belongs to the family of Inflammasomes that includes NLRP1 inflammasome (CPX-4261, CPX-4266, CPX-4269, CPX-4270 and CPX-4271), NLRP3 inflammasome (CPX-4241), NLRC4 inflammasome and AIM2 inflammasome (CPX-4243).","predictedComplex":false,"interactors":[{"ac":"EBI-21400351","identifier":"Q9JJ26","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JJ26/entry","name":"Mefv","description":"Pyrin","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24103","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-489700","identifier":"P29452","identifierLink":"https://www.uniprot.org/uniprotkb/P29452/entry","name":"Casp1","description":"Caspase-1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR47901","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6253348","identifier":"Q9EPB4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9EPB4/entry","name":"Pycard","description":"Apoptosis-associated speck-like protein containing a CARD","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46985","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4261","complexName":"NLRP1b inflammasome, allele-1 variant","organismName":"Mus musculus; 10090","description":"A pro-inflammatory thiol protease complex that is activated in response to pathogen infections and toxins such as anthrax lethal toxin and T. gondii infection and ATP depletion. Primarily acts in monocytes and macrophages. \r\n\r\nActivating platform for Caspase-1 (CPX-4242) through proximity-induced self-cleavage in an ATP-dependent reaction. \r\n\r\nActivated Caspase-1 cleaves interleukins 1beta (Il1b, P10749) and Il18 (P70380) releasing the mature cytokines which are involved in a variety of inflammatory processes and is also involved in pyroptosis of macrophages, a special case of cell death, associated with infection by intracellular pathogens where it cleaves Gsdmdc1 (Q9D8T2). \r\n\r\nIt belongs to the family of Inflammasomes that includes NLRP3 inflammasome (CPX-4241), NLRC4 inflammasome, AIM2 inflammasome (CPX-4243) and Pyrin inflammasome (CPX-4244).","predictedComplex":false,"interactors":[{"ac":"EBI-489700","identifier":"P29452","identifierLink":"https://www.uniprot.org/uniprotkb/P29452/entry","name":"Casp1","description":"Caspase-1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR47901","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9986823","identifier":"Q2LKW6","identifierLink":"https://www.uniprot.org/uniprotkb/Q2LKW6/entry","name":"Nlrp1b","description":"NACHT, LRR and PYD domains-containing protein 1b allele 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-4262","complexName":"LolCDE lipoprotein ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"Mediates the detachment of outer membrane-specific lipoproteins from the inner membrane. The recognition of lipoproteins by LolC and/or LolE occurs on the periplasmic side of the inner membrane. LolD hydrolyses ATP on the cytoplasmic side of the inner membrane providing the driving force for the release reaction. Member of a small subclass of eukaryote-type (EK-type) ABC transporters that uses mechano-transmission to perform work in the periplasm rather than for transmembrane transport.","predictedComplex":false,"interactors":[{"ac":"EBI-1125190","identifier":"P75958","identifierLink":"https://www.uniprot.org/uniprotkb/P75958/entry","name":"lolE","description":"Lipoprotein-releasing system transmembrane protein LolE","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30489","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15765497","identifier":"P0ADC3","identifierLink":"https://www.uniprot.org/uniprotkb/P0ADC3/entry","name":"lolC","description":"Lipoprotein-releasing system transmembrane protein LolC","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30489","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9136263","identifier":"P75957","identifierLink":"https://www.uniprot.org/uniprotkb/P75957/entry","name":"lolD","description":"Lipoprotein-releasing system ATP-binding protein LolD","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR24220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4263","complexName":"AcrAB-TolC multidrug efflux transport complex","organismName":"Escherichia coli (strain K12); 83333","description":"Responsible for the transport of xenobiotics, such as drugs, out of the cell, in particular from the periplasm.  Single-component efflux transporters remove toxic compounds from the cytoplasm to the periplasmic space where tolC-dependent transporters expel them from the cell. Capable of recognizing a wide range of dissimilar lipophilic and amphiphilic substrates that may differ in structure, size or electrical charge. These include beta-lactams, quinolones, tetracyclines, chloramphenicol and steroid hormones. Substrate specificity is conferred by a pair of large periplasmic loops containing more than 300 amino acid residues each. Member of the Resistance-Nodulation-Division (RND) family of efflux pumps.","predictedComplex":false,"interactors":[{"ac":"EBI-551006","identifier":"P31224","identifierLink":"https://www.uniprot.org/uniprotkb/P31224/entry","name":"acrB","description":"Multidrug efflux pump subunit AcrB","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32063","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-875601","identifier":"P0AE06","identifierLink":"https://www.uniprot.org/uniprotkb/P0AE06/entry","name":"acrA","description":"Multidrug efflux pump subunit AcrA","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30158","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-875614","identifier":"P02930","identifierLink":"https://www.uniprot.org/uniprotkb/P02930/entry","name":"tolC","description":"Outer membrane protein TolC","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4264","complexName":"AcrAD-TolC multidrug efflux transport complex","organismName":"Escherichia coli (strain K12); 83333","description":"Responsible for the transport of xenobiotics, such as drugs, out of the cell, in particular from the periplasm. Single-component efflux transporters remove toxic compounds from the cytoplasm to the periplasmic space where tolC-dependent transporters expel them from the cell. Transports hydrophilic substrates such as aminoglycosides and negatively charged beta-lactams. Substrate specificity is conferred by a pair of large periplasmic loops containing more than 300 amino acid residues each. Member of the Resistance-Nodulation-Division (RND) family of efflux pumps.","predictedComplex":false,"interactors":[{"ac":"EBI-548178","identifier":"P24177","identifierLink":"https://www.uniprot.org/uniprotkb/P24177/entry","name":"acrD","description":"Probable aminoglycoside efflux pump","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32063","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-875601","identifier":"P0AE06","identifierLink":"https://www.uniprot.org/uniprotkb/P0AE06/entry","name":"acrA","description":"Multidrug efflux pump subunit AcrA","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30158","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-875614","identifier":"P02930","identifierLink":"https://www.uniprot.org/uniprotkb/P02930/entry","name":"tolC","description":"Outer membrane protein TolC","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4265","complexName":"AcrEF-TolC multidrug efflux transport complex","organismName":"Escherichia coli (strain K12); 83333","description":"Responsible for the transport of xenobiotics, such as drugs, out of the cell, in particular from the periplasm. Single-component efflux transporters remove toxic compounds from the cytoplasm to the periplasmic space where tolC-dependent transporters expel them from the cell. Transports acriflavines and indoles. Member of the Resistance-Nodulation-Division (RND) family of efflux pumps. Expression of this system is generally low but it appears to be up-regulated when expression of AcrAB-TolC (CPX-4263) is impaired or in the presence of specific classes of xenobiotic.","predictedComplex":false,"interactors":[{"ac":"EBI-21406727","identifier":"P24180","identifierLink":"https://www.uniprot.org/uniprotkb/P24180/entry","name":"acrE","description":"Multidrug export protein AcrE","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30158","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-559218","identifier":"P24181","identifierLink":"https://www.uniprot.org/uniprotkb/P24181/entry","name":"acrF","description":"Multidrug export protein AcrF","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32063","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-875614","identifier":"P02930","identifierLink":"https://www.uniprot.org/uniprotkb/P02930/entry","name":"tolC","description":"Outer membrane protein TolC","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4266","complexName":"NLRP1b inflammasome, allele-2 variant","organismName":"Mus musculus; 10090","description":"A pro-inflammatory thiol protease complex that is activated in response to pathogen infections and toxins such as T. gondii infection. Primarily acts in monocytes and macrophages. \r\n\r\nActivating platform for Caspase-1 (CPX-4242) through proximity-induced self-cleavage in an ATP-dependent reaction. \r\n\r\nActivated Caspase-1 cleaves interleukins 1beta (Il1b, P10749) and Il18 (P70380) releasing the mature cytokines which are involved in a variety of inflammatory processes and is also involved in pyroptosis of macrophages, a special case of cell death, associated with infection by intracellular pathogens where it cleaves Gsdmdc1 (Q9D8T2). \r\n\r\nIt belongs to the family of Inflammasomes that includes NLRP3 inflammasome (CPX-4241), NLRC4 inflammasome, AIM2 inflammasome (CPX-4243) and Pyrin inflammasome (CPX-4244).","predictedComplex":false,"interactors":[{"ac":"EBI-21406909","identifier":"A1Z198","identifierLink":"https://www.uniprot.org/uniprotkb/A1Z198/entry","name":"Nlrp1b","description":"NACHT, LRR and PYD domains-containing protein 1b allele 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46985","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-489700","identifier":"P29452","identifierLink":"https://www.uniprot.org/uniprotkb/P29452/entry","name":"Casp1","description":"Caspase-1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR47901","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4268","complexName":"EmrAB-TolC multidrug efflux transport system","organismName":"Escherichia coli (strain K12); 83333","description":"Responsible for the transport of xenobiotics, such as drugs, out of the cell, in particular from the periplasm. Single-component efflux transporters remove toxic compounds from the cytoplasm to the periplasmic space where tolC-dependent transporters expel them from the cell. Responsible for the extrusion of hydrophobic xenobiotics such as carbonyl cyanide m-chlorophenyl-hydrazone (CCCP) and steroid hormones. Member of the major facilitator superfamily (MFS).","predictedComplex":false,"interactors":[{"ac":"EBI-1119547","identifier":"P27303","identifierLink":"https://www.uniprot.org/uniprotkb/P27303/entry","name":"emrA","description":"Multidrug export protein EmrA","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30386","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21407519","identifier":"P0AEJ0","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEJ0/entry","name":"emrB","description":"Multidrug export protein EmrB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR23501","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-875614","identifier":"P02930","identifierLink":"https://www.uniprot.org/uniprotkb/P02930/entry","name":"tolC","description":"Outer membrane protein TolC","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4269","complexName":"NLRP1b inflammasome, allele-3 variant","organismName":"Mus musculus; 10090","description":"A pro-inflammatory thiol protease complex that is activated in response to unknown stimuli. Primarily acts in monocytes and macrophages. \r\n\r\nActivating platform for Caspase-1 (CPX-4242) through proximity-induced self-cleavage in an ATP-dependent reaction. \r\n\r\nActivated Caspase-1 cleaves interleukins 1beta (Il1b, P10749) and Il18 (P70380) releasing the mature cytokines which are involved in a variety of inflammatory processes and is also involved in pyroptosis of macrophages, a special case of cell death, associated with infection by intracellular pathogens where it cleaves Gsdmdc1 (Q9D8T2). \r\n\r\nIt belongs to the family of Inflammasomes that includes NLRP3 inflammasome (CPX-4241), NLRC4 inflammasome, AIM2 inflammasome (CPX-4243) and Pyrin inflammasome (CPX-4244).","predictedComplex":false,"interactors":[{"ac":"EBI-21407005","identifier":"Q2LKV5","identifierLink":"https://www.uniprot.org/uniprotkb/Q2LKV5/entry","name":"Nlrp1b","description":"NACHT, LRR and PYD domains-containing protein 1b allele 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-489700","identifier":"P29452","identifierLink":"https://www.uniprot.org/uniprotkb/P29452/entry","name":"Casp1","description":"Caspase-1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR47901","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4270","complexName":"NLRP1b inflammasome, allele-5 variant","organismName":"Mus musculus; 10090","description":"A pro-inflammatory thiol protease complex that is activated in response to pathogen infections and toxins such as anthrax lethal toxin. Primarily acts in monocytes and macrophages. \r\n\r\nActivating platform for Caspase-1 (CPX-4242) through proximity-induced self-cleavage in an ATP-dependent reaction. \r\n\r\nActivated Caspase-1 cleaves interleukins 1beta (Il1b, P10749) and Il18 (P70380) releasing the mature cytokines which are involved in a variety of inflammatory processes and is also involved in pyroptosis of macrophages, a special case of cell death, associated with infection by intracellular pathogens where it cleaves Gsdmdc1 (Q9D8T2). \r\n\r\nIt belongs to the family of Inflammasomes that includes NLRP3 inflammasome (CPX-4241), NLRC4 inflammasome, AIM2 inflammasome (CPX-4243) and Pyrin inflammasome (CPX-4244).","predictedComplex":false,"interactors":[{"ac":"EBI-21407122","identifier":"Q0GKD5","identifierLink":"https://www.uniprot.org/uniprotkb/Q0GKD5/entry","name":"Nlrp1b","description":"NACHT, LRR and PYD domains-containing protein 1b allele 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-489700","identifier":"P29452","identifierLink":"https://www.uniprot.org/uniprotkb/P29452/entry","name":"Casp1","description":"Caspase-1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR47901","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4271","complexName":"NLRP1a inflammasome","organismName":"Mus musculus; 10090","description":"A pro-inflammatory thiol protease complex that is activated in response to unknown stimuli. Primarily acts in monocytes and macrophages. \r\n\r\nActivating platform for Caspase-1 (CPX-4242) through proximity-induced self-cleavage in an ATP-dependent reaction. \r\n\r\nActivated Caspase-1 cleaves interleukins 1beta (Il1b, P10749) and Il18 (P70380) releasing the mature cytokines which are involved in a variety of inflammatory processes and is also involved in pyroptosis of macrophages, a special case of cell death, associated with infection by intracellular pathogens where it cleaves Gsdmdc1 (Q9D8T2). \r\n\r\nIt belongs to the family of Inflammasomes that includes NLRP3 inflammasome (CPX-4241), NLRC4 inflammasome, AIM2 inflammasome (CPX-4243) and Pyrin inflammasome (CPX-4244).","predictedComplex":false,"interactors":[{"ac":"EBI-21407204","identifier":"Q2LKU9","identifierLink":"https://www.uniprot.org/uniprotkb/Q2LKU9/entry","name":"Nlrp1a","description":"NACHT, LRR and PYD domains-containing protein 1a","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46985","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-489700","identifier":"P29452","identifierLink":"https://www.uniprot.org/uniprotkb/P29452/entry","name":"Casp1","description":"Caspase-1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR47901","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2119","complexName":"MdtABC-TolC multidrug efflux transport complex","organismName":"Escherichia coli (strain K12); 83333","description":"Responsible for the transport of xenobiotics, such as drugs, out of the cell, in particular from the periplasm. Single-component efflux transporters remove toxic compounds from the cytoplasm to the periplasmic space where tolC-dependent transporters expel them from the cell. Responsible for the extrusion of xenobiotics such as novobiocin, bile salts, quinolones, fosfomycin, detergents, zinc and myricetin.","predictedComplex":false,"interactors":[{"ac":"EBI-1116694","identifier":"P76399","identifierLink":"https://www.uniprot.org/uniprotkb/P76399/entry","name":"mdtC","description":"Multidrug resistance protein MdtC","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32063","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21407281","identifier":"P76397","identifierLink":"https://www.uniprot.org/uniprotkb/P76397/entry","name":"mdtA","description":"Multidrug resistance protein MdtA","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30469","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-561416","identifier":"P76398","identifierLink":"https://www.uniprot.org/uniprotkb/P76398/entry","name":"mdtB","description":"Multidrug resistance protein MdtB","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32063","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-875614","identifier":"P02930","identifierLink":"https://www.uniprot.org/uniprotkb/P02930/entry","name":"tolC","description":"Outer membrane protein TolC","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4273","complexName":"EmrKY-TolC multidrug efflux transport system","organismName":"Escherichia coli (strain K12); 83333","description":"Responsible for the transport of xenobiotics, such as drugs, out of the cell, in particular from the periplasm. Single-component efflux transporters remove toxic compounds from the cytoplasm to the periplasmic space where tolC-dependent transporters expel them from the cell. Member of the major facilitator superfamily (MFS). Play an important role in the antibiotic resistance during biofilm formation and expression of both proteins is induced by antibiotics such as tetracycline.","predictedComplex":false,"interactors":[{"ac":"EBI-21418850","identifier":"P52599","identifierLink":"https://www.uniprot.org/uniprotkb/P52599/entry","name":"emrK","description":"Probable multidrug resistance protein EmrK","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30386","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-551374","identifier":"P52600","identifierLink":"https://www.uniprot.org/uniprotkb/P52600/entry","name":"emrY","description":"Probable multidrug resistance protein EmrY","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR23501","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-875614","identifier":"P02930","identifierLink":"https://www.uniprot.org/uniprotkb/P02930/entry","name":"tolC","description":"Outer membrane protein TolC","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4281","complexName":"PaoABC periplasmic aldehyde oxidoreductase","organismName":"Escherichia coli (strain K12); 83333","description":"A periplasmic aldehyde oxidoreductase that oxidises aldehydes to the corresponding carboxylic acids. Preferentially detoxifies aromatic aldehydes, excluding purines. At high doses, aromatic aldehydes can act as antimicrobial agents.","predictedComplex":false,"interactors":[{"ac":"EBI-1115437","identifier":"P77489","identifierLink":"https://www.uniprot.org/uniprotkb/P77489/entry","name":"paoC","description":"Aldehyde oxidoreductase molybdenum-binding subunit PaoC","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11908","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1115552","identifier":"P77324","identifierLink":"https://www.uniprot.org/uniprotkb/P77324/entry","name":"paoB","description":"Aldehyde oxidoreductase FAD-binding subunit PaoB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42659","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1115563","identifier":"P77165","identifierLink":"https://www.uniprot.org/uniprotkb/P77165/entry","name":"paoA","description":"Aldehyde oxidoreductase iron-sulfur-binding subunit PaoA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR45331","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11172266","identifier":"CHEBI:49601","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49601","name":"fe2s2 iron-sulfur cluster","description":"Fe2S2 iron-sulfur cluster","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-21444506","identifier":"CHEBI:71308","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:71308","name":"mo(vi)-molybdopterin cytosine dinucleotide(2-)","description":"Mo(VI)-molybdopterin cytosine dinucleotide(2-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-4284","complexName":"RbsABC ribose ABC transporter","organismName":"Escherichia coli (strain K12); 83333","description":"Required for the high affinity uptake of ribose, the molecular precursor for nucleic acid synthesis. Member of the ATP-binding cassette (ABC) transporter family, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1132449","identifier":"P04983","identifierLink":"https://www.uniprot.org/uniprotkb/P04983/entry","name":"rbsA","description":"Ribose import ATP-binding protein RbsA","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43790","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21444614","identifier":"P0AGI1","identifierLink":"https://www.uniprot.org/uniprotkb/P0AGI1/entry","name":"rbsC","description":"Ribose import permease protein RbsC","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32196","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-369930","identifier":"P02925","identifierLink":"https://www.uniprot.org/uniprotkb/P02925/entry","name":"rbsB","description":"Ribose import binding protein RbsB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR46847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4286","complexName":"Ferric-hydroxamate ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"Imports various ferric (Fe3+) hyroxamates such as coprogen or ferrichrome from the periplasm across the cytoplasmic membrane. Iron hydroxamates are transferred from fhuD to fhuB,  then translocates across the cytoplasmic membrane energized by fhuC-catalyzed ATP hydrolysis, which induces a conformational change in fhuB. Member of the ATP-binding cassette (ABC) transporter family, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1114151","identifier":"P07821","identifierLink":"https://www.uniprot.org/uniprotkb/P07821/entry","name":"fhuC","description":"Iron(3+)-hydroxamate import ATP-binding protein FhuC","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42771","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1114168","identifier":"P07822","identifierLink":"https://www.uniprot.org/uniprotkb/P07822/entry","name":"fhuD","description":"Iron(3+)-hydroxamate-binding protein FhuD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30532","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-553636","identifier":"P06972","identifierLink":"https://www.uniprot.org/uniprotkb/P06972/entry","name":"fhuB","description":"Iron(3+)-hydroxamate import system permease protein FhuB","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30472","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4301","complexName":"M-Calpain complex","organismName":"Mus musculus; 10090","description":"A calcium-dependent protease complex that processes the substrate by limited proteolysis rather than degrading it. In some cases the proteolytic action activates the substrate, for example, it cleaves Cdk5r1/p35 (P61809) into its p25 form that is associated with Alzheimer's disease in human. Involved in cytoskeletal remodeling, signal transduction and implicated in cell cycle regulation and apoptosis. Finely-balanced calpain homeostasis is required as both over and under-activation causes disease. Calpain complexes recognise their substrates based on a short peptide sequence. Inhibited by the intrinsically-unstructured calpastatin (P51125) by its tight binding to the calpain catalytic subunit.","predictedComplex":false,"interactors":[{"ac":"EBI-643151","identifier":"O08529","identifierLink":"https://www.uniprot.org/uniprotkb/O08529/entry","name":"Capn2","description":"Calpain-2 catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10183","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8319447","identifier":"O88456","identifierLink":"https://www.uniprot.org/uniprotkb/O88456/entry","name":"Capns1","description":"Calpain small subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46735","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4302","complexName":"mu-Calpain complex","organismName":"Homo sapiens; 9606","description":"A calcium-dependent protease complex that processes the substrate by limited proteolysis rather than degrading it. In some cases the proteolytic action activates the substrate, for example, it cleaves CDK5R1/p35 (Q15078) into its p25 form that is associated with Alzheimer's disease. Involved in cytoskeletal remodeling, signal transduction and implicated in cell cycle regulation and apoptosis. Finely-balanced calpain homeostasis is required as both over and under-activation causes disease. Calpain complexes recognise their substrates based on a short peptide sequence. Inhibited by the intrinsically-unstructured calpastatin (P20810) by its tight binding to the calpain catalytic subunit.","predictedComplex":false,"interactors":[{"ac":"EBI-1542113","identifier":"P07384","identifierLink":"https://www.uniprot.org/uniprotkb/P07384/entry","name":"CAPN1","description":"Calpain-1 catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10183","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-711828","identifier":"P04632","identifierLink":"https://www.uniprot.org/uniprotkb/P04632/entry","name":"CAPNS1","description":"Calpain small subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46735","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4304","complexName":"mu-Calpain complex","organismName":"Mus musculus; 10090","description":"A calcium-dependent protease complex that processes the substrate by limited proteolysis rather than degrading it. In some cases the proteolytic action activates the substrate, for example, it cleaves Cdk5r1/p35 (P61809) into its p25 form that is associated with Alzheimer's disease in human. Involved in cytoskeletal remodeling, signal transduction and implicated in cell cycle regulation and apoptosis. Finely-balanced calpain homeostasis is required as both over and under-activation causes disease. Calpain complexes recognise their substrates based on a short peptide sequence. Inhibited by the intrinsically-unstructured calpastatin (P51125) by its tight binding to the calpain catalytic subunit.","predictedComplex":false,"interactors":[{"ac":"EBI-6674024","identifier":"O35350","identifierLink":"https://www.uniprot.org/uniprotkb/O35350/entry","name":"Capn1","description":"Calpain-1 catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10183","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8319447","identifier":"O88456","identifierLink":"https://www.uniprot.org/uniprotkb/O88456/entry","name":"Capns1","description":"Calpain small subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46735","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4305","complexName":"DHIC complex","organismName":"Caenorhabditis elegans; 6239","description":"Inhibitory complex which modulates longevity by sequestering the heat-shock transcription factor hsf-1 to negatively regulate its binding to DNA and transcriptional activity. Phosphorylation of ddl-1, possibly by the insulin/IGF-1-like signalling (IIS) pathway, promotes the dissociation of the complex and activates the hsf-1-induced transcription of stress response and longevity genes.","predictedComplex":false,"interactors":[{"ac":"EBI-2916699","identifier":"G5EFT5","identifierLink":"https://www.uniprot.org/uniprotkb/G5EFT5/entry","name":"hsf-1","description":"Heat shock transcription factor hsf-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10015","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-311898","identifier":"Q9U3B7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9U3B7/entry","name":"hsb-1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR19424","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-313368","identifier":"O18195","identifierLink":"https://www.uniprot.org/uniprotkb/O18195/entry","name":"ddl-2","description":"WASH complex subunit homolog 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR23331","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-323542","identifier":"O01901","identifierLink":"https://www.uniprot.org/uniprotkb/O01901/entry","name":"ddl-1","description":"WASH complex subunit homolog 3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13015","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4306","complexName":"PETISCO, pid-1 variant","organismName":"Caenorhabditis elegans; 6239","description":"Involved in the processing of substrate RNAs in the gene silencing pathway. When bound to pid-1, it is specifically required for the biogenesis of 21U RNAs, which are a class of 21 nucleotide piRNAs that possess a uracil residue at the 5-prime end. pid-1 is required for stabilising 21U precursor RNA molecules, whilst ife-3 is required for the interaction with capped 21U precursor RNA molecules.","predictedComplex":false,"interactors":[{"ac":"EBI-2001908","identifier":"Q09293","identifierLink":"https://www.uniprot.org/uniprotkb/Q09293/entry","name":"tofu-6","description":"Embryonic developmental protein tofu-6","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-21447087","identifier":"Q20057","identifierLink":"https://www.uniprot.org/uniprotkb/Q20057/entry","name":"erh-2","description":"Enhancer of rudimentary homolog 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12373","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21447100","identifier":"Q19541","identifierLink":"https://www.uniprot.org/uniprotkb/Q19541/entry","name":"pid-1","description":"Protein pid-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-2415582","identifier":"O76616","identifierLink":"https://www.uniprot.org/uniprotkb/O76616/entry","name":"pid-3","description":"Protein pid-3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-330119","identifier":"O61955","identifierLink":"https://www.uniprot.org/uniprotkb/O61955/entry","name":"ife-3","description":"Eukaryotic translation initiation factor 4E-3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4307","complexName":"PETISCO, tost-1 variant","organismName":"Caenorhabditis elegans; 6239","description":"Involved in the processing of substrate RNAs. When bound to tost-1, it binds to splice leader SL1 RNA fragments. SL1 fragments are trans-spliced to the 5-prime ends of a large fraction of all mRNAs. Ife-3 is required for the interaction with capped RNA molecules. In contrast to the PETISCO, pid-1 variant complex (CPX-4306), the complex has a minor role in 21U RNA biogenesis, but is essential for embryogenesis.","predictedComplex":false,"interactors":[{"ac":"EBI-2001908","identifier":"Q09293","identifierLink":"https://www.uniprot.org/uniprotkb/Q09293/entry","name":"tofu-6","description":"Embryonic developmental protein tofu-6","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-21447087","identifier":"Q20057","identifierLink":"https://www.uniprot.org/uniprotkb/Q20057/entry","name":"erh-2","description":"Enhancer of rudimentary homolog 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12373","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21447173","identifier":"Q18490","identifierLink":"https://www.uniprot.org/uniprotkb/Q18490/entry","name":"tost-1","description":"Protein tost-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-2415582","identifier":"O76616","identifierLink":"https://www.uniprot.org/uniprotkb/O76616/entry","name":"pid-3","description":"Protein pid-3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-330119","identifier":"O61955","identifierLink":"https://www.uniprot.org/uniprotkb/O61955/entry","name":"ife-3","description":"Eukaryotic translation initiation factor 4E-3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4310","complexName":"Prolow-density lipoprotein receptor-related protein 1 complex","organismName":"Homo sapiens; 9606","description":"Endocytic, low-densitiy lipoprotein receptor involved in two major processes, as scavenger receptor in the internalisation of extracellular molecules and their clearance via the endosome and as transducer of multiple intracellular signal pathways. Often acts in corporation with other cell-surface receptors. LRP-1 is recycled to the plasma membrane. Involved in cholesterol import and clearance of a range of toxins. Ligands range from matrix metalloproteinases (MMP) and urokinase-type plasminogen activator (uPA-uPAR, CPX-487) or tissue-type plasminogen activator (Plat/tPA, P00750), bound directly to LRP-1 or in complex with their target inhibitor, e.g. plasminogen activator inhibitor type 1 (SERPINE1/PAI-1, CPX-483 and CPX-494), to amyloid-beta peptides. \r\n\r\nInstead of being internalised, LRP-1 ligands may also shed the extracellular domains of the alpha and beta chains resulting in an extracellular, soluble LRP-1 (sLRP-1) decoy receptor. \r\n\r\nAffects a variety of pathophysiological processes including lipid metabolism, neurodegenerative diseases (e.g. Alzheimer's disease), blood-brain-barrier integrity, cardiovascular disease, atherosclerosis and cancer.","predictedComplex":false,"interactors":[{"ac":"EBI-21448188","identifier":"Q07954-PRO_0000302751","identifierLink":"https://www.uniprot.org/uniprotkb/Q07954-PRO_0000302751/entry","name":"LRP1","description":"Low-density lipoprotein receptor-related protein 1 85 kDa subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-21448222","identifier":"Q07954-PRO_0000302750","identifierLink":"https://www.uniprot.org/uniprotkb/Q07954-PRO_0000302750/entry","name":"LRP1","description":"Low-density lipoprotein receptor-related protein 1 515 kDa subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-4311","complexName":"nrfl-1-aat-6 complex","organismName":"Caenorhabditis elegans; 6239","description":"Amino acid transporter complex that is required for the absorption of amino acids in the intestine. nrfl-1 sequesters the amino acid transporter aat-6 to the plasma membrane, where it probably mediates the uptake of the L-enantiomers of various amino acids, including L-glutamate.","predictedComplex":false,"interactors":[{"ac":"EBI-21449230","identifier":"Q22397","identifierLink":"https://www.uniprot.org/uniprotkb/Q22397/entry","name":"aat-6","description":"Amino acid transporter protein 6","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11785","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-313674","identifier":"G5EDM4","identifierLink":"https://www.uniprot.org/uniprotkb/G5EDM4/entry","name":"nrfl-1","description":"Na(+)/H(+) exchange regulatory cofactor-like protein nrfl-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR14191","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4312","complexName":"Taurine ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"A sulfonate-sulfur utilization system required for the import of taurine (2-aminoethanesulfonic acid, CHEBI:15891) as a source of sulfur. The complex is expressed only under conditions of sulfate or cysteine starvation. Member of the ATP-binding cassette (ABC) transporter family, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1116148","identifier":"Q47537","identifierLink":"https://www.uniprot.org/uniprotkb/Q47537/entry","name":"tauA","description":"Taurine-binding periplasmic protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30024","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1116160","identifier":"Q47538","identifierLink":"https://www.uniprot.org/uniprotkb/Q47538/entry","name":"tauB","description":"Taurine import ATP-binding protein TauB","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42788","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21450451","identifier":"Q47539","identifierLink":"https://www.uniprot.org/uniprotkb/Q47539/entry","name":"tauC","description":"Taurine transport system permease protein TauC","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30151","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4313","complexName":"Aliphatic sulfonate ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"A sulfonate-sulfur utilization system required for the import of aliphatic sulfonates as a source of sulfur. The complex is expressed only under conditions of sulfate or cysteine starvation. Member of the ATP-binding cassette (ABC) transporter family, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1121037","identifier":"P0AAI1","identifierLink":"https://www.uniprot.org/uniprotkb/P0AAI1/entry","name":"ssuB","description":"Aliphatic sulfonates import ATP-binding protein SsuB","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42788","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21450516","identifier":"P75853","identifierLink":"https://www.uniprot.org/uniprotkb/P75853/entry","name":"ssuA","description":"Putative aliphatic sulfonates-binding protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30024","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21450534","identifier":"P75851","identifierLink":"https://www.uniprot.org/uniprotkb/P75851/entry","name":"ssuC","description":"Putative aliphatic sulfonates transport permease protein SsuC","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30151","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4314","complexName":"Arabinose ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High-affinity arabinose transporter, also transports fructose and xylose. Member of the ATP-binding cassette (ABC) transporter family, prokaryote-type (PK-type) subfamily. Transcription of the araFGH operon is positively regulated by the AraC protein (P0A9E0) in the presence of arabinose and cAMP bound to a cAMP receptor protein.","predictedComplex":false,"interactors":[{"ac":"EBI-1112983","identifier":"P02924","identifierLink":"https://www.uniprot.org/uniprotkb/P02924/entry","name":"araF","description":"L-arabinose-binding periplasmic protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21450558","identifier":"P0AE26","identifierLink":"https://www.uniprot.org/uniprotkb/P0AE26/entry","name":"araH","description":"L-arabinose transport system permease protein AraH","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32196","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-559586","identifier":"P0AAF3","identifierLink":"https://www.uniprot.org/uniprotkb/P0AAF3/entry","name":"araG","description":"Arabinose import ATP-binding protein AraG","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43790","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4315","complexName":"Autoinducer-2 ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"ABC transporter complex involved in autoinducer 2 (AI-2,  (2R,4S)-2-methyltetrahydrofuran-2,3,3,4-tetrol, CHEBI:44800) import, small hormone-like organic molecules required for bacterial cell-to-cell communication. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily. Population-based multi-cellularity, has been termed quorum sensing. Extracellular AI-2 activity peaks during the mid- to late-exponential phase and rapidly decreases during entry into the stationary phase. The disappearance of extracellular AI-2 activity is due to its import by this complex.","predictedComplex":false,"interactors":[{"ac":"EBI-1124301","identifier":"P77257","identifierLink":"https://www.uniprot.org/uniprotkb/P77257/entry","name":"lsrA","description":"Autoinducer 2 import ATP-binding protein LsrA","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43790","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1132197","identifier":"P76142","identifierLink":"https://www.uniprot.org/uniprotkb/P76142/entry","name":"lsrB","description":"Autoinducer 2-binding protein LsrB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR46847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21450591","identifier":"P77672","identifierLink":"https://www.uniprot.org/uniprotkb/P77672/entry","name":"lsrC","description":"Autoinducer 2 import system permease protein LsrC","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32196","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21450604","identifier":"P0AFS1","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFS1/entry","name":"lsrD","description":"Autoinducer 2 import system permease protein LsrD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32196","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4316","complexName":"Branched chain amino acid ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High-affinity branched-chain amino acid transport system, catalysing the uptake of the branched chain amino acids: L-leucine, L-isoleucine and L-valine. livJ also interacts weakly with threonine, serine, and  alanine. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1116889","identifier":"P22731","identifierLink":"https://www.uniprot.org/uniprotkb/P22731/entry","name":"livF","description":"High-affinity branched-chain amino acid transport ATP-binding protein LivF","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43820","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1117331","identifier":"P0A9S7","identifierLink":"https://www.uniprot.org/uniprotkb/P0A9S7/entry","name":"livG","description":"High-affinity branched-chain amino acid transport ATP-binding protein LivG","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR45772","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1126731","identifier":"P0AD96","identifierLink":"https://www.uniprot.org/uniprotkb/P0AD96/entry","name":"livJ","description":"Leu/Ile/Val-binding protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR47151","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21450787","identifier":"P0AEX7","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEX7/entry","name":"livH","description":"High-affinity branched-chain amino acid transport system permease protein LivH","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11795","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21450814","identifier":"P22729","identifierLink":"https://www.uniprot.org/uniprotkb/P22729/entry","name":"livM","description":"High-affinity branched-chain amino acid transport system permease protein LivM","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30482","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4317","complexName":"Branched chain amino acid, leucine-specific ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High-affinity branched-chain amino acid transport system, catalysing the uptake of the branched chain amino acids, such as L-leucine and the non-polar, aromatic amino acid, phenylalanine. Amino acids such as isoleucine and valine are not thought to bind with appreciable affinity. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1116889","identifier":"P22731","identifierLink":"https://www.uniprot.org/uniprotkb/P22731/entry","name":"livF","description":"High-affinity branched-chain amino acid transport ATP-binding protein LivF","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43820","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1117331","identifier":"P0A9S7","identifierLink":"https://www.uniprot.org/uniprotkb/P0A9S7/entry","name":"livG","description":"High-affinity branched-chain amino acid transport ATP-binding protein LivG","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR45772","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1120064","identifier":"P04816","identifierLink":"https://www.uniprot.org/uniprotkb/P04816/entry","name":"livK","description":"Leucine-specific-binding protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR47151","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21450787","identifier":"P0AEX7","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEX7/entry","name":"livH","description":"High-affinity branched-chain amino acid transport system permease protein LivH","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11795","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21450814","identifier":"P22729","identifierLink":"https://www.uniprot.org/uniprotkb/P22729/entry","name":"livM","description":"High-affinity branched-chain amino acid transport system permease protein LivM","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30482","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4318","complexName":"Arginine ABC transporter complex, artI variant","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity arginine transporter.  Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1120651","identifier":"P30859","identifierLink":"https://www.uniprot.org/uniprotkb/P30859/entry","name":"artI","description":"Putative ABC transporter arginine-binding protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR35936","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1131813","identifier":"P0AE30","identifierLink":"https://www.uniprot.org/uniprotkb/P0AE30/entry","name":"artM","description":"Arginine ABC transporter permease protein ArtM","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30614","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544100","identifier":"P0AAF6","identifierLink":"https://www.uniprot.org/uniprotkb/P0AAF6/entry","name":"artP","description":"Arginine transport ATP-binding protein ArtP","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43166","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-559766","identifier":"P0AE34","identifierLink":"https://www.uniprot.org/uniprotkb/P0AE34/entry","name":"artQ","description":"Arginine ABC transporter permease protein ArtQ","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30133","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7181","complexName":"ESCRT-I complex, VPS37A-UBAP1 variant","organismName":"Homo sapiens; 9606","description":"The ESCRT machinery, consisting of ESCRT-0  (this complex), -I, -II (CPX-2506), -III (CPX-329) and -IV (VPS4A/B complex, CPX-338)  has been implicated in membrane scission steps, transforming a single, continuous bilayer into two distinct bilayers, either from within the neck of a vesicle budding away from the cytoplasm or from within a membrane tubule, while segregating cargo throughout the process. Membrane fission processes include: a) the sorting of multivesicular bodies (MVB) in the endocytic pathway; cargoes destined for inclusion into the MVB pathway are covalently modified with ubiquitin, recognized by ubiquitin-binding domains in the early ESCRTs (ESCRT-0, -I, and -II) and sequestered into endosomal microdomains that bud into the endosome as intralumenal vesicles aided by ESCRT-III, b) downregulation of cell-surface receptors, c) repair of plasma membrane wounds, d) abscission of the cellular bridge during cytokineses, d) nuclear envelope sealing by annular fusion and e) budding of virions (especially HIV-1) from the plasma membrane. The ESCRT machinery seems to play an indirect role in the proper functioning of cellular polarity and migration, the miRNA machinery and gene expression regulation. ESCRT-0 binds to and clusters ubiquitinated cargo for delivery into MVBs, and recruits clathrin, ubiquitin ligases, and deubiquitinating enzymes. ESCRT-0 recruits ESCRT-I which engages ESCRT-II to nucleate ESCRT-III polymerization. VPS4A/B complex, also known as ESCRT-IV, disassembles ESCRT-III to recycle its subunits. The ESCRT-III complex facilitates changes in membrane architecture by oligomerizing to form spiral, filament-like tubules, accumulation of which is associated with membrane constriction and fission. Disassembly of ESCRT-III by VPS4A/B may be a required step for fission.","predictedComplex":false,"interactors":[{"ac":"EBI-2850578","identifier":"Q8NEZ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NEZ2/entry","name":"VPS37A","description":"Vacuolar protein sorting-associated protein 37A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-346882","identifier":"Q99816","identifierLink":"https://www.uniprot.org/uniprotkb/Q99816/entry","name":"TSG101","description":"Tumor susceptibility gene 101 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23306","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727424","identifier":"Q9UK41","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK41/entry","name":"VPS28","description":"Vacuolar protein sorting-associated protein 28 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9641159","identifier":"Q9NZ09","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZ09/entry","name":"UBAP1","description":"Ubiquitin-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7201","complexName":"ESCRT-I complex, VPS37B-UBAP1 variant","organismName":"Homo sapiens; 9606","description":"The ESCRT machinery, consisting of ESCRT-0  (this complex), -I, -II (CPX-2506), -III (CPX-329) and -IV (VPS4A/B complex, CPX-338)  has been implicated in membrane scission steps, transforming a single, continuous bilayer into two distinct bilayers, either from within the neck of a vesicle budding away from the cytoplasm or from within a membrane tubule, while segregating cargo throughout the process. Membrane fission processes include: a) the sorting of multivesicular bodies (MVB) in the endocytic pathway; cargoes destined for inclusion into the MVB pathway are covalently modified with ubiquitin, recognized by ubiquitin-binding domains in the early ESCRTs (ESCRT-0, -I, and -II) and sequestered into endosomal microdomains that bud into the endosome as intralumenal vesicles aided by ESCRT-III, b) downregulation of cell-surface receptors, c) repair of plasma membrane wounds, d) abscission of the cellular bridge during cytokineses, d) nuclear envelope sealing by annular fusion and e) budding of virions (especially HIV-1) from the plasma membrane. The ESCRT machinery seems to play an indirect role in the proper functioning of cellular polarity and migration, the miRNA machinery and gene expression regulation. ESCRT-0 binds to and clusters ubiquitinated cargo for delivery into MVBs, and recruits clathrin, ubiquitin ligases, and deubiquitinating enzymes. ESCRT-0 recruits ESCRT-I which engages ESCRT-II to nucleate ESCRT-III polymerization. VPS4A/B complex, also known as ESCRT-IV, disassembles ESCRT-III to recycle its subunits. The ESCRT-III complex facilitates changes in membrane architecture by oligomerizing to form spiral, filament-like tubules, accumulation of which is associated with membrane constriction and fission. Disassembly of ESCRT-III by VPS4A/B may be a required step for fission.","predictedComplex":false,"interactors":[{"ac":"EBI-346882","identifier":"Q99816","identifierLink":"https://www.uniprot.org/uniprotkb/Q99816/entry","name":"TSG101","description":"Tumor susceptibility gene 101 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23306","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4400866","identifier":"Q9H9H4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H9H4/entry","name":"VPS37B","description":"Vacuolar protein sorting-associated protein 37B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727424","identifier":"Q9UK41","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK41/entry","name":"VPS28","description":"Vacuolar protein sorting-associated protein 28 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9641159","identifier":"Q9NZ09","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZ09/entry","name":"UBAP1","description":"Ubiquitin-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7202","complexName":"ESCRT-I complex, VPS37C-UBAP1 variant","organismName":"Homo sapiens; 9606","description":"The ESCRT machinery, consisting of ESCRT-0  (this complex), -I, -II (CPX-2506), -III (CPX-329) and -IV (VPS4A/B complex, CPX-338)  has been implicated in membrane scission steps, transforming a single, continuous bilayer into two distinct bilayers, either from within the neck of a vesicle budding away from the cytoplasm or from within a membrane tubule, while segregating cargo throughout the process. Membrane fission processes include: a) the sorting of multivesicular bodies (MVB) in the endocytic pathway; cargoes destined for inclusion into the MVB pathway are covalently modified with ubiquitin, recognized by ubiquitin-binding domains in the early ESCRTs (ESCRT-0, -I, and -II) and sequestered into endosomal microdomains that bud into the endosome as intralumenal vesicles aided by ESCRT-III, b) downregulation of cell-surface receptors, c) repair of plasma membrane wounds, d) abscission of the cellular bridge during cytokineses, d) nuclear envelope sealing by annular fusion and e) budding of virions (especially HIV-1) from the plasma membrane. The ESCRT machinery seems to play an indirect role in the proper functioning of cellular polarity and migration, the miRNA machinery and gene expression regulation. ESCRT-0 binds to and clusters ubiquitinated cargo for delivery into MVBs, and recruits clathrin, ubiquitin ligases, and deubiquitinating enzymes. ESCRT-0 recruits ESCRT-I which engages ESCRT-II to nucleate ESCRT-III polymerization. VPS4A/B complex, also known as ESCRT-IV, disassembles ESCRT-III to recycle its subunits. The ESCRT-III complex facilitates changes in membrane architecture by oligomerizing to form spiral, filament-like tubules, accumulation of which is associated with membrane constriction and fission. Disassembly of ESCRT-III by VPS4A/B may be a required step for fission.","predictedComplex":false,"interactors":[{"ac":"EBI-2559305","identifier":"A5D8V6","identifierLink":"https://www.uniprot.org/uniprotkb/A5D8V6/entry","name":"VPS37C","description":"Vacuolar protein sorting-associated protein 37C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-346882","identifier":"Q99816","identifierLink":"https://www.uniprot.org/uniprotkb/Q99816/entry","name":"TSG101","description":"Tumor susceptibility gene 101 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23306","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727424","identifier":"Q9UK41","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK41/entry","name":"VPS28","description":"Vacuolar protein sorting-associated protein 28 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9641159","identifier":"Q9NZ09","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZ09/entry","name":"UBAP1","description":"Ubiquitin-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7203","complexName":"ESCRT-I complex, VPS37D-UBAP1 variant","organismName":"Homo sapiens; 9606","description":"The ESCRT machinery, consisting of ESCRT-0  (this complex), -I, -II (CPX-2506), -III (CPX-329) and -IV (VPS4A/B complex, CPX-338)  has been implicated in membrane scission steps, transforming a single, continuous bilayer into two distinct bilayers, either from within the neck of a vesicle budding away from the cytoplasm or from within a membrane tubule, while segregating cargo throughout the process. Membrane fission processes include: a) the sorting of multivesicular bodies (MVB) in the endocytic pathway; cargoes destined for inclusion into the MVB pathway are covalently modified with ubiquitin, recognized by ubiquitin-binding domains in the early ESCRTs (ESCRT-0, -I, and -II) and sequestered into endosomal microdomains that bud into the endosome as intralumenal vesicles aided by ESCRT-III, b) downregulation of cell-surface receptors, c) repair of plasma membrane wounds, d) abscission of the cellular bridge during cytokineses, d) nuclear envelope sealing by annular fusion and e) budding of virions (especially HIV-1) from the plasma membrane. The ESCRT machinery seems to play an indirect role in the proper functioning of cellular polarity and migration, the miRNA machinery and gene expression regulation. ESCRT-0 binds to and clusters ubiquitinated cargo for delivery into MVBs, and recruits clathrin, ubiquitin ligases, and deubiquitinating enzymes. ESCRT-0 recruits ESCRT-I which engages ESCRT-II to nucleate ESCRT-III polymerization. VPS4A/B complex, also known as ESCRT-IV, disassembles ESCRT-III to recycle its subunits. The ESCRT-III complex facilitates changes in membrane architecture by oligomerizing to form spiral, filament-like tubules, accumulation of which is associated with membrane constriction and fission. Disassembly of ESCRT-III by VPS4A/B may be a required step for fission.","predictedComplex":false,"interactors":[{"ac":"EBI-346882","identifier":"Q99816","identifierLink":"https://www.uniprot.org/uniprotkb/Q99816/entry","name":"TSG101","description":"Tumor susceptibility gene 101 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23306","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727424","identifier":"Q9UK41","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK41/entry","name":"VPS28","description":"Vacuolar protein sorting-associated protein 28 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7604353","identifier":"Q86XT2","identifierLink":"https://www.uniprot.org/uniprotkb/Q86XT2/entry","name":"VPS37D","description":"Vacuolar protein sorting-associated protein 37D","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9641159","identifier":"Q9NZ09","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZ09/entry","name":"UBAP1","description":"Ubiquitin-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7205","complexName":"Signal peptidase complex, SEC11C variant","organismName":"Homo sapiens; 9606","description":"Catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. The complex cleaves the signal peptides of most secretory and many membrane proteins as soon as the lumenal domain of the translocating polypeptide is large enough to expose its cleavage site to the enzyme, during the translocation of the protein through the translocon pore into the endoplasmic reticulum. The complex specifically cleaves N-terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids","predictedComplex":false,"interactors":[{"ac":"EBI-1043352","identifier":"Q15005","identifierLink":"https://www.uniprot.org/uniprotkb/Q15005/entry","name":"SPCS2","description":"Signal peptidase complex subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13085","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2855401","identifier":"Q9BY50","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BY50/entry","name":"SEC11C","description":"Signal peptidase complex catalytic subunit SEC11C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10806","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6166040","identifier":"P61009","identifierLink":"https://www.uniprot.org/uniprotkb/P61009/entry","name":"SPCS3","description":"Signal peptidase complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12804","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8852196","identifier":"Q9Y6A9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6A9/entry","name":"SPCS1","description":"Signal peptidase complex subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13202","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7221","complexName":"ERGIC2-ERGIC3 retrograde receptor complex","organismName":"Homo sapiens; 9606","description":"Functions as a cargo receptor in both anterograde and retrograde protein trafficking. Transports proteins between the endoplasmic reticulum and Golgi and also returns endoplasmic reticulum resident proteins that have trafficked to Golgi compartments.","predictedComplex":false,"interactors":[{"ac":"EBI-4403663","identifier":"Q96RQ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q96RQ1/entry","name":"ERGIC2","description":"Endoplasmic reticulum-Golgi intermediate compartment protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10984","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-781551","identifier":"Q9Y282","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y282/entry","name":"ERGIC3","description":"Endoplasmic reticulum-Golgi intermediate compartment protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10984","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7241","complexName":"Mitochondrial transcription initiation complex","organismName":"Homo sapiens; 9606","description":"Responsible for the basal transcription of the human mitochondrial genome, producing mitochondrial rRNA, tRNA and mRNA, and the RNA primer required for replication of the mitochondrial genome","predictedComplex":false,"interactors":[{"ac":"EBI-1043912","identifier":"Q9H5Q4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H5Q4/entry","name":"TFB2M","description":"Dimethyladenosine transferase 2, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11727","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1049924","identifier":"Q00059","identifierLink":"https://www.uniprot.org/uniprotkb/Q00059/entry","name":"TFAM","description":"Transcription factor A, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48112","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355145","identifier":"O00411","identifierLink":"https://www.uniprot.org/uniprotkb/O00411/entry","name":"POLRMT","description":"DNA-directed RNA polymerase, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7261","complexName":"TREX transcription-export complex, DX39A variant","organismName":"Homo sapiens; 9606","description":"Selectively binds maturing mRNA at the messenger ribonucleoprotein complex 5'-end, splice junctions, and 3'-end and licenses mRNA for nuclear export by loading the global mRNA-export factor NXF1-NXT (CPX-725/CPX-2435) . Also acts to chaperone the nascent mRNA by inhibiting the formation of harmful DNA-RNA hybrids, (R-loops), thus protecting genome integrity. The THO subcomplex is recruited to the mRNP and delivers DDX39A, which clamps the mRNA. THO-DDX39A binds export adapters such as ALYREF and together they promote loading of  NXF1-NXT onto mRNA.. It  is predicted that the multiple variants of this complex may exist with different compositional rearrangements of its adapter subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-10198848","identifier":"Q9P127","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P127/entry","name":"LUZP4","description":"Leucine zipper protein 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22550","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1755078","identifier":"Q8NI27","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NI27/entry","name":"THOC2","description":"THO complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21597","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1765605","identifier":"Q96FV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q96FV9/entry","name":"THOC1","description":"THO complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13265","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1776152","identifier":"Q9BY77","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BY77/entry","name":"POLDIP3","description":"Polymerase delta-interacting protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19965","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2510823","identifier":"Q96J01","identifierLink":"https://www.uniprot.org/uniprotkb/Q96J01/entry","name":"THOC3","description":"THO complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22839","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2880668","identifier":"Q86W42","identifierLink":"https://www.uniprot.org/uniprotkb/Q86W42/entry","name":"THOC6","description":"THO complex subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347495","identifier":"P82979","identifierLink":"https://www.uniprot.org/uniprotkb/P82979/entry","name":"SARNP","description":"SAP domain-containing ribonucleoprotein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46551","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347640","identifier":"Q86V81","identifierLink":"https://www.uniprot.org/uniprotkb/Q86V81/entry","name":"ALYREF","description":"THO complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19965","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347794","identifier":"Q9Y3Y2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3Y2/entry","name":"CHTOP","description":"Chromatin target of PRMT1 protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48426","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348253","identifier":"O00148","identifierLink":"https://www.uniprot.org/uniprotkb/O00148/entry","name":"DDX39A","description":"ATP-dependent RNA helicase DDX39A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47958","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5280316","identifier":"Q13769","identifierLink":"https://www.uniprot.org/uniprotkb/Q13769/entry","name":"THOC5","description":"THO complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6657994","identifier":"Q53F19","identifierLink":"https://www.uniprot.org/uniprotkb/Q53F19/entry","name":"NCBP3","description":"Nuclear cap-binding protein subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16291","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-711389","identifier":"P84090","identifierLink":"https://www.uniprot.org/uniprotkb/P84090/entry","name":"ERH","description":"Enhancer of rudimentary homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12373","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-716286","identifier":"Q6I9Y2","identifierLink":"https://www.uniprot.org/uniprotkb/Q6I9Y2/entry","name":"THOC7","description":"THO complex subunit 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23405","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724553","identifier":"Q96QD9","identifierLink":"https://www.uniprot.org/uniprotkb/Q96QD9/entry","name":"FYTTD1","description":"UAP56-interacting factor","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21038","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-748480","identifier":"O75152","identifierLink":"https://www.uniprot.org/uniprotkb/O75152/entry","name":"ZC3H11A","description":"Zinc finger CCCH domain-containing protein 11A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15725","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1686","complexName":"TREX-2 transcription-export complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Couples SAGA (CPX-656)-dependent gene expression and transcription elongation to mRNA export at the inner side of the nuclear pore complex (NPC, CPX-824). The TREX-2 complex is tethered to the inner side of the NPC via the nucleoporins NUP1 (P20676) and NUP60 (P39705) and  facilitates the repositioning and association of actively transcribing genes with nuclear pores (gene gating). 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In early G1, the complex binds to E2F, CHR, CDE (cell cycle-dependent element), and CLE (CHR-like element) promoter sites and represses more than 800 cell cycle-dependent genes in quiescent cells, mediating TP53 activity. In the late stage of G1, DREAM-specific protein separates from the MuvB core (LIN9, LIN37, LIN52, LIN53, and LIN54) and then binds to MYBB (P10244) in the S phase, e, to form the MMB complex which transactivates cell-cycle genes related to the S/G2/M phase.","predictedComplex":false,"interactors":[{"ac":"EBI-1389411","identifier":"Q6MZP7","identifierLink":"https://www.uniprot.org/uniprotkb/Q6MZP7/entry","name":"LIN54","description":"Protein lin-54 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12446","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1389424","identifier":"Q5TKA1","identifierLink":"https://www.uniprot.org/uniprotkb/Q5TKA1/entry","name":"LIN9","description":"Protein lin-9 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21689","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1389456","identifier":"Q52LA3","identifierLink":"https://www.uniprot.org/uniprotkb/Q52LA3/entry","name":"LIN52","description":"Protein lin-52 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31489","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1389773","identifier":"Q15329","identifierLink":"https://www.uniprot.org/uniprotkb/Q15329/entry","name":"E2F5","description":"Transcription factor E2F5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12081","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-448943","identifier":"Q16254","identifierLink":"https://www.uniprot.org/uniprotkb/Q16254/entry","name":"E2F4","description":"Transcription factor E2F4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12081","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-620823","identifier":"Q09028","identifierLink":"https://www.uniprot.org/uniprotkb/Q09028/entry","name":"RBBP4","description":"Histone-binding protein RBBP4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-748884","identifier":"Q96GY3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GY3/entry","name":"LIN37","description":"Protein lin-37 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31336","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749713","identifier":"Q14186","identifierLink":"https://www.uniprot.org/uniprotkb/Q14186/entry","name":"TFDP1","description":"Transcription factor Dp-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12548","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752268","identifier":"Q14188","identifierLink":"https://www.uniprot.org/uniprotkb/Q14188/entry","name":"TFDP2","description":"Transcription factor Dp-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12548","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-971439","identifier":"Q08999","identifierLink":"https://www.uniprot.org/uniprotkb/Q08999/entry","name":"RBL2","description":"Retinoblastoma-like protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7462","complexName":"Myb-MuvB-FOXM1 transcriptional activation complex","organismName":"Homo sapiens; 9606","description":"Transcriptional activation complex which forms in the G2 phase and transactivates cell-cycle genes. Genes activated by Myb-MuvB  contain a cell-cycle homology region (CHR) DNA element in their promoters which is bound by LIN54","predictedComplex":false,"interactors":[{"ac":"EBI-1389411","identifier":"Q6MZP7","identifierLink":"https://www.uniprot.org/uniprotkb/Q6MZP7/entry","name":"LIN54","description":"Protein lin-54 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12446","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1389424","identifier":"Q5TKA1","identifierLink":"https://www.uniprot.org/uniprotkb/Q5TKA1/entry","name":"LIN9","description":"Protein lin-9 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21689","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1389456","identifier":"Q52LA3","identifierLink":"https://www.uniprot.org/uniprotkb/Q52LA3/entry","name":"LIN52","description":"Protein lin-52 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31489","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1389468","identifier":"P10244","identifierLink":"https://www.uniprot.org/uniprotkb/P10244/entry","name":"MYBL2","description":"Myb-related protein B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45614","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-620823","identifier":"Q09028","identifierLink":"https://www.uniprot.org/uniprotkb/Q09028/entry","name":"RBBP4","description":"Histone-binding protein RBBP4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-748884","identifier":"Q96GY3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GY3/entry","name":"LIN37","description":"Protein lin-37 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31336","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-866480","identifier":"Q08050","identifierLink":"https://www.uniprot.org/uniprotkb/Q08050/entry","name":"FOXM1","description":"Forkhead box protein M1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46878","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7481","complexName":"DNA-directed RNA polymerase II complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the transcription of RNA from a DNA template by acting as a nucleotidyl transferase that polymerizes ribonucleotides at the 3' end of an RNA transcript. Synthesizes precursors of mRNAs, and most snRNA and microRNAs.\r\n\r\nDuring a transcription cycle, Pol II, general transcription factors and the mediator complex (CPX-3227) assemble as the preinitiation complex (PIC) at the promoter. 11-15 base pairs of DNA surrounding the transcription start site are melted and the single-stranded DNA template strand of the promoter is positioned deeply within the central active site cleft of Pol II to form the open complex. After synthesis of about 30 bases of RNA, Pol II releases its contacts with the core promoter and the rest of the transcription machinery (promoter clearance) and enters the stage of transcription elongation in which it moves on the template as the transcript elongates. Pol II appears to oscillate between inactive and active conformations at each step of nucleotide addition.","predictedComplex":false,"interactors":[{"ac":"EBI-295301","identifier":"P24928","identifierLink":"https://www.uniprot.org/uniprotkb/P24928/entry","name":"POLR2A","description":"DNA-directed RNA polymerase II subunit RPB1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19376","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347928","identifier":"P62487","identifierLink":"https://www.uniprot.org/uniprotkb/P62487/entry","name":"POLR2G","description":"DNA-directed RNA polymerase II subunit RPB7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12709","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359505","identifier":"P52434","identifierLink":"https://www.uniprot.org/uniprotkb/P52434/entry","name":"POLR2H","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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9606","xrefs":[{"identifier":"PTHR11800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394737","identifier":"O15514","identifierLink":"https://www.uniprot.org/uniprotkb/O15514/entry","name":"POLR2D","description":"DNA-directed RNA polymerase II subunit RPB4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21297","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394753","identifier":"P52435","identifierLink":"https://www.uniprot.org/uniprotkb/P52435/entry","name":"POLR2J","description":"DNA-directed RNA polymerase II subunit RPB11-a","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13946","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395180","identifier":"P61218","identifierLink":"https://www.uniprot.org/uniprotkb/P61218/entry","name":"POLR2F","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47227","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395189","identifier":"P19388","identifierLink":"https://www.uniprot.org/uniprotkb/P19388/entry","name":"POLR2E","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10535","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395202","identifier":"P36954","identifierLink":"https://www.uniprot.org/uniprotkb/P36954/entry","name":"POLR2I","description":"DNA-directed RNA polymerase II subunit RPB9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395357","identifier":"P53803","identifierLink":"https://www.uniprot.org/uniprotkb/P53803/entry","name":"POLR2K","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-7482","complexName":"DNA-directed RNA polymerase III complex, POLR3GL variant","organismName":"Homo sapiens; 9606","description":"Catalyzes the transcription of RNA from an DNA template by acting as a nucleotidyl transferase that polymerizes ribonucleotides at the 3' end of an RNA transcript. Responsible for the transcription of genes encoding short non-coding RNAs, such as tRNA, 5S rRNA and U6 snRNA transcripts. \r\n\r\nPol III machinery recognizes conserved promoter elements located within the transcribed region, generally the box A and box B sequences, which contribute to the  D- and T-loops in the tRNA structure. POLR3F, POLR3GL and POLR3C play a role in transcription initiation whereas the POLR3D-POLR3E heterodimer is crucial for the correct recognition of the termination signals of class III genes. POLR3K is required for RNA cleavage. Pol III initiation does not require ATP hydrolysis to open a transcription bubble to isolate and secure the template strand in the catalytic site and Pol III is capable of reinitiating transcription more rapidly on the same gene after the first transcription cycle without being released (facilitated reinitiation), resulting in a higher initiation efficiency; this appears to require an POLR3K-dependent conformational change of Pol III.","predictedComplex":false,"interactors":[{"ac":"EBI-1055079","identifier":"O15160","identifierLink":"https://www.uniprot.org/uniprotkb/O15160/entry","name":"POLR1C","description":"DNA-directed RNA polymerases I and III subunit RPAC1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11023785","identifier":"Q9Y2Y1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2Y1/entry","name":"POLR3K","description":"DNA-directed RNA polymerase III subunit RPC10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2515048","identifier":"Q9NVU0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NVU0/entry","name":"POLR3E","description":"DNA-directed RNA polymerase III subunit RPC5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12069","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2515065","identifier":"Q9Y535","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y535/entry","name":"POLR3H","description":"DNA-directed RNA polymerase III subunit RPC8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12709","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2515106","identifier":"Q9NW08","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NW08/entry","name":"POLR3B","description":"DNA-directed RNA polymerase III subunit RPC2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20856","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2515113","identifier":"O14802","identifierLink":"https://www.uniprot.org/uniprotkb/O14802/entry","name":"POLR3A","description":"DNA-directed RNA polymerase III subunit RPC1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19376","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2654687","identifier":"O75575","identifierLink":"https://www.uniprot.org/uniprotkb/O75575/entry","name":"CRCP","description":"DNA-directed RNA polymerase III subunit RPC9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15561","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2687556","identifier":"P05423","identifierLink":"https://www.uniprot.org/uniprotkb/P05423/entry","name":"POLR3D","description":"DNA-directed RNA polymerase III subunit RPC4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13408","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2855862","identifier":"Q9BT43","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BT43/entry","name":"POLR3GL","description":"DNA-directed RNA polymerase III subunit RPC7-like","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15367","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359498","identifier":"P0DPB6","identifierLink":"https://www.uniprot.org/uniprotkb/P0DPB6/entry","name":"POLR1D","description":"DNA-directed RNA polymerases I and III subunit RPAC2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13946","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359505","identifier":"P52434","identifierLink":"https://www.uniprot.org/uniprotkb/P52434/entry","name":"POLR2H","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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9606","xrefs":[{"identifier":"PTHR10535","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395357","identifier":"P53803","identifierLink":"https://www.uniprot.org/uniprotkb/P53803/entry","name":"POLR2K","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5452779","identifier":"Q9BUI4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BUI4/entry","name":"POLR3C","description":"DNA-directed RNA polymerase III subunit RPC3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12949","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-710067","identifier":"Q9H1D9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H1D9/entry","name":"POLR3F","description":"DNA-directed RNA polymerase III subunit RPC6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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Purified Arp2/3 complex is inactive but stimulates rapid actin polymerization in the presence of activator proteins, the most potent type being the VCA (Verprolin, cofilin, acidic) domain-containing Wiskott-Aldrich syndrome protein (WASP) family members. The Arp2/3 complex appears to bind VCA and an existing actin filament in a cooperative manner. Upon activation, Arp2 and Arp3 move into the side-by-side arrangement of consecutive actin subunits along the short pitch helical axis of an actin filament, mimicking a filamentous actin dimer and creating a template for new filament assembly. The process appears to be ATP-dependent.","predictedComplex":false,"interactors":[{"ac":"EBI-138385","identifier":"P45888","identifierLink":"https://www.uniprot.org/uniprotkb/P45888/entry","name":"Arp2","description":"Actin-related protein 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-143351","identifier":"Q9VIM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VIM5/entry","name":"Arpc2","description":"Actin-related protein 2/3 complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12058","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-176768","identifier":"P32392","identifierLink":"https://www.uniprot.org/uniprotkb/P32392/entry","name":"Arp3","description":"Actin-related protein 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-178420","identifier":"Q9VMH2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VMH2/entry","name":"Arpc4","description":"Actin-related protein 2/3 complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22629","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-183402","identifier":"O97182","identifierLink":"https://www.uniprot.org/uniprotkb/O97182/entry","name":"Arpc1","description":"Actin-related protein 2/3 complex subunit","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10709","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-192564","identifier":"Q9VQD8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VQD8/entry","name":"Arpc5","description":"Actin-related protein 2/3 complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2109075","identifier":"Q9VF28","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VF28/entry","name":"Arpc3A","description":"Actin-related protein 2/3 complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12391","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2662","complexName":"DNA-directed RNA polymerase II complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the transcription of RNA from a DNA template by acting as a nucleotidyl transferase that polymerizes ribonucleotides at the 3' end of an RNA transcript. 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CBX2 may recognize H3K27me3 in the chromatin but this may not be the main driver of its interaction with chromatin.","predictedComplex":false,"interactors":[{"ac":"EBI-2341576","identifier":"P35226","identifierLink":"https://www.uniprot.org/uniprotkb/P35226/entry","name":"BMI1","description":"Polycomb complex protein BMI-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10825","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-725403","identifier":"P78364","identifierLink":"https://www.uniprot.org/uniprotkb/P78364/entry","name":"PHC1","description":"Polyhomeotic-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12247","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-745934","identifier":"Q14781","identifierLink":"https://www.uniprot.org/uniprotkb/Q14781/entry","name":"CBX2","description":"Chromobox protein homolog 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46860","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752313","identifier":"Q06587","identifierLink":"https://www.uniprot.org/uniprotkb/Q06587/entry","name":"RING1","description":"E3 ubiquitin-protein ligase RING1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7502","complexName":"Polycomb repressive complex 1, RING1-PCGF4-CBX2-PHC2 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin-protein ligase that acts as a transcriptional repressor by mediating the monoubiquitination of Lys-119 of histone H2A, compacting chromatin, stalling RNA polymerase II and transcriptionally silencing genes critical for development.  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CBX2 may recognize H3K27me3 in the chromatin but this may not be the main driver of its interaction with chromatin.","predictedComplex":false,"interactors":[{"ac":"EBI-2341576","identifier":"P35226","identifierLink":"https://www.uniprot.org/uniprotkb/P35226/entry","name":"BMI1","description":"Polycomb complex protein BMI-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10825","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-713786","identifier":"Q8IXK0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IXK0/entry","name":"PHC2","description":"Polyhomeotic-like protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12247","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-745934","identifier":"Q14781","identifierLink":"https://www.uniprot.org/uniprotkb/Q14781/entry","name":"CBX2","description":"Chromobox protein homolog 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46860","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752313","identifier":"Q06587","identifierLink":"https://www.uniprot.org/uniprotkb/Q06587/entry","name":"RING1","description":"E3 ubiquitin-protein ligase RING1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7504","complexName":"Polycomb repressive complex 1, RING1-PCGF4-CBX2-PHC3 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin-protein ligase that acts as a transcriptional repressor by mediating the monoubiquitination of Lys-119 of histone H2A, compacting chromatin, stalling RNA polymerase II and transcriptionally silencing genes critical for development.  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In S-phase, telomerase holoenzyme complex is targeted from Cajal bodies to telomeres by binding of TERT to the shelterin subunit, ACD (Q96AP0).","predictedComplex":false,"interactors":[{"ac":"EBI-1050064","identifier":"Q9NX24","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NX24/entry","name":"NHP2","description":"H/ACA ribonucleoprotein complex subunit 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1642169","identifier":"Q9NPE3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPE3/entry","name":"NOP10","description":"H/ACA ribonucleoprotein complex subunit 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1772203","identifier":"O14746","identifierLink":"https://www.uniprot.org/uniprotkb/O14746/entry","name":"TERT","description":"Telomerase reverse transcriptase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12066","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1772365","identifier":"URS00004A7003_9606","identifierLink":"http://rnacentral.org/rna/URS00004A7003_9606","name":"terc_human_rna","description":"Human telomerase RNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"ribonucleic acid","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2510382","identifier":"Q9NY12","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NY12/entry","name":"GAR1","description":"H/ACA ribonucleoprotein complex subunit 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23237","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2563542","identifier":"Q9BUR4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BUR4/entry","name":"WRAP53","description":"Telomerase Cajal body protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13211","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-713091","identifier":"O60832","identifierLink":"https://www.uniprot.org/uniprotkb/O60832/entry","name":"DKC1","description":"H/ACA ribonucleoprotein complex subunit DKC1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23127","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4881","complexName":"DNA-directed RNA polymerase holoenzyme complex, Sigma70 variant","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the transcription of RNA from an DNA template by acting as a nucleotidyl transferase that polymerizes ribonucleotides at the 3-prime end of an RNA transcript. Five subunits, rpoA/alpha, rpoB/beta, rpoC/beta-prime and rpoZ/omega form the catalytic core. To initiate promoter specific DNA transcription, the core enzyme has to bind a sigma factor, which helps to direct the polymerase to specific promoters. rpoD/Sigma70 is the primary or housekeeping sigma factor which preferentially transcribes genes associated with fast growth such as ribosomal operons. rpoD is composed of four domains: region 1.1, regions 1.2-2.4, regions 3.0-3.2 and regions 4.1-4.2 which  bind to promoter DNA as part of the holoenzyme; domains 2, 3 and 4 recognize the promoter DNA sequences of -10, extended -10, and -35, respectively.","predictedComplex":false,"interactors":[{"ac":"EBI-370560","identifier":"P0A800","identifierLink":"https://www.uniprot.org/uniprotkb/P0A800/entry","name":"rpoZ","description":"DNA-directed RNA polymerase subunit omega","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-543604","identifier":"P0A8T7","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8T7/entry","name":"rpoC","description":"DNA-directed RNA polymerase subunit beta'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR19376","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544985","identifier":"P0A7Z4","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7Z4/entry","name":"rpoA","description":"DNA-directed RNA polymerase subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32108","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544996","identifier":"P0A8V2","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8V2/entry","name":"rpoB","description":"DNA-directed RNA polymerase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR20856","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-545104","identifier":"P00579","identifierLink":"https://www.uniprot.org/uniprotkb/P00579/entry","name":"rpoD","description":"RNA polymerase sigma factor RpoD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30603","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-4883","complexName":"DNA-directed RNA polymerase holoenzyme complex, SigmaS variant","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the transcription of RNA from an DNA template by acting as a nucleotidyl transferase that polymerizes ribonucleotides at the 3-prime end of an RNA transcript. Five subunits, rpoA/alpha, rpoB/beta, rpoC/beta-prime and rpoZ/omega form the catalytic core. To initiate promoter specific DNA transcription, the core enzyme has to bind a sigma factor, which helps to direct the polymerase to specific promoters. rpoS efficiently transcribes genes involved in stress responses (including include starvation, hyperosmolarity, pH downshift, or non-optimal high or low temperature) and secondary metabolism as well as RNAs from intergenic regions. In conditions such as nutrient starvation or oxidative stress, rpoS is believed to take over transcription of genes important for cell survival that are under rpoD control during faster growth. Genes under the control of rpoS are characterized by promoter sequences very similar to rpoD-dependent genes but differ in conservation of the upstream promoter element and of the -35 sequence, and in the sequence immediately upstream of the -10 promoter element.","predictedComplex":false,"interactors":[{"ac":"EBI-370560","identifier":"P0A800","identifierLink":"https://www.uniprot.org/uniprotkb/P0A800/entry","name":"rpoZ","description":"DNA-directed RNA polymerase subunit omega","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-543604","identifier":"P0A8T7","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8T7/entry","name":"rpoC","description":"DNA-directed RNA polymerase subunit beta'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR19376","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544985","identifier":"P0A7Z4","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7Z4/entry","name":"rpoA","description":"DNA-directed RNA polymerase subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32108","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544996","identifier":"P0A8V2","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8V2/entry","name":"rpoB","description":"DNA-directed RNA polymerase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR20856","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-557581","identifier":"P13445","identifierLink":"https://www.uniprot.org/uniprotkb/P13445/entry","name":"rpoS","description":"RNA polymerase sigma factor RpoS","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30603","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-4884","complexName":"DNA-directed RNA polymerase holoenzyme complex, Sigma54 variant","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the transcription of RNA from an DNA template by acting as a nucleotidyl transferase that polymerizes ribonucleotides at the 3-prime end of an RNA transcript.  Five subunits, rpoA/alpha, rpoB/beta, rpoC/beta-prime and rpoZ/omega form the catalytic core. To initiate promoter specific DNA transcription, the core enzyme has to bind a sigma factor, which helps to direct the polymerase to specific promoters. rpoN acts as a master switch to turn on genes involved in nitrogen assimilation, motility, host colonization, and biofilm formation. rpoN promoters additionally encode an insulator sequence to dampen unwanted translation, preventing accidental expression of rpoN-controlled genes arising from transcriptional read-through. This is due to the presence of loosely defined, short CT-rich motifs of 3-5 bp (CTmers), where the strength of silencing was dependent on the number and the position of the CTmers.","predictedComplex":false,"interactors":[{"ac":"EBI-370560","identifier":"P0A800","identifierLink":"https://www.uniprot.org/uniprotkb/P0A800/entry","name":"rpoZ","description":"DNA-directed RNA polymerase subunit omega","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-543604","identifier":"P0A8T7","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8T7/entry","name":"rpoC","description":"DNA-directed RNA polymerase subunit beta'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR19376","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544985","identifier":"P0A7Z4","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7Z4/entry","name":"rpoA","description":"DNA-directed RNA polymerase subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32108","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544996","identifier":"P0A8V2","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8V2/entry","name":"rpoB","description":"DNA-directed RNA polymerase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR20856","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-557571","identifier":"P24255","identifierLink":"https://www.uniprot.org/uniprotkb/P24255/entry","name":"rpoN","description":"RNA polymerase sigma-54 factor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32248","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-4885","complexName":"DNA-directed RNA polymerase holoenzyme complex, SigmaE variant","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the transcription of RNA from an DNA template by acting as a nucleotidyl transferase that polymerizes ribonucleotides at the 3-prime end of an RNA transcript.  Five subunits, rpoA/alpha, rpoB/beta, rpoC/beta-prime and rpoZ/omega form the catalytic core. To initiate promoter specific DNA transcription, the core enzyme has to bind a sigma factor, which helps to direct the polymerase to specific promoters. rpoE transcribes genes involved in envelope stress response, responding to extracellular stress and the resulting disruption of proteins in the outer membrane or periplasm leading to an accumulation of misfolded and/or mis-translocated outer membrane proteins or lipopolysaccharide within the periplasm. Induces biofilm formation and appears to play a role in the virulence of some pathogenic strains.","predictedComplex":false,"interactors":[{"ac":"EBI-1129580","identifier":"P0AGB6","identifierLink":"https://www.uniprot.org/uniprotkb/P0AGB6/entry","name":"rpoE","description":"ECF RNA polymerase sigma-E factor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43133","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-370560","identifier":"P0A800","identifierLink":"https://www.uniprot.org/uniprotkb/P0A800/entry","name":"rpoZ","description":"DNA-directed RNA polymerase subunit omega","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-543604","identifier":"P0A8T7","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8T7/entry","name":"rpoC","description":"DNA-directed RNA polymerase subunit beta'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR19376","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544985","identifier":"P0A7Z4","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7Z4/entry","name":"rpoA","description":"DNA-directed RNA polymerase subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32108","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544996","identifier":"P0A8V2","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8V2/entry","name":"rpoB","description":"DNA-directed RNA polymerase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR20856","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-4886","complexName":"DNA-directed RNA polymerase holoenzyme complex, SigmaF variant","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the transcription of RNA from an DNA template by acting as a nucleotidyl transferase that polymerizes ribonucleotides at the 3' end of an RNA transcript. Five subunits, rpoA/alpha, rpoB/beta, rpoC/beta' and rpoZ/omega form the catalytic core. To initiate promoter specific DNA transcription, the core enzyme has to bind a sigma factor, which helps to direct the polymerase to specific promoters. rpoF transcribes genes involved in motility and flagellar synthesis including a set of the structural genes for flagella formation, and the chemotaxis genes encoding sensor of environmental signals affecting motility control.","predictedComplex":false,"interactors":[{"ac":"EBI-370560","identifier":"P0A800","identifierLink":"https://www.uniprot.org/uniprotkb/P0A800/entry","name":"rpoZ","description":"DNA-directed RNA polymerase subunit omega","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-543604","identifier":"P0A8T7","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8T7/entry","name":"rpoC","description":"DNA-directed RNA polymerase subunit beta'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR19376","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544985","identifier":"P0A7Z4","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7Z4/entry","name":"rpoA","description":"DNA-directed RNA polymerase subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32108","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544996","identifier":"P0A8V2","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8V2/entry","name":"rpoB","description":"DNA-directed RNA polymerase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR20856","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549807","identifier":"P0AEM6","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEM6/entry","name":"fliA","description":"RNA polymerase sigma factor FliA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30385","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-4887","complexName":"DNA-directed RNA polymerase holoenzyme complex, SigmaH variant","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the transcription of RNA from an DNA template by acting as a nucleotidyl transferase that polymerizes ribonucleotides at the 3' end of an RNA transcript. Five subunits, rpoA/alpha, rpoB/beta, rpoC/beta' and rpoZ/omega form the catalytic core. To initiate promoter specific DNA transcription, the core enzyme has to bind a sigma factor, which helps to direct the polymerase to specific promoters. rpoH acts in response to higher temperature, markedly and transiently inducing a set of heat-shock proteins which control the folding, assembly, transport, repair and degradation of various proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-370560","identifier":"P0A800","identifierLink":"https://www.uniprot.org/uniprotkb/P0A800/entry","name":"rpoZ","description":"DNA-directed RNA polymerase subunit omega","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-543604","identifier":"P0A8T7","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8T7/entry","name":"rpoC","description":"DNA-directed RNA polymerase subunit beta'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR19376","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544985","identifier":"P0A7Z4","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7Z4/entry","name":"rpoA","description":"DNA-directed RNA polymerase subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32108","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544996","identifier":"P0A8V2","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8V2/entry","name":"rpoB","description":"DNA-directed RNA polymerase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR20856","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-555342","identifier":"P0AGB3","identifierLink":"https://www.uniprot.org/uniprotkb/P0AGB3/entry","name":"rpoH","description":"RNA polymerase sigma factor RpoH","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30376","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-4888","complexName":"DNA-directed RNA polymerase holoenzyme complex, Sigma fecI variant","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the transcription of RNA from an DNA template by acting as a nucleotidyl transferase that polymerizes ribonucleotides at the 3' end of an RNA transcript.  Five subunits, rpoA/alpha, rpoB/beta, rpoC/beta' and rpoZ/omega form the catalytic core. To initiate promoter specific DNA transcription, the core enzyme has to bind a sigma factor, which helps to direct the polymerase to specific promoters. fecI is required for initiation of transcription of the ferric citrate transport genes required for the receptor of the ferric-citrate outer membrane transporter complex (CPX-3576) and the components of the ferric-citrate ABC transporter complex (CPX-4403).","predictedComplex":false,"interactors":[{"ac":"EBI-1133773","identifier":"P23484","identifierLink":"https://www.uniprot.org/uniprotkb/P23484/entry","name":"fecI","description":"Ferric citrate uptake sigma factor FecI","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43133","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-370560","identifier":"P0A800","identifierLink":"https://www.uniprot.org/uniprotkb/P0A800/entry","name":"rpoZ","description":"DNA-directed RNA polymerase subunit omega","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-543604","identifier":"P0A8T7","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8T7/entry","name":"rpoC","description":"DNA-directed RNA polymerase subunit beta'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR19376","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544985","identifier":"P0A7Z4","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7Z4/entry","name":"rpoA","description":"DNA-directed RNA polymerase subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32108","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544996","identifier":"P0A8V2","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8V2/entry","name":"rpoB","description":"DNA-directed RNA polymerase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR20856","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-4901","complexName":"rpod-rsd sigma-antisigma complex","organismName":"Escherichia coli (strain K12); 83333","description":"Regulates RpoD-mediated transcription activation by preventing the interaction between the primary sigma factor RpoD with DNA-directed RNA polymerase (RNAP) and with promoter DNA.The complex forms only during the stationary phase possibly due to rsd preferentially binding the non-phosphorylated form of the phosphoenolpyruvate-dependent phosphotransferase system control protein ptsH/HPr (P0AA04), which is the dominant form of HPr when cells are growing exponentially. Sequestration of rpoD into this complex biases the competition between rpoD and alternative Sigma factors for the available core RNAP.","predictedComplex":false,"interactors":[{"ac":"EBI-1134364","identifier":"P0AFX4","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFX4/entry","name":"rsd","description":"Regulator of sigma D","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-545104","identifier":"P00579","identifierLink":"https://www.uniprot.org/uniprotkb/P00579/entry","name":"rpoD","description":"RNA polymerase sigma factor RpoD","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30603","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1839","complexName":"alpha-1,6-mannosyltransferase complex, M-Pol II variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Role in the initiation and extension of an alpha -1,6-linked polymannose backbone as a first step in mannan synthesis, a branched polymer attached to the glycans of many of the proteins destined for the cell wall. May play the major role in the the extension of the mannan backbone after it is initiated by M-Pol I (CPX-1672).","predictedComplex":false,"interactors":[{"ac":"EBI-11043","identifier":"P50108","identifierLink":"https://www.uniprot.org/uniprotkb/P50108/entry","name":"MNN10","description":"Probable alpha-1,6-mannosyltransferase MNN10","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31306","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11052","identifier":"P46985","identifierLink":"https://www.uniprot.org/uniprotkb/P46985/entry","name":"MNN11","description":"Probable alpha-1,6-mannosyltransferase MNN11","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31306","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11082","identifier":"P39107","identifierLink":"https://www.uniprot.org/uniprotkb/P39107/entry","name":"MNN9","description":"Mannan polymerase complexes subunit MNN9","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2595","identifier":"P32629","identifierLink":"https://www.uniprot.org/uniprotkb/P32629/entry","name":"ANP1","description":"Mannan polymerase II complex ANP1 subunit","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8430","identifier":"P47124","identifierLink":"https://www.uniprot.org/uniprotkb/P47124/entry","name":"HOC1","description":"Putative glycosyltransferase HOC1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31834","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4943","complexName":"Exocyst, EXOC6 variant","organismName":"Homo sapiens; 9606","description":"Recruited to sites of active exocytosis and membrane expansion, where it mediates the tethering of secretory vesicles to the plasma membrane in preparation for soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein receptor (SNARE)-mediated membrane fusion. The targeting of secretory vesicles to the plasma membrane involves direct interactions of the Exocyst with PI(4,5)P2. In addition, a number of small GTP-binding proteins interact with components of the exocyst and regulate the assembly, localization, and function of this complex.\r\nThe Exocyst participates in a number of biological processes such as ciliogenesis, migration, autophagy, trafficking and cytokinesis.","predictedComplex":false,"interactors":[{"ac":"EBI-1045313","identifier":"Q9NV70","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NV70/entry","name":"EXOC1","description":"Exocyst complex component 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1052278","identifier":"O60645","identifierLink":"https://www.uniprot.org/uniprotkb/O60645/entry","name":"EXOC3","description":"Exocyst complex component 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21292","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1223394","identifier":"Q8TAG9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAG9/entry","name":"EXOC6","description":"Exocyst complex component 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12702","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355383","identifier":"Q96A65","identifierLink":"https://www.uniprot.org/uniprotkb/Q96A65/entry","name":"EXOC4","description":"Exocyst complex component 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14146","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465715","identifier":"Q96KP1","identifierLink":"https://www.uniprot.org/uniprotkb/Q96KP1/entry","name":"EXOC2","description":"Exocyst complex component 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13043","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-720048","identifier":"Q9UPT5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UPT5/entry","name":"EXOC7","description":"Exocyst complex component 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12542","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742102","identifier":"Q8IYI6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IYI6/entry","name":"EXOC8","description":"Exocyst complex component 8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21426","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-949824","identifier":"O00471","identifierLink":"https://www.uniprot.org/uniprotkb/O00471/entry","name":"EXOC5","description":"Exocyst complex component 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12100","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4944","complexName":"Exocyst, EXOC6B variant","organismName":"Homo sapiens; 9606","description":"Recruited to sites of active exocytosis and membrane expansion, where it mediates the tethering of secretory vesicles to the plasma membrane in preparation for soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein receptor (SNARE)-mediated membrane fusion. The targeting of secretory vesicles to the plasma membrane involves direct interactions of the Exocyst with PI(4,5)P2. In addition, a number of small GTP-binding proteins interact with components of the exocyst and regulate the assembly, localization, and function of this complex.\r\nThe Exocyst participates in a number of biological processes such as ciliogenesis, migration, autophagy, trafficking and cytokinesis. \r\n\r\nGenetic anomalies of EXOC6B seem to associate to a wide spectra of mental and neurological disorders, including autism, epilepsy and developmental delay.","predictedComplex":false,"interactors":[{"ac":"EBI-1045313","identifier":"Q9NV70","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NV70/entry","name":"EXOC1","description":"Exocyst complex component 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1052278","identifier":"O60645","identifierLink":"https://www.uniprot.org/uniprotkb/O60645/entry","name":"EXOC3","description":"Exocyst complex component 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21292","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2690026","identifier":"Q9Y2D4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2D4/entry","name":"EXOC6B","description":"Exocyst complex component 6B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12702","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355383","identifier":"Q96A65","identifierLink":"https://www.uniprot.org/uniprotkb/Q96A65/entry","name":"EXOC4","description":"Exocyst complex component 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14146","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465715","identifier":"Q96KP1","identifierLink":"https://www.uniprot.org/uniprotkb/Q96KP1/entry","name":"EXOC2","description":"Exocyst complex component 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13043","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-720048","identifier":"Q9UPT5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UPT5/entry","name":"EXOC7","description":"Exocyst complex component 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12542","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742102","identifier":"Q8IYI6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IYI6/entry","name":"EXOC8","description":"Exocyst complex component 8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21426","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-949824","identifier":"O00471","identifierLink":"https://www.uniprot.org/uniprotkb/O00471/entry","name":"EXOC5","description":"Exocyst complex component 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12100","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4945","complexName":"Coagulation factor IXa complex","organismName":"Homo sapiens; 9606","description":"Part of the intrinsic blood coagulation pathway (contact activation pathway). When bound to factor VIIIa (CPX-929) forms the intrinsic tenase complex that cleaves Arg-|-Ile bonds of factor X (P00742) by limited proteolysis to form active factor Xa (CPX-6215) in the presence of vitamin K, Ca2+ ions, phospholipids and factor VII (P08709). The coagulation pathway is terminated when fibrinogen is cleaved to fibrin which in turn polymerizes to produce a clot. \r\n\r\nIts zymogen form is activated by selective cleavage of Arg-|-Ala and Arg-|-Val bonds by limited proteolysis by factor XI (CPX-6205) to form active factor IXa. Factor VIIa-TF complex (CPX-2808) also contributes to its activation. Inhibited by antithrombin (SERPINC1, P01008). \r\n\r\nDefects in the coagulation pathway lead to hemophilia B or venous thrombosis.","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-22185597","identifier":"P00740-PRO_0000027757","identifierLink":"https://www.uniprot.org/uniprotkb/P00740-PRO_0000027757/entry","name":"F9","description":"Coagulation factor IXa light chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-22185613","identifier":"P00740-PRO_0000027759","identifierLink":"https://www.uniprot.org/uniprotkb/P00740-PRO_0000027759/entry","name":"F9","description":"Coagulation factor IXa heavy chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-4947","complexName":"NLRP1 inflammasome, variant 1","organismName":"Danio rerio; 7955","description":"A pro-inflammatory thiol protease complex that assembles in the cytosol in response to pathogens and other damage-associated signals and plays a critical role in innate immunity and inflammation. Activating platform for caspa through proximity-induced self-cleavage in an ATP-dependent reaction. Activated caspa causes the initial cleavage of pro-il1b (E0WCW4), the first step in the activation process of this protein. This is followed by the recruitment of caspb (CPX-4948), which is activated and further cleaves  il1b resulting in il1b maturation and secretion in the extracellular milieu.","predictedComplex":false,"interactors":[{"ac":"EBI-22186214","identifier":"A0A386CAB9","identifierLink":"https://www.uniprot.org/uniprotkb/A0A386CAB9/entry","name":"nlrp1","description":"NACHT, LRR and PYD domains-containing protein 1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Danio rerio; 7955","xrefs":[{"identifier":"PTHR45690","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6374180","identifier":"Q9I9L7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9I9L7/entry","name":"caspa","description":"Caspase a","stochiometry":null,"interactorType":"protein","organismName":"Danio rerio; 7955","xrefs":[{"identifier":"PTHR10454","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6374201","identifier":"Q9I9N6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9I9N6/entry","name":"pycard","description":"Apoptosis-associated speck-like protein containing a CARD","stochiometry":null,"interactorType":"protein","organismName":"Danio rerio; 7955","xrefs":[{"identifier":"PTHR46985","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4948","complexName":"NLRP1 inflammasome, variant 2","organismName":"Danio rerio; 7955","description":"A pro-inflammatory thiol protease complex that assembles in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation. Activating platform for caspa and caspb through proximity-induced self-cleavage in ATP-dependent reactions. Pro-caspa is preferentially recruited and then activated. . Activated caspa  (CPX-4947) causes the initial cleavage of pro-il1b (E0WCW4), the first step in the activation process of this protein. This is followed by the recruitment of caspb, which is activated and further cleaves  il1b resulting in il1b maturation and secretion in the extracellular milieu.","predictedComplex":false,"interactors":[{"ac":"EBI-22186214","identifier":"A0A386CAB9","identifierLink":"https://www.uniprot.org/uniprotkb/A0A386CAB9/entry","name":"nlrp1","description":"NACHT, LRR and PYD domains-containing protein 1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Danio rerio; 7955","xrefs":[{"identifier":"PTHR45690","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22186253","identifier":"Q504J1","identifierLink":"https://www.uniprot.org/uniprotkb/Q504J1/entry","name":"caspb","description":"Caspase b","stochiometry":null,"interactorType":"protein","organismName":"Danio rerio; 7955","xrefs":[{"identifier":"PTHR10454","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6374180","identifier":"Q9I9L7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9I9L7/entry","name":"caspa","description":"Caspase a","stochiometry":null,"interactorType":"protein","organismName":"Danio rerio; 7955","xrefs":[{"identifier":"PTHR10454","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6374201","identifier":"Q9I9N6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9I9N6/entry","name":"pycard","description":"Apoptosis-associated speck-like protein containing a CARD","stochiometry":null,"interactorType":"protein","organismName":"Danio rerio; 7955","xrefs":[{"identifier":"PTHR46985","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4962","complexName":"CyclinY-CDK17 complex","organismName":"Caenorhabditis elegans; 6239","description":"Cyclin-dependent serine/threonine-protein kinase complex, which is required to traffic presynaptic components to axons. Regulates the trafficking of synaptic vesicle precursors in DA motor neurons by promoting anterograde trafficking to the axon and preventing dynein-dependent trafficking to the dendrite. May also regulate synaptic vesicle trafficking in DD motor neurons and in RIA interneurons.","predictedComplex":false,"interactors":[{"ac":"EBI-2696495","identifier":"P34624","identifierLink":"https://www.uniprot.org/uniprotkb/P34624/entry","name":"cyy-1","description":"Cyclin-Y","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR14248","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2918577","identifier":"Q8I7M8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8I7M8/entry","name":"pct-1","description":"Cyclin-dependent kinase 17","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4981","complexName":"Complement component C1q complex","organismName":"Mus musculus; 10090","description":"Recognition unit of the classical pathway of complement which associates with the Ca2+ - dependent C1r(2)-C1s(2) tetramer to form C1 (CPX-4984), the first component of the classical complement system. The complex's role in C1 is the recognition of immune complexes, or other molecules, which trigger the classical pathway of the complement system. Independent of complement activation C1q appears to have additional roles in homeostasis and cellular development, superoxide (O2-) production by neutrophils, blood coagulation and neurological synapse pruning.","predictedComplex":false,"interactors":[{"ac":"EBI-20567414","identifier":"Q02105","identifierLink":"https://www.uniprot.org/uniprotkb/Q02105/entry","name":"C1qc","description":"Complement C1q subcomponent subunit C","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15427","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2794395","identifier":"P14106","identifierLink":"https://www.uniprot.org/uniprotkb/P14106/entry","name":"C1qb","description":"Complement C1q subcomponent subunit B","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15427","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-299840","identifier":"P98086","identifierLink":"https://www.uniprot.org/uniprotkb/P98086/entry","name":"C1qa","description":"Complement C1q subcomponent subunit A","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15427","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4982","complexName":"Exocyst, Exoc6 variant","organismName":"Mus musculus; 10090","description":"Recruited to sites of active exocytosis and membrane expansion, where it mediates the tethering of secretory vesicles to the plasma membrane in preparation for soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein receptor (SNARE)-mediated membrane fusion. The targeting of secretory vesicles to the plasma membrane involves direct interactions of the Exocyst with PI(4,5)P2. In addition, a number of small GTP-binding proteins interact with components of the exocyst and regulate the assembly, localization, and function of this complex.\r\nThe Exocyst participates in a number of biological processes such as ciliogenesis, migration, autophagy, trafficking and cytokinesis.","predictedComplex":false,"interactors":[{"ac":"EBI-772648","identifier":"O35382","identifierLink":"https://www.uniprot.org/uniprotkb/O35382/entry","name":"Exoc4","description":"Exocyst complex component 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14146","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-775332","identifier":"O35250","identifierLink":"https://www.uniprot.org/uniprotkb/O35250/entry","name":"Exoc7","description":"Exocyst complex component 7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12542","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-775347","identifier":"Q6PGF7","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PGF7/entry","name":"Exoc8","description":"Exocyst complex component 8","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21426","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-775555","identifier":"Q3TPX4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TPX4/entry","name":"Exoc5","description":"Exocyst complex component 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12100","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-775567","identifier":"Q9D4H1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D4H1/entry","name":"Exoc2","description":"Exocyst complex component 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13043","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-775577","identifier":"Q6KAR6","identifierLink":"https://www.uniprot.org/uniprotkb/Q6KAR6/entry","name":"Exoc3","description":"Exocyst complex component 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21292","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8321006","identifier":"Q8R3S6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R3S6/entry","name":"Exoc1","description":"Exocyst complex component 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9202179","identifier":"Q8R313","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R313/entry","name":"Exoc6","description":"Exocyst complex component 6","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12702","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4983","complexName":"Exocyst, Exoc6b variant","organismName":"Mus musculus; 10090","description":"Recruited to sites of active exocytosis and membrane expansion, where it mediates the tethering of secretory vesicles to the plasma membrane in preparation for soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein receptor (SNARE)-mediated membrane fusion. The targeting of secretory vesicles to the plasma membrane involves direct interactions of the Exocyst with PI(4,5)P2. In addition, a number of small GTP-binding proteins interact with components of the exocyst and regulate the assembly, localization, and function of this complex.\r\nThe Exocyst participates in a number of biological processes such as ciliogenesis, migration, autophagy, trafficking and cytokinesis.","predictedComplex":false,"interactors":[{"ac":"EBI-22195966","identifier":"A6H5Z3","identifierLink":"https://www.uniprot.org/uniprotkb/A6H5Z3/entry","name":"Exoc6b","description":"Exocyst complex component 6B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12702","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-772648","identifier":"O35382","identifierLink":"https://www.uniprot.org/uniprotkb/O35382/entry","name":"Exoc4","description":"Exocyst complex component 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14146","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-775332","identifier":"O35250","identifierLink":"https://www.uniprot.org/uniprotkb/O35250/entry","name":"Exoc7","description":"Exocyst complex component 7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12542","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-775347","identifier":"Q6PGF7","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PGF7/entry","name":"Exoc8","description":"Exocyst complex component 8","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21426","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-775555","identifier":"Q3TPX4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TPX4/entry","name":"Exoc5","description":"Exocyst complex component 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12100","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-775567","identifier":"Q9D4H1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D4H1/entry","name":"Exoc2","description":"Exocyst complex component 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13043","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-775577","identifier":"Q6KAR6","identifierLink":"https://www.uniprot.org/uniprotkb/Q6KAR6/entry","name":"Exoc3","description":"Exocyst complex component 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21292","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8321006","identifier":"Q8R3S6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R3S6/entry","name":"Exoc1","description":"Exocyst complex component 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4984","complexName":"Complement C1 complex, C1ra-C1sa variant","organismName":"Mus musculus; 10090","description":"The first component of the classical serum complement system. In the presence of calcium, the C1q complex (CPX-4981) associates with the C1S-C1R-C1R-C1S tetramer. When C1q binds to an activating target, a conformational change triggers the auto-activation of the associated C1R protease (converting the pro-enzyme into an activated form), which activates C1S. C1S then cleaves the Arg-|-Ala bond in complement component C4 to form C4a and C4b, and the Lys(or Arg)-|-Lys bond in complement component C2 to form C2a and C2b. The C1r and C1s genes are duplicated in the mouse: C1ra and C1sa are homologous to the human genes, whereas C1rb and C1sb (CPX-4985) are reported to be expressed exclusively in two male reproductive accessory glands.","predictedComplex":false,"interactors":[{"ac":"EBI-22195732","identifier":"CPX-4981","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-4981","name":"Complement component C1q complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-22196402","identifier":"Q8CG16-PRO_0000027581","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CG16-PRO_0000027581/entry","name":"C1ra","description":"Complement C1r-A subcomponent heavy chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-22196409","identifier":"Q8CG16-PRO_0000027582","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CG16-PRO_0000027582/entry","name":"C1ra","description":"Complement C1r-A subcomponent light chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-22196447","identifier":"Q8CG14-PRO_0000042194","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CG14-PRO_0000042194/entry","name":"C1s1","description":"Complement C1s-A subcomponent heavy chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-22196453","identifier":"Q8CG14-PRO_0000042195","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CG14-PRO_0000042195/entry","name":"C1s1","description":"Complement C1s-A subcomponent light chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-4985","complexName":"Complement C1 complex, C1rb-C1sb variant","organismName":"Mus musculus; 10090","description":"The first component of the classical serum complement system. In the presence of calcium, the C1q complex (CPX-4981) associates with the C1S-C1R-C1R-C1S tetramer. When C1q binds to an activating target, a conformational change triggers the auto-activation of the associated C1R protease (converting the pro-enzyme into an activated form), which activates C1S. C1S then cleaves the Arg-|-Ala bond in complement component C4 to form C4a and C4b, and the Lys(or Arg)-|-Lys bond in complement component C2 to form C2a and C2b. The C1r and C1s genes are duplicated in the mouse: C1ra and C1sa (CPX-4984) are homologous to the human genes, whereas C1rb and C1sb are reported to be expressed exclusively in two male reproductive accessory glands.","predictedComplex":false,"interactors":[{"ac":"EBI-22195732","identifier":"CPX-4981","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-4981","name":"Complement component C1q complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-22196561","identifier":"Q8CFG9-PRO_0000042188","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CFG9-PRO_0000042188/entry","name":"C1rb","description":"Complement C1r-B subcomponent heavy chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-22196567","identifier":"Q8CFG9-PRO_0000042189","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CFG9-PRO_0000042189/entry","name":"C1rb","description":"Complement C1r-B subcomponent light chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-22196605","identifier":"Q8CFG8-PRO_0000042197","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CFG8-PRO_0000042197/entry","name":"C1s2","description":"Complement C1s-B subcomponent heavy chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-22196612","identifier":"Q8CFG8-PRO_0000042198","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CFG8-PRO_0000042198/entry","name":"C1s2","description":"Complement C1s-B subcomponent light chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-5001","complexName":"CPLANE complex","organismName":"Homo sapiens; 9606","description":"Plays a key role in ciliogenesis, in the definition of cell polarity and in embryonic development. \r\nInteracts with CPLANE1 (Q9H799) and CPLANE2 (Q9BU20) to recruit peripheral IFT-A proteins to basal bodies. IFT-A (CPX-5021) and IFT-B (CPX-5022) are reported to control retrograde and anterograde traffic, respectively. In this way the CPLANE complex regulates cilia formation by controlling the organisation of the apical actin cytoskeleton and the positioning of the basal bodies at the apical cell surface, which in turn is essential for the normal orientation of elongating ciliary microtubules.\r\n\r\nMutations of CPLANE complex subunits are associated with ciliopathies.","predictedComplex":false,"interactors":[{"ac":"EBI-11762696","identifier":"Q9ULD6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ULD6/entry","name":"INTU","description":"Protein inturned","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2826290","identifier":"O95876","identifierLink":"https://www.uniprot.org/uniprotkb/O95876/entry","name":"WDPCP","description":"WD repeat-containing and planar cell polarity effector protein fritz homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13667","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-750341","identifier":"Q9BT04","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BT04/entry","name":"FUZ","description":"Protein fuzzy homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13559","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5021","complexName":"Intraflagellar transport complex A","organismName":"Homo sapiens; 9606","description":"IFT particles, composed of the IFT-A and IFT-B (CPX-5022) complexes, enable bidirectional motility along axoneme microtubules essential for the formation (ciliogenesis) and maintenance of cilia that assemble within a membrane projection from the cell surface. Outward or anterograde movement from the cell body to the ciliary tip  is powered by kinesin-2 while the inward or retrograde movement back to the cell body is powered by cytoplasmic Dynein-2 motor. Required to recruit TULP3 (O75386) to primary cilia to allow entry into cilia of G protein-coupled receptors (GPCRs). Interacts with the BBSome complex (CPX-1908) to mediate ciliary transport.\r\n\r\nPatients with mutations in IFT43 develop ciliopathies.","predictedComplex":false,"interactors":[{"ac":"EBI-10189681","identifier":"Q96FT9","identifierLink":"https://www.uniprot.org/uniprotkb/Q96FT9/entry","name":"IFT43","description":"Intraflagellar transport protein 43 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR33724","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11903679","identifier":"Q8NEZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NEZ3/entry","name":"WDR19","description":"WD repeat-containing protein 19","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14920","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2805994","identifier":"Q9HBG6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HBG6/entry","name":"IFT122","description":"Intraflagellar transport protein 122 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12764","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2851301","identifier":"Q7Z4L5","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z4L5/entry","name":"TTC21B","description":"Tetratricopeptide repeat protein 21B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14699","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-308494","identifier":"Q96RY7","identifierLink":"https://www.uniprot.org/uniprotkb/Q96RY7/entry","name":"IFT140","description":"Intraflagellar transport protein 140 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15722","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-766448","identifier":"Q9P2L0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P2L0/entry","name":"WDR35","description":"WD repeat-containing protein 35","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16517","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5022","complexName":"Intraflagellar transport complex B","organismName":"Homo sapiens; 9606","description":"IFT particles, composed of the IFT-A (CPX-5021) and IFT-B complexes, enable bidirectional motility along axoneme microtubules essential for the formation (ciliogenesis) and maintenance of cilia that assemble within a membrane projection from the cell surface. Outward or anterograde movement from the cell body to the ciliary tip  is powered by kinesin-2 while the inward or retrograde movement back to the cell body is powered by cytoplasmic Dynein-2 motor. Required to recruit TULP3 (O75386) to primary cilia to allow entry into cilia of G protein-coupled receptors (GPCRs). Interacts with the BBSome complex (CPX-1908) to mediate ciliary transport.\r\n\r\nPatients with mutations in IFT-B complex subunits develop ciliopathies.","predictedComplex":false,"interactors":[{"ac":"EBI-1044125","identifier":"Q9H7X7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H7X7/entry","name":"IFT22","description":"Intraflagellar transport protein 22 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11321879","identifier":"Q8WYA0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WYA0/entry","name":"IFT81","description":"Intraflagellar transport protein 81 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15614","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11321887","identifier":"A0AVF1","identifierLink":"https://www.uniprot.org/uniprotkb/A0AVF1/entry","name":"IFT56","description":"Intraflagellar transport protein 56","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14781","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11321900","identifier":"Q96LB3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96LB3/entry","name":"IFT74","description":"Intraflagellar transport protein 74 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31432","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11339918","identifier":"Q9NQC8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NQC8/entry","name":"IFT46","description":"Intraflagellar transport protein 46 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13376","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11927321","identifier":"Q9Y366","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y366/entry","name":"IFT52","description":"Intraflagellar transport protein 52 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12969","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2815009","identifier":"Q9UG01","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UG01/entry","name":"IFT172","description":"Intraflagellar transport protein 172 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15722","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2831704","identifier":"Q9P2H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P2H3/entry","name":"IFT80","description":"Intraflagellar transport protein 80 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24098","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347427","identifier":"Q13099","identifierLink":"https://www.uniprot.org/uniprotkb/Q13099/entry","name":"IFT88","description":"Intraflagellar transport protein 88 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6958994","identifier":"Q8N4P2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N4P2/entry","name":"IFT70B","description":"Intraflagellar transport protein 70B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20931","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-725672","identifier":"Q9NWB7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NWB7/entry","name":"IFT57","description":"Intraflagellar transport protein 57 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16011","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-739780","identifier":"Q96AJ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q96AJ1/entry","name":"CLUAP1","description":"Clusterin-associated protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21547","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744203","identifier":"Q8IY31","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IY31/entry","name":"IFT20","description":"Intraflagellar transport protein 20 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31978","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-747093","identifier":"Q9BW83","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BW83/entry","name":"IFT27","description":"Intraflagellar transport protein 27 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47979","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-747101","identifier":"Q9Y547","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y547/entry","name":"IFT25","description":"Intraflagellar transport protein 25 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR33906","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-928811","identifier":"Q8TDR0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TDR0/entry","name":"TRAF3IP1","description":"TRAF3-interacting protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31363","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5024","complexName":"rpoS-rssB sigma-antisigma complex","organismName":"Escherichia coli (strain K12); 83333","description":"Regulates RpoD-mediated transcription activation by triggering degradation of rpoS by the ClpXP endopeptidase complex (CPX-3176). The complex forms under normal growth conditions but its formation is inhibited by the presence of anti-adaptor proteins: iraP (P0AAN9) specifically induced in response to phosphate starvation, iraD (P39375) which is specifically induced in response to DNA damage and iraM (P75987) which is specifically induced in response to magnesium starvation. rpoS is rapidly degraded by ClpXP in exponentially growing cells, but degradation stops as cells enter stationary phase.","predictedComplex":false,"interactors":[{"ac":"EBI-1122979","identifier":"P0AEV1","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEV1/entry","name":"rssB","description":"Regulator of RpoS","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR48111","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-557581","identifier":"P13445","identifierLink":"https://www.uniprot.org/uniprotkb/P13445/entry","name":"rpoS","description":"RNA polymerase sigma factor RpoS","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30603","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5025","complexName":"Dynein-1 complex, variant 1","organismName":"Homo sapiens; 9606","description":"Multi-protein molecular motor. Dynein-1 is one of three major classes of dynein, which share a conserved motor domain that couples ATP hydrolysis with conformational changes to power intracellular retrograde movement of cargoes including vesicles and organelles along microtubules within the cytoplasm.\r\n\r\nMutations in DYNC1H1 have been implicated in neurological disorders including an axonal form of Charcot-Marie-Tooth disease.","predictedComplex":false,"interactors":[{"ac":"EBI-1176455","identifier":"P63172","identifierLink":"https://www.uniprot.org/uniprotkb/P63172/entry","name":"DYNLT1","description":"Dynein light chain Tctex-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-349105","identifier":"P63167","identifierLink":"https://www.uniprot.org/uniprotkb/P63167/entry","name":"DYNLL1","description":"Dynein light chain 1, cytoplasmic","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356015","identifier":"Q14204","identifierLink":"https://www.uniprot.org/uniprotkb/Q14204/entry","name":"DYNC1H1","description":"Cytoplasmic dynein 1 heavy chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372128","identifier":"Q9NP97","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NP97/entry","name":"DYNLRB1","description":"Dynein light chain roadblock-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-715294","identifier":"O43237","identifierLink":"https://www.uniprot.org/uniprotkb/O43237/entry","name":"DYNC1LI2","description":"Cytoplasmic dynein 1 light intermediate chain 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12688","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742998","identifier":"Q13409","identifierLink":"https://www.uniprot.org/uniprotkb/Q13409/entry","name":"DYNC1I2","description":"Cytoplasmic dynein 1 intermediate chain 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5026","complexName":"CPLANE complex","organismName":"Mus musculus; 10090","description":"Plays a key role in ciliogenesis, in the definition of cell polarity and in embryonic development. \r\nInteracts with Cplane1 (Q8CE72) and Cplane2 (A2A825) to recruit peripheral IFT-A proteins to basal bodies. IFT-A (CPX-5027) and IFT-B (CPX-5028) are reported to control retrograde and anterograde traffic, respectively. In this way the CPLANE complex regulates cilia formation by controlling the organisation of the apical actin cytoskeleton and the positioning of the basal bodies at the apical cell surface, which in turn is essential for the normal orientation of elongating ciliary microtubules.","predictedComplex":false,"interactors":[{"ac":"EBI-16356699","identifier":"Q8C456","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C456/entry","name":"Wdpcp","description":"WD repeat-containing and planar cell polarity effector protein fritz homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13667","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22225802","identifier":"Q3UYI6","identifierLink":"https://www.uniprot.org/uniprotkb/Q3UYI6/entry","name":"Fuz","description":"Protein fuzzy homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13559","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22225839","identifier":"Q059U7","identifierLink":"https://www.uniprot.org/uniprotkb/Q059U7/entry","name":"Intu","description":"Protein inturned","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5027","complexName":"Intraflagellar transport complex A","organismName":"Mus musculus; 10090","description":"IFT particles, composed of the IFT-A and IFT-B (CPX-5022) complexes, enable bidirectional motility along axoneme microtubules essential for the formation (ciliogenesis) and maintenance of cilia that assemble within a membrane projection from the cell surface. Outward or anterograde movement from the cell body to the ciliary tip  is powered by kinesin-2 while the inward or retrograde movement back to the cell body is powered by cytoplasmic Dynein-2 motor. Required to recruit Tulp3 (O88413) to primary cilia to allow entry into cilia of G protein-coupled receptors (GPCRs). Interacts with the BBSome complex (CPX-1909) to mediate ciliary transport.","predictedComplex":false,"interactors":[{"ac":"EBI-16011374","identifier":"Q3UGF1","identifierLink":"https://www.uniprot.org/uniprotkb/Q3UGF1/entry","name":"Wdr19","description":"WD repeat-containing protein 19","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14920","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22225953","identifier":"E9PY46","identifierLink":"https://www.uniprot.org/uniprotkb/E9PY46/entry","name":"Ift140","description":"Intraflagellar transport protein 140 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15722","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22226001","identifier":"Q9DA69","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DA69/entry","name":"Ift43","description":"Intraflagellar transport protein 43 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR33724","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22226023","identifier":"Q0HA38","identifierLink":"https://www.uniprot.org/uniprotkb/Q0HA38/entry","name":"Ttc21b","description":"Tetratricopeptide repeat protein 21B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14699","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22226055","identifier":"Q8BND3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BND3/entry","name":"Wdr35","description":"WD repeat-containing protein 35","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16517","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4283871","identifier":"Q6NWV3","identifierLink":"https://www.uniprot.org/uniprotkb/Q6NWV3/entry","name":"Ift122","description":"Intraflagellar transport protein 122 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12764","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5028","complexName":"Intraflagellar transport complex B","organismName":"Mus musculus; 10090","description":"IFT particles, composed of the IFT-A and IFT-B (CPX-5022) complexes, enable bidirectional motility along axoneme microtubules essential for the formation (ciliogenesis) and maintenance of cilia that assemble within a membrane projection from the cell surface. Outward or anterograde movement from the cell body to the ciliary tip  is powered by kinesin-2 while the inward or retrograde movement back to the cell body is powered by cytoplasmic Dynein-2 motor. Required to recruit Tulp3 (O88413) to primary cilia to allow entry into cilia of G protein-coupled receptors (GPCRs). Interacts with the BBSome complex (CPX-1909) to mediate ciliary transport.","predictedComplex":false,"interactors":[{"ac":"EBI-11571155","identifier":"Q9D0P8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D0P8/entry","name":"Ift27","description":"Intraflagellar transport protein 27 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR47979","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11571307","identifier":"Q9DAI2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DAI2/entry","name":"Ift22","description":"Intraflagellar transport protein 22 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16077253","identifier":"Q61025","identifierLink":"https://www.uniprot.org/uniprotkb/Q61025/entry","name":"Ift20","description":"Intraflagellar transport protein 20 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR31978","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16726521","identifier":"Q149C2","identifierLink":"https://www.uniprot.org/uniprotkb/Q149C2/entry","name":"Traf3ip1","description":"TRAF3-interacting protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR31363","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20975111","identifier":"Q9DB07","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DB07/entry","name":"Ift46","description":"Intraflagellar transport protein 46 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13376","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22226614","identifier":"Q8R3P7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R3P7/entry","name":"Cluap1","description":"Clusterin-associated protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21547","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22226681","identifier":"Q6VH22","identifierLink":"https://www.uniprot.org/uniprotkb/Q6VH22/entry","name":"Ift172","description":"Intraflagellar transport protein 172 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15722","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22226739","identifier":"Q9D6H2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D6H2/entry","name":"Ift25","description":"Intraflagellar transport protein 25 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR33906","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22226773","identifier":"Q8BS45","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BS45/entry","name":"Ift56","description":"Intraflagellar transport protein 56","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14781","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22226804","identifier":"Q8BXG3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BXG3/entry","name":"Ift57","description":"Intraflagellar transport protein 57 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16011","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22226841","identifier":"Q8BKE9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BKE9/entry","name":"Ift74","description":"Intraflagellar transport protein 74 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR31432","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22226885","identifier":"Q8K057","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K057/entry","name":"Ift80","description":"Intraflagellar transport protein 80 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24098","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22226927","identifier":"O35594","identifierLink":"https://www.uniprot.org/uniprotkb/O35594/entry","name":"Ift81","description":"Intraflagellar transport protein 81 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15614","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22226958","identifier":"Q61371","identifierLink":"https://www.uniprot.org/uniprotkb/Q61371/entry","name":"Ift88","description":"Intraflagellar transport protein 88 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR44117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22227042","identifier":"Q9CY00","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CY00/entry","name":"Ift70b","description":"Intraflagellar transport protein 70B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR20931","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6959048","identifier":"Q62559","identifierLink":"https://www.uniprot.org/uniprotkb/Q62559/entry","name":"Ift52","description":"Intraflagellar transport protein 52 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12969","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5029","complexName":"BORC complex","organismName":"Homo sapiens; 9606","description":"Lysosome associated multi-subunit protein complex that promotes lysosome positioning at the cytosolic face of lysosomal membrane through coupling to the small GTPase ARL8B (Q9NVJ2). This initiates a chain of interactions that promotes the kinesin-dependent movement of lysosomes toward the plus ends of microtubules in the peripheral cytoplasm. \r\n\r\nBORC interacts with the Ragulator complex (CPX-4741) to regulate late endosomal/lysosomal size in response to glucose levels.","predictedComplex":false,"interactors":[{"ac":"EBI-10193358","identifier":"Q96GS4","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GS4/entry","name":"BORCS6","description":"BLOC-1-related complex subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13440","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-296723","identifier":"O95295","identifierLink":"https://www.uniprot.org/uniprotkb/O95295/entry","name":"SNAPIN","description":"SNARE-associated protein Snapin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348630","identifier":"P78537","identifierLink":"https://www.uniprot.org/uniprotkb/P78537/entry","name":"BLOC1S1","description":"Biogenesis of lysosome-related organelles complex 1 subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465872","identifier":"Q6QNY1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6QNY1/entry","name":"BLOC1S2","description":"Biogenesis of lysosome-related organelles complex 1 subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46479","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6151489","identifier":"Q96B45","identifierLink":"https://www.uniprot.org/uniprotkb/Q96B45/entry","name":"BORCS7","description":"BLOC-1-related complex subunit 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31397","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-739657","identifier":"Q9BQD3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BQD3/entry","name":"KXD1","description":"KxDL motif-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13511","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744076","identifier":"Q96FH0","identifierLink":"https://www.uniprot.org/uniprotkb/Q96FH0/entry","name":"BORCS8","description":"BLOC-1-related complex subunit 8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21146","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-747707","identifier":"Q969J3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969J3/entry","name":"BORCS5","description":"BLOC-1-related complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31634","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5041","complexName":"Glutamate synthase [NADPH] complex","organismName":"Escherichia coli (strain K12); 83333","description":"Glutamate synthase complex that plays a key role in assimilating nitrogen by catalyzing the conversion of L-glutamine and 2-oxoglutarate into two molecules of L-glutamate. One of the glutamate molecules enters back into the cycle, enabling glnA (P0A9C5) to produces glutamine from ammonia, glutamate and ATP, and the other represents net ammonia incorporation. gltBD is active in a low nitrogen evironment, whilst gdhA (P00370) glutamate dehydrogenase activity dominates in high nitrogen conditions.","predictedComplex":false,"interactors":[{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-544293","identifier":"P09832","identifierLink":"https://www.uniprot.org/uniprotkb/P09832/entry","name":"gltD","description":"Glutamate synthase [NADPH] small chain","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42783","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-551179","identifier":"P09831","identifierLink":"https://www.uniprot.org/uniprotkb/P09831/entry","name":"gltB","description":"Glutamate synthase [NADPH] large chain","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11938","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5043","complexName":"BLOC-3 complex","organismName":"Homo sapiens; 9606","description":"A guanine exchange factor (GEF) complex required for the biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules. \r\n\r\nActs as GEF for RAB32 (Q13637) and RAB38 (P57729), promoting the exchange of GDP to GTP, converting them into an active GTP-bound form and inducing their recruitment to membrane. Once active, both interact with the AP-1 (CPX-5047, CPX-5048 and CPX-5049), the AP-3 (CPX-5051 and CPX-5052) and the BLOC-2 (CPX-5044) adapter complexes, to regulate cargo delivery to nascent melanosomes and platelet dense granules.\r\n\r\nMutations in HPS1 are the most frequent cause of Hermansky-Pudlak syndrome.","predictedComplex":false,"interactors":[{"ac":"EBI-704347","identifier":"Q92902","identifierLink":"https://www.uniprot.org/uniprotkb/Q92902/entry","name":"HPS1","description":"BLOC-3 complex member HPS1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-704377","identifier":"Q9NQG7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NQG7/entry","name":"HPS4","description":"BLOC-3 complex member HPS4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14407","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5044","complexName":"BLOC-2 complex","organismName":"Homo sapiens; 9606","description":"Adaptor complex required for the biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules. \r\n\r\nOnce RAB32 (Q13637) and RAB38 (P57729) are activated by BLOC-3 (CPX-5043), they interact with AP-3 (CPX-5051 and CPX-5052), AP-1 (CPX-5047, CPX-5048 and CPX-5049) and BLOC-2 complexes which function as adaptor complexes on early/recycling endosome tubules, where cargo are loaded into vesicles or transport intermediates and transported to nascent melanosomes and platelet dense granules.\r\n\r\nMutations in HPS genes are frequent cause of Hermansky-Pudlak syndrome.","predictedComplex":false,"interactors":[{"ac":"EBI-10962552","identifier":"Q9UPZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UPZ3/entry","name":"HPS5","description":"BLOC-2 complex member HPS5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23287","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16781620","identifier":"Q969F9","identifierLink":"https://www.uniprot.org/uniprotkb/Q969F9/entry","name":"HPS3","description":"BLOC-2 complex member HPS3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-721349","identifier":"Q86YV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q86YV9/entry","name":"HPS6","description":"BLOC-2 complex member HPS6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14696","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5046","complexName":"FtsH-HflKC complex","organismName":"Escherichia coli (strain K12); 83333","description":"Formation of this complex prevents the proteolytic cleavage of ftsH substrates such as unfolded secY (P0AGA2), the rpoH transcription factor (P0AGB3) and CII (P03042) the key tetrameric transcription factor determining the lysis/lysogeny decision for coliphage lambda.","predictedComplex":false,"interactors":[{"ac":"EBI-548381","identifier":"P0AAI3","identifierLink":"https://www.uniprot.org/uniprotkb/P0AAI3/entry","name":"ftsH","description":"ATP-dependent zinc metalloprotease FtsH","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR23076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-551642","identifier":"P0ABC3","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABC3/entry","name":"hflC","description":"Modulator of FtsH protease HflC","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42911","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-558599","identifier":"P0ABC7","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABC7/entry","name":"hflK","description":"Modulator of FtsH protease HflK","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43327","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5047","complexName":"Ubiquitous AP-1 Adaptor complex, sigma1a variant","organismName":"Homo sapiens; 9606","description":"Adaptor complex that orchestrates the formation of membrane coats that mediate cargo selection and vesicle budding, for example by linking clathrin to the membrane surface of trans-Golgi network vesicles. Also recruits proteins involved in downstream vesicle functions such as motility, vesicle tethering and fusion with the target organelle. Required for the biogenesis of specialised organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules.\r\n\r\nOnce RAB32 (Q13637) and RAB38 (P57729) are activated by BLOC-3 (CPX-5043), they interact with AP-3 (CPX-5051 and CPX-5052), AP-1 and BLOC-2 (CPX-5044) complexes which function as adaptor complexes on early/recycling endosome tubules, where cargoes are loaded into vesicles or transport intermediates and transported to nascent melanosomes and platelet dense granules.\r\n\r\nMutations in AP1S1 are related to the MEDNIK syndrome.","predictedComplex":false,"interactors":[{"ac":"EBI-1171303","identifier":"Q10567","identifierLink":"https://www.uniprot.org/uniprotkb/Q10567/entry","name":"AP1B1","description":"AP-1 complex subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-447609","identifier":"O43747","identifierLink":"https://www.uniprot.org/uniprotkb/O43747/entry","name":"AP1G1","description":"AP-1 complex subunit gamma-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-516199","identifier":"P61966","identifierLink":"https://www.uniprot.org/uniprotkb/P61966/entry","name":"AP1S1","description":"AP-1 complex subunit sigma-1A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-541426","identifier":"Q9BXS5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BXS5/entry","name":"AP1M1","description":"AP-1 complex subunit mu-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5048","complexName":"Ubiquitous AP-1 Adaptor complex, sigma1b variant","organismName":"Homo sapiens; 9606","description":"Adaptor complex that orchestrates the formation of membrane coats that mediate cargo selection and vesicle budding, for example by linking clathrin to the membrane surface of trans-Golgi network vesicles. Also recruits proteins involved in downstream vesicle functions such as motility, vesicle tethering and fusion with the target organelle. Required for the biogenesis of specialised organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules.\r\n\r\nOnce RAB32 (Q13637) and RAB38 (P57729) are activated by BLOC-3 (CPX-5043), they interact with AP-3 (CPX-5051 and CPX-5052), AP-1 and BLOC-2 (CPX-5044) complexes which function as adaptor complexes on early/recycling endosome tubules, where cargoes are loaded into vesicles or transport intermediates and transported to nascent melanosomes and platelet dense granules.\r\n\r\nMutations in AP1S2 are related to the Pettigrew syndrome.","predictedComplex":false,"interactors":[{"ac":"EBI-1054374","identifier":"P56377","identifierLink":"https://www.uniprot.org/uniprotkb/P56377/entry","name":"AP1S2","description":"AP-1 complex subunit sigma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1171303","identifier":"Q10567","identifierLink":"https://www.uniprot.org/uniprotkb/Q10567/entry","name":"AP1B1","description":"AP-1 complex subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-447609","identifier":"O43747","identifierLink":"https://www.uniprot.org/uniprotkb/O43747/entry","name":"AP1G1","description":"AP-1 complex subunit gamma-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-541426","identifier":"Q9BXS5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BXS5/entry","name":"AP1M1","description":"AP-1 complex subunit mu-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5049","complexName":"Ubiquitous AP-1 Adaptor complex, sigma1c variant","organismName":"Homo sapiens; 9606","description":"Adaptor complex that orchestrates the formation of membrane coats that mediate cargo selection and vesicle budding, for example by linking clathrin to the membrane surface of trans-Golgi network vesicles. Also recruits proteins involved in downstream vesicle functions such as motility, vesicle tethering and fusion with the target organelle. Required for the biogenesis of specialised organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules.\r\n\r\nOnce RAB32 (Q13637) and RAB38 (P57729) are activated by BLOC-3 (CPX-5043), they interact with AP-3 (CPX-5051 and CPX-5052), AP-1 and BLOC-2 (CPX-5044) complexes which function as adaptor complexes on early/recycling endosome tubules, where cargoes are loaded into vesicles or transport intermediates and transported to nascent melanosomes and platelet dense granules.\r\n\r\nPhe4Cys and Arg33Trp mutations in AP1S3 are related to pustular psoriasis.","predictedComplex":false,"interactors":[{"ac":"EBI-1171303","identifier":"Q10567","identifierLink":"https://www.uniprot.org/uniprotkb/Q10567/entry","name":"AP1B1","description":"AP-1 complex subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3923129","identifier":"Q96PC3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96PC3/entry","name":"AP1S3","description":"AP-1 complex subunit sigma-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-447609","identifier":"O43747","identifierLink":"https://www.uniprot.org/uniprotkb/O43747/entry","name":"AP1G1","description":"AP-1 complex subunit gamma-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-541426","identifier":"Q9BXS5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BXS5/entry","name":"AP1M1","description":"AP-1 complex subunit mu-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5050","complexName":"Endothelial AP-1 Adaptor complex, sigma1a variant","organismName":"Homo sapiens; 9606","description":"Adaptor complex that links clathrin to the membrane surface of trans-Golgi network vesicles and is involved in basolateral transport and the polarized sorting of vesicle in epithelial cells.\r\n\r\nReduced expression of AP1M2 was reported in patients affected by colorectal cancer and by Crohn's disease.","predictedComplex":false,"interactors":[{"ac":"EBI-1171303","identifier":"Q10567","identifierLink":"https://www.uniprot.org/uniprotkb/Q10567/entry","name":"AP1B1","description":"AP-1 complex subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-447609","identifier":"O43747","identifierLink":"https://www.uniprot.org/uniprotkb/O43747/entry","name":"AP1G1","description":"AP-1 complex subunit gamma-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-516199","identifier":"P61966","identifierLink":"https://www.uniprot.org/uniprotkb/P61966/entry","name":"AP1S1","description":"AP-1 complex subunit sigma-1A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752250","identifier":"Q9Y6Q5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6Q5/entry","name":"AP1M2","description":"AP-1 complex subunit mu-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5051","complexName":"Ubiquitous AP-3 Adaptor complex, sigma3a variant","organismName":"Homo sapiens; 9606","description":"Adaptor complex that links clathrin to the membrane surface of endosomal vesicles and is required for the biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules. \r\n\r\nOnce RAB32 (Q13637) and RAB38 (P57729) are activated by BLOC-3 (CPX-5043), they interact with AP-3, AP-1 (CPX-5047, CPX-5048 and CPX-5049) and BLOC-2 (CPX-5044) complexes which function as adaptor complexes on early/recycling endosome tubules, where cargoes are loaded into vesicles or transport intermediates and transported to nascent melanosomes and platelet dense granules.\r\n\r\nDefects in AP-3 are related to Hermansky-Pudlak syndrome.","predictedComplex":false,"interactors":[{"ac":"EBI-1044383","identifier":"O00203","identifierLink":"https://www.uniprot.org/uniprotkb/O00203/entry","name":"AP3B1","description":"AP-3 complex subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1051639","identifier":"O14617","identifierLink":"https://www.uniprot.org/uniprotkb/O14617/entry","name":"AP3D1","description":"AP-3 complex subunit delta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22781","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2371151","identifier":"Q9Y2T2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2T2/entry","name":"AP3M1","description":"AP-3 complex subunit mu-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4289921","identifier":"Q92572","identifierLink":"https://www.uniprot.org/uniprotkb/Q92572/entry","name":"AP3S1","description":"AP-3 complex subunit sigma-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5052","complexName":"Ubiquitous AP-3 Adaptor complex, sigma3b variant","organismName":"Homo sapiens; 9606","description":"Adaptor complex that links clathrin to the membrane surface of endosomal vesicles and is required for the biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules. \r\n\r\nOnce RAB32 (Q13637) and RAB38 (P57729) are activated by BLOC-3 (CPX-5043), they interact with AP-3, AP-1 (CPX-5047, CPX-5048 and CPX-5049) and BLOC-2 (CPX-5044) complexes which function as adaptor complexes on early/recycling endosome tubules, where cargoes are loaded into vesicles or transport intermediates and transported to nascent melanosomes and platelet dense granules.\r\n\r\nDefects in AP-3 are related to the Hermansky-Pudlak syndrome.","predictedComplex":false,"interactors":[{"ac":"EBI-1044383","identifier":"O00203","identifierLink":"https://www.uniprot.org/uniprotkb/O00203/entry","name":"AP3B1","description":"AP-3 complex subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1051639","identifier":"O14617","identifierLink":"https://www.uniprot.org/uniprotkb/O14617/entry","name":"AP3D1","description":"AP-3 complex subunit delta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22781","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2371151","identifier":"Q9Y2T2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2T2/entry","name":"AP3M1","description":"AP-3 complex subunit mu-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3914571","identifier":"P59780","identifierLink":"https://www.uniprot.org/uniprotkb/P59780/entry","name":"AP3S2","description":"AP-3 complex subunit sigma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5053","complexName":"Neuronal AP-3 Adaptor complex, sigma3b variant","organismName":"Homo sapiens; 9606","description":"Adaptor complex that links clathrin to the membrane surface of synaptic endosomal vesicles and is required for their sorting, vesiculation and recycling.\r\n\r\nDefects in AP-3 are related to Hermansky-Pudlak syndrome.","predictedComplex":false,"interactors":[{"ac":"EBI-1051639","identifier":"O14617","identifierLink":"https://www.uniprot.org/uniprotkb/O14617/entry","name":"AP3D1","description":"AP-3 complex subunit delta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22781","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11603351","identifier":"P53677","identifierLink":"https://www.uniprot.org/uniprotkb/P53677/entry","name":"AP3M2","description":"AP-3 complex subunit mu-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1642811","identifier":"Q13367","identifierLink":"https://www.uniprot.org/uniprotkb/Q13367/entry","name":"AP3B2","description":"AP-3 complex subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3914571","identifier":"P59780","identifierLink":"https://www.uniprot.org/uniprotkb/P59780/entry","name":"AP3S2","description":"AP-3 complex subunit sigma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5055","complexName":"Neuronal AP-3 Adaptor complex, sigma3a variant","organismName":"Homo sapiens; 9606","description":"Adaptor complex that links clathrin to the membrane surface of synaptic endosomal vesicles and is required for their sorting, vesiculation and recycling.\r\n\r\nDefects in AP-3 are related to  Hermansky-Pudlak syndrome.","predictedComplex":false,"interactors":[{"ac":"EBI-1051639","identifier":"O14617","identifierLink":"https://www.uniprot.org/uniprotkb/O14617/entry","name":"AP3D1","description":"AP-3 complex subunit delta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22781","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11603351","identifier":"P53677","identifierLink":"https://www.uniprot.org/uniprotkb/P53677/entry","name":"AP3M2","description":"AP-3 complex subunit mu-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1642811","identifier":"Q13367","identifierLink":"https://www.uniprot.org/uniprotkb/Q13367/entry","name":"AP3B2","description":"AP-3 complex subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4289921","identifier":"Q92572","identifierLink":"https://www.uniprot.org/uniprotkb/Q92572/entry","name":"AP3S1","description":"AP-3 complex subunit sigma-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5056","complexName":"HypAB Ni-hydrogenase maturation complex","organismName":"Escherichia coli (strain K12); 83333","description":"Required for the synthesis of the NiFe(CN)2(CO)bimetallic cofactor present in the active site of [NiFe]-hydrogenases (CPX-281, CPX-282, CPX-317). The hypB GTPase has two nickel binding sites, one of which (the lower affinity site) is embedded in the GTPase motifs and metal binding to this site modulates GTP hydrolysis. On formation of the complex, nickel moves from the G-domain site of hypB to hypA and the complex then dissociates. hypA subsequently docks on the large subunit of the hydrogenase precursor protein to deliver the nickel ion.","predictedComplex":false,"interactors":[{"ac":"EBI-2296617","identifier":"CHEBI:49786","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49786","name":"nickel(2+)","description":"Nickel(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-558261","identifier":"P0AAN3","identifierLink":"https://www.uniprot.org/uniprotkb/P0AAN3/entry","name":"hypB","description":"Hydrogenase maturation factor HypB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6290024","identifier":"P0A700","identifierLink":"https://www.uniprot.org/uniprotkb/P0A700/entry","name":"hypA","description":"Hydrogenase maturation factor HypA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34535","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-5061","complexName":"BORC complex","organismName":"Mus musculus; 10090","description":"Lysosome associated multi-subunit protein complex that promotes lysosome positioning at the cytosolic face of lysosomal membrane through coupling to the small GTPase Arl8b (Q9CQW2). This initiates a chain of interactions that promotes the kinesin-dependent movement of lysosomes toward the plus ends of microtubules in the peripheral cytoplasm. \r\n\r\nBORC interacts with the Ragulator complex (CPX-4761) to regulate late endosomal/lysosomal size in response to glucose levels.","predictedComplex":false,"interactors":[{"ac":"EBI-22274143","identifier":"Q9D920","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D920/entry","name":"Borcs5","description":"BLOC-1-related complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR31634","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22304965","identifier":"Q9CRC6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CRC6/entry","name":"Borcs7","description":"BLOC-1-related complex subunit 7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR31397","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22304976","identifier":"Q9D6Y4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D6Y4/entry","name":"Borcs8","description":"BLOC-1-related complex subunit 8","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21146","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22304988","identifier":"Q80XH1","identifierLink":"https://www.uniprot.org/uniprotkb/Q80XH1/entry","name":"Kxd1","description":"KxDL motif-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13511","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-309395","identifier":"Q9D6W8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D6W8/entry","name":"Borcs6","description":"BLOC-1-related complex subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13440","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6170267","identifier":"Q9CWG9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CWG9/entry","name":"Bloc1s2","description":"Biogenesis of lysosome-related organelles complex 1 subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46479","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6170320","identifier":"Q9Z266","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z266/entry","name":"Snapin","description":"SNARE-associated protein Snapin","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR31305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6170351","identifier":"O55102","identifierLink":"https://www.uniprot.org/uniprotkb/O55102/entry","name":"Bloc1s1","description":"Biogenesis of lysosome-related organelles complex 1 subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5081","complexName":"lep-2-lep-5-lin-28 ubiquitin ligase complex","organismName":"Caenorhabditis elegans; 6239","description":"A ribonucleoprotein complex, which targets the heterchronic protein lin-28 for degradation by the proteasome through ubiquitination by lep-2. This promotes the larval to adult transition and the sexual maturation of the nervous system in males.","predictedComplex":false,"interactors":[{"ac":"EBI-1771770","identifier":"P92186","identifierLink":"https://www.uniprot.org/uniprotkb/P92186/entry","name":"lin-28","description":"Protein lin-28","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR46109","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25401741","identifier":"URS0000B3BFE5_6239","identifierLink":"http://rnacentral.org/rna/URS0000B3BFE5_6239","name":"lep5_caeel_lncrna","description":"lep-5 lncRNA","stochiometry":null,"interactorType":"long non-coding ribonucleic acid","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-6739202","identifier":"Q9N373","identifierLink":"https://www.uniprot.org/uniprotkb/Q9N373/entry","name":"lep-2","description":"E3 ubiquitin-protein ligase makorin","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11224","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5083","complexName":"BLOC-3 complex","organismName":"Mus musculus; 10090","description":"A guanine exchange factor (GEF) complex required for the biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules. \r\n\r\nActs as GEF for Rab32 (Q9CZE3) and Rab38 (Q8QZZ8), promoting the exchange of GDP to GTP, converting them into an active GTP-bound form and inducing their recruitment to membrane. Once active, both interact with the AP-1, the AP-3 and the BLOC-2 (CPX-5084) adaptor complexes, to regulate cargo delivery to nascent melanosomes and platelet dense granules.","predictedComplex":false,"interactors":[{"ac":"EBI-22273738","identifier":"Q99KG7","identifierLink":"https://www.uniprot.org/uniprotkb/Q99KG7/entry","name":"Hps4","description":"BLOC-3 complex member HPS4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14407","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22305132","identifier":"O08983","identifierLink":"https://www.uniprot.org/uniprotkb/O08983/entry","name":"Hps1","description":"BLOC-3 complex member HPS1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5084","complexName":"BLOC-2 complex","organismName":"Mus musculus; 10090","description":"Adaptor complex required for the biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules. \r\n\r\nOnce Rab32 (Q9CZE3) and Rab38 (Q8QZZ8) are activated by BLOC-3 (CPX-5083), they interact with AP-3 (CPX-5145, CPX-5146, CPX-5147, CPX-5148), AP-1 (CPX-5141, CPX-5142, CPX-5143, CPX-5144) and BLOC-2 complexes which function as adaptor complexes on early/recycling endosome tubules, where cargo are loaded into vesicles or transport intermediates and transported to nascent melanosomes and platelet dense granules.","predictedComplex":false,"interactors":[{"ac":"EBI-22305191","identifier":"Q91VB4","identifierLink":"https://www.uniprot.org/uniprotkb/Q91VB4/entry","name":"Hps3","description":"BLOC-2 complex member HPS3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR28633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22305213","identifier":"P59438","identifierLink":"https://www.uniprot.org/uniprotkb/P59438/entry","name":"Hps5","description":"BLOC-2 complex member HPS5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23287","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8345158","identifier":"Q8BLY7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BLY7/entry","name":"Hps6","description":"BLOC-2 complex member HPS6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14696","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5101","complexName":"Coagulation factor IXa complex","organismName":"Mus musculus; 10090","description":"Part of the intrinsic blood coagulation pathway (contact activation pathway). When bound to factor VIIIa (Q06194) forms the intrinsic tenase complex that cleaves Arg-|-Ile bonds of factor X (O88947) by limited proteolysis to form active factor X (factor Xa) in the presence of vitamin K, Ca2+ ions, phospholipids and factor VII (P70375). The coagulation pathway is terminated when fibrinogen is cleaved to fibrin which in turn polymerizes to produce a clot. \r\n\r\nIts zymogen form is activated by selective cleavage of Arg-|-Ala and Arg-|-Val bonds by limited proteolysis by factor XI (Q91Y47) to form active factor IXa. Factor VIIa-TF complex (CPX-279) also contributes to its activation.","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-25295404","identifier":"P16294-PRO_0000027762","identifierLink":"https://www.uniprot.org/uniprotkb/P16294-PRO_0000027762/entry","name":"F9","description":"Coagulation factor IXa light chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-25295410","identifier":"P16294-PRO_0000027764","identifierLink":"https://www.uniprot.org/uniprotkb/P16294-PRO_0000027764/entry","name":"F9","description":"Coagulation factor IXa heavy chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-5122","complexName":"XdhABC xanthine dehydrogenase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Cytoplasmic xanthine dehydrogenase complex which uses NAD+ as terminal electron acceptor. Predominantly converts xanthine and hypoxanthine to uric acid and participates in limited purine salvage.","predictedComplex":false,"interactors":[{"ac":"EBI-11172266","identifier":"CHEBI:49601","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49601","name":"fe2s2 iron-sulfur cluster","description":"Fe2S2 iron-sulfur cluster","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1126204","identifier":"Q46800","identifierLink":"https://www.uniprot.org/uniprotkb/Q46800/entry","name":"xdhB","description":"Putative xanthine dehydrogenase FAD-binding subunit XdhB","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42659","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1130622","identifier":"Q46801","identifierLink":"https://www.uniprot.org/uniprotkb/Q46801/entry","name":"xdhC","description":"Putative xanthine dehydrogenase iron-sulfur-binding subunit XdhC","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-25298746","identifier":"CHEBI:71302","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:71302","name":"moo2-molybdopterin cofactor(2-)","description":"MoO2-molybdopterin cofactor(2-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2932304","identifier":"Q46799","identifierLink":"https://www.uniprot.org/uniprotkb/Q46799/entry","name":"xdhA","description":"Putative xanthine dehydrogenase molybdenum-binding subunit XdhA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-5123","complexName":"XerCD site-specific tyrosine recombinase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the cutting and rejoining of two consecutive pairs of recombining strands of DNA molecules thus ensuring segregation of the circular bacterial chromosome during replication. Binds to specific 11 base pair consensus sequences that are separated by a 6-8 base pair central region (the dif region) at the borders of which the DNA strands are cleaved and exchanged. xerC binds to one repeat and XerD to the other, two dif sites bound by XerCD can then be synapsed by protein-protein interactions between the two dif-XerCD complexes. The synapse of (XerCD-dif)2 is not catalytically competent; the presence of the DNA translocase ftsK (P46889) is required for cleavage to occur. xerC exchanges the top pair of DNA strands and xerD exchanges the bottom strands. Xer recombination also contributes to the segregational stability of a variety of natural multicopy plasmids by resolving multimeric forms arising from homologous recombination","predictedComplex":false,"interactors":[{"ac":"EBI-1133806","identifier":"P0A8P6","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8P6/entry","name":"xerC","description":"Tyrosine recombinase XerC","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30349","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-559681","identifier":"P0A8P8","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8P8/entry","name":"xerD","description":"Tyrosine recombinase XerD","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30349","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5124","complexName":"RuvAB Holliday junction DNA helicase complex","organismName":"Escherichia coli (strain K12); 83333","description":"ATP-dependent helicase that catalyzes Holliday junction branch migration,  the process by which base pairs on homologous DNA strands are consecutively exchanged at a Holliday junction, moving the branch point up or down the DNA sequence. RuvAB unwinds the duplex DNA, final  resolution requires the subsequent formation of the RuvABC complex (CPX-5125). The removal of these four-way DNA intermediates during late-stage recombination: is crucial for chromosome segregation.","predictedComplex":false,"interactors":[{"ac":"EBI-555119","identifier":"P0A809","identifierLink":"https://www.uniprot.org/uniprotkb/P0A809/entry","name":"ruvA","description":"Holliday junction branch migration complex subunit RuvA","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33796","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-557878","identifier":"P0A812","identifierLink":"https://www.uniprot.org/uniprotkb/P0A812/entry","name":"ruvB","description":"Holliday junction branch migration complex subunit RuvB","stochiometry":"minValue: 12, maxValue: 12","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42848","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5125","complexName":"RuvABC Holliday junction resolvase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the final resolution of branch migration, the process by which base pairs on homologous DNA strands are consecutively exchanged at a Holliday junction, moving the branch point up or down the DNA sequence. RuvAB (CPX-5124) is an ATP-dependent helicase that unwinds the duplex DNA. RuvC protein binds to the RuvAB complex and cleaves Holliday  junctions by introducing symmetrically opposed nicks in strands of like polarity, at or near the junction. To ensure that both strands of the junction are cleaved before the enzyme dissociates, the rate of second-strand cleavage is accelerated by several orders of magnitude compared to the first. The removal of these four-way DNA intermediates during late-stage recombination is crucial for chromosome segregation.","predictedComplex":false,"interactors":[{"ac":"EBI-1123014","identifier":"P0A814","identifierLink":"https://www.uniprot.org/uniprotkb/P0A814/entry","name":"ruvC","description":"Crossover junction endodeoxyribonuclease RuvC","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30194","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25298910","identifier":"CPX-5124","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-5124","name":"RuvAB Holliday junction DNA helicase complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-5126","complexName":"RecOR complex","organismName":"Escherichia coli (strain K12); 83333","description":"Required for recA (P0A7G6) loading onto single-stranded DNA binding protein (ssb, P0AGE0)-coated ssDNA. When ssb is prebound to single-stranded DNA, it creates a significant kinetic barrier to recA nucleation and thus inhibits the ATP-driven homologous pairing and strand exchange of DNA molecules necessary for DNA recombinational repair. RecOR may stimulate recA nucleation by creating a suitable DNA binding site on ssb-coated ssDNA and/or activate the intrinsic capacity of recA to displace ssb and nucleate on single-stranded DNA.","predictedComplex":false,"interactors":[{"ac":"EBI-1117436","identifier":"P0A7H6","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7H6/entry","name":"recR","description":"Recombination protein RecR","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30446","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1129540","identifier":"P0A7H3","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7H3/entry","name":"recO","description":"DNA repair protein RecO","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33991","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5141","complexName":"Ubiquitous AP-1 Adaptor complex, sigma1a variant","organismName":"Mus musculus; 10090","description":"Adaptor complex that orchestrates the formation of membrane coats that mediate cargo selection and vesicle budding, for example by linking clathrin to the membrane surface of trans-Golgi network vesicles. Also recruits proteins involved in downstream vesicle functions such as motility, vesicle tethering and fusion with the target organelle. Required for the biogenesis of specialised organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules.\r\n\r\nOnce Rab32 (Q9CZE3) and Rab38 (Q8QZZ8) are activated by BLOC-3 (CPX-5083), they interact with AP-3 (CPX-5145 and CPX-5146), AP-1 and BLOC-2 (CPX-5084) complexes which function as adaptor complexes on early/recycling endosome tubules, where cargoes are loaded into vesicles or transport intermediates and transported to nascent melanosomes and platelet dense granules.","predictedComplex":false,"interactors":[{"ac":"EBI-1040251","identifier":"P35585","identifierLink":"https://www.uniprot.org/uniprotkb/P35585/entry","name":"Ap1m1","description":"AP-1 complex subunit mu-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1040262","identifier":"P22892","identifierLink":"https://www.uniprot.org/uniprotkb/P22892/entry","name":"Ap1g1","description":"AP-1 complex subunit gamma-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348937","identifier":"O35643","identifierLink":"https://www.uniprot.org/uniprotkb/O35643/entry","name":"Ap1b1","description":"AP-1 complex subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-516247","identifier":"P61967","identifierLink":"https://www.uniprot.org/uniprotkb/P61967/entry","name":"Ap1s1","description":"AP-1 complex subunit sigma-1A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5142","complexName":"Ubiquitous AP-1 Adaptor complex, sigma1b variant","organismName":"Mus musculus; 10090","description":"Adaptor complex that orchestrates the formation of membrane coats that mediate cargo selection and vesicle budding, for example by linking clathrin to the membrane surface of trans-Golgi network vesicles. Also recruits proteins involved in downstream vesicle functions such as motility, vesicle tethering and fusion with the target organelle. Required for the biogenesis of specialised organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules.\r\n\r\nOnce Rab32 (Q9CZE3) and Rab38 (Q8QZZ8) are activated by BLOC-3 (CPX-5083), they interact with AP-3 (CPX-5145 and CPX-5146), AP-1 and BLOC-2 (CPX-5084) complexes which function as adaptor complexes on early/recycling endosome tubules, where cargoes are loaded into vesicles or transport intermediates and transported to nascent melanosomes and platelet dense granules.","predictedComplex":false,"interactors":[{"ac":"EBI-1040251","identifier":"P35585","identifierLink":"https://www.uniprot.org/uniprotkb/P35585/entry","name":"Ap1m1","description":"AP-1 complex subunit mu-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1040262","identifier":"P22892","identifierLink":"https://www.uniprot.org/uniprotkb/P22892/entry","name":"Ap1g1","description":"AP-1 complex subunit gamma-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348937","identifier":"O35643","identifierLink":"https://www.uniprot.org/uniprotkb/O35643/entry","name":"Ap1b1","description":"AP-1 complex subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-516302","identifier":"Q9DB50","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DB50/entry","name":"Ap1s2","description":"AP-1 complex subunit sigma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5143","complexName":"Ubiquitous AP-1 Adaptor complex, sigma1c variant","organismName":"Mus musculus; 10090","description":"Adaptor complex that orchestrates the formation of membrane coats that mediate cargo selection and vesicle budding, for example by linking clathrin to the membrane surface of trans-Golgi network vesicles. Also recruits proteins involved in downstream vesicle functions such as motility, vesicle tethering and fusion with the target organelle. Required for the biogenesis of specialised organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules.\r\n\r\nOnce Rab32 (Q9CZE3) and Rab38 (Q8QZZ8) are activated by BLOC-3 (CPX-5083), they interact with AP-3 (CPX-5145 and CPX-5146), AP-1 and BLOC-2 (CPX-5084) complexes which function as adaptor complexes on early/recycling endosome tubules, where cargoes are loaded into vesicles or transport intermediates and transported to nascent melanosomes and platelet dense granules.","predictedComplex":false,"interactors":[{"ac":"EBI-1040251","identifier":"P35585","identifierLink":"https://www.uniprot.org/uniprotkb/P35585/entry","name":"Ap1m1","description":"AP-1 complex subunit mu-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1040262","identifier":"P22892","identifierLink":"https://www.uniprot.org/uniprotkb/P22892/entry","name":"Ap1g1","description":"AP-1 complex subunit gamma-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25301088","identifier":"Q7TN05","identifierLink":"https://www.uniprot.org/uniprotkb/Q7TN05/entry","name":"Ap1s3","description":"AP-1 complex subunit sigma-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348937","identifier":"O35643","identifierLink":"https://www.uniprot.org/uniprotkb/O35643/entry","name":"Ap1b1","description":"AP-1 complex subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5144","complexName":"Endothelial AP-1 Adaptor complex, sigma1a variant","organismName":"Mus musculus; 10090","description":"Adaptor complex that links clathrin to the membrane surface of trans-Golgi network vesicles and is involved in basolateral transport and the polarized sorting of vesicle in epithelial cells.","predictedComplex":false,"interactors":[{"ac":"EBI-1040262","identifier":"P22892","identifierLink":"https://www.uniprot.org/uniprotkb/P22892/entry","name":"Ap1g1","description":"AP-1 complex subunit gamma-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348937","identifier":"O35643","identifierLink":"https://www.uniprot.org/uniprotkb/O35643/entry","name":"Ap1b1","description":"AP-1 complex subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-516247","identifier":"P61967","identifierLink":"https://www.uniprot.org/uniprotkb/P61967/entry","name":"Ap1s1","description":"AP-1 complex subunit sigma-1A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8392734","identifier":"Q9WVP1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WVP1/entry","name":"Ap1m2","description":"AP-1 complex subunit mu-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5145","complexName":"Ubiquitous AP-3 Adaptor complex, sigma3a variant","organismName":"Mus musculus; 10090","description":"Adaptor complex that links clathrin to the membrane surface of endosomal vesicles and is required for the biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules. \r\n\r\nOnce Rab32 (Q9CZE3) and Rab38 (Q8QZZ8) are activated by BLOC-3 (CPX-5083), they interact with AP-3, AP-1 (CPX-5141, CPX-5142 and CPX-5143) and BLOC-2 (CPX-5084) complexes which function as adaptor complexes on early/recycling endosome tubules, where cargoes are loaded into vesicles or transport intermediates and transported to nascent melanosomes and platelet dense granules.","predictedComplex":false,"interactors":[{"ac":"EBI-643061","identifier":"Q9Z1T1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z1T1/entry","name":"Ap3b1","description":"AP-3 complex subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-775247","identifier":"O54774","identifierLink":"https://www.uniprot.org/uniprotkb/O54774/entry","name":"Ap3d1","description":"AP-3 complex subunit delta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22781","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9085419","identifier":"Q9DCR2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DCR2/entry","name":"Ap3s1","description":"AP-3 complex subunit sigma-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9085473","identifier":"Q9JKC8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JKC8/entry","name":"Ap3m1","description":"AP-3 complex subunit mu-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5146","complexName":"Ubiquitous AP-3 Adaptor complex, sigma3b variant","organismName":"Mus musculus; 10090","description":"Adaptor complex that links clathrin to the membrane surface of endosomal vesicles and is required for the biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules. \r\n\r\nOnce Rab32 (Q9CZE3) and Rab38 (Q8QZZ8) are activated by BLOC-3 (CPX-5083), they interact with AP-3, AP-1 (CPX-5141, CPX-5142 and CPX-5143) and BLOC-2 (CPX-5084) complexes which function as adaptor complexes on early/recycling endosome tubules, where cargoes are loaded into vesicles or transport intermediates and transported to nascent melanosomes and platelet dense granules.","predictedComplex":false,"interactors":[{"ac":"EBI-643061","identifier":"Q9Z1T1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z1T1/entry","name":"Ap3b1","description":"AP-3 complex subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-775247","identifier":"O54774","identifierLink":"https://www.uniprot.org/uniprotkb/O54774/entry","name":"Ap3d1","description":"AP-3 complex subunit delta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22781","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9085443","identifier":"Q8BSZ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BSZ2/entry","name":"Ap3s2","description":"AP-3 complex subunit sigma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9085473","identifier":"Q9JKC8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JKC8/entry","name":"Ap3m1","description":"AP-3 complex subunit mu-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5147","complexName":"Neuronal AP-3 Adaptor complex, sigma3a variant","organismName":"Mus musculus; 10090","description":"Adaptor complex that links clathrin to the membrane surface of synaptic endosomal vesicles and is required for their sorting, vesiculation and recycling.","predictedComplex":false,"interactors":[{"ac":"EBI-6273157","identifier":"Q9JME5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JME5/entry","name":"Ap3b2","description":"AP-3 complex subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-775247","identifier":"O54774","identifierLink":"https://www.uniprot.org/uniprotkb/O54774/entry","name":"Ap3d1","description":"AP-3 complex subunit delta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22781","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-775262","identifier":"Q8R2R9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R2R9/entry","name":"Ap3m2","description":"AP-3 complex subunit mu-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9085419","identifier":"Q9DCR2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DCR2/entry","name":"Ap3s1","description":"AP-3 complex subunit sigma-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5148","complexName":"Neuronal AP-3 Adaptor complex, sigma3b variant","organismName":"Mus musculus; 10090","description":"Adaptor complex that links clathrin to the membrane surface of synaptic endosomal vesicles and is required for their sorting, vesiculation and recycling.","predictedComplex":false,"interactors":[{"ac":"EBI-6273157","identifier":"Q9JME5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JME5/entry","name":"Ap3b2","description":"AP-3 complex subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-775247","identifier":"O54774","identifierLink":"https://www.uniprot.org/uniprotkb/O54774/entry","name":"Ap3d1","description":"AP-3 complex subunit delta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22781","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-775262","identifier":"Q8R2R9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R2R9/entry","name":"Ap3m2","description":"AP-3 complex subunit mu-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9085443","identifier":"Q8BSZ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BSZ2/entry","name":"Ap3s2","description":"AP-3 complex subunit sigma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5149","complexName":"AP-2 Adaptor complex, alpha1 variant","organismName":"Homo sapiens; 9606","description":"Adaptor complex that links clathrin to the membrane surface of a vesicle, and the cargo receptors during receptor/clathrin mediated endocytosis. \r\nTogether with CLASP proteins (a family of microtubule-associated proteins involved in attachment of microtubules to the cell cortex), it binds to the phosphatidylinositol 4,5-bisphosphate (PIP2) moieties of the inner side of the plasma membrane, recognizes LL and Y-X-X-Phi (Phi = hydrophobic residue) endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules and serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. It also seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface.\r\n\r\nMutations in AP2S1 and AP2M1 have been identified as cause of familial hypocalciuric hypercalcemia (FHH) type 3 and epileptic encephalopathy, respectively. AP2A1 has been identified as a gene locus that is linked to Alzheimer’s disease.","predictedComplex":false,"interactors":[{"ac":"EBI-297662","identifier":"P53680","identifierLink":"https://www.uniprot.org/uniprotkb/P53680/entry","name":"AP2S1","description":"AP-2 complex subunit sigma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-297683","identifier":"Q96CW1","identifierLink":"https://www.uniprot.org/uniprotkb/Q96CW1/entry","name":"AP2M1","description":"AP-2 complex subunit mu","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353552","identifier":"O95782","identifierLink":"https://www.uniprot.org/uniprotkb/O95782/entry","name":"AP2A1","description":"AP-2 complex subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-432924","identifier":"P63010","identifierLink":"https://www.uniprot.org/uniprotkb/P63010/entry","name":"AP2B1","description":"AP-2 complex subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5150","complexName":"AP-2 Adaptor complex, alpha2 variant","organismName":"Homo sapiens; 9606","description":"Adaptor complex that links clathrin to the membrane surface of a vesicle, and the cargo receptors during receptor/clathrin mediated endocytosis. \r\nTogether with CLASP proteins (a family of microtubule-associated proteins involved in attachment of microtubules to the cell cortex), it binds to the phosphatidylinositol 4,5-bisphosphate (PIP2) moieties of the inner side of the plasma membrane, recognizes LL and Y-X-X-Phi (Phi = hydrophobic residue) endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules and serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. It also seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface.\r\n\r\nMutations in AP2S1 and AP2M1 have been identified as the cause of familial hypocalciuric hypercalcemia (FHH) type 3 and epileptic encephalopathy, respectively. AP2A2 has been identified as a gene locus that is linked to Alzheimer's disease.","predictedComplex":false,"interactors":[{"ac":"EBI-1642835","identifier":"O94973","identifierLink":"https://www.uniprot.org/uniprotkb/O94973/entry","name":"AP2A2","description":"AP-2 complex subunit alpha-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-297662","identifier":"P53680","identifierLink":"https://www.uniprot.org/uniprotkb/P53680/entry","name":"AP2S1","description":"AP-2 complex subunit sigma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-297683","identifier":"Q96CW1","identifierLink":"https://www.uniprot.org/uniprotkb/Q96CW1/entry","name":"AP2M1","description":"AP-2 complex subunit mu","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-432924","identifier":"P63010","identifierLink":"https://www.uniprot.org/uniprotkb/P63010/entry","name":"AP2B1","description":"AP-2 complex subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5151","complexName":"AP-4 Adaptor complex","organismName":"Homo sapiens; 9606","description":"Adaptor complex that forms a non clathrin-associated coat on vesicles departing the trans-Golgi network (TGN) and may be involved in the targeting of proteins from the trans-Golgi network to the endosomal-lysosomal system. AP-4 is involved in the recognition and binding of tyrosine-based sorting signals found in the cytoplasmic part of cargos, but may also recognize other types of sorting signal.\r\n\r\nAP-4 is expressed at lower levels compared to AP-1, -2 and -3 complexes, however its expression is acutely sensitive to disturbances in clathrin-mediated trafficking, and seems to be upregulated as a compensatory mechanism.\r\n\r\nMutation in genes coding for AP-4 subunits are found in patients affected by spasticity, intellectual disability, microcephaly and cerebral palsy.","predictedComplex":false,"interactors":[{"ac":"EBI-1047606","identifier":"Q9Y6B7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6B7/entry","name":"AP4B1","description":"AP-4 complex subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1222435","identifier":"Q9UPM8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UPM8/entry","name":"AP4E1","description":"AP-4 complex subunit epsilon-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2115780","identifier":"Q9Y587","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y587/entry","name":"AP4S1","description":"AP-4 complex subunit sigma-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3914106","identifier":"O00189","identifierLink":"https://www.uniprot.org/uniprotkb/O00189/entry","name":"AP4M1","description":"AP-4 complex subunit mu-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5152","complexName":"AP-2 Adaptor complex, alpha1 variant","organismName":"Mus musculus; 10090","description":"Adaptor complex that links clathrin to the membrane surface of a vesicle, and the cargo receptors during receptor/clathrin mediated endocytosis. \r\nTogether with CLASP proteins (a family of microtubule-associated proteins involved in attachment of microtubules to the cell cortex), it binds to the phosphatidylinositol 4,5-bisphosphate (PIP2) moieties of the inner side of the plasma membrane, recognizes LL and Y-X-X-Phi (Phi = hydrophobic residue) endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules and serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. It also seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface.","predictedComplex":false,"interactors":[{"ac":"EBI-1033702","identifier":"P62743","identifierLink":"https://www.uniprot.org/uniprotkb/P62743/entry","name":"Ap2s1","description":"AP-2 complex subunit sigma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-297703","identifier":"P84091","identifierLink":"https://www.uniprot.org/uniprotkb/P84091/entry","name":"Ap2m1","description":"AP-2 complex subunit mu","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-775189","identifier":"P17426","identifierLink":"https://www.uniprot.org/uniprotkb/P17426/entry","name":"Ap2a1","description":"AP-2 complex subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-775229","identifier":"Q9DBG3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DBG3/entry","name":"Ap2b1","description":"AP-2 complex subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5153","complexName":"AP-2 Adaptor complex, alpha2 variant","organismName":"Mus musculus; 10090","description":"Adaptor complex that links clathrin to the membrane surface of a vesicle, and the cargo receptors during receptor/clathrin mediated endocytosis. \r\nTogether with CLASP proteins (a family of microtubule-associated proteins involved in attachment of microtubules to the cell cortex), it binds to the phosphatidylinositol 4,5-bisphosphate (PIP2) moieties of the inner side of the plasma membrane, recognizes LL and Y-X-X-Phi (Phi = hydrophobic residue) endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules and serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. It also seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface.","predictedComplex":false,"interactors":[{"ac":"EBI-1033702","identifier":"P62743","identifierLink":"https://www.uniprot.org/uniprotkb/P62743/entry","name":"Ap2s1","description":"AP-2 complex subunit sigma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-297703","identifier":"P84091","identifierLink":"https://www.uniprot.org/uniprotkb/P84091/entry","name":"Ap2m1","description":"AP-2 complex subunit mu","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-775215","identifier":"P17427","identifierLink":"https://www.uniprot.org/uniprotkb/P17427/entry","name":"Ap2a2","description":"AP-2 complex subunit alpha-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-775229","identifier":"Q9DBG3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DBG3/entry","name":"Ap2b1","description":"AP-2 complex subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5154","complexName":"AP-4 Adaptor complex","organismName":"Mus musculus; 10090","description":"Adaptor complex that forms a non clathrin-associated coat on vesicles departing the trans-Golgi network (TGN) and may be involved in the targeting of proteins from the trans-Golgi network to the endosomal-lysosomal system. AP-4 is involved in the recognition and binding of tyrosine-based sorting signals found in the cytoplasmic part of cargos, but may also recognize other types of sorting signal.\r\n\r\nAP-4 is expressed at lower levels compared to AP-1, -2 and -3 complexes, however its expression is acutely sensitive to disturbances in clathrin-mediated trafficking, and seems to be upregulated as a compensatory mechanism.","predictedComplex":false,"interactors":[{"ac":"EBI-25301188","identifier":"Q80V94","identifierLink":"https://www.uniprot.org/uniprotkb/Q80V94/entry","name":"Ap4e1","description":"AP-4 complex subunit epsilon-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25301211","identifier":"Q9JKC7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JKC7/entry","name":"Ap4m1","description":"AP-4 complex subunit mu-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25301240","identifier":"Q9WV76","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WV76/entry","name":"Ap4b1","description":"AP-4 complex subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25301274","identifier":"Q9WVL1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WVL1/entry","name":"Ap4s1","description":"AP-4 complex subunit sigma-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5156","complexName":"ERalpha-NCOA2 activated estrogen receptor complex","organismName":"Homo sapiens; 9606","description":"Member of the nuclear receptor (NR) family of ligand-regulated transcription factor complexes controlling the expression of numerous genes. Like other NRs, estrogen receptor alpha (ESR1) contains a DNA-binding and a ligand-binding domain (DBD, LBD). In the absence of an agonist ligand, the complex recruits the corepressor proteins NCoR or SMRT and associated factors such as histone deacetylases (HDAC) or DNA-methyl transferases that may lead to an inactive condensed chromatin structure, preventing transcription. Upon ligand binding, ESR1 undergoes a conformational change that results in the release of corepressors, and transcriptional coactivators such as NCOA2 (SRC2) are recruited to the LBD, which activates transcription. ESR1 is able to form heterodimers with a range of other NRs, such as ESR2 (Q92731), retinoic acid receptor (RARs & RXRs) or thyroid hormone receptors","predictedComplex":false,"interactors":[{"ac":"EBI-78473","identifier":"P03372","identifierLink":"https://www.uniprot.org/uniprotkb/P03372/entry","name":"ESR1","description":"Estrogen receptor","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-81236","identifier":"Q15596","identifierLink":"https://www.uniprot.org/uniprotkb/Q15596/entry","name":"NCOA2","description":"Nuclear receptor coactivator 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5157","complexName":"Ribonucleoside-diphosphate reductase 2 complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the reduction of ribonucleotides to the corresponding deoxyribonucleotides, an essential step in the de novo synthesis of monomeric precursors for DNA replication and repair. The binding of effector dATP alters the active site to select for pyrimidines over purines, whereas effectors dGTP and TTP select for substrates ADP and GDP, respectively.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1121841","identifier":"P37146","identifierLink":"https://www.uniprot.org/uniprotkb/P37146/entry","name":"nrdF","description":"Ribonucleoside-diphosphate reductase 2 subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR23409","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1129936","identifier":"P39452","identifierLink":"https://www.uniprot.org/uniprotkb/P39452/entry","name":"nrdE","description":"Ribonucleoside-diphosphate reductase 2 subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11573","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5158","complexName":"Imidazole glycerol phosphate synthase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Essential enzyme on the pathway synthesizing L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate, catalyzing the closure of the imidazole ring thus also providing the substrate for de novo purine biosynthesis. Converts the biosynthetic intermediate 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-β-D-ribosyl)imidazole-4-carboxamide (PRFAR, CHEBI:27735) to D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate(2-) (IGP, CHEBI:58278) and 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide(2-) (AICAR, CHEBI:58475). The hisH glutaminase hydrolysis of glutamine yields ammonia which acts as a nitrogen source for the synthesis of histidine and purines.","predictedComplex":false,"interactors":[{"ac":"EBI-1126953","identifier":"P60595","identifierLink":"https://www.uniprot.org/uniprotkb/P60595/entry","name":"hisH","description":"Imidazole glycerol phosphate synthase subunit HisH","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9151168","identifier":"P60664","identifierLink":"https://www.uniprot.org/uniprotkb/P60664/entry","name":"hisF","description":"Imidazole glycerol phosphate synthase subunit HisF","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR21235","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5159","complexName":"3-isopropylmalate dehydratase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyses the stereo-specific isomerisation of 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate, the second step in the biosynthesis of leucine.","predictedComplex":false,"interactors":[{"ac":"EBI-1113528","identifier":"P30126","identifierLink":"https://www.uniprot.org/uniprotkb/P30126/entry","name":"leuD","description":"3-isopropylmalate dehydratase small subunit","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43345","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1113576","identifier":"P0A6A6","identifierLink":"https://www.uniprot.org/uniprotkb/P0A6A6/entry","name":"leuC","description":"3-isopropylmalate dehydratase large subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43822","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-5161","complexName":"3-phenylpropionate/cinnamic acid dioxygenase","organismName":"Escherichia coli (strain K12); 83333","description":"Protects against the toxic effect of dioxygenases by converting 3-phenylpropionic acid into 3-phenylpropionate-dihydrodiol  and cinnamic acid into cinnamic acid-dihydrodiol.","predictedComplex":false,"interactors":[{"ac":"EBI-1115311","identifier":"P0ABR5","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABR5/entry","name":"hcaE","description":"3-phenylpropionate/cinnamic acid dioxygenase subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43756","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11172266","identifier":"CHEBI:49601","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49601","name":"fe2s2 iron-sulfur cluster","description":"Fe2S2 iron-sulfur cluster","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1129356","identifier":"P0ABW0","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABW0/entry","name":"hcaC","description":"3-phenylpropionate/cinnamic acid dioxygenase ferredoxin subunit","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR21496","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1129389","identifier":"P77650","identifierLink":"https://www.uniprot.org/uniprotkb/P77650/entry","name":"hcaD","description":"3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43557","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11472102","identifier":"CHEBI:24875","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:24875","name":"iron cation","description":"iron cation","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-25397633","identifier":"Q47140","identifierLink":"https://www.uniprot.org/uniprotkb/Q47140/entry","name":"hcaF","description":"3-phenylpropionate/cinnamic acid dioxygenase subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR41534","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-5181","complexName":"AP-5 Adaptor complex","organismName":"Homo sapiens; 9606","description":"Adaptor complex that forms a non clathrin-associated coat on vesicles and is involved in endosomal trafficking.\r\n\r\nAP-5 is expressed at lower than AP-1, -2 and -3 complexes.\r\n\r\nAP-5 deficiency is associated with progressive spastic paraplegia.","predictedComplex":false,"interactors":[{"ac":"EBI-5917258","identifier":"Q9H0R1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H0R1/entry","name":"AP5M1","description":"AP-5 complex subunit mu-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5917279","identifier":"Q2VPB7","identifierLink":"https://www.uniprot.org/uniprotkb/Q2VPB7/entry","name":"AP5B1","description":"AP-5 complex subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR34033","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5917463","identifier":"Q9NUS5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NUS5/entry","name":"AP5S1","description":"AP-5 complex subunit sigma-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16120","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-740938","identifier":"O43299","identifierLink":"https://www.uniprot.org/uniprotkb/O43299/entry","name":"AP5Z1","description":"AP-5 complex subunit zeta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46488","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5182","complexName":"AP-5 Adaptor complex","organismName":"Mus musculus; 10090","description":"Adaptor complex that forms a non clathrin-associated coat on vesicles and is involved in endosomal trafficking.\r\n\r\nAP-5 is expressed at lower levels than AP-1, -2 and -3 complexes.","predictedComplex":false,"interactors":[{"ac":"EBI-25372567","identifier":"Q8BJ63","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BJ63/entry","name":"Ap5m1","description":"AP-5 complex subunit mu-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25372598","identifier":"Q3U829","identifierLink":"https://www.uniprot.org/uniprotkb/Q3U829/entry","name":"Ap5z1","description":"AP-5 complex subunit zeta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46488","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25372621","identifier":"Q9D742","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D742/entry","name":"Ap5s1","description":"AP-5 complex subunit sigma-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16120","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25372642","identifier":"Q3TAP4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TAP4/entry","name":"Ap5b1","description":"AP-5 complex subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR34033","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5201","complexName":"Glycyl-tRNA synthetase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyses the esterificaion of glycine to its cognate tRNA with the concomitant hydrolysis of ATP. The activated amino acid is transferred to the 3-OH group of a glycine-accepting tRNA. Also synthesises dinuceloside polyphosphates, which may play a role in the regulation of cell functions, for example by serving as RNA caps, thus influencing RNA turnover.","predictedComplex":false,"interactors":[{"ac":"EBI-551191","identifier":"P00960","identifierLink":"https://www.uniprot.org/uniprotkb/P00960/entry","name":"glyQ","description":"Glycine--tRNA ligase alpha subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-551400","identifier":"P00961","identifierLink":"https://www.uniprot.org/uniprotkb/P00961/entry","name":"glyS","description":"Glycine--tRNA ligase beta subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30075","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5222","complexName":"Phenylalanyl-tRNA synthetase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyses the esterificaion of phenylalanine to its cognate tRNA with the concomitant hydrolysis of ATP. The activated amino acid is transferred to the 2-OH group of a phenylalanine-accepting tRNA.","predictedComplex":false,"interactors":[{"ac":"EBI-555676","identifier":"P08312","identifierLink":"https://www.uniprot.org/uniprotkb/P08312/entry","name":"pheS","description":"Phenylalanine--tRNA ligase alpha subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11538","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-555713","identifier":"P07395","identifierLink":"https://www.uniprot.org/uniprotkb/P07395/entry","name":"pheT","description":"Phenylalanine--tRNA ligase beta subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10947","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-5225","complexName":"28S mitochondrial small ribosomal subunit","organismName":"Homo sapiens; 9606","description":"Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). Responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. The mitochondrial ribosome (mitoribosome) is responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. All proteins synthesized by human mitoribosomes are hydrophobic, integral membrane proteins and some require prosthetic groups for folding and functioning. The mitoribosomes are tethered to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. The inner membrane protein MRPL45 aligns the mitochondrial peptide exit tunnel with the membrane insertion machinery and supports the transfer of the mitochondrial nascent peptides towards the membrane.\r\nThe mt-SSU binds mRNA, is involved in accurate initiation and decoding, and undergoes large-scale conformational changes during the elongation cycle.\r\n\r\nMutations in mitochondrial ribosome subunits have been found associated to cardiomyopathies, developmental abnormalities, cancer and hearing loss (ototoxicity).","predictedComplex":false,"interactors":[{"ac":"EBI-1045956","identifier":"O60783","identifierLink":"https://www.uniprot.org/uniprotkb/O60783/entry","name":"MRPS14","description":"Small ribosomal subunit protein uS14m","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19836","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1046443","identifier":"Q9Y2R5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2R5/entry","name":"MRPS17","description":"Small ribosomal subunit protein uS17m","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24088","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1046734","identifier":"P82663","identifierLink":"https://www.uniprot.org/uniprotkb/P82663/entry","name":"MRPS25","description":"Small ribosomal subunit protein mS25","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13274","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1048271","identifier":"P82664","identifierLink":"https://www.uniprot.org/uniprotkb/P82664/entry","name":"MRPS10","description":"Small ribosomal subunit protein uS10m","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1048516","identifier":"P82930","identifierLink":"https://www.uniprot.org/uniprotkb/P82930/entry","name":"MRPS34","description":"Small ribosomal subunit protein mS34","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28589","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1049319","identifier":"Q9Y3D3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3D3/entry","name":"MRPS16","description":"Small ribosomal subunit protein bS16m","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12919","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1050752","identifier":"P82650","identifierLink":"https://www.uniprot.org/uniprotkb/P82650/entry","name":"MRPS22","description":"Small ribosomal subunit protein mS22","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13071","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1054270","identifier":"Q9Y3D9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3D9/entry","name":"MRPS23","description":"Small ribosomal subunit protein mS23","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15925","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1054287","identifier":"P82675","identifierLink":"https://www.uniprot.org/uniprotkb/P82675/entry","name":"MRPS5","description":"Small ribosomal subunit protein uS5m","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13718","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1054973","identifier":"Q9Y2R9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2R9/entry","name":"MRPS7","description":"Small ribosomal subunit protein uS7m","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11205","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1055789","identifier":"Q96EL2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96EL2/entry","name":"MRPS24","description":"Small ribosomal subunit protein uS3m","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21244","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2211879","identifier":"Q92552","identifierLink":"https://www.uniprot.org/uniprotkb/Q92552/entry","name":"MRPS27","description":"Small ribosomal subunit protein mS27","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21393","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2371859","identifier":"P82912","identifierLink":"https://www.uniprot.org/uniprotkb/P82912/entry","name":"MRPS11","description":"Small ribosomal subunit protein uS11m","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11759","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2372155","identifier":"P82921","identifierLink":"https://www.uniprot.org/uniprotkb/P82921/entry","name":"MRPS21","description":"Small ribosomal subunit protein bS21m","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21109","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2513649","identifier":"P82673","identifierLink":"https://www.uniprot.org/uniprotkb/P82673/entry","name":"MRPS35","description":"Small ribosomal subunit protein mS35","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13490","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25408176","identifier":"URS000044DFF6_9606","identifierLink":"http://rnacentral.org/rna/URS000044DFF6_9606","name":"rrna_12s_human","description":"human mitochondrially encoded 12S rRNA","stochiometry":null,"interactorType":"ribosomal rna","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2688704","identifier":"Q9Y291","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y291/entry","name":"MRPS33","description":"Small ribosomal subunit protein mS33","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13362","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2880040","identifier":"P82914","identifierLink":"https://www.uniprot.org/uniprotkb/P82914/entry","name":"MRPS15","description":"Small ribosomal subunit protein uS15m","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46685","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2880048","identifier":"Q9Y399","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y399/entry","name":"MRPS2","description":"Small ribosomal subunit protein uS2m","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12534","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355912","identifier":"P51398","identifierLink":"https://www.uniprot.org/uniprotkb/P51398/entry","name":"DAP3","description":"Small ribosomal subunit protein mS29","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12810","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-448665","identifier":"Q9NWT8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NWT8/entry","name":"AURKAIP1","description":"Small ribosomal subunit protein mS38","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32035","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5325249","identifier":"Q9Y2Q9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2Q9/entry","name":"MRPS28","description":"Small ribosomal subunit protein bS1m","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13447","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5453854","identifier":"Q9Y3D5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3D5/entry","name":"MRPS18C","description":"Small ribosomal subunit protein bS18m","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 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Responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. The mitochondrial ribosome (mitoribosome) is responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. All proteins synthesized by human mitoribosomes are hydrophobic, integral membrane proteins and some require prosthetic groups for folding and functioning. The mitoribosomes are tethered to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. The inner membrane protein MRPL45 aligns the mitochondrial peptide exit tunnel with the membrane insertion machinery and supports the transfer of the mitochondrial nascent peptides towards the membrane.\r\n\r\nMutations in mitochondrial ribosome subunits have been found associated to cardiomyopathies, developmental abnormalities, cancer and hearing loss (ototoxicity).","predictedComplex":false,"interactors":[{"ac":"EBI-1043145","identifier":"Q8N983","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N983/entry","name":"MRPL43","description":"Large ribosomal subunit protein mL43","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21396","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1043903","identifier":"Q6P1L8","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P1L8/entry","name":"MRPL14","description":"Large ribosomal subunit protein uL14m","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 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PabA generates ammonia from glutamine, PabB then synthesizes 4-amino-4-deoxychorismate from chorismate and ammonia.","predictedComplex":false,"interactors":[{"ac":"EBI-1132589","identifier":"P00903","identifierLink":"https://www.uniprot.org/uniprotkb/P00903/entry","name":"pabA","description":"Aminodeoxychorismate synthase component 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43418","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-562685","identifier":"P05041","identifierLink":"https://www.uniprot.org/uniprotkb/P05041/entry","name":"pabB","description":"Aminodeoxychorismate synthase component 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11236","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-5261","complexName":"40S cytosolic small ribosomal subunit","organismName":"Mus musculus; 10090","description":"Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). 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10090","xrefs":[{"identifier":"PTHR10871","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-354261","identifier":"P62702","identifierLink":"https://www.uniprot.org/uniprotkb/P62702/entry","name":"Rps4x","description":"Small ribosomal subunit protein eS4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11581","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-354350","identifier":"P62082","identifierLink":"https://www.uniprot.org/uniprotkb/P62082/entry","name":"Rps7","description":"Small ribosomal subunit protein eS7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11278","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4282373","identifier":"P62983","identifierLink":"https://www.uniprot.org/uniprotkb/P62983/entry","name":"Rps27a","description":"Ubiquitin-ribosomal protein eS31 fusion protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10666","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4285534","identifier":"P62245","identifierLink":"https://www.uniprot.org/uniprotkb/P62245/entry","name":"Rps15a","description":"Small ribosomal subunit protein uS8","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11758","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4286041","identifier":"P62858","identifierLink":"https://www.uniprot.org/uniprotkb/P62858/entry","name":"Rps28","description":"Small ribosomal subunit protein eS28","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10769","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4286141","identifier":"P14131","identifierLink":"https://www.uniprot.org/uniprotkb/P14131/entry","name":"Rps16","description":"Small ribosomal subunit protein uS9","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21569","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-522873","identifier":"Q9CZX8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CZX8/entry","name":"Rps19","description":"Small ribosomal subunit protein eS19","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11710","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6260945","identifier":"P62852","identifierLink":"https://www.uniprot.org/uniprotkb/P62852/entry","name":"Rps25","description":"Small ribosomal subunit protein eS25","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6260985","identifier":"P62855","identifierLink":"https://www.uniprot.org/uniprotkb/P62855/entry","name":"Rps26","description":"Small ribosomal subunit protein eS26","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12538","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-773974","identifier":"P25444","identifierLink":"https://www.uniprot.org/uniprotkb/P25444/entry","name":"Rps2","description":"Small ribosomal subunit protein uS5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13718","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-773982","identifier":"P97351","identifierLink":"https://www.uniprot.org/uniprotkb/P97351/entry","name":"Rps3a","description":"Small ribosomal subunit protein eS1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11830","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7977806","identifier":"P60867","identifierLink":"https://www.uniprot.org/uniprotkb/P60867/entry","name":"Rps20","description":"Small ribosomal subunit protein uS10","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11700","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8313545","identifier":"P62267","identifierLink":"https://www.uniprot.org/uniprotkb/P62267/entry","name":"Rps23","description":"Small ribosomal subunit protein uS12","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11652","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8328629","identifier":"P62281","identifierLink":"https://www.uniprot.org/uniprotkb/P62281/entry","name":"Rps11","description":"Small ribosomal subunit protein uS17","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10744","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8328840","identifier":"P97461","identifierLink":"https://www.uniprot.org/uniprotkb/P97461/entry","name":"Rps5","description":"Small ribosomal subunit protein uS7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11205","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8328982","identifier":"P63323","identifierLink":"https://www.uniprot.org/uniprotkb/P63323/entry","name":"Rps12","description":"Small ribosomal subunit protein eS12","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11843","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9987039","identifier":"P62274","identifierLink":"https://www.uniprot.org/uniprotkb/P62274/entry","name":"Rps29","description":"Small ribosomal subunit protein uS14","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12010","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5281","complexName":"HypEF Ni-hydrogenase maturation complex","organismName":"Escherichia coli (strain K12); 83333","description":"Required for the synthesis of the NiFe(CN)2(CO)bimetallic cofactor present in the active site of [NiFe]-hydrogenases (CPX-281, CPX-282, CPX-317). 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The hybG protein delivers Fe and CO2 to hypD, where CO is generated and the cyano groups are transferred to the iron by the HypEF complex (CPX-5281). 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The HypCDE complex delivers the Fe(CN)2CO group to the precursor of the hydrogenase large subunit.","predictedComplex":false,"interactors":[{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-552654","identifier":"P0AAM3","identifierLink":"https://www.uniprot.org/uniprotkb/P0AAM3/entry","name":"hypC","description":"Hydrogenase maturation factor HypC","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR35177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-552711","identifier":"P24192","identifierLink":"https://www.uniprot.org/uniprotkb/P24192/entry","name":"hypD","description":"Hydrogenase maturation factor HypD","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30149","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-552743","identifier":"P24193","identifierLink":"https://www.uniprot.org/uniprotkb/P24193/entry","name":"hypE","description":"Carbamoyl dehydratase HypE","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30303","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5285","complexName":"McrBC 5-methylcytosine-specific restriction endonuclease complex","organismName":"Escherichia coli (strain K12); 83333","description":"A DNA endonuclease that acts as an antiphage defense system by specifically cleaving invading DNA that are methylated. McrBC specifically cleaves DNA containing the recognition sequence 5prime-G/A(5mC)-3prime, where 5mC can be 5-methylcytosine, 5-hydroxymethylcytosine, or 4-methylcytosine.","predictedComplex":false,"interactors":[{"ac":"EBI-25407271","identifier":"P15006","identifierLink":"https://www.uniprot.org/uniprotkb/P15006/entry","name":"mcrC","description":"Type IV methyl-directed restriction enzyme EcoKMcrBC","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR38733","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-552513","identifier":"P15005","identifierLink":"https://www.uniprot.org/uniprotkb/P15005/entry","name":"mcrB","description":"Type IV methyl-directed restriction enzyme EcoKMcrB subunit","stochiometry":"minValue: 12, maxValue: 12","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR37291","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1892","complexName":"Mitochondrial inner membrane peptidase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Processes certain precursor proteins that are exported from the matrix into the inner membrane or the intermembrane space. The two IMP subunits are associated with the inner membrane, and their catalytic sites are exposed to the intermembrane space. The IMP1 and IMP2 proteins both display proteolytic activity and have non-overlapping substrate specificities. IMP1 has been shown to catalyse the maturation of cytochrome oxidase subunit 2, cytochrome b2 and the 32-kDa form of NADH-dependent cytochrome b5 reductase, while IMP2 participates in the second processing step during the maturation of cytochrome c1. SOM1 appears to functions as a molecular chaperone, which binds to specific substrates and directs them to the catalytic site.","predictedComplex":false,"interactors":[{"ac":"EBI-3401183","identifier":"P28627","identifierLink":"https://www.uniprot.org/uniprotkb/P28627/entry","name":"IMP1","description":"Mitochondrial inner membrane protease subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12383","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3401205","identifier":"Q05676","identifierLink":"https://www.uniprot.org/uniprotkb/Q05676/entry","name":"SOM1","description":"Protein SOM1, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-9231","identifier":"P46972","identifierLink":"https://www.uniprot.org/uniprotkb/P46972/entry","name":"IMP2","description":"Mitochondrial inner membrane protease subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46041","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5301","complexName":"28S mitochondrial small ribosomal subunit","organismName":"Mus musculus; 10090","description":"Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). Responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. The mitochondrial ribosome (mitoribosome) is responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. All proteins synthesized by mouse mitoribosomes are hydrophobic, integral membrane proteins and some require prosthetic groups for folding and functioning. The mitoribosomes are tethered to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. The inner membrane protein Mrpl45 aligns the mitochondrial peptide exit tunnel with the membrane insertion machinery and supports the transfer of the mitochondrial nascent peptides towards the membrane.\r\nThe mt-SSU binds mRNA, is involved in accurate initiation and decoding, and undergoes large-scale conformational changes during the elongation cycle.","predictedComplex":false,"interactors":[{"ac":"EBI-16369911","identifier":"Q8BJZ4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BJZ4/entry","name":"Mrps35","description":"Small ribosomal subunit protein mS35","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13490","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16370037","identifier":"Q14C51","identifierLink":"https://www.uniprot.org/uniprotkb/Q14C51/entry","name":"Ptcd3","description":"Small ribosomal subunit protein mS39","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16276","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21286817","identifier":"O35680","identifierLink":"https://www.uniprot.org/uniprotkb/O35680/entry","name":"Mrps12","description":"Small ribosomal subunit protein uS12m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11652","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25413158","identifier":"URS00002411EE_10090","identifierLink":"http://rnacentral.org/rna/URS00002411EE_10090","name":"rrna_12s_mouse","description":"mouse mitochondrially encoded 12S rRNA","stochiometry":null,"interactorType":"ribosomal rna","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-25413241","identifier":"Q99N84","identifierLink":"https://www.uniprot.org/uniprotkb/Q99N84/entry","name":"Mrps18b","description":"Small ribosomal subunit protein mS40","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13329","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25413265","identifier":"Q8BK72","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BK72/entry","name":"Mrps27","description":"Small ribosomal subunit protein mS27","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21393","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25413344","identifier":"Q9DCJ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DCJ7/entry","name":"Aurkaip1","description":"Small ribosomal subunit protein mS38","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR32035","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25413373","identifier":"Q9CQA6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQA6/entry","name":"Chchd1","description":"Small ribosomal subunit protein mS37","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR31278","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25413394","identifier":"Q80ZK0","identifierLink":"https://www.uniprot.org/uniprotkb/Q80ZK0/entry","name":"Mrps10","description":"Small ribosomal subunit protein uS10m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25413409","identifier":"Q9DCA2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DCA2/entry","name":"Mrps11","description":"Small ribosomal subunit protein uS11m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11759","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25413429","identifier":"Q9CPX7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CPX7/entry","name":"Mrps16","description":"Small ribosomal subunit protein bS16m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12919","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25413447","identifier":"Q8R2L5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R2L5/entry","name":"Mrps18c","description":"Small ribosomal subunit protein bS18m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13479","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25413467","identifier":"Q924T2","identifierLink":"https://www.uniprot.org/uniprotkb/Q924T2/entry","name":"Mrps2","description":"Small ribosomal subunit protein uS2m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12534","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25413489","identifier":"P58059","identifierLink":"https://www.uniprot.org/uniprotkb/P58059/entry","name":"Mrps21","description":"Small ribosomal subunit protein bS21m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21109","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25413509","identifier":"Q8VE22","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VE22/entry","name":"Mrps23","description":"Small ribosomal subunit protein mS23","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15925","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25413534","identifier":"Q9D125","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D125/entry","name":"Mrps25","description":"Small ribosomal subunit protein mS25","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13274","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25413553","identifier":"Q80ZS3","identifierLink":"https://www.uniprot.org/uniprotkb/Q80ZS3/entry","name":"Mrps26","description":"Small ribosomal subunit protein mS26","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21035","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25413567","identifier":"Q9CY16","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CY16/entry","name":"Mrps28","description":"Small ribosomal subunit protein bS1m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13447","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25413581","identifier":"Q61733","identifierLink":"https://www.uniprot.org/uniprotkb/Q61733/entry","name":"Mrps31","description":"Small ribosomal subunit protein mS31","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13231","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25413601","identifier":"Q9D2R8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D2R8/entry","name":"Mrps33","description":"Small ribosomal subunit protein mS33","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13362","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25413616","identifier":"Q99N87","identifierLink":"https://www.uniprot.org/uniprotkb/Q99N87/entry","name":"Mrps5","description":"Small ribosomal subunit protein uS5m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13718","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25413637","identifier":"P58064","identifierLink":"https://www.uniprot.org/uniprotkb/P58064/entry","name":"Mrps6","description":"Small ribosomal subunit protein bS6m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21011","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25413656","identifier":"Q80X85","identifierLink":"https://www.uniprot.org/uniprotkb/Q80X85/entry","name":"Mrps7","description":"Small ribosomal subunit protein uS7m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11205","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25413679","identifier":"Q9D7N3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D7N3/entry","name":"Mrps9","description":"Small ribosomal subunit protein uS9m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21569","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6393447","identifier":"Q9ER88","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ER88/entry","name":"Dap3","description":"Small ribosomal subunit protein mS29","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12810","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6393471","identifier":"Q9CXW2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CXW2/entry","name":"Mrps22","description":"Small ribosomal subunit protein mS22","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13071","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7503003","identifier":"Q9DC71","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DC71/entry","name":"Mrps15","description":"Small ribosomal subunit protein uS15m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46685","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8362662","identifier":"Q9JIK9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JIK9/entry","name":"Mrps34","description":"Small ribosomal subunit protein mS34","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR28589","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8369907","identifier":"Q9CR88","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CR88/entry","name":"Mrps14","description":"Small ribosomal subunit protein uS14m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR19836","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8370137","identifier":"Q9CQV5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQV5/entry","name":"Mrps24","description":"Small ribosomal subunit protein uS3m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21244","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8587231","identifier":"Q9CQE3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQE3/entry","name":"Mrps17","description":"Small ribosomal subunit protein uS17m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24088","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5302","complexName":"39S mitochondrial large ribosomal subunit","organismName":"Mus musculus; 10090","description":"Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). Responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. The mitochondrial ribosome (mitoribosome) is responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. All proteins synthesized by mouse mitoribosomes are hydrophobic, integral membrane proteins and some require prosthetic groups for folding and functioning. The mitoribosomes are tethered to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. The inner membrane protein Mrpl45 aligns the mitochondrial peptide exit tunnel with the membrane insertion machinery and supports the transfer of the mitochondrial nascent peptides towards the membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-11517069","identifier":"Q9CQF0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQF0/entry","name":"Mrpl11","description":"Large ribosomal subunit protein uL11m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11661","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11519253","identifier":"Q99N93","identifierLink":"https://www.uniprot.org/uniprotkb/Q99N93/entry","name":"Mrpl16","description":"Large ribosomal subunit protein uL16m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11568906","identifier":"Q9JKF7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JKF7/entry","name":"Mrpl39","description":"Large ribosomal subunit protein mL39","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR42753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20313947","identifier":"O35972","identifierLink":"https://www.uniprot.org/uniprotkb/O35972/entry","name":"Mrpl23","description":"Large ribosomal subunit protein uL23m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12059","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25413845","identifier":"URS000058010A_10090","identifierLink":"http://rnacentral.org/rna/URS000058010A_10090","name":"rrna_16s_mouse","description":"mouse mitochondrially encoded 16S rRNA","stochiometry":null,"interactorType":"ribosomal rna","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-25415534","identifier":"Q9CQL5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQL5/entry","name":"Mrpl18","description":"Large ribosomal subunit protein uL18m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12899","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25415553","identifier":"Q8K2M0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K2M0/entry","name":"Mrpl38","description":"Large ribosomal subunit protein mL38","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11362","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25415573","identifier":"Q9D0Y8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D0Y8/entry","name":"Mrpl52","description":"Large ribosomal subunit protein mL52","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR34090","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25415593","identifier":"Q9CPW3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CPW3/entry","name":"Mrpl54","description":"Large ribosomal subunit protein mL54","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR28595","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25415625","identifier":"Q8R035","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R035/entry","name":"Mrpl58","description":"Large ribosomal subunit protein mL62","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11075","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25415651","identifier":"Q99N94","identifierLink":"https://www.uniprot.org/uniprotkb/Q99N94/entry","name":"Mrpl9","description":"Large ribosomal subunit protein bL9m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21368","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25415671","identifier":"Q9D1I6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D1I6/entry","name":"Mrpl14","description":"Large ribosomal subunit protein uL14m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21037","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25415690","identifier":"Q9CPR5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CPR5/entry","name":"Mrpl15","description":"Large ribosomal subunit protein uL15m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12934","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25415716","identifier":"Q9D8P4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D8P4/entry","name":"Mrpl17","description":"Large ribosomal subunit protein bL17m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14413","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25415738","identifier":"Q9D338","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D338/entry","name":"Mrpl19","description":"Large ribosomal subunit protein bL19m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15680","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25415760","identifier":"Q9CQL4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQL4/entry","name":"Mrpl20","description":"Large ribosomal subunit protein bL20m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10986","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25415783","identifier":"Q9D1N9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D1N9/entry","name":"Mrpl21","description":"Large ribosomal subunit protein bL21m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21349","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25415807","identifier":"Q9CQ06","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQ06/entry","name":"Mrpl24","description":"Large ribosomal subunit protein uL24m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12903","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25415839","identifier":"Q9D1B9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D1B9/entry","name":"Mrpl28","description":"Large ribosomal subunit protein bL28m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13528","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25415861","identifier":"Q9D7N6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D7N6/entry","name":"Mrpl30","description":"Large ribosomal subunit protein uL30m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15892","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25415886","identifier":"Q9DCI9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DCI9/entry","name":"Mrpl32","description":"Large ribosomal subunit protein bL32m","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 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The assembly process leads to a tight connection between the fusing membranes and initiates membrane fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-16572","identifier":"P28791","identifierLink":"https://www.uniprot.org/uniprotkb/P28791/entry","name":"SEC20","description":"Protein transport protein SEC20","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12825","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16577","identifier":"P22214","identifierLink":"https://www.uniprot.org/uniprotkb/P22214/entry","name":"SEC22","description":"Protein transport protein SEC22","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45837","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20016","identifier":"P41834","identifierLink":"https://www.uniprot.org/uniprotkb/P41834/entry","name":"UFE1","description":"Syntaxin UFE1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15959","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23881","identifier":"P53146","identifierLink":"https://www.uniprot.org/uniprotkb/P53146/entry","name":"USE1","description":"Protein transport protein USE1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5321","complexName":"Endosomal SNARE complex TLG2-VTI1-TLG1-SNC2","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SNARE complex required for the fusion of endosomal vesicles with the trans-Golgi network. Mediates membrane fusion through the spontaneous assembly of four complementary SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) motifs. SNAREs bind to each other in-trans, that is, with SNAREs anchored in each apposed tethered membrane. The assembly process leads to a tight connection between the fusing membranes and initiates membrane fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-17512","identifier":"P33328","identifierLink":"https://www.uniprot.org/uniprotkb/P33328/entry","name":"SNC2","description":"Synaptobrevin homolog 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19302","identifier":"Q08144","identifierLink":"https://www.uniprot.org/uniprotkb/Q08144/entry","name":"TLG2","description":"t-SNARE affecting a late Golgi compartment protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20519","identifier":"Q04338","identifierLink":"https://www.uniprot.org/uniprotkb/Q04338/entry","name":"VTI1","description":"t-SNARE VTI1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21230","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-38705","identifier":"Q03322","identifierLink":"https://www.uniprot.org/uniprotkb/Q03322/entry","name":"TLG1","description":"t-SNARE affecting a late Golgi compartment protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5322","complexName":"Endosomal SNARE complex TLG2-VTI1-TLG1-SNC1","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SNARE complex required for the fusion of endosomal vesicles with the trans-Golgi network. Mediates membrane fusion through the spontaneous assembly of four complementary SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) motifs. SNAREs bind to each other in-trans, that is, with SNAREs anchored in each apposed tethered membrane. The assembly process leads to a tight connection between the fusing membranes and initiates membrane fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-19302","identifier":"Q08144","identifierLink":"https://www.uniprot.org/uniprotkb/Q08144/entry","name":"TLG2","description":"t-SNARE affecting a late Golgi compartment protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20519","identifier":"Q04338","identifierLink":"https://www.uniprot.org/uniprotkb/Q04338/entry","name":"VTI1","description":"t-SNARE VTI1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21230","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2123541","identifier":"P31109","identifierLink":"https://www.uniprot.org/uniprotkb/P31109/entry","name":"SNC1","description":"Synaptobrevin homolog 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-38705","identifier":"Q03322","identifierLink":"https://www.uniprot.org/uniprotkb/Q03322/entry","name":"TLG1","description":"t-SNARE affecting a late Golgi compartment protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5341","complexName":"DBF20-MOB1 kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Probable role in exit from mitosis during the cell cycle. 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Phosphorylates chitin synthase CHS2 (P14180) to regulate cytokinesis.","predictedComplex":false,"interactors":[{"ac":"EBI-11119","identifier":"P40484","identifierLink":"https://www.uniprot.org/uniprotkb/P40484/entry","name":"MOB1","description":"DBF2 kinase activator protein MOB1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5588","identifier":"P32328","identifierLink":"https://www.uniprot.org/uniprotkb/P32328/entry","name":"DBF20","description":"Serine/threonine-protein kinase DBF20","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24356","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5342","complexName":"RXRalpha-NCOA1 activated retinoic acid receptor complex","organismName":"Homo sapiens; 9606","description":"Member of the nuclear receptor (NR) family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. 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Upon ligand binding, RXRs undergo a conformational change that results in the release of corepressors and transcriptional coactivators, such as NCOA1, are recruited to the LBD which activates transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-455189","identifier":"Q15788","identifierLink":"https://www.uniprot.org/uniprotkb/Q15788/entry","name":"NCOA1","description":"Nuclear receptor coactivator 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-78598","identifier":"P19793","identifierLink":"https://www.uniprot.org/uniprotkb/P19793/entry","name":"RXRA","description":"Retinoic acid receptor RXR-alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5343","complexName":"RXRalpha-NCOA1 activated retinoic acid receptor complex","organismName":"Mus musculus; 10090","description":"Member of the nuclear receptor (NR) family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. The 9-cis retinoic acid receptor (retinoid X receptor, Rxra) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including the all-trans retinoic acid receptors (RARs). Like other NRs, Rxra contains DNA-binding and ligand-binding domain (DBD, LBD). In the absence of agonist, the complex recruits the corepressor proteins NCoR or SMRT and associated factors such as histone deacetylases or DNA-methyl transferases that may lead to an inactive condensed chromatin structure, preventing transcription. Upon ligand binding, RXRs undergo a conformational change that results in the release of corepressors and transcriptional coactivators, such as Ncoa1, are recruited to the LBD which activates transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-11171952","identifier":"P70365","identifierLink":"https://www.uniprot.org/uniprotkb/P70365/entry","name":"Ncoa1","description":"Nuclear receptor coactivator 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-346715","identifier":"P28700","identifierLink":"https://www.uniprot.org/uniprotkb/P28700/entry","name":"Rxra","description":"Retinoic acid receptor RXR-alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5361","complexName":"tRNA uridine 5-carboxymethylaminomethyl modification complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the formation of a carboxymethylaminomethyl (cmnm)4 group at the 5 position of the wobble uridine (U34) of tRNAs reading 2-fold degenerated codons ending with A or G. This modification (cmnm5U34) combined with thiolation at the 2 position favors the interaction with A and G but suppresses base pairing with C and U and plays a regulatory role in gene expression.","predictedComplex":false,"interactors":[{"ac":"EBI-550977","identifier":"P0A6U3","identifierLink":"https://www.uniprot.org/uniprotkb/P0A6U3/entry","name":"mnmG","description":"tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11806","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-550986","identifier":"P25522","identifierLink":"https://www.uniprot.org/uniprotkb/P25522/entry","name":"mnmE","description":"tRNA modification GTPase MnmE","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42714","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-967750","identifier":"CHEBI:29103","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29103","name":"potassium(1+)","description":"Potassium (1+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-5381","complexName":"Alternative pathway fluid-phase C3 convertase complex C3(H2O)Bb","organismName":"Homo sapiens; 9606","description":"A serine-type endopeptidase complex of the alternative pathway of complement activation of the innate immune system. Cleaves Complement C3 precurser (P01024) into anaphylatoxin C3A (P01024-PRO_0000005910) and nascent convertase core-component C3b (CPX-973). Restricted to the fluid-phase. \r\n\r\nC3(H2O)Bb convertase is very unstable and readily inactivated by Factor H (P08603) thus regulating the amount of spontaneously available C3 convertase initiating the alternative pathway. \r\n\r\nLack of protection, due to familial mutations in the complement genes or the presence of autoantibodies against regulators has been linked to atypical hemolytic uremic syndrome (aHUS) and C3 glomerulopathies (C3G) in kidneys and age-related macular degeneration (AMD) in eyes. Conditions of chronic and acute inflammations, as in rheumatoid arthritis, strokes, and heart attacks, become aggravated by complement activation against the disturbed tissue.","predictedComplex":false,"interactors":[{"ac":"EBI-21988629","identifier":"P00751-PRO_0000027547","identifierLink":"https://www.uniprot.org/uniprotkb/P00751-PRO_0000027547/entry","name":"CFB","description":"Complement factor B Bb","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25436489","identifier":"P01024-PRO_0000005909","identifierLink":"https://www.uniprot.org/uniprotkb/P01024-PRO_0000005909/entry","name":"C3","description":"Complement C3 alpha chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-6863145","identifier":"P01024-PRO_0000005908","identifierLink":"https://www.uniprot.org/uniprotkb/P01024-PRO_0000005908/entry","name":"C3","description":"Complement C3 beta chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-1887","complexName":"Vacuolar SNARE complex VAM3-VTI1-VAM7-YKT6","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SNARE complex required for autophagosome-vacuole fusion. Mediates membrane fusion through the spontaneous assembly of four complementary SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) motifs. SNAREs bind to each other in-trans, that is, with SNAREs anchored in each apposed tethered membrane. The assembly process leads to a tight connection between the linked membranes and initiates membrane fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-20227","identifier":"Q12241","identifierLink":"https://www.uniprot.org/uniprotkb/Q12241/entry","name":"VAM3","description":"Syntaxin VAM3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20232","identifier":"P32912","identifierLink":"https://www.uniprot.org/uniprotkb/P32912/entry","name":"VAM7","description":"Vacuolar morphogenesis protein 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20519","identifier":"Q04338","identifierLink":"https://www.uniprot.org/uniprotkb/Q04338/entry","name":"VTI1","description":"t-SNARE VTI1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21230","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26982","identifier":"P36015","identifierLink":"https://www.uniprot.org/uniprotkb/P36015/entry","name":"YKT6","description":"Synaptobrevin homolog YKT6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45806","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5401","complexName":"Vacuolar SNARE complex VAM3-VTI1-VAM7-NYV1","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SNARE complex required for homotypic vacuole fusion and is important for vacuole formation. SNARE assembly also appears to promote Ca2+ release from the vacuole lumen. Mediates membrane fusion through the spontaneous assembly of four complementary SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) motifs. SNAREs bind to each other in-trans, that is, with SNAREs anchored in each apposed tethered membrane. The assembly process leads to a tight connection between the linked membranes and initiates membrane fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-20227","identifier":"Q12241","identifierLink":"https://www.uniprot.org/uniprotkb/Q12241/entry","name":"VAM3","description":"Syntaxin VAM3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20232","identifier":"P32912","identifierLink":"https://www.uniprot.org/uniprotkb/P32912/entry","name":"VAM7","description":"Vacuolar morphogenesis protein 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20519","identifier":"Q04338","identifierLink":"https://www.uniprot.org/uniprotkb/Q04338/entry","name":"VTI1","description":"t-SNARE VTI1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21230","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-35465","identifier":"Q12255","identifierLink":"https://www.uniprot.org/uniprotkb/Q12255/entry","name":"NYV1","description":"Vacuolar v-SNARE NYV1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21136","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5421","complexName":"Endosomal SNARE complex PEP12-VTI1-SYN8-YKT6","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SNARE complex required for transport from the Golgi to endosomes. Mediates membrane fusion through the spontaneous assembly of four complementary SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) motifs. SNAREs bind to each other in-trans, that is, with SNAREs anchored in each apposed tethered membrane. The assembly process leads to a tight connection between the linked membranes and initiates membrane fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-13098","identifier":"P32854","identifierLink":"https://www.uniprot.org/uniprotkb/P32854/entry","name":"PEP12","description":"Syntaxin PEP12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18483","identifier":"P31377","identifierLink":"https://www.uniprot.org/uniprotkb/P31377/entry","name":"SYN8","description":"Syntaxin-8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20519","identifier":"Q04338","identifierLink":"https://www.uniprot.org/uniprotkb/Q04338/entry","name":"VTI1","description":"t-SNARE VTI1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21230","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26982","identifier":"P36015","identifierLink":"https://www.uniprot.org/uniprotkb/P36015/entry","name":"YKT6","description":"Synaptobrevin homolog YKT6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45806","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5422","complexName":"Endosomal SNARE complex PEP12-VTI1-TLG1-YKT6","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SNARE complex required for transport from the Golgi to endosomes. Mediates membrane fusion through the spontaneous assembly of four complementary SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) motifs. SNAREs bind to each other in-trans, that is, with SNAREs anchored in each apposed tethered membrane. The assembly process leads to a tight connection between the linked membranes and initiates membrane fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-13098","identifier":"P32854","identifierLink":"https://www.uniprot.org/uniprotkb/P32854/entry","name":"PEP12","description":"Syntaxin PEP12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20519","identifier":"Q04338","identifierLink":"https://www.uniprot.org/uniprotkb/Q04338/entry","name":"VTI1","description":"t-SNARE VTI1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21230","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26982","identifier":"P36015","identifierLink":"https://www.uniprot.org/uniprotkb/P36015/entry","name":"YKT6","description":"Synaptobrevin homolog YKT6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45806","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-38705","identifier":"Q03322","identifierLink":"https://www.uniprot.org/uniprotkb/Q03322/entry","name":"TLG1","description":"t-SNARE affecting a late Golgi compartment protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5423","complexName":"Endosomal SNARE complex PEP12-VTI1-TLG1-SNC1","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SNARE complex required for transport from the Golgi to endosomes. Mediates membrane fusion through the spontaneous assembly of four complementary SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) motifs. SNAREs bind to each other in-trans, that is, with SNAREs anchored in each apposed tethered membrane. The assembly process leads to a tight connection between the linked membranes and initiates membrane fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-13098","identifier":"P32854","identifierLink":"https://www.uniprot.org/uniprotkb/P32854/entry","name":"PEP12","description":"Syntaxin PEP12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20519","identifier":"Q04338","identifierLink":"https://www.uniprot.org/uniprotkb/Q04338/entry","name":"VTI1","description":"t-SNARE VTI1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21230","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2123541","identifier":"P31109","identifierLink":"https://www.uniprot.org/uniprotkb/P31109/entry","name":"SNC1","description":"Synaptobrevin homolog 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-38705","identifier":"Q03322","identifierLink":"https://www.uniprot.org/uniprotkb/Q03322/entry","name":"TLG1","description":"t-SNARE affecting a late Golgi compartment protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5424","complexName":"Endosomal SNARE complex PEP12-VTI1-SYN8-SNC1","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SNARE complex required for transport from the Golgi to endosomes. Mediates membrane fusion through the spontaneous assembly of four complementary SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) motifs. SNAREs bind to each other in-trans, that is, with SNAREs anchored in each apposed tethered membrane. The assembly process leads to a tight connection between the linked membranes and initiates membrane fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-13098","identifier":"P32854","identifierLink":"https://www.uniprot.org/uniprotkb/P32854/entry","name":"PEP12","description":"Syntaxin PEP12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18483","identifier":"P31377","identifierLink":"https://www.uniprot.org/uniprotkb/P31377/entry","name":"SYN8","description":"Syntaxin-8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20519","identifier":"Q04338","identifierLink":"https://www.uniprot.org/uniprotkb/Q04338/entry","name":"VTI1","description":"t-SNARE VTI1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21230","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2123541","identifier":"P31109","identifierLink":"https://www.uniprot.org/uniprotkb/P31109/entry","name":"SNC1","description":"Synaptobrevin homolog 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4319","complexName":"Arginine ABC transporter complex, artJ variant","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity arginine transporter. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1120642","identifier":"P30860","identifierLink":"https://www.uniprot.org/uniprotkb/P30860/entry","name":"artJ","description":"ABC transporter arginine-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR35936","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1131813","identifier":"P0AE30","identifierLink":"https://www.uniprot.org/uniprotkb/P0AE30/entry","name":"artM","description":"Arginine ABC transporter permease protein ArtM","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30614","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544100","identifier":"P0AAF6","identifierLink":"https://www.uniprot.org/uniprotkb/P0AAF6/entry","name":"artP","description":"Arginine transport ATP-binding protein ArtP","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43166","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-559766","identifier":"P0AE34","identifierLink":"https://www.uniprot.org/uniprotkb/P0AE34/entry","name":"artQ","description":"Arginine ABC transporter permease protein ArtQ","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30133","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4320","complexName":"D-allose ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity D-allose binding transporter, also capable of the low-affinity transport of D-ribose. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-21451227","identifier":"P32720","identifierLink":"https://www.uniprot.org/uniprotkb/P32720/entry","name":"alsC","description":"D-allose transport system permease protein AlsC","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32196","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-562166","identifier":"P32721","identifierLink":"https://www.uniprot.org/uniprotkb/P32721/entry","name":"alsA","description":"D-allose import ATP-binding protein AlsA","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43790","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-906901","identifier":"P39265","identifierLink":"https://www.uniprot.org/uniprotkb/P39265/entry","name":"alsB","description":"D-allose-binding periplasmic protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR46847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4321","complexName":"Dipeptide ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"D,D-dipeptide transporter that imports D-alanyl-D-alanine for use as an energy source under starvation conditions, ensuring that this is a a component of peptidoglycan that can be recycled by the cell. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily. Thought to have evolved from the general dipeptide (Dpp) transporter complex (CPX-4345),","predictedComplex":false,"interactors":[{"ac":"EBI-1118707","identifier":"P77463","identifierLink":"https://www.uniprot.org/uniprotkb/P77463/entry","name":"ddpC","description":"Probable D,D-dipeptide transport system permease protein DdpC","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43386","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1124237","identifier":"P77622","identifierLink":"https://www.uniprot.org/uniprotkb/P77622/entry","name":"ddpF","description":"Probable D,D-dipeptide transport ATP-binding protein DdpF","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43776","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-548189","identifier":"P77308","identifierLink":"https://www.uniprot.org/uniprotkb/P77308/entry","name":"ddpB","description":"Probable D,D-dipeptide transport system permease protein DdpB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43163","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-548554","identifier":"P76128","identifierLink":"https://www.uniprot.org/uniprotkb/P76128/entry","name":"ddpA","description":"Probable D,D-dipeptide-binding periplasmic protein DdpA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30290","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-556984","identifier":"P77268","identifierLink":"https://www.uniprot.org/uniprotkb/P77268/entry","name":"ddpD","description":"Probable D,D-dipeptide transport ATP-binding protein DdpD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43297","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4322","complexName":"Cyclin-dependent protein kinase 5 holoenzyme complex","organismName":"Caenorhabditis elegans; 6239","description":"A proline-directed serine/threonine kinase complex that functions in neuronal activities unrelated to cell-cycle progression. Regulates the axonal transport of synaptic vesicle precursors by inhibiting dynein-mediated retrograde transport In DA motor neurons. Regulates the trafficking of dense-core vesicles in DA and DB motor neurons by promoting anterograde trafficking to the axon and preventing dynein-dependent trafficking to the dendrite","predictedComplex":false,"interactors":[{"ac":"EBI-2420667","identifier":"G5ECH7","identifierLink":"https://www.uniprot.org/uniprotkb/G5ECH7/entry","name":"cdk-5","description":"Cyclin-dependent-like kinase 5","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2420673","identifier":"Q22695","identifierLink":"https://www.uniprot.org/uniprotkb/Q22695/entry","name":"cdka-1","description":"Cyclin-dependent kinase 5 activator 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR23401","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4323","complexName":"Galactofuranose ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity galactofuranose transporter enabling carbon scavenging via the utilization of rarer furanose forms of sugars. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1128941","identifier":"P39325","identifierLink":"https://www.uniprot.org/uniprotkb/P39325/entry","name":"ytfQ","description":"Galactofuranose-binding protein YtfQ","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR46847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21452138","identifier":"Q6BEX0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6BEX0/entry","name":"ytfR","description":"Galactofuranose transporter ATP-binding protein YtfR","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43790","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21452159","identifier":"P37772","identifierLink":"https://www.uniprot.org/uniprotkb/P37772/entry","name":"yjfF","description":"Inner membrane ABC transporter permease protein YjfF","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32196","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-554774","identifier":"P39328","identifierLink":"https://www.uniprot.org/uniprotkb/P39328/entry","name":"ytfT","description":"Galactofuranose transporter permease protein YtfT","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32196","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4324","complexName":"Glutamate/aspartate ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity transporter of glutamate and aspartate. Member of the ATP-binding cassette (ABC) transporter family, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-21452196","identifier":"P0AER5","identifierLink":"https://www.uniprot.org/uniprotkb/P0AER5/entry","name":"gltK","description":"Glutamate/aspartate import permease protein GltK","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30614","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-557303","identifier":"P0AER3","identifierLink":"https://www.uniprot.org/uniprotkb/P0AER3/entry","name":"gltJ","description":"Glutamate/aspartate import permease protein GltJ","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30614","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-558243","identifier":"P0AAG3","identifierLink":"https://www.uniprot.org/uniprotkb/P0AAG3/entry","name":"gltL","description":"Glutamate/aspartate import ATP-binding protein GltL","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43166","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9121846","identifier":"P37902","identifierLink":"https://www.uniprot.org/uniprotkb/P37902/entry","name":"gltI","description":"Glutamate/aspartate import solute-binding protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30085","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4325","complexName":"Glutathione ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High-affinity glutathione transporter. Member of the ATP-binding cassette (ABC) transporter family, prokaryote-type (PK-type) subfamily. Glutathione is required for reducing oxygen species and peroxides and acts against xenobiotics and drugs by the formation and excretion of glutathione S conjugates.","predictedComplex":false,"interactors":[{"ac":"EBI-1120235","identifier":"P75798","identifierLink":"https://www.uniprot.org/uniprotkb/P75798/entry","name":"gsiC","description":"Glutathione transport system permease protein GsiC","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43163","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21452300","identifier":"P75796","identifierLink":"https://www.uniprot.org/uniprotkb/P75796/entry","name":"gsiA","description":"Glutathione import ATP-binding protein GsiA","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43776","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21452320","identifier":"P75797","identifierLink":"https://www.uniprot.org/uniprotkb/P75797/entry","name":"gsiB","description":"Glutathione-binding protein GsiB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30290","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21452341","identifier":"P75799","identifierLink":"https://www.uniprot.org/uniprotkb/P75799/entry","name":"gsiD","description":"Glutathione transport system permease protein GsiD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43386","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4328","complexName":"Histidine ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High-affinity polar amino acid transporter, in particular linked to the import of histidine but also binds arginine, ornithine and lysine.. Member of the ATP-binding cassette (ABC) transporter family, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1115638","identifier":"P0AEU0","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEU0/entry","name":"hisJ","description":"Histidine-binding periplasmic protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR35936","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1120883","identifier":"P07109","identifierLink":"https://www.uniprot.org/uniprotkb/P07109/entry","name":"hisP","description":"Histidine/lysine/arginine/ornithine transport ATP-binding protein HisP","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43166","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21452654","identifier":"P0AEU3","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEU3/entry","name":"hisM","description":"Histidine/lysine/arginine/ornithine transport system permease protein HisM","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30450","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21452671","identifier":"P52094","identifierLink":"https://www.uniprot.org/uniprotkb/P52094/entry","name":"hisQ","description":"Histidine/lysine/arginine/ornithine transport system permease protein HisQ","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30133","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4329","complexName":"Polar amino acid ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High-affinity polar amino acid transporter. Member of the ATP-binding cassette (ABC) transporter family, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1120883","identifier":"P07109","identifierLink":"https://www.uniprot.org/uniprotkb/P07109/entry","name":"hisP","description":"Histidine/lysine/arginine/ornithine transport ATP-binding protein HisP","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43166","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15775597","identifier":"P09551","identifierLink":"https://www.uniprot.org/uniprotkb/P09551/entry","name":"argT","description":"Lysine/arginine/ornithine-binding periplasmic protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR35936","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21452654","identifier":"P0AEU3","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEU3/entry","name":"hisM","description":"Histidine/lysine/arginine/ornithine transport system permease protein HisM","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30450","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21452671","identifier":"P52094","identifierLink":"https://www.uniprot.org/uniprotkb/P52094/entry","name":"hisQ","description":"Histidine/lysine/arginine/ornithine transport system permease protein HisQ","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30133","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4341","complexName":"Beta-methyl-D-galactoside/galactose ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity transproter for beta-methyl-D-galactoside and galactose. Member of the ATP-binding cassette (ABC) transporter family, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-21454024","identifier":"P23200","identifierLink":"https://www.uniprot.org/uniprotkb/P23200/entry","name":"mglC","description":"Galactose/methyl galactoside import permease protein MglC","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32196","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-370848","identifier":"P0AAG8","identifierLink":"https://www.uniprot.org/uniprotkb/P0AAG8/entry","name":"mglA","description":"Galactose/methyl galactoside import ATP-binding protein MglA","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43790","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-552369","identifier":"P0AEE5","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEE5/entry","name":"mglB","description":"D-galactose/methyl-galactoside binding periplasmic protein MglB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4342","complexName":"Molybdate ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity transporter of molybdate and tungstate. Member of the ATP-binding cassette (ABC) transporter family, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1115113","identifier":"P0AF01","identifierLink":"https://www.uniprot.org/uniprotkb/P0AF01/entry","name":"modB","description":"Molybdenum transport system permease protein ModB","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30183","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1120112","identifier":"P09833","identifierLink":"https://www.uniprot.org/uniprotkb/P09833/entry","name":"modC","description":"Molybdenum import ATP-binding protein ModC","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43514","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1128158","identifier":"P37329","identifierLink":"https://www.uniprot.org/uniprotkb/P37329/entry","name":"modA","description":"Molybdate-binding protein ModA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30632","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4343","complexName":"Murein tripeptide ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity transporter of the cell wall component murein tripeptide (Mtp, l-Ala-gamma-D-Glu-meso-diaminopimelic acid, CHEBI:61564), which contains a D-amino acid and a gamma-peptide linkage. Diaminopimelic acid (DAP) is then used for peptidoglycan biosynthesis.Import allows recycling of DAP from either exogenous sources or DAP that is released by the N-acetylmuramoyl-l-alanine amidase AmiD (P75820) outer membrane amidase into the periplasm during cell growth. Member of the ATP-binding cassette (ABC) transporter family, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1123038","identifier":"P77737","identifierLink":"https://www.uniprot.org/uniprotkb/P77737/entry","name":"oppF","description":"Oligopeptide transport ATP-binding protein OppF","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43776","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21454422","identifier":"P0AFH2","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFH2/entry","name":"oppB","description":"Oligopeptide transport system permease protein OppB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30465","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21454439","identifier":"P0AFH6","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFH6/entry","name":"oppC","description":"Oligopeptide transport system permease protein OppC","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43386","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21454459","identifier":"P77348","identifierLink":"https://www.uniprot.org/uniprotkb/P77348/entry","name":"mppA","description":"Periplasmic murein peptide-binding protein MppA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30290","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-560815","identifier":"P76027","identifierLink":"https://www.uniprot.org/uniprotkb/P76027/entry","name":"oppD","description":"Oligopeptide transport ATP-binding protein OppD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43297","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4344","complexName":"Oligopeptide ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity transporter of oligopeptides that can accept peptides from 2 to 5 residues in length, with the highest affinity for tripeptides. Member of the ATP-binding cassette (ABC) transporter family, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1123030","identifier":"P23843","identifierLink":"https://www.uniprot.org/uniprotkb/P23843/entry","name":"oppA","description":"Periplasmic oligopeptide-binding protein OppA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30290","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1123038","identifier":"P77737","identifierLink":"https://www.uniprot.org/uniprotkb/P77737/entry","name":"oppF","description":"Oligopeptide transport ATP-binding protein OppF","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43776","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21454422","identifier":"P0AFH2","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFH2/entry","name":"oppB","description":"Oligopeptide transport system permease protein OppB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30465","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21454439","identifier":"P0AFH6","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFH6/entry","name":"oppC","description":"Oligopeptide transport system permease protein OppC","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43386","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-560815","identifier":"P76027","identifierLink":"https://www.uniprot.org/uniprotkb/P76027/entry","name":"oppD","description":"Oligopeptide transport ATP-binding protein OppD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43297","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4345","complexName":"Heme/dipeptide ABC transporter complex, dppA variant","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity peptide transporter which has a preference for dipeptides. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily. Also transports heme and the heme precursor delta-aminolevulinic acid (ALA, CHEBI:17549), though it should be noted that the Escherichia coli K12 laboratory strain is missing a heme outer membrane receptor. The dpp operon is up-regulated during exponential growth.","predictedComplex":false,"interactors":[{"ac":"EBI-545801","identifier":"P0AEF8","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEF8/entry","name":"dppB","description":"Dipeptide transport system permease protein DppB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43163","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-548206","identifier":"P0AAG0","identifierLink":"https://www.uniprot.org/uniprotkb/P0AAG0/entry","name":"dppD","description":"Dipeptide transport ATP-binding protein DppD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43297","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-548667","identifier":"P0AEG1","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEG1/entry","name":"dppC","description":"Dipeptide transport system permease protein DppC","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43386","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-554666","identifier":"P23847","identifierLink":"https://www.uniprot.org/uniprotkb/P23847/entry","name":"dppA","description":"Dipeptide-binding protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30290","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-849273","identifier":"P37313","identifierLink":"https://www.uniprot.org/uniprotkb/P37313/entry","name":"dppF","description":"Dipeptide transport ATP-binding protein DppF","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43776","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4346","complexName":"Heme/dipeptide ABC transporter complex, mppA variant","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity peptide transporter which has a preference for dipeptides. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily. Also transports heme and the heme precursor delta-aminolevulinic acid (ALA, CHEBI:17549), though it should be noted that the Escherichia coli K12 laboratory strain is missing a heme outer membrane receptor. The dpp operon is up-regulated during exponential growth.","predictedComplex":false,"interactors":[{"ac":"EBI-21454459","identifier":"P77348","identifierLink":"https://www.uniprot.org/uniprotkb/P77348/entry","name":"mppA","description":"Periplasmic murein peptide-binding protein MppA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30290","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-545801","identifier":"P0AEF8","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEF8/entry","name":"dppB","description":"Dipeptide transport system permease protein DppB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43163","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-548206","identifier":"P0AAG0","identifierLink":"https://www.uniprot.org/uniprotkb/P0AAG0/entry","name":"dppD","description":"Dipeptide transport ATP-binding protein DppD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43297","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-548667","identifier":"P0AEG1","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEG1/entry","name":"dppC","description":"Dipeptide transport system permease protein DppC","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43386","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-849273","identifier":"P37313","identifierLink":"https://www.uniprot.org/uniprotkb/P37313/entry","name":"dppF","description":"Dipeptide transport ATP-binding protein DppF","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43776","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4348","complexName":"Nickel ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity nickel transporter. Transport observed in the presence of L- (but not D-) histidine, as Ni-(L-His)2, suggesting that nickel-speciation in different growth environments may affect the mechanism of nickel transport. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily. The nik operon is expressed under anaerobic growth conditions","predictedComplex":false,"interactors":[{"ac":"EBI-21455530","identifier":"P33591","identifierLink":"https://www.uniprot.org/uniprotkb/P33591/entry","name":"nikB","description":"Nickel transport system permease protein NikB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43163","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21455546","identifier":"P0AFA9","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFA9/entry","name":"nikC","description":"Nickel transport system permease protein NikC","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43386","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549236","identifier":"P33593","identifierLink":"https://www.uniprot.org/uniprotkb/P33593/entry","name":"nikD","description":"Nickel import ATP-binding protein NikD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR24220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-555182","identifier":"P33590","identifierLink":"https://www.uniprot.org/uniprotkb/P33590/entry","name":"nikA","description":"Nickel-binding periplasmic protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30290","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-555189","identifier":"P33594","identifierLink":"https://www.uniprot.org/uniprotkb/P33594/entry","name":"nikE","description":"Nickel import ATP-binding protein NikE","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43776","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4362","complexName":"Peptide ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"Probable high affinity peptide transporter. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily.  Imports Microcin C (McC), a peptide-nucleotide antibiotic, which targets aspartyl-tRNA synthetase (P21889). Analogues require a minimal peptide chain length of 6 amino acids and the presence of an N-terminal formyl-methionyl-arginyl sequence for uptake.","predictedComplex":false,"interactors":[{"ac":"EBI-1127936","identifier":"P33913","identifierLink":"https://www.uniprot.org/uniprotkb/P33913/entry","name":"yejA","description":"Uncharacterized protein YejA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30290","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21456246","identifier":"P0AFU0","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFU0/entry","name":"yejB","description":"Inner membrane ABC transporter permease protein YejB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30465","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-545567","identifier":"P33915","identifierLink":"https://www.uniprot.org/uniprotkb/P33915/entry","name":"yejE","description":"Inner membrane ABC transporter permease protein YejE","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30325","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-560808","identifier":"P33916","identifierLink":"https://www.uniprot.org/uniprotkb/P33916/entry","name":"yejF","description":"Uncharacterized ABC transporter ATP-binding protein YejF","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR24220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4381","complexName":"Phosphate ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity phosphate transporter. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily. Expressed by the pstSCAB-phoU operon which is induced in response to low levels of environmental phosphate. Sufficient Pi generates a signal through the PstSCAB2 transporter that leads to repression of this operon.","predictedComplex":false,"interactors":[{"ac":"EBI-21458513","identifier":"P07654","identifierLink":"https://www.uniprot.org/uniprotkb/P07654/entry","name":"pstA","description":"Phosphate transport system permease protein PstA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42922","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21458532","identifier":"P0AGH8","identifierLink":"https://www.uniprot.org/uniprotkb/P0AGH8/entry","name":"pstC","description":"Phosphate transport system permease protein PstC","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30425","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-547448","identifier":"P0AAH0","identifierLink":"https://www.uniprot.org/uniprotkb/P0AAH0/entry","name":"pstB","description":"Phosphate import ATP-binding protein PstB","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43423","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-555320","identifier":"P0AG82","identifierLink":"https://www.uniprot.org/uniprotkb/P0AG82/entry","name":"pstS","description":"Phosphate-binding protein PstS","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42996","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4382","complexName":"Phosphonate ABC transporter complex","organismName":"Escherichia coli; 562","description":"High affinity phosphonate (phosphorus-containing organic molecules in which the P atom is linked directly to C in a stable chemical bond) transporter.  Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily. Also has the ability to take up phosphate in the absence of canonical phosphate-transport systems. E. coli K-12 laboratory strains do not express the PhnE permease, due to the presence of an 8 bp insertion in phnE, and consequently are unable to take up phosphonates. This cryptic mutation readily reverts and most E.coli strains carry a functional phnE gene.","predictedComplex":false,"interactors":[{"ac":"EBI-25775445","identifier":"A0A2P9E102","identifierLink":"https://www.uniprot.org/uniprotkb/A0A2P9E102/entry","name":"ptxA","description":null,"stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli; 562","xrefs":[]},{"ac":"EBI-25775462","identifier":null,"identifierLink":null,"name":"e1j3c2_ecolx","description":null,"stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli MS 124-1; 679205","xrefs":[]},{"ac":"EBI-63466264","identifier":"A0A376FQ92","identifierLink":"https://www.uniprot.org/uniprotkb/A0A376FQ92/entry","name":"phnD","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli; 562","xrefs":[]}]},{"complexAC":"CPX-4383","complexName":"Spermidine ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity spermidine importer, a polycation that interacts with negatively charged molecules such as DNA, RNA and proteins that plays a role in stress response.  Also imports other polyamines such as putrescine. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1122293","identifier":"P0AFK9","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFK9/entry","name":"potD","description":"Spermidine/putrescine-binding periplasmic protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1122336","identifier":"P69874","identifierLink":"https://www.uniprot.org/uniprotkb/P69874/entry","name":"potA","description":"Spermidine/putrescine import ATP-binding protein PotA","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42781","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21458944","identifier":"P0AFK4","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFK4/entry","name":"potB","description":"Spermidine/putrescine transport system permease protein PotB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42929","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-560400","identifier":"P0AFK6","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFK6/entry","name":"potC","description":"Spermidine/putrescine transport system permease protein PotC","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43848","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4384","complexName":"Putrescine ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity  putrescine importer, a polycation that interacts with negatively charged molecules such as DNA, RNA and proteins that plays a role in stress response. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1120633","identifier":"P31133","identifierLink":"https://www.uniprot.org/uniprotkb/P31133/entry","name":"potF","description":"Putrescine-binding periplasmic protein PotF","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21944834","identifier":"P0AFL1","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFL1/entry","name":"potI","description":"Putrescine transport system permease protein PotI","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43848","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9140295","identifier":"P31134","identifierLink":"https://www.uniprot.org/uniprotkb/P31134/entry","name":"potG","description":"Putrescine transport ATP-binding protein PotG","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42781","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9147630","identifier":"P31135","identifierLink":"https://www.uniprot.org/uniprotkb/P31135/entry","name":"potH","description":"Putrescine transport system permease protein PotH","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42929","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4385","complexName":"Sulfate/thiosulfate ABC transporter complex, cypP variant","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity sulfate and thiosulfate transporter.  Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-21459122","identifier":"P16701","identifierLink":"https://www.uniprot.org/uniprotkb/P16701/entry","name":"cysU","description":"Sulfate transport system permease protein CysT","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30406","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-552215","identifier":"P0AEB0","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEB0/entry","name":"cysW","description":"Sulfate transport system permease protein CysW","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30406","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-556404","identifier":"P16676","identifierLink":"https://www.uniprot.org/uniprotkb/P16676/entry","name":"cysA","description":"Sulfate/thiosulfate import ATP-binding protein CysA","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43514","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-560567","identifier":"P16700","identifierLink":"https://www.uniprot.org/uniprotkb/P16700/entry","name":"cysP","description":"Thiosulfate-binding protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30368","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4386","complexName":"Sulfate/thiosulfate ABC transporter complex, sbp variant","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity sulfate and thiosulfate transporter. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1134039","identifier":"P0AG78","identifierLink":"https://www.uniprot.org/uniprotkb/P0AG78/entry","name":"sbp","description":"Sulfate-binding protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30368","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21459122","identifier":"P16701","identifierLink":"https://www.uniprot.org/uniprotkb/P16701/entry","name":"cysU","description":"Sulfate transport system permease protein CysT","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30406","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-552215","identifier":"P0AEB0","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEB0/entry","name":"cysW","description":"Sulfate transport system permease protein CysW","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30406","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-556404","identifier":"P16676","identifierLink":"https://www.uniprot.org/uniprotkb/P16676/entry","name":"cysA","description":"Sulfate/thiosulfate import ATP-binding protein CysA","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43514","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4387","complexName":"Thiamine ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity thiamine transporter. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily. Thiamine is required for the synthesis of thiamine pyrophosphate (TPP), a required cofactor in  central  metabolism as an  electron  carrier  and nucleophile for such enzymes as pyruvate dehydrogenase (CPX-3943) and acetolactate  synthase  (CPX-3575). The operon is transcriptionally repressed in the presence of excess thiamine.","predictedComplex":false,"interactors":[{"ac":"EBI-1113491","identifier":"P31548","identifierLink":"https://www.uniprot.org/uniprotkb/P31548/entry","name":"thiQ","description":"Thiamine import ATP-binding protein ThiQ","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42781","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1113509","identifier":"P31550","identifierLink":"https://www.uniprot.org/uniprotkb/P31550/entry","name":"thiB","description":"Thiamine-binding periplasmic protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30006","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9147676","identifier":"P31549","identifierLink":"https://www.uniprot.org/uniprotkb/P31549/entry","name":"thiP","description":"Thiamine transport system permease protein ThiP","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30183","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4388","complexName":"Xylose ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity D-xylose transporter. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily. May also transport D-ribose.","predictedComplex":false,"interactors":[{"ac":"EBI-1129513","identifier":"P37387","identifierLink":"https://www.uniprot.org/uniprotkb/P37387/entry","name":"xylF","description":"D-xylose-binding periplasmic protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1133100","identifier":"P37388","identifierLink":"https://www.uniprot.org/uniprotkb/P37388/entry","name":"xylG","description":"Xylose import ATP-binding protein XylG","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43790","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9142961","identifier":"P0AGI4","identifierLink":"https://www.uniprot.org/uniprotkb/P0AGI4/entry","name":"xylH","description":"Xylose transport system permease protein XylH","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32196","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4389","complexName":"YcjNOP ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"Putative sugar transporter. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-21459692","identifier":"P0AFR7","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFR7/entry","name":"ycjO","description":"Inner membrane ABC transporter permease protein YcjO","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30193","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21459707","identifier":"P77716","identifierLink":"https://www.uniprot.org/uniprotkb/P77716/entry","name":"ycjP","description":"Inner membrane ABC transporter permease protein YcjP","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32243","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21464064","identifier":"P77481","identifierLink":"https://www.uniprot.org/uniprotkb/P77481/entry","name":"ycjV","description":"Putative uncharacterized ABC transporter ATP-binding protein YcjV","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-560007","identifier":"P76042","identifierLink":"https://www.uniprot.org/uniprotkb/P76042/entry","name":"ycjN","description":"Putative ABC transporter periplasmic-binding protein YcjN","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43649","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4402","complexName":"mTORC2 complex","organismName":"Homo sapiens; 9606","description":"Serine/threonine protein kinase complex that regulates cellular processes including cell growth, survival and organization of the cytoskeleton in response to hormones and growth factors by way of, directly or indirectly, affecting the phosphorylation of several substrate proteins.\r\n\r\nWhile rapamycin acutely and directly inhibits mTORC1 (CPX-503), only chronic administration of rapamycin can inhibit mTORC2 in some, but not all, cell lines or tissues. \r\n\r\nThere is also emerging evidence for a role for mTORC2 in cancer.","predictedComplex":false,"interactors":[{"ac":"EBI-1387196","identifier":"Q6R327","identifierLink":"https://www.uniprot.org/uniprotkb/Q6R327/entry","name":"RICTOR","description":"Rapamycin-insensitive companion of mTOR","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13298","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1387467","identifier":"P85299","identifierLink":"https://www.uniprot.org/uniprotkb/P85299/entry","name":"PRR5","description":"Proline-rich protein 5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32428","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1387471","identifier":"Q9BVC4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BVC4/entry","name":"MLST8","description":"Target of rapamycin complex subunit LST8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359260","identifier":"P42345","identifierLink":"https://www.uniprot.org/uniprotkb/P42345/entry","name":"MTOR","description":"Serine/threonine-protein kinase mTOR","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749938","identifier":"Q9BPZ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BPZ7/entry","name":"MAPKAP1","description":"Target of rapamycin complex 2 subunit MAPKAP1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13335","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4403","complexName":"Ferric-citrate ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity ferric citrate transporter which imports ferric citrate transported across the outer membrane by the ferric-citrate outer membrane transporter complex  (CPX-3576). Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1132949","identifier":"P15031","identifierLink":"https://www.uniprot.org/uniprotkb/P15031/entry","name":"fecE","description":"Fe(3+) dicitrate transport ATP-binding protein FecE","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42771","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21464100","identifier":"P15029","identifierLink":"https://www.uniprot.org/uniprotkb/P15029/entry","name":"fecD","description":"Fe(3+) dicitrate transport system permease protein FecD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30472","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21464115","identifier":"P15030","identifierLink":"https://www.uniprot.org/uniprotkb/P15030/entry","name":"fecC","description":"Fe(3+) dicitrate transport system permease protein FecC","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30472","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549614","identifier":"P15028","identifierLink":"https://www.uniprot.org/uniprotkb/P15028/entry","name":"fecB","description":"Fe(3+) dicitrate-binding periplasmic protein FecB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]}]},{"complexAC":"CPX-4404","complexName":"Ferric-enterobactin ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity ferric-enterobactin transporter. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily. Transports Fe3+ complexed to the catecholate ferric enterobactin across the inner membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-1118908","identifier":"P23878","identifierLink":"https://www.uniprot.org/uniprotkb/P23878/entry","name":"fepC","description":"Ferric enterobactin transport ATP-binding protein FepC","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42771","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21464297","identifier":"P23876","identifierLink":"https://www.uniprot.org/uniprotkb/P23876/entry","name":"fepD","description":"Ferric enterobactin transport system permease protein FepD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30472","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21464313","identifier":"P23877","identifierLink":"https://www.uniprot.org/uniprotkb/P23877/entry","name":"fepG","description":"Ferric enterobactin transport system permease protein FepG","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30472","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-554525","identifier":"P0AEL6","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEL6/entry","name":"fepB","description":"Ferric enterobactin-binding periplasmic protein FepB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30532","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4406","complexName":"L-cystine ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity L-cystine and L-cysteine transporter, will also import  DL-2,6-diaminopimelic acid and L-cystathionine. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1123268","identifier":"P0AFT2","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFT2/entry","name":"tcyL","description":"L-cystine transport system permease protein TcyL","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30614","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-550368","identifier":"P0AEM9","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEM9/entry","name":"tcyJ","description":"L-cystine-binding protein TcyJ","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR35936","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-552920","identifier":"P37774","identifierLink":"https://www.uniprot.org/uniprotkb/P37774/entry","name":"tcyN","description":"L-cystine transport system ATP-binding protein TcyN","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43166","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4407","complexName":"Zinc ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity zinc transporter. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily. The expression of znuABC is repressed by the zinc uptake regulator, Zur, which acts as a dimer, containing four zinc ions in its active repressor form, when it competes with RNA polymerase for  znuABC promoter occupancy.","predictedComplex":false,"interactors":[{"ac":"EBI-21464562","identifier":"P39172","identifierLink":"https://www.uniprot.org/uniprotkb/P39172/entry","name":"znuA","description":"High-affinity zinc uptake system protein ZnuA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21464586","identifier":"P39832","identifierLink":"https://www.uniprot.org/uniprotkb/P39832/entry","name":"znuB","description":"High-affinity zinc uptake system membrane protein ZnuB","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30477","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-562252","identifier":"P0A9X1","identifierLink":"https://www.uniprot.org/uniprotkb/P0A9X1/entry","name":"znuC","description":"Zinc import ATP-binding protein ZnuC","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42734","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4422","complexName":"Putative peptide ABC transporter","organismName":"Escherichia coli (strain K12); 83333","description":"ATP-binding cassette (ABC) transporter of unknown ligand specificity from the subgroup of peptide-uptake transporters. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-21465228","identifier":"P0AGH3","identifierLink":"https://www.uniprot.org/uniprotkb/P0AGH3/entry","name":"sapB","description":"Putrescine export system permease protein SapB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43163","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-547032","identifier":"P0AGH5","identifierLink":"https://www.uniprot.org/uniprotkb/P0AGH5/entry","name":"sapC","description":"Putrescine export system permease protein SapC","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43386","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549564","identifier":"Q47622","identifierLink":"https://www.uniprot.org/uniprotkb/Q47622/entry","name":"sapA","description":"Probable ABC transporter periplasmic-binding protein SapA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30290","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-558281","identifier":"P0AAH4","identifierLink":"https://www.uniprot.org/uniprotkb/P0AAH4/entry","name":"sapD","description":"Putrescine export system ATP-binding protein SapD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43297","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-558765","identifier":"P0AAH8","identifierLink":"https://www.uniprot.org/uniprotkb/P0AAH8/entry","name":"sapF","description":"Putrescine export system ATP-binding protein SapF","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43776","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4423","complexName":"Matrilin-1 complex","organismName":"Homo sapiens; 9606","description":"A cartilage extracellular matrix complex that mediates interactions between major components of the extracellular matrix such as collagens and proteoglycans and contributes to their fibrillar network.","predictedComplex":false,"interactors":[{"ac":"EBI-20828128","identifier":"P21941","identifierLink":"https://www.uniprot.org/uniprotkb/P21941/entry","name":"MATN1","description":"Matrilin-1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4424","complexName":"Reelin complex","organismName":"Homo sapiens; 9606","description":"Extracellular matrix, multifunctional signal glycoprotein complex that is secreted by Cajal-Retzius cells in marginal regions of the cerebral cortex and the hippocampus in the embryonic brain and by GABAergic interneurons in the adult brain. \r\n\r\nBinds to a variety of membrane receptors, such as the extracellular domains of lipoprotein receptors VLDLR (P98155) and LRP8 (APOER2, Q14114), both in a calcium-dependent manner, to Cadherin-related neuronal receptors (CNRs) or to alpha3beta1 integrin (CPX-1797). Receptor binding induces phosphorylation cascades, usually initiated by the phosphorylation of intracellular receptor adaptor protein DAB1 (O75553) or kinase LIMK1 (P53667). Also modulates phosphorylation of TAU (P10636). Eventually, Reelin induces receptor clustering, particularly of VLDLR, and internalization of a Reelin-receptor complex results in Reelin degradation. \r\n\r\nReeling-induced signaling affects the dynamics of the actin and microtubular cytoskeleton as well as membrane trafficking through the regulation of the activity of small GTPases. It affects polarization, differentiation, neuronal migration and layer formation in the cerebral cortex, the hippocampus or the cerebellum of the embryonic brain as well as migration of sympathetic preganglionic neurons in the spinal cord, where it seems to act as a barrier to neuronal migration. Also affects neuron growth, maturation, and synaptic activity in the postnatal and adult brain. \r\n\r\nAbnormal Reelin expression in the brain can cause a range of neurologically-abnormal symptoms, including tremors, ataxia, lissencephaly, cerebellar hypoplasia and malformation of cellular layers throughout the brain and it is implicated in a number of neuropsychiatric disorders including autism, schizophrenia, bipolar disorder, depression and Alzheimer's disease.","predictedComplex":false,"interactors":[{"ac":"EBI-21325699","identifier":"P78509","identifierLink":"https://www.uniprot.org/uniprotkb/P78509/entry","name":"RELN","description":"Reelin","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11841","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4425","complexName":"BRCA1-A complex","organismName":"Homo sapiens; 9606","description":"Deubiquitinase complex that predominantly binds polyubiquitin chains and specifically recognizes Lys-63-linked ubiquitinated histones H2A and H2AX (P16104) at DNA lesions sites, and targets the BRCA1-BARD1 heterodimer (CPX-715) to sites of DNA damage at double-strand breaks (DSBs). \r\n\r\nCritical for G2-M checkpoint control in response to ionising radiation, to ensure that entry into mitosis is transiently inhibited to avoid aberrant chromosome segregation. \r\n\r\nBRCA1-A complex may play an important role in breast and ovarian cancers.","predictedComplex":false,"interactors":[{"ac":"EBI-12519282","identifier":"CPX-715","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-715","name":"BRCA1-BARD1 complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-1263451","identifier":"Q6UWZ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q6UWZ7/entry","name":"ABRAXAS1","description":"BRCA1-A complex subunit Abraxas 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31728","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-725300","identifier":"Q96RL1","identifierLink":"https://www.uniprot.org/uniprotkb/Q96RL1/entry","name":"UIMC1","description":"BRCA1-A complex subunit RAP80","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-745725","identifier":"Q9NWV8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NWV8/entry","name":"BABAM1","description":"BRISC and BRCA1-A complex member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15660","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-750352","identifier":"P46736","identifierLink":"https://www.uniprot.org/uniprotkb/P46736/entry","name":"BRCC3","description":"Lys-63-specific deubiquitinase BRCC36","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10410","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-949389","identifier":"Q9NXR7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NXR7/entry","name":"BABAM2","description":"BRISC and BRCA1-A complex member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15189","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-4426","complexName":"BRCA1-B complex","organismName":"Homo sapiens; 9606","description":"DNA helicase complex that binds and unwids DNA in a 5-prime to 3-prime direction during S phase at DNA damage sites. \r\n\r\nBRCA1-B complex is required for replication stress induced checkpoint control and DNA repair through homologous recombination (HR). \r\n\r\nMutations in binding regions of BRCA1 and BRIP1 proteins are associated with Fanconi anemia and familial breast cancer.","predictedComplex":false,"interactors":[{"ac":"EBI-12519282","identifier":"CPX-715","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-715","name":"BRCA1-BARD1 complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-308302","identifier":"Q92547","identifierLink":"https://www.uniprot.org/uniprotkb/Q92547/entry","name":"TOPBP1","description":"DNA topoisomerase 2-binding protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13561","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3509650","identifier":"Q9BX63","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BX63/entry","name":"BRIP1","description":"Fanconi anemia group J protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11472","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4441","complexName":"BRCA1-C complex","organismName":"Homo sapiens; 9606","description":"Endo- and Exonuclease complex that plays a central role in double-stranded break repair (DSB), DNA recombination, maintenance of telomere integrity and meiosis. It possesses single-strand endonuclease activity and double-strand-specific 3-prime-5-prime exonuclease activity, which are provided by MRN.\r\n \r\nThe complex formation of BRCA1-CtIP-MRN is important for facilitating DSB resection to generate single-stranded DNA that is needed for homologous recombination-mediated DSB repair, a process that also involves EXO1 (Q9UQ84) and DNA2 (P51530). \r\n\r\nIt is required for tolerance to etoposide during DNA replication, for DNA topoisomerase 2-DNA adduct removal, and for subsequent processing of DNA ends to generate a 3-prime ssDNA. \r\n\r\nIt is critical for G2-M checkpoint control in response to ionising radiation, to ensure that entry into mitosis is transiently inhibited to avoid aberrant chromosome segregation. \r\n\r\nBRCA1-C complex is also important for restart of stalled replication forks.","predictedComplex":false,"interactors":[{"ac":"EBI-12519282","identifier":"CPX-715","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-715","name":"BRCA1-BARD1 complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-21497713","identifier":"CPX-4442","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-4442","name":"MRN double-strand break repair complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-745715","identifier":"Q99708","identifierLink":"https://www.uniprot.org/uniprotkb/Q99708/entry","name":"RBBP8","description":"DNA endonuclease RBBP8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15107","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4442","complexName":"MRN double-strand break repair complex","organismName":"Homo sapiens; 9606","description":"Endo- and exonuclease complex that plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. It possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11.The complex may also be required for DNA damage signaling via activation of the ATM kinase (Q13315). In telomeres the MRN complex may modulate t-loop formation.\r\n\r\nMRN complex is part of the BRCA1-C complex (CPX-4441).\r\n\r\nMRE11, RAD50 and NBS1 are known tumor suppressors. Loss of function of any of these proteins results in genome instability. Defective MRN function has been linked to many types of cancer. Hypomorphic mutations in any of the human genes for MRN result in cancer predisposing genome-instability syndromes: mutations in the MRE11 and NBS1 genes cause ataxia telangiectasia-like disorder (ATLD) and Nijmegen breakage syndrome (NBS), respectively.","predictedComplex":false,"interactors":[{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-396513","identifier":"P49959","identifierLink":"https://www.uniprot.org/uniprotkb/P49959/entry","name":"MRE11","description":"Double-strand break repair protein MRE11","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-494844","identifier":"O60934","identifierLink":"https://www.uniprot.org/uniprotkb/O60934/entry","name":"NBN","description":"Nibrin","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12162","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-495494","identifier":"Q92878","identifierLink":"https://www.uniprot.org/uniprotkb/Q92878/entry","name":"RAD50","description":"DNA repair protein RAD50","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18867","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-4443","complexName":"Sodium/lithium ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"ABC transporter complex implicated in multi-drug resistance, exhibiting dual functionality as a drug efflux pump, binding tetracyclines, and a Na+ (Li+)/H+ antiporter. Member of the ATP-binding cassette (ABC) superfamily of transporters, eukaryote-type (EK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1122023","identifier":"P0AFQ2","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFQ2/entry","name":"ybhS","description":"Probable multidrug ABC transporter permease YbhS","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15772862","identifier":"P0AFP9","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFP9/entry","name":"ybhR","description":"Probable multidrug ABC transporter permease YbhR","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-547696","identifier":"P0A9U1","identifierLink":"https://www.uniprot.org/uniprotkb/P0A9U1/entry","name":"ybhF","description":"Probable multidrug ABC transporter ATP-binding protein YbhF","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43038","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4446","complexName":"YdcSTUV ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"Putative putreceine transporter, may also act as the channel for double-stranded DNA uptake during natural transformation. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1116705","identifier":"P76108","identifierLink":"https://www.uniprot.org/uniprotkb/P76108/entry","name":"ydcS","description":"Bifunctional polyhydroxybutyrate synthase / ABC transporter periplasmic binding protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21498007","identifier":"P77795","identifierLink":"https://www.uniprot.org/uniprotkb/P77795/entry","name":"ydcT","description":"Uncharacterized ABC transporter ATP-binding protein YdcT","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42781","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21498025","identifier":"P77156","identifierLink":"https://www.uniprot.org/uniprotkb/P77156/entry","name":"ydcU","description":"Inner membrane ABC transporter permease protein YdcU","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42929","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21498038","identifier":"P0AFR9","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFR9/entry","name":"ydcV","description":"Inner membrane ABC transporter permease protein YdcV","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43357","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4449","complexName":"Low affinity betaine ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"Low-affinity betaine transporter. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1127677","identifier":"P33362","identifierLink":"https://www.uniprot.org/uniprotkb/P33362/entry","name":"yehZ","description":"Glycine betaine-binding protein YehZ","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-21498643","identifier":"P33359","identifierLink":"https://www.uniprot.org/uniprotkb/P33359/entry","name":"yehW","description":"Glycine betaine uptake system permease protein YehW","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-545876","identifier":"P33361","identifierLink":"https://www.uniprot.org/uniprotkb/P33361/entry","name":"yehY","description":"Glycine betaine uptake system permease protein YehY","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-555983","identifier":"P33360","identifierLink":"https://www.uniprot.org/uniprotkb/P33360/entry","name":"yehX","description":"Glycine betaine uptake system ATP-binding protein YehX","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4450","complexName":"Putative amino acid ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"Transporter complex, predicted to import polar amino acids. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1127595","identifier":"P45769","identifierLink":"https://www.uniprot.org/uniprotkb/P45769/entry","name":"yhdZ","description":"Uncharacterized amino-acid ABC transporter ATP-binding protein YhdZ","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43166","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21649383","identifier":"P45767","identifierLink":"https://www.uniprot.org/uniprotkb/P45767/entry","name":"yhdX","description":"Putative amino-acid ABC transporter permease protein YhdX","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30614","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-542412","identifier":"P45768","identifierLink":"https://www.uniprot.org/uniprotkb/P45768/entry","name":"yhdY","description":"Inner membrane amino-acid ABC transporter permease protein YhdY","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30614","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8768629","identifier":"P45766","identifierLink":"https://www.uniprot.org/uniprotkb/P45766/entry","name":"yhdW","description":"Putative amino-acid ABC transporter-binding protein YhdW","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30085","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4461","complexName":"Prolow-density lipoprotein receptor-related protein 1 complex","organismName":"Mus musculus; 10090","description":"Endocytic, low-densitiy lipoprotein receptor involved in two major processes, as scavenger receptor in the internalisation of extracellular molecules and their clearance via the endosome and as transducer of multiple intracellular signal pathways. Often acts in corporation with other cell-surface receptors. Lrp-1 is recycled to the plasma membrane. Involved in cholesterol import and clearance of a range of toxins. Ligands range from matrix metalloproteinases (MMP) and urokinase-type plasminogen activator (uPA-uPAR, CPX-510) or tissue-type plasminogen activator (Plat/tPA, P11214), bound directly to Lrp-1 or in complex with their target inhibitor, e.g. plasminogen activator inhibitor type 1 (Serpine1/PAI-1, CPX-495 and CPX-518), to amyloid-beta peptides. \r\n\r\nInstead of being internalised, Lrp-1 ligands may also shed the extracellular domains of the alpha and beta chains resulting in an extracellular, soluble LRP-1 (sLRP-1) decoy receptor.","predictedComplex":false,"interactors":[{"ac":"EBI-21915681","identifier":"Q91ZX7-PRO_0000302753","identifierLink":"https://www.uniprot.org/uniprotkb/Q91ZX7-PRO_0000302753/entry","name":"Lrp1","description":"Low-density lipoprotein receptor-related protein 1 515 kDa subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-21915690","identifier":"Q91ZX7-PRO_0000302754","identifierLink":"https://www.uniprot.org/uniprotkb/Q91ZX7-PRO_0000302754/entry","name":"Lrp1","description":"Low-density lipoprotein receptor-related protein 1 85 kDa subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-4462","complexName":"Prolow-density lipoprotein receptor-related protein 1 complex","organismName":"Rattus norvegicus; 10116","description":"Endocytic, low-densitiy lipoprotein receptor involved in two major processes, as scavenger receptor in the internalisation of extracellular molecules and their clearance via the endosome and as transducer of multiple intracellular signal pathways. Often acts in corporation with other cell-surface receptors. Lrp-1 is recycled to the plasma membrane. Involved in cholesterol import and clearance of a range of toxins. Ligands range from matrix metalloproteinases (MMP) and urokinase-type plasminogen activator (uPA-uPAR, P29598 and P49616) or tissue-type plasminogen activator (Plat/tPA, P19637), bound directly to Lrp-1 or in complex with their target inhibitor, e.g. plasminogen activator inhibitor type 1 (Serpine1/PAI-1, P20961), to amyloid-beta peptides. \r\n\r\nInstead of being internalised, Lrp-1 ligands may also shed the extracellular domains of the alpha and beta chains resulting in an extracellular, soluble LRP-1 (sLRP-1) decoy receptor.","predictedComplex":false,"interactors":[{"ac":"EBI-1571324","identifier":"G3V928","identifierLink":"https://www.uniprot.org/uniprotkb/G3V928/entry","name":"Lrp1","description":"Prolow-density lipoprotein receptor-related protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR24270","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4463","complexName":"Matrilin-1 complex","organismName":"Mus musculus; 10090","description":"A cartilage extracellular matrix complex that mediates interactions between major components of the extracellular matrix such as collagens and proteoglycans and contributes to their fibrillar network.","predictedComplex":false,"interactors":[{"ac":"EBI-310060","identifier":"P51942","identifierLink":"https://www.uniprot.org/uniprotkb/P51942/entry","name":"Matn1","description":"Matrilin-1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4464","complexName":"Matrilin-2 complex","organismName":"Homo sapiens; 9606","description":"A extracellular matrix complex that mediates interactions between major components of the extracellular matrix and contributes to their fibrillar network. Compared to cartilage-specific Matrilin-1 and -3, Matrilin-2 and -4 have a broad tissue distribution.","predictedComplex":false,"interactors":[{"ac":"EBI-949020","identifier":"O00339","identifierLink":"https://www.uniprot.org/uniprotkb/O00339/entry","name":"MATN2","description":"Matrilin-2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4465","complexName":"YnjBCD ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"ATP-binding cassette (ABC) transporter of unknown ligand specificity. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-15775374","identifier":"P76223","identifierLink":"https://www.uniprot.org/uniprotkb/P76223/entry","name":"ynjB","description":"Protein YnjB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21916149","identifier":"P76224","identifierLink":"https://www.uniprot.org/uniprotkb/P76224/entry","name":"ynjC","description":"Inner membrane ABC transporter permease protein YnjC","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30183","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21916163","identifier":"P76909","identifierLink":"https://www.uniprot.org/uniprotkb/P76909/entry","name":"ynjD","description":"Uncharacterized ABC transporter ATP-binding protein YnjD","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42781","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4467","complexName":"Matrilin-2 complex","organismName":"Mus musculus; 10090","description":"A extracellular matrix complex that mediates interactions between major components of the extracellular matrix and contributes to their fibrillar network. Compared to cartilage-specific Matrilin-1 and -3, Matrilin-2 and -4 have a broad tissue distribution.","predictedComplex":false,"interactors":[{"ac":"EBI-642537","identifier":"O08746","identifierLink":"https://www.uniprot.org/uniprotkb/O08746/entry","name":"Matn2","description":"Matrilin-2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4468","complexName":"YphDEF ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"ATP-binding cassette (ABC) transporter of unknown ligand specificity. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1117501","identifier":"P77269","identifierLink":"https://www.uniprot.org/uniprotkb/P77269/entry","name":"yphF","description":"ABC transporter periplasmic-binding protein YphF","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1129412","identifier":"P77509","identifierLink":"https://www.uniprot.org/uniprotkb/P77509/entry","name":"yphE","description":"Uncharacterized ABC transporter ATP-binding protein YphE","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43790","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21916251","identifier":"P77315","identifierLink":"https://www.uniprot.org/uniprotkb/P77315/entry","name":"yphD","description":"Probable ABC transporter permease protein YphD","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32196","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4469","complexName":"Matrilin-3 complex","organismName":"Homo sapiens; 9606","description":"A skeletal extracellular matrix complex that mediates interactions between major components of the extracellular matrix such as collagens and proteoglycans and contributes to their fibrillar network. \r\n\r\nAssociated with a range of bone and cartilage malformation diseases, such as osteoarthritis.","predictedComplex":false,"interactors":[{"ac":"EBI-6262458","identifier":"O15232","identifierLink":"https://www.uniprot.org/uniprotkb/O15232/entry","name":"MATN3","description":"Matrilin-3","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4471","complexName":"Sulfate adenylyltransferase complex","organismName":"Escherichia coli (strain K12); 83333","description":"An sulfate adenylyltransferase complex that activates sulfate through adenylation to form adenosine 5-phosphosulfate (APS, CHEBI:58243). Catalyzes and couples the Gibbs potentials of GTP hydrolysis to the synthesis of APS. This is the first step in the sulfate assimilation pathway required for the biosynthesis of sulfur-containing amino acids and cofactors, and sulfated metabolites.","predictedComplex":false,"interactors":[{"ac":"EBI-1130200","identifier":"P21156","identifierLink":"https://www.uniprot.org/uniprotkb/P21156/entry","name":"cysD","description":"Sulfate adenylyltransferase subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43196","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-559728","identifier":"P23845","identifierLink":"https://www.uniprot.org/uniprotkb/P23845/entry","name":"cysN","description":"Sulfate adenylyltransferase subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR23115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4472","complexName":"mTORC2 complex","organismName":"Mus musculus; 10090","description":"Serine/threonine protein kinase complex that regulates cellular processes including cell growth, survival and organization of the cytoskeleton in response to hormones and growth factors by way of, directly or indirectly, affecting the phosphorylation of several substrate proteins.\r\n\r\nWhile rapamycin acutely and directly inhibits mTORC1 (CPX-4473), only chronic administration of rapamycin can inhibit mTORC2 in some, but not all, cell lines or tissues.","predictedComplex":false,"interactors":[{"ac":"EBI-1571628","identifier":"Q9JLN9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JLN9/entry","name":"Mtor","description":"Serine/threonine-protein kinase mTOR","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1790802","identifier":"Q9DCJ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DCJ1/entry","name":"Mlst8","description":"Target of rapamycin complex subunit LST8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR19842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21917322","identifier":"Q812A5","identifierLink":"https://www.uniprot.org/uniprotkb/Q812A5/entry","name":"Prr5","description":"Proline-rich protein 5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR32428","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4286572","identifier":"Q6QI06","identifierLink":"https://www.uniprot.org/uniprotkb/Q6QI06/entry","name":"Rictor","description":"Rapamycin-insensitive companion of mTOR","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13298","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7978758","identifier":"Q8BKH7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BKH7/entry","name":"Mapkap1","description":"Target of rapamycin complex 2 subunit MAPKAP1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13335","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4473","complexName":"mTORC1 complex","organismName":"Mus musculus; 10090","description":"Serine/threonine protein kinase complex that regulates cellular metabolism, growth and survival in response to hormones, growth factors, nutrients, energy and stress signals by way of, directly or indirectly, affecting the phosphorylation of at least 800 proteins. Key pathways regulated by mTORC1 include: protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis; pyrimidine biosynthesis pathway; ribosome synthesis by activating RNA polymerase III-dependent transcription; lipid synthesis; mitochondrial biogenesis to maintain energy homeostasis; negative regulation of autophagy; feedback control on upstream growth factor signaling; regulation of microtubules. Inactivated by Rapamycin, stress and starvation, which, consequently, induces autophagy and ensures that cells grow only during favourable conditions. mTORC1 plays a role in cancer and obesity. Subcellular localization varies and may ensure precise spatial and temporal control of cell growth.","predictedComplex":false,"interactors":[{"ac":"EBI-1571628","identifier":"Q9JLN9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JLN9/entry","name":"Mtor","description":"Serine/threonine-protein kinase mTOR","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1790802","identifier":"Q9DCJ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DCJ1/entry","name":"Mlst8","description":"Target of rapamycin complex subunit LST8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR19842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4567273","identifier":"Q8K4Q0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K4Q0/entry","name":"Rptor","description":"Regulatory-associated protein of mTOR","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12848","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4474","complexName":"Nuclear pore complex","organismName":"Mus musculus; 10090","description":"The nuclear pore complex (NPC) is a large assembly embedded in the nuclear envelope of eukaryotic cells. The NPC exclusively mediates all transport between cytoplasm and nucleus. A single NPC in a human cell can transport up to 80 MDa of material within 1 second. 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10090","xrefs":[{"identifier":"PTHR23138","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8338913","identifier":"Q8R4R6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R4R6/entry","name":"Nup35","description":"Nucleoporin NUP35","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8339734","identifier":"Q8BTS4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BTS4/entry","name":"Nup54","description":"Nuclear pore complex protein Nup54","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13000","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8341160","identifier":"Q63850","identifierLink":"https://www.uniprot.org/uniprotkb/Q63850/entry","name":"Nup62","description":"Nuclear pore glycoprotein p62","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12084","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8372895","identifier":"Q8R0G9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R0G9/entry","name":"Nup133","description":"Nuclear pore complex protein Nup133","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13405","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8372944","identifier":"Q8CJF7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CJF7/entry","name":"Ahctf1","description":"Protein ELYS","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21583","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8458495","identifier":"Q8R322","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R322/entry","name":"Gle1","description":"mRNA export factor GLE1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8458895","identifier":"Q8K3Z9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K3Z9/entry","name":"Pom121","description":"Nuclear envelope pore membrane protein POM 121","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23193","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8460031","identifier":"P59235","identifierLink":"https://www.uniprot.org/uniprotkb/P59235/entry","name":"Nup43","description":"Nucleoporin Nup43","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22652","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8572338","identifier":"Q6ZQG1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6ZQG1/entry","name":"Nup205","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 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Activation of the MCM complex at origins by cyclin-dependent kinases and the cdc-7 protein kinase (O01493) leads to initiation of DNA synthesis. MCM2-7 complexes unwind the double stranded DNA at the origins, recruit DNA polymerases and initiate DNA synthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-2001978","identifier":"O16297","identifierLink":"https://www.uniprot.org/uniprotkb/O16297/entry","name":"mcm-7","description":"DNA replication licensing factor MCM7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2006682","identifier":"Q95XQ8","identifierLink":"https://www.uniprot.org/uniprotkb/Q95XQ8/entry","name":"mcm-4","description":"DNA replication licensing factor mcm-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2006759","identifier":"P34647","identifierLink":"https://www.uniprot.org/uniprotkb/P34647/entry","name":"mcm-6","description":"DNA replication licensing factor mcm-6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21923194","identifier":"Q21902","identifierLink":"https://www.uniprot.org/uniprotkb/Q21902/entry","name":"mcm-5","description":"DNA replication licensing factor mcm-5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-318007","identifier":"Q9XVR7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XVR7/entry","name":"mcm-3","description":"DNA replication licensing factor MCM3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-323002","identifier":"Q9XXI9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XXI9/entry","name":"mcm-2","description":"DNA replication licensing factor MCM2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4501","complexName":"Matrilin-3 complex","organismName":"Mus musculus; 10090","description":"A skeletal extracellular matrix complex that mediates interactions between major components of the extracellular matrix such as collagens and proteoglycans and contributes to their fibrillar network.","predictedComplex":false,"interactors":[{"ac":"EBI-21924161","identifier":"O35701","identifierLink":"https://www.uniprot.org/uniprotkb/O35701/entry","name":"Matn3","description":"Matrilin-3","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4502","complexName":"GINS complex","organismName":"Mus musculus; 10090","description":"Required for the initiation of replication and for replication fork progression, mediating interactions with replication factors. 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Also appears to interact with and stimulate the polymerase activities of DNA polymerase epsilon  complex (CPX-2109) and the DNA polymerase alpha:primase complex (CPX-2088).","predictedComplex":false,"interactors":[{"ac":"EBI-21924257","identifier":"Q9CZ15","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CZ15/entry","name":"Gins1","description":"DNA replication complex GINS protein PSF1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12914","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21924276","identifier":"Q9CY94","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CY94/entry","name":"Gins3","description":"DNA replication complex GINS protein PSF3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22768","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8585854","identifier":"Q9D600","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D600/entry","name":"Gins2","description":"DNA replication complex GINS protein PSF2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12772","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8587025","identifier":"Q99LZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q99LZ3/entry","name":"Gins4","description":"DNA replication complex GINS protein SLD5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21206","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4503","complexName":"Matrilin-1 - Matrilin-3 complex","organismName":"Homo sapiens; 9606","description":"A skeletal extracellular matrix complex that mediates interactions between major components of the extracellular matrix such as collagens and proteoglycans and contributes to their fibrillar network. Apparently restricted to epiphyseal growth and articular cartilage in foetal and neonatal tissues.","predictedComplex":false,"interactors":[{"ac":"EBI-20828128","identifier":"P21941","identifierLink":"https://www.uniprot.org/uniprotkb/P21941/entry","name":"MATN1","description":"Matrilin-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6262458","identifier":"O15232","identifierLink":"https://www.uniprot.org/uniprotkb/O15232/entry","name":"MATN3","description":"Matrilin-3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4504","complexName":"Matrilin-1 - Matrilin-3 complex","organismName":"Mus musculus; 10090","description":"A skeletal extracellular matrix complex that mediates interactions between major components of the extracellular matrix such as collagens and proteoglycans and contributes to their fibrillar network. Apparently restricted to epiphyseal growth and articular cartilage in foetal and neonatal tissues.","predictedComplex":false,"interactors":[{"ac":"EBI-21924161","identifier":"O35701","identifierLink":"https://www.uniprot.org/uniprotkb/O35701/entry","name":"Matn3","description":"Matrilin-3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-310060","identifier":"P51942","identifierLink":"https://www.uniprot.org/uniprotkb/P51942/entry","name":"Matn1","description":"Matrilin-1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4521","complexName":"Matrilin-1 complex","organismName":"Bos taurus; 9913","description":"A cartilage extracellular matrix complex that mediates interactions between major components of the extracellular matrix such as collagens and proteoglycans and contributes to their fibrillar network.","predictedComplex":false,"interactors":[{"ac":"EBI-5281273","identifier":"E1BMV3","identifierLink":"https://www.uniprot.org/uniprotkb/E1BMV3/entry","name":"MATN1","description":"Matrilin-1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4522","complexName":"Matrilin-3 complex","organismName":"Bos taurus; 9913","description":"A skeletal extracellular matrix complex that mediates interactions between major components of the extracellular matrix such as collagens and proteoglycans and contributes to their fibrillar network.","predictedComplex":false,"interactors":[{"ac":"EBI-5281261","identifier":"F1MD94","identifierLink":"https://www.uniprot.org/uniprotkb/F1MD94/entry","name":"MATN3","description":"Matrilin-3","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4523","complexName":"Matrilin-1 - Matrilin-3 complex","organismName":"Bos taurus; 9913","description":"A skeletal extracellular matrix complex that mediates interactions between major components of the extracellular matrix such as collagens and proteoglycans and contributes to their fibrillar network. Apparently restricted to epiphyseal growth and articular cartilage in foetal and neonatal tissues.","predictedComplex":false,"interactors":[{"ac":"EBI-5281261","identifier":"F1MD94","identifierLink":"https://www.uniprot.org/uniprotkb/F1MD94/entry","name":"MATN3","description":"Matrilin-3","stochiometry":null,"interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5281273","identifier":"E1BMV3","identifierLink":"https://www.uniprot.org/uniprotkb/E1BMV3/entry","name":"MATN1","description":"Matrilin-1","stochiometry":null,"interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4524","complexName":"Reelin complex","organismName":"Mus musculus; 10090","description":"Extracellular matrix, multifunctional signal glycoprotein complex that is secreted by Cajal-Retzius cells in marginal regions of the cerebral cortex and the hippocampus in the embryonic brain and by GABAergic interneurons in the adult brain. \r\n\r\nBinds to a variety of membrane receptors, such as the extracellular domains of lipoprotein receptors Vldlr (P98156) and Lrp8 (APOER2, Q924X6), both in a calcium-dependent manner, to Cadherin-related neuronal receptors (CNRs) or to alpha3beta1 integrin (CPX-3117). Receptor binding induces phosphorylation cascades, usually initiated by the phosphorylation of intracellular receptor adaptor protein DabB1 (P97318) or kinase Limk1 (P53668). Also modulates phosphorylation of Tau (P10637). Eventually, Reelin induces receptor clustering, particularly of VLDLR, and internalization of a Reelin-receptor complex results in Reelin degradation. \r\n\r\nReeling-induced signaling affects the dynamics of the actin and microtubular cytoskeleton as well as membrane trafficking through the regulation of the activity of small GTPases. It affects polarization, differentiation, neuronal migration and layer formation in the cerebral cortex, the hippocampus or the cerebellum of the embryonic brain as well as migration of sympathetic preganglionic neurons in the spinal cord, where it seems to act as a barrier to neuronal migration. Also affects neuron growth, maturation, and synaptic activity in the postnatal and adult brain.","predictedComplex":false,"interactors":[{"ac":"EBI-9248666","identifier":"Q60841","identifierLink":"https://www.uniprot.org/uniprotkb/Q60841/entry","name":"Reln","description":"Reelin","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11841","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4526","complexName":"CMG helicase complex","organismName":"Homo sapiens; 9606","description":"DNA helicase that unwinds or rearranges duplex DNA during replication, recombination and repair.\r\n\r\nSurrounds the leading strand during DNA replication and recruits the DNA polymerase epsilon complex (CPX-2108) for leading-strand synthesis. CDC45 adds the GINS complex (CPX-787) onto each MCM complex (CPX-2940) to form two active CMG helicases that surround each strand of parental DNA. CMG then translocates along single-strand DNA in the 3-prime to 5-prime direction for bidirectional replication.The complex unwinds duplex regions up to 500 bp.\r\n\r\nDefects in CMG complex appear to correlate with genome instability and cancer.","predictedComplex":false,"interactors":[{"ac":"EBI-12552729","identifier":"CPX-787","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-787","name":"GINS complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-374969","identifier":"O75419","identifierLink":"https://www.uniprot.org/uniprotkb/O75419/entry","name":"CDC45","description":"Cell division control protein 45 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10507","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-913604","identifier":"CPX-2940","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-2940","name":"MCM complex","description":"MCM2-7 heterohexamer","stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-4541","complexName":"CMG helicase complex","organismName":"Mus musculus; 10090","description":"DNA helicase that unwinds or rearranges duplex DNA during replication, recombination and repair.\r\n\r\nSurrounds the leading strand during DNA replication and recruits the DNA polymerase epsilon complex (CPX-2109) for leading-strand synthesis. CDC45 adds the GINS complex (CPX-4502) onto each MCM complex (CPX-2941) to form two active CMG helicases that surround each strand of parental DNA. CMG then translocates along single-strand DNA in the 3-prime to 5-prime direction for bidirectional replication.The complex unwinds duplex regions up to 500 bp.","predictedComplex":false,"interactors":[{"ac":"EBI-21924203","identifier":"CPX-4502","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-4502","name":"GINS complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-4286086","identifier":"Q9Z1X9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z1X9/entry","name":"Cdc45","description":"Cell division control protein 45 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10507","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-913651","identifier":"CPX-2941","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-2941","name":"MCM complex","description":"MCM2-7 heterohexamer","stochiometry":null,"interactorType":"stable complex","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-4562","complexName":"PPP1CA-PPP1R15A protein phosphatase 1 complex","organismName":"Homo sapiens; 9606","description":"A serine/threonine-protein phosphatase complex that dephosphorylates the translation initiation factor EIF2S1 (eIF-2A, P05198), thus reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress. The complex down-regulates the TGF-beta signaling pathway by promoting dephosphorylation of TGFB1 (P01137).","predictedComplex":false,"interactors":[{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-357253","identifier":"P62136","identifierLink":"https://www.uniprot.org/uniprotkb/P62136/entry","name":"PPP1CA","description":"Serine/threonine-protein phosphatase PP1-alpha catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11668","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714746","identifier":"O75807","identifierLink":"https://www.uniprot.org/uniprotkb/O75807/entry","name":"PPP1R15A","description":"Protein phosphatase 1 regulatory subunit 15A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16489","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1932","complexName":"Maltose ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity maltose transporter, binding maltooligosaccharides up to seven glucose units long. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1118919","identifier":"P02916","identifierLink":"https://www.uniprot.org/uniprotkb/P02916/entry","name":"malF","description":"Maltose/maltodextrin transport system permease protein MalF","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR47314","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-369910","identifier":"P0AEX9","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEX9/entry","name":"malE","description":"Maltose/maltodextrin-binding periplasmic protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30061","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-550803","identifier":"P68187","identifierLink":"https://www.uniprot.org/uniprotkb/P68187/entry","name":"malK","description":"Maltose/maltodextrin import ATP-binding protein MalK","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43875","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6400985","identifier":"P68183","identifierLink":"https://www.uniprot.org/uniprotkb/P68183/entry","name":"malG","description":"Maltose/maltodextrin transport system permease protein MalG","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32243","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2114","complexName":"Methionine ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity methionine transporter. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1114713","identifier":"P28635","identifierLink":"https://www.uniprot.org/uniprotkb/P28635/entry","name":"metQ","description":"D-methionine-binding lipoprotein MetQ","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30429","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-541886","identifier":"P30750","identifierLink":"https://www.uniprot.org/uniprotkb/P30750/entry","name":"metN","description":"Methionine import ATP-binding protein MetN","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43166","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8769561","identifier":"P31547","identifierLink":"https://www.uniprot.org/uniprotkb/P31547/entry","name":"metI","description":"D-methionine transport system permease protein MetI","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30450","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4601","complexName":"Glutathione/cysteine ABC exporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"Eukaryotic-type ATP-binding cassette transporter which exports low molecular weight thiols  (CHEBI:29917), glutathione (CHEBI:16856) and cysteine (CHEBI:15356) to the periplasm, thus playing  redox balancing role in the periplasm. Required for the correct assembly of cytochrome bd (CPX-268)-type quinol oxidases, haem ligation during the assembly of c-type cytochromes and the disulfide folding of periplasmic and secreted protein. Structural modelling has identified a potential haem-binding site on the periplasmic surface of the complex which may be important in redox sensing and tolerance to nitric oxide.","predictedComplex":false,"interactors":[{"ac":"EBI-1115859","identifier":"P23886","identifierLink":"https://www.uniprot.org/uniprotkb/P23886/entry","name":"cydC","description":"Glutathione/L-cysteine transport system ATP-binding/permease protein CydC","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR24222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1129376","identifier":"P29018","identifierLink":"https://www.uniprot.org/uniprotkb/P29018/entry","name":"cydD","description":"Glutathione/L-cysteine transport system ATP-binding/permease protein CydD","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR24221","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4602","complexName":"FtsEX ABC cell division complex","organismName":"Escherichia coli (strain K12); 83333","description":"Member of a small subclass of eukaryote-type (EK-type) ABC transporters that uses mechano-transmission to perform work in the periplasm rather than for transmembrane transport. Involved in the recruitment of proteins to the Z ring of the divisome by activating the membrane anchor protein ftsA (P0ABH0), thus ensuring the safe separation of daughter cells during division. Also participates in the activation and regulation of septal peptidoglycan (sPG) synthesis and is responsible for the activation of hydrolases which split sPG to form new cell poles by recruiting envC (P37690), the activator of the cell wall hydrolases amiA (P36548) and amiB (P26365), to the septum.","predictedComplex":false,"interactors":[{"ac":"EBI-1119111","identifier":"P0AC30","identifierLink":"https://www.uniprot.org/uniprotkb/P0AC30/entry","name":"ftsX","description":"Cell division protein FtsX","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR47755","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-550637","identifier":"P0A9R7","identifierLink":"https://www.uniprot.org/uniprotkb/P0A9R7/entry","name":"ftsE","description":"Cell division ATP-binding protein FtsE","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR24220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4621","complexName":"CCM complex","organismName":"Mus musculus; 10090","description":"Forms a signalling platform, responsible for maintaining integrity of endothelial permeability. Plays a key role in the integrity of the endothelial tubule networks at the initial stages of vasculogenesis. Appears to act primarily by inhibiting RhoA-associated kinase (ROCK) activation and thus regulating  Rhoa (Q9QUI0) signaling however distinct patterns of interacting proteins for each CCM protein has been observed.","predictedComplex":false,"interactors":[{"ac":"EBI-21986270","identifier":"Q8K2Y9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K2Y9/entry","name":"Ccm2","description":"Cerebral cavernous malformations protein 2 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21642","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21986299","identifier":"Q8VE70","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VE70/entry","name":"Pdcd10","description":"Programmed cell death protein 10","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13250","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21986340","identifier":"Q6S5J6","identifierLink":"https://www.uniprot.org/uniprotkb/Q6S5J6/entry","name":"Krit1","description":"Krev interaction trapped protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13283","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4622","complexName":"Signal recognition particle receptor complex","organismName":"Mus musculus; 10090","description":"Mediates the co-translational targeting of membrane and secretory proteins. The signal recognition particle (SRP) binds to 9-12 large hydrophobic residues that constitute the signal sequences of nascent proteins as they emerge from the exit tunnel of the ribosome. The resulting targeting complex, composed of the SRP and the ribosome-nascent chain complex, then docks with the Signal recognition particle receptor.  This interaction catalyzes the GTP-dependent transfer of the nascent chain from SRP to the protein translocation apparatus in the ER membrane. Following GTP hydrolysis, the complex dissociates.","predictedComplex":false,"interactors":[{"ac":"EBI-6908733","identifier":"P47758","identifierLink":"https://www.uniprot.org/uniprotkb/P47758/entry","name":"Srprb","description":"Signal recognition particle receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11485","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8381906","identifier":"Q9DBG7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DBG7/entry","name":"Srpra","description":"Signal recognition particle receptor subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR43134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-989053","identifier":"CHEBI:15996","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15996","name":"gtp","description":"guanosine triphosphate - GTP","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-4625","complexName":"ubc-13-uev-1 ubiquitin-conjugating enzyme E2 complex","organismName":"Caenorhabditis elegans; 6239","description":"Implicated in the non-proteolytic regulation of signaling pathways by contributing to the addition of lysine 63-linked ubiquitin chains to proteins. Transfers the thioester-bound donor ubiquitin from ubc-13 onto the uev-1 catalytically inactive E2 variant. The heterodimer then catalyzes the formation of multiubiquitin chains linked by isopeptide bonds between Lys-63 and the C-terminus of the next monomer in the chain. This type of polyubiquitination does not lead to protein degradation by the proteasome but instead mediates activation of target genes by activating intracellular signaling cascades.","predictedComplex":false,"interactors":[{"ac":"EBI-321456","identifier":"O45495","identifierLink":"https://www.uniprot.org/uniprotkb/O45495/entry","name":"uev-1","description":"Ubiquitin-conjugating enzyme E2 variant 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-321502","identifier":"Q95XX0","identifierLink":"https://www.uniprot.org/uniprotkb/Q95XX0/entry","name":"ubc-13","description":"Ubiquitin-conjugating enzyme E2 13","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4628","complexName":"daf-37-daf-38 complex","organismName":"Caenorhabditis elegans; 6239","description":"G-protein coupled receptor complex, which mediates cAMP inhibition in response to dauer-inducing pheromones such as the ascaroside (2R)-5-oxohexan-2-yl 3,6-dideoxy-α-L-arabino-hexopyranoside (CHEBI:78812). Plays a role in controlling dauer formation.","predictedComplex":false,"interactors":[{"ac":"EBI-21986801","identifier":"Q18321","identifierLink":"https://www.uniprot.org/uniprotkb/Q18321/entry","name":"daf-37","description":"G-protein coupled receptor daf-37","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR46641","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21986821","identifier":"Q9U320","identifierLink":"https://www.uniprot.org/uniprotkb/Q9U320/entry","name":"daf-38","description":"G-protein coupled receptor daf-38","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24230","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4629","complexName":"C3PO endoribonuclease complex","organismName":"Mus musculus; 10090","description":"Endoribonuclease complex which functions as the component 3 promoter of RISC (RNA-induced silencing complex). Cleaves the fragmented siRNA passenger strands and facilitates the activation of RNA-induced silencing complex (RISC), the effector complex of RNA interference (RNAi), and thus plays a role in post-transcriptional repression of gene expression through down-regulation of translation or induction of mRNA degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-2910751","identifier":"Q9QZE7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9QZE7/entry","name":"Tsnax","description":"Translin-associated protein X","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10741","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8311824","identifier":"Q62348","identifierLink":"https://www.uniprot.org/uniprotkb/Q62348/entry","name":"Tsn","description":"Translin","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10741","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-4641","complexName":"Matrilin-4 complex","organismName":"Homo sapiens; 9606","description":"A extracellular matrix complex that mediates interactions between major components of the extracellular matrix and contributes to their fibrillar network. Compared to cartilage-specific Matrilin-1 and -3, Matrilin-2 and -4 have a broad tissue distribution.","predictedComplex":false,"interactors":[{"ac":"EBI-3957150","identifier":"O95460","identifierLink":"https://www.uniprot.org/uniprotkb/O95460/entry","name":"MATN4","description":"Matrilin-4","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4661","complexName":"Matrilin-4 complex","organismName":"Mus musculus; 10090","description":"A extracellular matrix complex that mediates interactions between major components of the extracellular matrix and contributes to their fibrillar network. Compared to cartilage-specific Matrilin-1 and -3, Matrilin-2 and -4 have a broad tissue distribution.","predictedComplex":false,"interactors":[{"ac":"EBI-21990740","identifier":"O89029","identifierLink":"https://www.uniprot.org/uniprotkb/O89029/entry","name":"Matn4","description":"Matrilin-4","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4663","complexName":"Osteoprotegerin complex","organismName":"Homo sapiens; 9606","description":"A soluble decoy receptor for osteoclastogenic cytokine TNFSF11/RANKL (O14788). Binding of osteoprotegerin to cytokine TNFSF11 prevents the cytokine from binding its receptor TNFRSF11A/RANK (Q9Y6Q6) and thus inhibits osteoclastogenesis. Bone homeostasis seems to depend on the local ratio between cytokine and decoy receptor. Osteoprotegerin may also play a role in preventing arterial calcification. Plays some as yet to-be-defined role in mammary gland physiology and hormone-driven epithelial proliferation during pregnancy and may act as a protective factor in bone microenvironment by preventing breast cancer-induced bone loss and reducing intra-osseous tumour growth. \r\n\r\nAlso possible decoy receptor for pro-apoptotic cytokine TNFSF10/TRAIL (P50591) which competes with TNFSF11 and releases the inhibition of osteoclastogenesis. In vitro, binding affinity is 500x higher for TNFSF11 than TNFSF10. Binding of osteoprotegerin to TNFSF10 appears to contribute to tumour growth of breast cancer cells and progression at the primary tumour site.","predictedComplex":false,"interactors":[{"ac":"EBI-15481185","identifier":"O00300","identifierLink":"https://www.uniprot.org/uniprotkb/O00300/entry","name":"TNFRSF11B","description":"Tumor necrosis factor receptor superfamily member 11B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4681","complexName":"YiaMNO tripartite ATP-independent periplasmic transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"ATP-independant, proton-motive-force-driven transporter which utilises an extracytoplasmic solute receptor (ESR) protein to recognize and bind specific ligands with high affinity. The ligand which this transporter binds is unclear but yiaO has been shown to bind  2,3-diketo-L-gulonate (CHEBI:57441), a breakdown product of L-ascorbate (CHEBI:38290). Deletion of the yiaMNO genes resulted in delays in the transition from exponential growth to the stationary phase, decreased high-salt survival and a reduction in biofilm formation.","predictedComplex":false,"interactors":[{"ac":"EBI-21993009","identifier":"P37674","identifierLink":"https://www.uniprot.org/uniprotkb/P37674/entry","name":"yiaM","description":"2,3-diketo-L-gulonate TRAP transporter small permease protein YiaM","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR35011","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21993023","identifier":"P37675","identifierLink":"https://www.uniprot.org/uniprotkb/P37675/entry","name":"yiaN","description":"2,3-diketo-L-gulonate TRAP transporter large permease protein YiaN","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33362","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21993039","identifier":"P37676","identifierLink":"https://www.uniprot.org/uniprotkb/P37676/entry","name":"yiaO","description":"2,3-diketo-L-gulonate-binding periplasmic protein YiaO","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33376","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4683","complexName":"N,N'-diacetylchitobiose-specific enzyme II complex","organismName":"Escherichia coli (strain K12); 83333","description":"Involved in the transport of the chitin disaccharide N,N'-diacetylchitobiose (GlcNAc2) and N,N',N''-triacetyl chitotriose (GlcNAc3) across the cell membrane as part of the phosphoenolpyruvate:sugar phosphotransferase system (PTS).  A phosphoryl group is transferred from hpr (P0AA04) to chbA (IIA), from chbA to chbB (IIB) and finally from chbB onto the incoming sugar bound to membrane-embedded chbC (IIC).","predictedComplex":false,"interactors":[{"ac":"EBI-1121924","identifier":"P69791","identifierLink":"https://www.uniprot.org/uniprotkb/P69791/entry","name":"chbA","description":"PTS system N,N'-diacetylchitobiose-specific EIIA component","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34382","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1128186","identifier":"P69795","identifierLink":"https://www.uniprot.org/uniprotkb/P69795/entry","name":"chbB","description":"PTS system N,N'-diacetylchitobiose-specific EIIB component","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34581","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-878640","identifier":"P17334","identifierLink":"https://www.uniprot.org/uniprotkb/P17334/entry","name":"chbC","description":"PTS system N,N'-diacetylchitobiose-specific EIIC component","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33989","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4701","complexName":"BRCA1-BARD1 complex","organismName":"Mus musculus; 10090","description":"A ligase complex that catalyses monoubiquitylation of heterologous substrates (especially core nucleosome histones) and Lys-6-linked polyubiquitylation of itself and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Unusually, autopolyubiquitylation activates its ubiquitin ligase function >20-fold rather than marking the protein for degredation. Plays a central role in the control of the cell cycle in response to DNA damage. \r\n\r\nIs a subcomplex of at least three mutually exclusive complexes: BRCA1-A (CPX-4702), BRCA1-B (CPX-4721) and BRCA1-C (CPX-4722).","predictedComplex":false,"interactors":[{"ac":"EBI-1790207","identifier":"O70445","identifierLink":"https://www.uniprot.org/uniprotkb/O70445/entry","name":"Bard1","description":"BRCA1-associated RING domain protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24171","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6876136","identifier":"P48754","identifierLink":"https://www.uniprot.org/uniprotkb/P48754/entry","name":"Brca1","description":"Breast cancer type 1 susceptibility protein homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13763","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4702","complexName":"BRCA1-A complex","organismName":"Mus musculus; 10090","description":"Deubiquitinase complex that predominantly binds polyubiquitin chains and specifically recognizes Lys-63-linked ubiquitinated histones H2A and H2afx (P27661) at DNA lesions sites, and targets the BRCA1-BARD1 heterodimer (CPX-4701) to sites of DNA damage at double-strand breaks (DSBs). \r\n\r\nCritical for G2-M checkpoint control in response to ionising radiation, to ensure that entry into mitosis is transiently inhibited to avoid aberrant chromosome segregation.","predictedComplex":false,"interactors":[{"ac":"EBI-12735562","identifier":"Q8K3W0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K3W0/entry","name":"Babam2","description":"BRISC and BRCA1-A complex member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15189","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21994288","identifier":"CPX-4701","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-4701","name":"BRCA1-BARD1 complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-21994384","identifier":"Q3UI43","identifierLink":"https://www.uniprot.org/uniprotkb/Q3UI43/entry","name":"Babam1","description":"BRISC and BRCA1-A complex member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15660","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21994421","identifier":"Q8BPZ8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BPZ8/entry","name":"Abraxas1","description":"BRCA1-A complex subunit Abraxas 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR31728","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7068640","identifier":"Q5U5Q9","identifierLink":"https://www.uniprot.org/uniprotkb/Q5U5Q9/entry","name":"Uimc1","description":"BRCA1-A complex subunit RAP80","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8360920","identifier":"P46737","identifierLink":"https://www.uniprot.org/uniprotkb/P46737/entry","name":"Brcc3","description":"Lys-63-specific deubiquitinase BRCC36","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10410","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-4703","complexName":"MRN double-strand break repair complex","organismName":"Mus musculus; 10090","description":"Endo- and exonuclease complex that plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. It possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by Mre11.The complex may also be required for DNA damage signaling via activation of the Atm kinase (Q62388). In telomeres the MRN complex may modulate t-loop formation.\r\n\r\nMRN complex is part of the BRCA1-C complex (CPX-4722).","predictedComplex":false,"interactors":[{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2014813","identifier":"Q61216","identifierLink":"https://www.uniprot.org/uniprotkb/Q61216/entry","name":"Mre11","description":"Double-strand break repair protein MRE11","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2014834","identifier":"P70388","identifierLink":"https://www.uniprot.org/uniprotkb/P70388/entry","name":"Rad50","description":"DNA repair protein RAD50","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18867","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2014862","identifier":"Q9R207","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R207/entry","name":"Nbn","description":"Nibrin","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12162","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-4721","complexName":"BRCA1-B complex","organismName":"Mus musculus; 10090","description":"DNA helicase complex that binds and unwids DNA in a 5-prime to 3-prime direction during S phase at DNA damage sites. \r\n\r\nBRCA1-B complex is required for replication stress induced checkpoint control and DNA repair through homologous recombination (HR).","predictedComplex":false,"interactors":[{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-21994288","identifier":"CPX-4701","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-4701","name":"BRCA1-BARD1 complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-22014755","identifier":"Q5SXJ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q5SXJ3/entry","name":"Brip1","description":"Fanconi anemia group J protein homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11472","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-527248","identifier":"Q6ZQF0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6ZQF0/entry","name":"Topbp1","description":"DNA topoisomerase 2-binding protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13561","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4722","complexName":"BRCA1-C complex","organismName":"Mus musculus; 10090","description":"Endo- and Exonuclease complex that plays a central role in double-stranded break repair (DSB), DNA recombination, maintenance of telomere integrity and meiosis. It possesses single-strand endonuclease activity and double-strand-specific 3-prime-5-prime exonuclease activity, which are provided by MRN.\r\n \r\nThe complex formation of BRCA1-CtIP-MRN is important for facilitating DSB resection to generate single-stranded DNA that is needed for homologous recombination-mediated DSB repair, a process that also involves Exo1 (Q9QZ11) and Dna2 (Q6ZQJ5). \r\n\r\nIt is required for tolerance to etoposide during DNA replication, for DNA topoisomerase 2-DNA adduct removal, and for subsequent processing of DNA ends to generate a 3-prime ssDNA. \r\n\r\nIt is critical for G2-M checkpoint control in response to ionising radiation, to ensure that entry into mitosis is transiently inhibited to avoid aberrant chromosome segregation. \r\n\r\nBRCA1-C complex is also important for restart of stalled replication forks.","predictedComplex":false,"interactors":[{"ac":"EBI-16764284","identifier":"Q80YR6","identifierLink":"https://www.uniprot.org/uniprotkb/Q80YR6/entry","name":"Rbbp8","description":"DNA endonuclease RBBP8","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15107","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21994288","identifier":"CPX-4701","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-4701","name":"BRCA1-BARD1 complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-21994460","identifier":"CPX-4703","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-4703","name":"MRN double-strand break repair complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-4741","complexName":"Ragulator complex","organismName":"Homo sapiens; 9606","description":"Involved in amino acid sensing and activation of mTORC1(CPX-503) promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPases and the membrane sensor SLC38A9 (Q8NBW4) which couples amino acid transport to activation of complex, Ragulator functions as a guanine nucleotide exchange factor activating the small Rag GTPases. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. LAMTOR1 is directly responsible for anchoring the Ragulator complex to membranes. Also required for late endosomes/lysosomes biogenesis, it may regulate both the recycling of receptors through endosomes and the MAPK signaling pathway through recruitment of some of its components to late endosomes.","predictedComplex":false,"interactors":[{"ac":"EBI-1038192","identifier":"Q9UHA4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UHA4/entry","name":"LAMTOR3","description":"Ragulator complex protein LAMTOR3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13378","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2643704","identifier":"Q9Y2Q5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2Q5/entry","name":"LAMTOR2","description":"Ragulator complex protein LAMTOR2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13323","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5658976","identifier":"Q0VGL1","identifierLink":"https://www.uniprot.org/uniprotkb/Q0VGL1/entry","name":"LAMTOR4","description":"Ragulator complex protein LAMTOR4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR33967","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-713382","identifier":"O43504","identifierLink":"https://www.uniprot.org/uniprotkb/O43504/entry","name":"LAMTOR5","description":"Ragulator complex protein LAMTOR5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13342","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-715385","identifier":"Q6IAA8","identifierLink":"https://www.uniprot.org/uniprotkb/Q6IAA8/entry","name":"LAMTOR1","description":"Ragulator complex protein LAMTOR1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13401","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4742","complexName":"Catalase complex","organismName":"Homo sapiens; 9606","description":"A heme-binding peroxidase that reduces hydrogen peroxide to water and oxygen thus protecting cells from its toxic effects. Protects hemoglobin by removing over half of the hydrogen peroxide generated in erythrocytes.","predictedComplex":false,"interactors":[{"ac":"EBI-2432181","identifier":"P04040","identifierLink":"https://www.uniprot.org/uniprotkb/P04040/entry","name":"CAT","description":"Catalase","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11465","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-8785164","identifier":"CHEBI:16474","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16474","name":"nadph","description":"NADPH","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-4743","complexName":"Curli secretion complex","organismName":"Escherichia coli (strain K12); 83333","description":"Secretion complex required for the production of Curli, a class of functional amyloid fibers that serve as protein scaffolds in the extracellular biofilm matrix. \r\n\r\nUnstructured CSGA (P28307), the major curli subunit, is transported into the periplasmic space by the SecYEG translocon (CPX-1096) and maintained in a soluble, secretion-competent state by CSGC prior to delivery to the outer membrane CSGG pore by the periplasmic accessory protein CSGE. CSGE assembles into a nonameric ring that caps the periplasmic vestibule of the CSGG pore. The GSGE-GSGG pore fully or partially entraps the 129-residue CSGA, leads to a decrease in its conformational space, creating an entropic potential favouring polypeptide folding and facilitating its entropy-driven diffusion across the outer membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-16121579","identifier":"P0AE95","identifierLink":"https://www.uniprot.org/uniprotkb/P0AE95/entry","name":"csgE","description":"Curli production assembly/transport component CsgE","stochiometry":"minValue: 9, maxValue: 9","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-6405292","identifier":"P0AEA2","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEA2/entry","name":"csgG","description":"Curli production assembly/transport component CsgG","stochiometry":"minValue: 9, maxValue: 9","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR41164","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-873","complexName":"Nuclear pore complex","organismName":"Homo sapiens; 9606","description":"The nuclear pore complex (NPC) is a large assembly embedded in the nuclear envelope of eukaryotic cells. The NPC exclusively mediates all transport between cytoplasm and nucleus. A single NPC in a human cell can transport up to 80 MDa of material within 1 second. 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The nuclear basket subunits play an active role in transcription, transcriptional memory and chromatin organization by recruiting members of the transcription machinery to the nuclear side of the NCP.","predictedComplex":false,"interactors":[{"ac":"EBI-11009","identifier":"Q02455","identifierLink":"https://www.uniprot.org/uniprotkb/Q02455/entry","name":"MLP1","description":"Protein MLP1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR18898","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11698","identifier":"Q02629","identifierLink":"https://www.uniprot.org/uniprotkb/Q02629/entry","name":"NUP100","description":"Nucleoporin NUP100/NSP100","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23198","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11703","identifier":"Q02630","identifierLink":"https://www.uniprot.org/uniprotkb/Q02630/entry","name":"NUP116","description":"Nucleoporin NUP116/NSP116","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 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559292","xrefs":[{"identifier":"PTHR10971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25261","identifier":"P40457","identifierLink":"https://www.uniprot.org/uniprotkb/P40457/entry","name":"MLP2","description":"Protein MLP2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR18898","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25846","identifier":"P47054","identifierLink":"https://www.uniprot.org/uniprotkb/P47054/entry","name":"NUP192","description":"Nucleoporin NUP192","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31344","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27321","identifier":"Q03790","identifierLink":"https://www.uniprot.org/uniprotkb/Q03790/entry","name":"NUP53","description":"Nucleoporin NUP53","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3035","identifier":"Q05166","identifierLink":"https://www.uniprot.org/uniprotkb/Q05166/entry","name":"ASM4","description":"Nucleoporin ASM4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34287","identifier":"Q12445","identifierLink":"https://www.uniprot.org/uniprotkb/Q12445/entry","name":"POM34","description":"Nucleoporin POM34","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28003","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6240","identifier":"Q02647","identifierLink":"https://www.uniprot.org/uniprotkb/Q02647/entry","name":"DYN2","description":"Dynein light chain 1, cytoplasmic","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7635","identifier":"Q12315","identifierLink":"https://www.uniprot.org/uniprotkb/Q12315/entry","name":"GLE1","description":"mRNA export factor GLE1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4761","complexName":"Ragulator complex","organismName":"Mus musculus; 10090","description":"Involved in amino acid sensing and activation of mTORC1 (CPX-4473) promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPases and the membrane sensor SLC38A9 (Q8BGD6) which couples amino acid transport to activation of complex, Ragulator functions as a guanine nucleotide exchange factor activating the small Rag GTPases. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. LAMTOR1 is directly responsible for anchoring the Ragulator complex to membranes. Also required for late endosomes/lysosomes biogenesis, it may regulate both the recycling of receptors through endosomes and the MAPK signaling pathway through recruitment of some of its components to late endosomes.","predictedComplex":false,"interactors":[{"ac":"EBI-1038198","identifier":"Q9JHS3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JHS3/entry","name":"Lamtor2","description":"Ragulator complex protein LAMTOR2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13323","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1039530","identifier":"O88653","identifierLink":"https://www.uniprot.org/uniprotkb/O88653/entry","name":"Lamtor3","description":"Ragulator complex protein LAMTOR3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13378","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8328730","identifier":"Q9CQ22","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQ22/entry","name":"Lamtor1","description":"Ragulator complex protein LAMTOR1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13401","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8334398","identifier":"Q9D1L9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D1L9/entry","name":"Lamtor5","description":"Ragulator complex protein LAMTOR5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13342","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9986803","identifier":"Q8CF66","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CF66/entry","name":"Lamtor4","description":"Ragulator complex protein LAMTOR4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR33967","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4763","complexName":"Osteoprotegerin complex","organismName":"Mus musculus; 10090","description":"A soluble decoy receptor for osteoclastogenic cytokine Tnfsf11/Rankl (O35235). Binding of osteoprotegerin to cytokine Tnfsf11 prevents the cytokine from binding its receptor Tnfrsf11a/Rank (O35305) and thus inhibits osteoclastogenesis. Bone homeostasis seems to depend on the local ratio between cytokine and decoy receptor. Osteoprotegerin may also play a role in preventing arterial calcification. Plays some as yet to-be-defined role in mammary gland physiology and hormone-driven epithelial proliferation during pregnancy and may act as a protective factor in bone microenvironment by preventing breast cancer-induced bone loss and reducing intra-osseous tumour growth. \r\n\r\nAlso possible decoy receptor for pro-apoptotic cytokine Tnfsf10/Trail (P50591) which competes with Tnfsf11 and releases the inhibition of osteoclastogenesis. In vitro, binding affinity is 500x higher for Tnfsf11 than Tnfsf10. Binding of osteoprotegerin to Tnfsf10 appears to contribute to tumour growth of breast cancer cells and progression at the primary tumour site.","predictedComplex":false,"interactors":[{"ac":"EBI-16015871","identifier":"O08712","identifierLink":"https://www.uniprot.org/uniprotkb/O08712/entry","name":"Tnfrsf11b","description":"Tumor necrosis factor receptor superfamily member 11B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4767","complexName":"Catalase complex","organismName":"Mus musculus; 10090","description":"A heme-binding peroxidase that reduces hydrogen peroxide to water and oxygen thus protecting cells from its toxic effects. Protects hemoglobin by removing over half of the hydrogen peroxide generated in erythrocytes.","predictedComplex":false,"interactors":[{"ac":"EBI-2924912","identifier":"P24270","identifierLink":"https://www.uniprot.org/uniprotkb/P24270/entry","name":"Cat","description":"Catalase","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11465","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-8785164","identifier":"CHEBI:16474","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16474","name":"nadph","description":"NADPH","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-4768","complexName":"Catalase complex","organismName":"Bos taurus; 9913","description":"A heme-binding peroxidase that reduces hydrogen peroxide to water and oxygen thus protecting cells from its toxic effects. Protects hemoglobin by removing over half of the hydrogen peroxide generated in erythrocytes.","predictedComplex":false,"interactors":[{"ac":"EBI-15482262","identifier":"P00432","identifierLink":"https://www.uniprot.org/uniprotkb/P00432/entry","name":"CAT","description":"Catalase","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR11465","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-8785164","identifier":"CHEBI:16474","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16474","name":"nadph","description":"NADPH","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-4781","complexName":"Citrate lyase complex","organismName":"Escherichia coli (strain K12); 83333","description":"An anaerobic citrate lyase transferase that also catalyzes the cleavage of citrate to acetate and oxaloacetate. The citrate molecule is very stable, and needs to be activated prior to cleavage by forming a thioester bond with the enzyme.\r\n\r\nThe enzyme is a complex of three subunits, one of them a dedicated acyl carrier protein which is synthesized in an apo form, and is converted to its holo form by the covalent binding of a prosthetic S-acetyl-O-[2'-(5-phosphoribosyl)-3'-dephospho-CoA]-L-serine(3-) group, resulting in the formation of an inactive citrate-lyase. To be fully catalytically active, the SH-group of the enzyme-bound CoA-derivative is converted to an acetyl-thioester by a citrate lyase ligase (citC, P77390).","predictedComplex":false,"interactors":[{"ac":"EBI-1119230","identifier":"P69330","identifierLink":"https://www.uniprot.org/uniprotkb/P69330/entry","name":"citD","description":"Citrate lyase acyl carrier protein","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-22053091","identifier":"P75726","identifierLink":"https://www.uniprot.org/uniprotkb/P75726/entry","name":"citF","description":"Citrate lyase alpha chain","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR40596","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25405433","identifier":"CHEBI:137976","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:137976","name":"s-acetyl-o-[2'-(5-phosphoribosyl)-3'-dephospho-coa]-l-serine(3-) residue","description":"S-acetyl-O-[2'-(5-phosphoribosyl)-3'-dephospho-CoA]-L-serine(3-) residue","stochiometry":"minValue: 6, maxValue: 6","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-550867","identifier":"P0A9I1","identifierLink":"https://www.uniprot.org/uniprotkb/P0A9I1/entry","name":"citE","description":"Citrate lyase subunit beta","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32308","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 6, maxValue: 6","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-4783","complexName":"Anthranilate synthase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the two-step formation of anthranilate, an intermediate in the biosynthesis of L-tryptophan, from chorismate and glutamine. The glutamine-binding beta subunit (trpGD) provides the glutamine amidotransferase activity which generates ammonia as a substrate and then delivers this to the active site of the large alpha subunit  (trpE) to produce anthranilate from ammonia and chorismate. Cooperatively binds and is inhibited by tryptophan, binding is competitive with chorismate binding but not at the same site.","predictedComplex":false,"interactors":[{"ac":"EBI-1118772","identifier":"P00895","identifierLink":"https://www.uniprot.org/uniprotkb/P00895/entry","name":"trpE","description":"Anthranilate synthase component 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11236","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9275092","identifier":"P00904","identifierLink":"https://www.uniprot.org/uniprotkb/P00904/entry","name":"trpGD","description":"Bifunctional protein TrpGD","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43418","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-4821","complexName":"unc-51-atg-13 complex","organismName":"Caenorhabditis elegans; 6239","description":"Serine/threonine kinase complex. Essential for autophagy during nutrient deprivation, a catabolic process that sequesters undesired cellular material into autophagosomes for delivery to lysosomes for degradation. The complex is recruited to preautophagosomes by lgg-1 (Q09490) and is in turn required for the recruitment of other autophagy proteins, and for autophagosome formation.","predictedComplex":false,"interactors":[{"ac":"EBI-22054893","identifier":"P34379","identifierLink":"https://www.uniprot.org/uniprotkb/P34379/entry","name":"atg-13","description":"Autophagy-related protein 13 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13430","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-329049","identifier":"Q23023","identifierLink":"https://www.uniprot.org/uniprotkb/Q23023/entry","name":"unc-51","description":"Serine/threonine-protein kinase unc-51","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24348","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4822","complexName":"Glutamine ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity glutamine transporter, member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily, a polar amino acid uptake transporter. The GLH periplasmic binding protein has a Kd of 3 x 10-7 M for glutamine and gamma-glutamylhydrazide and gamma-glutamylhydroxamate competitively inhibit both the binding reaction and the uptake of glutamine by intact cells.","predictedComplex":false,"interactors":[{"ac":"EBI-1120383","identifier":"P10346","identifierLink":"https://www.uniprot.org/uniprotkb/P10346/entry","name":"glnQ","description":"Glutamine transport ATP-binding protein GlnQ","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43166","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1120408","identifier":"P0AEQ3","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEQ3/entry","name":"glnH","description":"Glutamine-binding periplasmic protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR35936","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22055134","identifier":"P0AEQ6","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEQ6/entry","name":"glnP","description":"Glutamine transport system permease protein GlnP","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30614","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4841","complexName":"Anaerobic glycerol-3-phosphate dehydrogenase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyses the oxidation of glycerol-3-phosphate to dihyroxyacetone phosphate using fumarate or nitrate as an electron acceptor. GlpABC is a respiratory enzyme. Anaerobic growth of E. coli with glycerol and fumarate induces expression of anaerobic glycerol-3-phosphate dehydrogenase and fumarate reductase and is associated with proton translocation and the generation of a proton motive force.","predictedComplex":false,"interactors":[{"ac":"EBI-1119412","identifier":"P0A9C0","identifierLink":"https://www.uniprot.org/uniprotkb/P0A9C0/entry","name":"glpA","description":"Anaerobic glycerol-3-phosphate dehydrogenase subunit A","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11985","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-545752","identifier":"P13033","identifierLink":"https://www.uniprot.org/uniprotkb/P13033/entry","name":"glpB","description":"Anaerobic glycerol-3-phosphate dehydrogenase subunit B","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43400","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-907280","identifier":"P0A996","identifierLink":"https://www.uniprot.org/uniprotkb/P0A996/entry","name":"glpC","description":"Anaerobic glycerol-3-phosphate dehydrogenase subunit C","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32479","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9663515","identifier":"CHEBI:58210","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58210","name":"fmn(3-)","description":"FMN(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-4862","complexName":"Alkyl hydroperoxide reductase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Serves as a primary hydroperoxide scavenger that reduces organic hydroperoxides and and peroxinitrite to water or alcohols, thereby preventing protein oxidation, lipid peroxidation and DNA damage. A conserved redox-active cysteine residue (Cys-47), the peroxidatic cysteine (C(P)), in the active site of one ahpC molecule is responsible for a nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue (Cys-166), the resolving cysteine (C(R)) located at the C-terminus of a second subunit of ahpC to form a disulfide bridge. Oxidized ahpC is regenerated by electron donation via the disulphide center (-CxxC-) in the N-terminal domain of ahpF, resulting in reduction of the ahpC cysteines to their thiol form using either NADH or NADPH as an electron donor.","predictedComplex":false,"interactors":[{"ac":"EBI-547397","identifier":"P0AE08","identifierLink":"https://www.uniprot.org/uniprotkb/P0AE08/entry","name":"ahpC","description":"Alkyl hydroperoxide reductase C","stochiometry":"minValue: 10, maxValue: 10","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10681","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-907438","identifier":"P35340","identifierLink":"https://www.uniprot.org/uniprotkb/P35340/entry","name":"ahpF","description":"Alkyl hydroperoxide reductase subunit F","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR48105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-276","complexName":"5-hydroxytryptamine-3A/C receptor complex","organismName":"Homo sapiens; 9606","description":"Inward-rectifying, ligand-gated ion channel, which when activated by 5-hydroxytryptamine (5-HT, serotonin) causes fast neuronal depolarization and excitation or modulation of neurotransmitter release depending on their neuronal localisation (central and/or peripheral nervous system). A cation-specific, but otherwise relatively non-selective, ion channel with low conductance. Ca2+-permeability is related to subunit composition with 5HT3A homopentamers being more permeable than 5HT3A/B heteropentamers. \r\n\r\nFound pre- and post-synaptically but with different properties - pre-synaptic 5-HT3 receptors are predominantly calcium-permeant while post-synaptic receptors are permeant to Na+ and K+. Also Mg2+ permeant. Pre-synaptic depolarisations are generally slower than post-synaptic depolarisations. \r\n\r\n5-HT3 receptors increase the frequency of spontaneous excitatory post-synaptic currents (sEPSCs) or miniature EPSCs (mEPSCs). These may be related to 5-HT3-induced depolarisation of pre-synaptic membranes and subsequent activation of cholinergic or glutamatergic neurotransmissions or evoked excitatory post-synaptic currents (eEPSCs) or spontaneous inhibitory post-synaptic currents (sIPSCs) related to GABAergic neurotransmissions post-synaptic 5-HT3 receptor activation. \r\n\r\nHigh levels of expression are found in the vagal terminals of the dorsal vagal complex where it is involved in the vomiting reflex (especially post-operative and chemotherapy- and radiation-induced vomiting and nausea), in the amygdala and the hippocampi. 5-HT3 receptor antagonists therefore act as effective anti-emetic drugs. Lower levels of expression are found in the forebrain with higher relative expression in the striatum than the cortical regions. \r\n\r\nInvolved in processes associated with emotion, cognition, memory and pain perception. \r\n\r\nInvolved in ganglionic transmission in the myenteric plexus in the mucosal layer and expressed in the gastrointestinal (GI) tract serotonin mediates control over a variety of physiological functions such as the contraction/relaxation of smooth muscle, and peristaltic and secretory reflexes, directly or indirectly through intrinsic primary afferent neurons. \r\n\r\nPlays an important role in the regulation of inflammation and immune responses in the peripheral nervous system. \r\n\r\nActivation of 5-HT3 receptors on visceral afferents in some irritable bowel syndrome (IBS) patients results in visceral hypersensitivity. \r\n\r\nChaperone proteins assist assembly, modifications and export from the ER followed by transport in vesicle-like structures along microtubules to the plasma membrane where they typically form clusters in F-actin-rich regions.","predictedComplex":false,"interactors":[{"ac":"EBI-9008743","identifier":"P46098","identifierLink":"https://www.uniprot.org/uniprotkb/P46098/entry","name":"HTR3A","description":"5-hydroxytryptamine receptor 3A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008753","identifier":"Q8WXA8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WXA8/entry","name":"HTR3C","description":"5-hydroxytryptamine receptor 3C","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-277","complexName":"5-hydroxytryptamine-3A/B receptor complex","organismName":"Rattus norvegicus; 10116","description":"Inward-rectifying, ligand-gated ion channel, which when activated by 5-hydroxytryptamine (5-HT, serotonin) causes fast neuronal depolarization and excitation or modulation of neurotransmitter release depending on their neuronal localisation (central and/or peripheral nervous system). A cation-specific, but otherwise relatively non-selective, ion channel with low conductance. Ca2+-permeability is related to subunit composition with 5HT3A homopentamers being more permeable than 5HT3A/B heteropentamers. \r\n\r\nFound pre- and post-synaptically but with different properties - pre-synaptic 5-HT3 receptors are predominantly calcium-permeant while post-synaptic receptors are permeant to Na+ and K+. Also Mg2+ permeant. Pre-synaptic depolarisations are generally slower than post-synaptic depolarisations. \r\n\r\n5-HT3 receptors increase the frequency of spontaneous excitatory post-synaptic currents (sEPSCs) or miniature EPSCs (mEPSCs). These may be related to 5-HT3-induced depolarisation of pre-synaptic membranes and subsequent activation of cholinergic or glutamatergic neurotransmissions or evoked excitatory post-synaptic currents (eEPSCs) or spontaneous inhibitory post-synaptic currents (sIPSCs) related to GABAergic neurotransmissions post-synaptic 5-HT3 receptor activation. \r\n\r\nDue to different residues in transmembrane domain M2 of the 5-HT3A and 5-HT3B subunits the 5-HT3A/B heteromeric receptors are more efficient conductors than 5-HT3A homomeric receptors and have increased agonist and antagonist affinity. Homomeric receptors recover faster from desensitisation but are probably less prevalent in vivo. \r\n\r\nHigh levels of expression are found in the vagal terminals of the dorsal vagal complex, in the amygdala and the hippocampi. Lower levels of expression are found in the forebrain with lower relative expression in the striatum than the cortical regions. \r\n\r\nInvolved in processes associated with emotion, cognition, memory and pain perception. \r\n\r\nInvolved in ganglionic transmission in the myenteric plexus in the mucosal layer and expressed in the gastrointestinal (GI) tract serotonin mediates control over a variety of physiological functions such as the contraction/relaxation of smooth muscle, and peristaltic and secretory reflexes, directly or indirectly through intrinsic primary afferent neurons. \r\n\r\nPlays an important role in the regulation of inflammation and immune responses in the peripheral nervous system. \r\n\r\nChaperone proteins assist assembly, modifications and export from the ER followed by transport in vesicle-like structures along microtubules to the plasma membrane where they typically form clusters in F-actin-rich regions.","predictedComplex":false,"interactors":[{"ac":"EBI-9008535","identifier":"Q9JJ16","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JJ16/entry","name":"Htr3b","description":"5-hydroxytryptamine receptor 3B","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008540","identifier":"P35563","identifierLink":"https://www.uniprot.org/uniprotkb/P35563/entry","name":"Htr3a","description":"5-hydroxytryptamine receptor 3A","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-278","complexName":"5-hydroxytryptamine-3A receptor complex","organismName":"Rattus norvegicus; 10116","description":"Inward-rectifying, ligand-gated ion channel, which when activated by 5-hydroxytryptamine (5-HT, serotonin) causes fast neuronal depolarization and excitation or modulation of neurotransmitter release depending on their neuronal localisation (central and/or peripheral nervous system). A cation-specific, but otherwise relatively non-selective, ion channel with low conductance. Ca2+-permeability is related to subunit composition with 5HT3A homopentamers being more permeable than 5HT3A/B heteropentamers. \r\n\r\nFound pre- and post-synaptically but with different properties - pre-synaptic 5-HT3 receptors are predominantly calcium-permeant while post-synaptic receptors are permeant to Na+ and K+. Also Mg2+ permeant. Pre-synaptic depolarisations are generally slower than post-synaptic depolarisations. \r\n\r\n5-HT3 receptors increase the frequency of spontaneous excitatory post-synaptic currents (sEPSCs) or miniature EPSCs (mEPSCs). These may be related to 5-HT3-induced depolarisation of pre-synaptic membranes and subsequent activation of cholinergic or glutamatergic neurotransmissions or evoked excitatory post-synaptic currents (eEPSCs) or spontaneous inhibitory post-synaptic currents (sIPSCs) related to GABAergic neurotransmissions post-synaptic 5-HT3 receptor activation. \r\n\r\nDue to different residues in transmembrane domain M2 of the 5-HT3A and 5-HT3B subunits the 5-HT3A/B heteromeric receptors are more efficient conductors than 5-HT3A homomeric receptors and have increased agonist and antagonist affinity. Homomeric receptors recover faster from desensitisation but are probably less prevalent in vivo. \r\n\r\nHigh levels of expression are found in the vagal terminals of the dorsal vagal complex, in the amygdala and the hippocampi. Lower levels of expression are found in the forebrain with lower relative expression in the striatum than the cortical regions. \r\n\r\nInvolved in processes associated with emotion, cognition, memory and pain perception. \r\n\r\nInvolved in ganglionic transmission in the myenteric plexus in the mucosal layer and expressed in the gastrointestinal (GI) tract serotonin mediates control over a variety of physiological functions such as the contraction/relaxation of smooth muscle, and peristaltic and secretory reflexes, directly or indirectly through intrinsic primary afferent neurons. \r\n\r\nPlays an important role in the regulation of inflammation and immune responses in the peripheral nervous system. \r\n\r\nChaperone proteins assist assembly, modifications and export from the ER followed by transport in vesicle-like structures along microtubules to the plasma membrane where they typically form clusters in F-actin-rich regions.","predictedComplex":false,"interactors":[{"ac":"EBI-9008540","identifier":"P35563","identifierLink":"https://www.uniprot.org/uniprotkb/P35563/entry","name":"Htr3a","description":"5-hydroxytryptamine receptor 3A","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-279","complexName":"Coagulation factor VIIa - tissue factor complex","organismName":"Mus musculus; 10090","description":"A serine-type endopeptidase complex of the extrinsic blood coagulation pathway (tissue factor pathway) whose formation in the plasma membrane initiates the blood coagulation process by initiating the cell-surface assembly and propagation of the coagulation protease cascade. Activates coagulation factors IX (P16294) and X (O88947) by limited proteolysis to form active factors IX and X (factors IXa and Xa). Selectively cleavages of Arg-|-Ile bonds in factor X to form factor Xa. The coagulation pathway is terminated when fibrinogen is cleaved to fibrin which in turn polymerizes to produce a clot. \r\n\r\nIts zymogen form is activated by selective cleavage of Arg-|-Ile bonds to form active factor VIIa. Activation is triggered by trauma and minor proteolysis by thrombin (FIIa, P19221), factor Xa (O88947), factor XIa (Q91Y47) and factor XIIa (Q80YC5). Also constitutively activated at very low levels. Inhibited by complex formation with TFPI (O54819) and factor Xa.","predictedComplex":false,"interactors":[{"ac":"EBI-11295604","identifier":"P20352-PRO_0000033639","identifierLink":"https://www.uniprot.org/uniprotkb/P20352-PRO_0000033639/entry","name":"F3","description":"Tissue factor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-11296301","identifier":"P70375-PRO_0000027733","identifierLink":"https://www.uniprot.org/uniprotkb/P70375-PRO_0000027733/entry","name":"F7","description":"Factor VII light chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-11296307","identifier":"P70375-PRO_0000027734","identifierLink":"https://www.uniprot.org/uniprotkb/P70375-PRO_0000027734/entry","name":"F7","description":"Factor VII heavy chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 9, maxValue: 9","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-280","complexName":"GABA-A receptor, alpha-4/beta-3/delta","organismName":"Rattus norvegicus; 10116","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-11296648","identifier":"P28471","identifierLink":"https://www.uniprot.org/uniprotkb/P28471/entry","name":"Gabra4","description":"Gamma-aminobutyric acid receptor subunit alpha-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11296683","identifier":"P18506","identifierLink":"https://www.uniprot.org/uniprotkb/P18506/entry","name":"Gabrd","description":"Gamma-aminobutyric acid receptor subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6257937","identifier":"P63079","identifierLink":"https://www.uniprot.org/uniprotkb/P63079/entry","name":"Gabrb3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-281","complexName":"Hydrogenase-1 complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the reversible oxidation of hydrogen (H2) to protons and electrons. Maximally produced during fermentation and under various types of stress such as carbon and phosphate starvation, osmotic up shift, and stationary phase conditions. Hydrogenase-1 is oxygen tolerant and contains the special proximal (relative to the active site) [Fe4S3] cluster that can rapidly undergo two successive one-electron oxidations within a narrow potential range. The additional two electrons required to reduce the attacking O2 to two water molecules  can originate from either the two-electron oxidation of Ni(I) to Ni(III) or the one-electron oxidation of Ni(II) to Ni(III) at the active site, the latter coupled to the one-electron oxidation of the [Fe4S4] medial cluster.","predictedComplex":false,"interactors":[{"ac":"EBI-11297461","identifier":"CHEBI:21137","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:21137","name":"tri-mu-sulfido-mu3-sulfido-triiron","description":"tri-mu-sulfido-mu3-sulfido-triiron","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1134138","identifier":"P0AAM1","identifierLink":"https://www.uniprot.org/uniprotkb/P0AAM1/entry","name":"hyaC","description":"Probable Ni/Fe-hydrogenase 1 B-type cytochrome subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30485","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2296617","identifier":"CHEBI:49786","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49786","name":"nickel(2+)","description":"Nickel(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-851493","identifier":"P0ACD8","identifierLink":"https://www.uniprot.org/uniprotkb/P0ACD8/entry","name":"hyaB","description":"Hydrogenase-1 large chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42958","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9124108","identifier":"P69739","identifierLink":"https://www.uniprot.org/uniprotkb/P69739/entry","name":"hyaA","description":"Hydrogenase-1 small chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30013","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-282","complexName":"Hydrogenase-2 complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the reversible oxidation of hydrogen (H2) to protons and electrons. Strongly upregulated during microaerobic and anaerobic respiration when H2 is used as an electron donor to reduce menaquinone to its quinol, with subsequent electron transfer to fumarate.","predictedComplex":false,"interactors":[{"ac":"EBI-11297461","identifier":"CHEBI:21137","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:21137","name":"tri-mu-sulfido-mu3-sulfido-triiron","description":"tri-mu-sulfido-mu3-sulfido-triiron","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-11302677","identifier":"P0AAJ8-PRO_0000042273","identifierLink":"https://www.uniprot.org/uniprotkb/P0AAJ8-PRO_0000042273/entry","name":"hybA","description":"Hydrogenase-2 operon protein HybA","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-11302684","identifier":"P69741-PRO_0000013430","identifierLink":"https://www.uniprot.org/uniprotkb/P69741-PRO_0000013430/entry","name":"hybO","description":"Hydrogenase-2 small chain","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-11302692","identifier":"P0ACE0-PRO_0000013407","identifierLink":"https://www.uniprot.org/uniprotkb/P0ACE0-PRO_0000013407/entry","name":"hybC","description":"Hydrogenase-2 large chain","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-11302699","identifier":"P37180","identifierLink":"https://www.uniprot.org/uniprotkb/P37180/entry","name":"hybB","description":"Probable Ni/Fe-hydrogenase 2 b-type cytochrome subunit","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30074","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":"minValue: 6, maxValue: 6","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2296617","identifier":"CHEBI:49786","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49786","name":"nickel(2+)","description":"Nickel(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-283","complexName":"NMDA receptor complex, GluN1-GluN2A","organismName":"Rattus norvegicus; 10116","description":"Voltage-gated ion channel of the ionotrophic glutamate receptor (iGluR) family that is characterised by high calcium permeability and very slow deactivation. Activated by simultaneous binding of glycine to GluN1 and L-glutamate to GluN2. Blocked by physiological concentrations of extracellular magnesium which is released by membrane depolarization. \r\n\r\nPredominantly post-synaptic receptor that mediates mostly the late/slow phase of the majority of the fast excitatory neurotransmission in the mammalian brain where it plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. \r\n\r\nCombinations of different receptor isoforms and their splice variants result in formation of ion channels with distinct spatio-temporal expression patterns and pharmacological and electrophysiological properties. \r\n\r\nReplacement of one or more subunits with GluN3A (Q9R1M7) or GluN3B (Q8VHN2) subunits results in relatively Ca2+-impermeable cation channels that are resistant to Mg2+.","predictedComplex":false,"interactors":[{"ac":"EBI-630970","identifier":"Q00959","identifierLink":"https://www.uniprot.org/uniprotkb/Q00959/entry","name":"Grin2a","description":"Glutamate receptor ionotropic, NMDA 2A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-877897","identifier":"P35439","identifierLink":"https://www.uniprot.org/uniprotkb/P35439/entry","name":"Grin1","description":"Glutamate receptor ionotropic, NMDA 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-284","complexName":"NMDA receptor complex, GluN1-GluN2B","organismName":"Rattus norvegicus; 10116","description":"Voltage-gated ion channel of the ionotrophic glutamate receptor (iGluR) family that is characterised by high calcium permeability and very slow deactivation. Activated by simultaneous binding of glycine to GluN1 and L-glutamate to GluN2. Blocked by physiological concentrations of extracellular magnesium which is released by membrane depolarization. \r\n\r\nPredominantly post-synaptic receptor that mediates mostly the late/slow phase of the majority of the fast excitatory neurotransmission in the mammalian brain where it plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. \r\n\r\nCombinations of different receptor isoforms and their splice variants result in formation of ion channels with distinct spatiotemporal expression patterns and pharmacological and electrophysiological properties. \r\n\r\nReplacement of one or more subunits with GluN3A (Q9R1M7) or GluN3B (Q8VHN2) subunits results in relatively Ca2+-impermeable cation channels that are resistant to Mg2+.","predictedComplex":false,"interactors":[{"ac":"EBI-396905","identifier":"Q00960","identifierLink":"https://www.uniprot.org/uniprotkb/Q00960/entry","name":"Grin2b","description":"Glutamate receptor ionotropic, NMDA 2B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-877897","identifier":"P35439","identifierLink":"https://www.uniprot.org/uniprotkb/P35439/entry","name":"Grin1","description":"Glutamate receptor ionotropic, NMDA 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-285","complexName":"NMDA receptor complex, GluN1-GluN2B","organismName":"Homo sapiens; 9606","description":"Voltage-gated ion channel of the ionotrophic glutamate receptor (iGluR) family that is characterised by high calcium permeability and very slow deactivation. Activated by simultaneous binding of glycine to GluN1 and L-glutamate to GluN2. Blocked by physiological concentrations of extracellular magnesium which is released by membrane depolarization. \r\n\r\nPredominantly post-synaptic receptor that mediates mostly the late/slow phase of the majority of the fast excitatory neurotransmission in the mammalian brain where it plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. \r\n\r\nCombinations of different receptor isoforms and their splice variants result in formation of ion channels with distinct spatiotemporal expression patterns and pharmacological and electrophysiological properties. \r\n\r\nReplacement of one or more subunits with GluN3A (Q8TCU5) or GluN3B (O60391) subunits results in relatively Ca2+-impermeable cation channels that are resistant to Mg2+. \r\n\r\nDysfunctional NMDA receptors are implicated in various neurological disorders and injuries including depression, schizophrenia, Alzheimer's and Parkinson's disease, chronic and neuropathic pain, as well as neuronal loss following ischaemia or stroke.","predictedComplex":false,"interactors":[{"ac":"EBI-2256942","identifier":"Q13224","identifierLink":"https://www.uniprot.org/uniprotkb/Q13224/entry","name":"GRIN2B","description":"Glutamate receptor ionotropic, NMDA 2B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-998542","identifier":"Q05586","identifierLink":"https://www.uniprot.org/uniprotkb/Q05586/entry","name":"GRIN1","description":"Glutamate receptor ionotropic, NMDA 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-286","complexName":"NMDA receptor complex, GluN1-GluN2C","organismName":"Homo sapiens; 9606","description":"Voltage-gated ion channel of the ionotrophic glutamate receptor (iGluR) family that is characterised by high calcium permeability and very slow deactivation. Activated by simultaneous binding of glycine to GluN1 and L-glutamate to GluN2. Blocked by physiological concentrations of extracellular magnesium which is released by membrane depolarization. \r\n\r\nPredominantly post-synaptic receptor that mediates mostly the late/slow phase of the majority of the fast excitatory neurotransmission in the mammalian brain where it plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. \r\n\r\nCombinations of different receptor isoforms and their splice variants result in formation of ion channels with distinct spatiotemporal expression patterns and pharmacological and electrophysiological properties. \r\n\r\nReplacement of one or more subunits with GluN3A (Q8TCU5) or GluN3B (O60391) subunits results in relatively Ca2+-impermeable cation channels that are resistant to Mg2+. \r\n\r\nDysfunctional NMDA receptors are implicated in various neurological disorders and injuries including depression, schizophrenia, Alzheimer's and Parkinson's disease, chronic and neuropathic pain, as well as neuronal loss following ischaemia or stroke.","predictedComplex":false,"interactors":[{"ac":"EBI-8285963","identifier":"Q14957","identifierLink":"https://www.uniprot.org/uniprotkb/Q14957/entry","name":"GRIN2C","description":"Glutamate receptor ionotropic, NMDA 2C","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-998542","identifier":"Q05586","identifierLink":"https://www.uniprot.org/uniprotkb/Q05586/entry","name":"GRIN1","description":"Glutamate receptor ionotropic, NMDA 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-287","complexName":"NMDA receptor complex, GluN1-GluN2C","organismName":"Rattus norvegicus; 10116","description":"Voltage-gated ion channel of the ionotrophic glutamate receptor (iGluR) family that is characterised by high calcium permeability and very slow deactivation. Activated by simultaneous binding of glycine to GluN1 and L-glutamate to GluN2. Blocked by physiological concentrations of extracellular magnesium which is released by membrane depolarization. \r\n\r\nPredominantly post-synaptic receptor that mediates mostly the late/slow phase of the majority of the fast excitatory neurotransmission in the mammalian brain where it plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. \r\n\r\nCombinations of different receptor isoforms and their splice variants result in formation of ion channels with distinct spatiotemporal expression patterns and pharmacological and electrophysiological properties. \r\n\r\nReplacement of one or more subunits with GluN3A (Q9R1M7) or GluN3B (Q8VHN2) subunits results in relatively Ca2+-impermeable cation channels that are resistant to Mg2+.","predictedComplex":false,"interactors":[{"ac":"EBI-631045","identifier":"Q00961","identifierLink":"https://www.uniprot.org/uniprotkb/Q00961/entry","name":"Grin2c","description":"Glutamate receptor ionotropic, NMDA 2C","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-877897","identifier":"P35439","identifierLink":"https://www.uniprot.org/uniprotkb/P35439/entry","name":"Grin1","description":"Glutamate receptor ionotropic, NMDA 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-288","complexName":"NMDA receptor complex, GluN1-GluN2D","organismName":"Rattus norvegicus; 10116","description":"Voltage-gated ion channel of the ionotrophic glutamate receptor (iGluR) family that is characterised by high calcium permeability and very slow deactivation. Activated by simultaneous binding of glycine to GluN1 and L-glutamate to GluN2. Blocked by physiological concentrations of extracellular magnesium which is released by membrane depolarization. \r\n\r\nPredominantly post-synaptic receptor that mediates mostly the late/slow phase of the majority of the fast excitatory neurotransmission in the mammalian brain where it plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. \r\n\r\nCombinations of different receptor isoforms and their splice variants result in formation of ion channels with distinct spatiotemporal expression patterns and pharmacological and electrophysiological properties. \r\n\r\nReplacement of one or more subunits with GluN3A (Q9R1M7) or GluN3B (Q8VHN2) subunits results in relatively Ca2+-impermeable cation channels that are resistant to Mg2+.","predictedComplex":false,"interactors":[{"ac":"EBI-631067","identifier":"Q62645","identifierLink":"https://www.uniprot.org/uniprotkb/Q62645/entry","name":"Grin2d","description":"Glutamate receptor ionotropic, NMDA 2D","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-877897","identifier":"P35439","identifierLink":"https://www.uniprot.org/uniprotkb/P35439/entry","name":"Grin1","description":"Glutamate receptor ionotropic, NMDA 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-289","complexName":"NMDA receptor complex, GluN1-GluN2D","organismName":"Homo sapiens; 9606","description":"Voltage-gated ion channel of the ionotrophic glutamate receptor (iGluR) family that is characterised by high calcium permeability and very slow deactivation. Activated by simultaneous binding of glycine to GluN1 and L-glutamate to GluN2. Blocked by physiological concentrations of extracellular magnesium which is released by membrane depolarization. \r\n\r\nPredominantly post-synaptic receptor that mediates mostly the late/slow phase of the majority of the fast excitatory neurotransmission in the mammalian brain where it plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. \r\n\r\nCombinations of different receptor isoforms and their splice variants result in formation of ion channels with distinct spatiotemporal expression patterns and pharmacological and electrophysiological properties. \r\n\r\nReplacement of one or more subunits with GluN3A (Q8TCU5) or GluN3B (O60391) subunits results in relatively Ca2+-impermeable cation channels that are resistant to Mg2+. \r\n\r\nDysfunctional NMDA receptors are implicated in various neurological disorders and injuries including depression, schizophrenia, Alzheimer's and Parkinson's disease, chronic and neuropathic pain, as well as neuronal loss following ischaemia or stroke.","predictedComplex":false,"interactors":[{"ac":"EBI-1754030","identifier":"O15399","identifierLink":"https://www.uniprot.org/uniprotkb/O15399/entry","name":"GRIN2D","description":"Glutamate receptor ionotropic, NMDA 2D","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-998542","identifier":"Q05586","identifierLink":"https://www.uniprot.org/uniprotkb/Q05586/entry","name":"GRIN1","description":"Glutamate receptor ionotropic, NMDA 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-290","complexName":"NMDA receptor complex, GluN1-GluN2A","organismName":"Mus musculus; 10090","description":"Voltage-gated ion channel of the ionotrophic glutamate receptor (iGluR) family that is characterised by high calcium permeability and very slow deactivation. Activated by simultaneous binding of glycine to GluN1 and L-glutamate to GluN2. Blocked by physiological concentrations of extracellular magnesium which is released by membrane depolarization. \r\n\r\nPredominantly post-synaptic receptor that mediates mostly the late/slow phase of the majority of the fast excitatory neurotransmission in the mammalian brain where it plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. \r\n\r\nCombinations of different receptor isoforms and their splice variants result in formation of ion channels with distinct spatiotemporal expression patterns and pharmacological and electrophysiological properties. \r\n\r\nReplacement of one or more subunits with GluN3A (A2AIR5) or GluN3B (Q91ZU9) subunits results in relatively Ca2+-impermeable cation channels that are resistant to Mg2+.","predictedComplex":false,"interactors":[{"ac":"EBI-400084","identifier":"P35438","identifierLink":"https://www.uniprot.org/uniprotkb/P35438/entry","name":"Grin1","description":"Glutamate receptor ionotropic, NMDA 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-400115","identifier":"P35436","identifierLink":"https://www.uniprot.org/uniprotkb/P35436/entry","name":"Grin2a","description":"Glutamate receptor ionotropic, NMDA 2A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-291","complexName":"NMDA receptor complex, GluN1-GluN2B","organismName":"Mus musculus; 10090","description":"Voltage-gated ion channel of the ionotrophic glutamate receptor (iGluR) family that is characterised by high calcium permeability and very slow deactivation. Activated by simultaneous binding of glycine to GluN1 and L-glutamate to GluN2. Blocked by physiological concentrations of extracellular magnesium which is released by membrane depolarization. \r\n\r\nPredominantly post-synaptic receptor that mediates mostly the late/slow phase of the majority of the fast excitatory neurotransmission in the mammalian brain where it plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. \r\n\r\nCombinations of different receptor isoforms and their splice variants result in formation of ion channels with distinct spatiotemporal expression patterns and pharmacological and electrophysiological properties. \r\n\r\nReplacement of one or more subunits with GluN3A (A2AIR5) or GluN3B (Q91ZU9) subunits results in relatively Ca2+-impermeable cation channels that are resistant to Mg2+.","predictedComplex":false,"interactors":[{"ac":"EBI-400084","identifier":"P35438","identifierLink":"https://www.uniprot.org/uniprotkb/P35438/entry","name":"Grin1","description":"Glutamate receptor ionotropic, NMDA 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-400125","identifier":"Q01097","identifierLink":"https://www.uniprot.org/uniprotkb/Q01097/entry","name":"Grin2b","description":"Glutamate receptor ionotropic, NMDA 2B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-292","complexName":"NMDA receptor complex, GluN1-GluN2C","organismName":"Mus musculus; 10090","description":"Voltage-gated ion channel of the ionotrophic glutamate receptor (iGluR) family that is characterised by high calcium permeability and very slow deactivation. Activated by simultaneous binding of glycine to GluN1 and L-glutamate to GluN2. Blocked by physiological concentrations of extracellular magnesium which is released by membrane depolarization. \r\n\r\nPredominantly post-synaptic receptor that mediates mostly the late/slow phase of the majority of the fast excitatory neurotransmission in the mammalian brain where it plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. \r\n\r\nCombinations of different receptor isoforms and their splice variants result in formation of ion channels with distinct spatiotemporal expression patterns and pharmacological and electrophysiological properties. \r\n\r\nReplacement of one or more subunits with GluN3A (A2AIR5) or GluN3B (Q91ZU9) subunits results in relatively Ca2+-impermeable cation channels that are resistant to Mg2+.","predictedComplex":false,"interactors":[{"ac":"EBI-2314786","identifier":"Q01098","identifierLink":"https://www.uniprot.org/uniprotkb/Q01098/entry","name":"Grin2c","description":"Glutamate receptor ionotropic, NMDA 2C","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-400084","identifier":"P35438","identifierLink":"https://www.uniprot.org/uniprotkb/P35438/entry","name":"Grin1","description":"Glutamate receptor ionotropic, NMDA 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-293","complexName":"NMDA receptor complex, GluN1-GluN2D","organismName":"Mus musculus; 10090","description":"Voltage-gated ion channel of the ionotrophic glutamate receptor (iGluR) family that is characterised by high calcium permeability and very slow deactivation. Activated by simultaneous binding of glycine to GluN1 and L-glutamate to GluN2. Blocked by physiological concentrations of extracellular magnesium which is released by membrane depolarization. \r\n\r\nPredominantly post-synaptic receptor that mediates mostly the late/slow phase of the majority of the fast excitatory neurotransmission in the mammalian brain where it plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. \r\n\r\nCombinations of different receptor isoforms and their splice variants result in formation of ion channels with distinct spatiotemporal expression patterns and pharmacological and electrophysiological properties. \r\n\r\nReplacement of one or more subunits with GluN3A (A2AIR5) or GluN3B (Q91ZU9) subunits results in relatively Ca2+-impermeable cation channels that are resistant to Mg2+.","predictedComplex":false,"interactors":[{"ac":"EBI-2309422","identifier":"Q03391","identifierLink":"https://www.uniprot.org/uniprotkb/Q03391/entry","name":"Grin2d","description":"Glutamate receptor ionotropic, NMDA 2D","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-400084","identifier":"P35438","identifierLink":"https://www.uniprot.org/uniprotkb/P35438/entry","name":"Grin1","description":"Glutamate receptor ionotropic, NMDA 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-294","complexName":"NMDA receptor complex, GluN1-GluN2A-GluN2B","organismName":"Homo sapiens; 9606","description":"Voltage-gated ion channel of the ionotrophic glutamate receptor (iGluR) family that is characterised by high calcium permeability and very slow deactivation. Activated by simultaneous binding of glycine to GluN1 and L-glutamate to GluN2. Blocked by physiological concentrations of extracellular magnesium which is released by membrane depolarization. \r\n\r\nPredominantly post-synaptic receptor that mediates mostly the late/slow phase of the majority of the fast excitatory neurotransmission in the mammalian brain where it plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. \r\n\r\nCombinations of different receptor isoforms and their splice variants result in formation of ion channels with distinct spatiotemporal expression patterns and pharmacological and electrophysiological properties. \r\n\r\nReplacement of one or more subunits with GluN3A (Q8TCU5) or GluN3B (O60391) subunits results in relatively Ca2+-impermeable cation channels that are resistant to Mg2+. \r\n\r\nDysfunctional NMDA receptors are implicated in various neurological disorders and injuries including depression, schizophrenia, Alzheimer's and Parkinson's disease, chronic and neuropathic pain, as well as neuronal loss following ischaemia or stroke.","predictedComplex":false,"interactors":[{"ac":"EBI-2256942","identifier":"Q13224","identifierLink":"https://www.uniprot.org/uniprotkb/Q13224/entry","name":"GRIN2B","description":"Glutamate receptor ionotropic, NMDA 2B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7249937","identifier":"Q12879","identifierLink":"https://www.uniprot.org/uniprotkb/Q12879/entry","name":"GRIN2A","description":"Glutamate receptor ionotropic, NMDA 2A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-998542","identifier":"Q05586","identifierLink":"https://www.uniprot.org/uniprotkb/Q05586/entry","name":"GRIN1","description":"Glutamate receptor ionotropic, NMDA 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-295","complexName":"NMDA receptor complex, GluN1-GluN2A-GluN2B","organismName":"Rattus norvegicus; 10116","description":"Voltage-gated ion channel of the ionotrophic glutamate receptor (iGluR) family that is characterised by high calcium permeability and very slow deactivation. Activated by simultaneous binding of glycine to GluN1 and L-glutamate to GluN2. Blocked by physiological concentrations of extracellular magnesium which is released by membrane depolarization. \r\n\r\nPredominantly post-synaptic receptor that mediates mostly the late/slow phase of the majority of the fast excitatory neurotransmission in the mammalian brain where it plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. \r\n\r\nCombinations of different receptor isoforms and their splice variants result in formation of ion channels with distinct spatiotemporal expression patterns and pharmacological and electrophysiological properties. \r\n\r\nReplacement of one or more subunits with GluN3A (Q8TCU5) or GluN3B (O60391) subunits results in relatively Ca2+-impermeable cation channels that are resistant to Mg2+.","predictedComplex":false,"interactors":[{"ac":"EBI-396905","identifier":"Q00960","identifierLink":"https://www.uniprot.org/uniprotkb/Q00960/entry","name":"Grin2b","description":"Glutamate receptor ionotropic, NMDA 2B","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-630970","identifier":"Q00959","identifierLink":"https://www.uniprot.org/uniprotkb/Q00959/entry","name":"Grin2a","description":"Glutamate receptor ionotropic, NMDA 2A","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-877897","identifier":"P35439","identifierLink":"https://www.uniprot.org/uniprotkb/P35439/entry","name":"Grin1","description":"Glutamate receptor ionotropic, NMDA 1","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-296","complexName":"NMDA receptor complex, GluN1-GluN2A-GluN2B","organismName":"Mus musculus; 10090","description":"Voltage-gated ion channel of the ionotrophic glutamate receptor (iGluR) family that is characterised by high calcium permeability and very slow deactivation. Activated by simultaneous binding of glycine to GluN1 and L-glutamate to GluN2. Blocked by physiological concentrations of extracellular magnesium which is released by membrane depolarization. \r\n\r\nPredominantly post-synaptic receptor that mediates mostly the late/slow phase of the majority of the fast excitatory neurotransmission in the mammalian brain where it plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. \r\n\r\nCombinations of different receptor isoforms and their splice variants result in formation of ion channels with distinct spatiotemporal expression patterns and pharmacological and electrophysiological properties. \r\n\r\nReplacement of one or more subunits with GluN3A (Q8TCU5) or GluN3B (O60391) subunits results in relatively Ca2+-impermeable cation channels that are resistant to Mg2+.","predictedComplex":false,"interactors":[{"ac":"EBI-400084","identifier":"P35438","identifierLink":"https://www.uniprot.org/uniprotkb/P35438/entry","name":"Grin1","description":"Glutamate receptor ionotropic, NMDA 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-400115","identifier":"P35436","identifierLink":"https://www.uniprot.org/uniprotkb/P35436/entry","name":"Grin2a","description":"Glutamate receptor ionotropic, NMDA 2A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-400125","identifier":"Q01097","identifierLink":"https://www.uniprot.org/uniprotkb/Q01097/entry","name":"Grin2b","description":"Glutamate receptor ionotropic, NMDA 2B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-297","complexName":"CMG helicase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"DNA helicase that unwinds or rearranges duplex DNA during replication, recombination and repair. Surrounds the leading strand during DNA replication and recruits the DNA polymerase epsilon complex (CPX-2110) for leading-strand synthesis. CDC45 adds the GINS complex (CPX-1641) onto each MCM2-7 complex (CPX-2944) to form two active CMG helicases that surround each strand of parental DNA. CMG then translocates along single-strand DNA in the 3-prime to 5-prime direction for bidirectional replication. The complex unwinds duplex regions up to 500 bp.","predictedComplex":false,"interactors":[{"ac":"EBI-2315509","identifier":"CPX-1641","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-1641","name":"GINS complex","description":"GINS complex","stochiometry":null,"interactorType":"stable complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-4292","identifier":"Q08032","identifierLink":"https://www.uniprot.org/uniprotkb/Q08032/entry","name":"CDC45","description":"Cell division control protein 45","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10507","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-913756","identifier":"CPX-2944","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-2944","name":"MCM complex","description":"MCM2-7 heterohexamer","stochiometry":null,"interactorType":"stable complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-298","complexName":"BCL-XL complex","organismName":"Homo sapiens; 9606","description":"Anti-apoptotic key regulator of the intrinsic apoptotic pathway, preventing activation of the cell death mediators BAX and BAK, one or both of which are required for the execution phase of apoptosis, preventing the release of mitochondrial proteins. Normally cytosolic, binds to the membrane upon activation by caspase cleavage.","predictedComplex":false,"interactors":[{"ac":"EBI-287195","identifier":"Q07817-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q07817-1/entry","name":"BCL2L1","description":"Bcl-2-like protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-299","complexName":"BCL-XL complex","organismName":"Mus musculus; 10090","description":"Anti-apoptotic key regulator of the intrinsic apoptotic pathway, preventing activation of the cell death mediators BAX and BAK, one or both of which are required for the execution phase of apoptosis. Preventing the release of mitochondrial proteins. Normally cytosolic, binds to the membrane upon activation by caspase cleavage.","predictedComplex":false,"interactors":[{"ac":"EBI-526380","identifier":"Q64373-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q64373-1/entry","name":"Bcl2l1","description":"Bcl-2-like protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-300","complexName":"BCL-XL complex","organismName":"Rattus norvegicus; 10116","description":"Anti-apoptotic key regulator of the intrinsic apoptotic pathway, preventing activation of the cell death mediators BAX and BAK, one or both of which are required for the execution phase of apoptosis. Preventing the release of mitochondrial proteins. Normally cytosolic, binds to the membrane upon activation by caspase cleavage.","predictedComplex":false,"interactors":[{"ac":"EBI-287204","identifier":"P53563-1","identifierLink":"https://www.uniprot.org/uniprotkb/P53563-1/entry","name":"Bcl2l1","description":"Bcl-2-like protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-301","complexName":"GID E3 ubiquitin ligase complex, GID4 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"E3 ubiquitin ligase complex that triggers polyubiquitylation and subsequent proteasomal degradation of the gluconeogenic enzymes fructose-1,6-bisphosphatase (P09201), phosphoenolpyruvate carboxykinase (P10963) and  cytoplasmic malate dehydrogenase (P22133). The complex functions as the N-recognin of the GID-mediated proteolytic system termed the Pro/N-degron pathway and targets proteins by recognizing their N-terminal Pro residues or a Pro at position 2.","predictedComplex":false,"interactors":[{"ac":"EBI-20304","identifier":"P38263","identifierLink":"https://www.uniprot.org/uniprotkb/P38263/entry","name":"VID24","description":"GID complex substrate-recognition subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14534","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21727","identifier":"P25569","identifierLink":"https://www.uniprot.org/uniprotkb/P25569/entry","name":"GID7","description":"GID complex subunit 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22838","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-24173","identifier":"P53076","identifierLink":"https://www.uniprot.org/uniprotkb/P53076/entry","name":"VID30","description":"GID complex subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12864","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-24957","identifier":"P40547","identifierLink":"https://www.uniprot.org/uniprotkb/P40547/entry","name":"VID28","description":"GID complex subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15651","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25137","identifier":"P40492","identifierLink":"https://www.uniprot.org/uniprotkb/P40492/entry","name":"FYV10","description":"GID complex subunit 9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12170","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27276","identifier":"P40208","identifierLink":"https://www.uniprot.org/uniprotkb/P40208/entry","name":"GID8","description":"GID complex subunit 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12864","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-38868","identifier":"Q12508","identifierLink":"https://www.uniprot.org/uniprotkb/Q12508/entry","name":"RMD5","description":"E3 ubiquitin-protein ligase RMD5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12170","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-302","complexName":"Mitochondrial pyruvate carrier, fermentative isoform","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"The fermentative isoform of the mitochondrial pyruvate carrier resides in the mitochondrial inner membrane and mediates uptake of pyruvate into the mitochondrion during growth on fermentable carbon sources such as glucose.","predictedComplex":false,"interactors":[{"ac":"EBI-23845","identifier":"P53157","identifierLink":"https://www.uniprot.org/uniprotkb/P53157/entry","name":"MPC1","description":"Mitochondrial pyruvate carrier 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14154","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-24818","identifier":"P38857","identifierLink":"https://www.uniprot.org/uniprotkb/P38857/entry","name":"MPC2","description":"Mitochondrial pyruvate carrier 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14154","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-303","complexName":"Mitochondrial pyruvate carrier, respiratory isoform","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"The respiratory isoform of the mitochondrial pyruvate carrier resides in the mitochondrial inner membrane and mediates uptake of pyruvate into the mitochondrion during growth on respiratory carbon sources such as ethanol and glycerol.","predictedComplex":false,"interactors":[{"ac":"EBI-23568","identifier":"P53311","identifierLink":"https://www.uniprot.org/uniprotkb/P53311/entry","name":"MPC3","description":"Mitochondrial pyruvate carrier 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14154","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23845","identifier":"P53157","identifierLink":"https://www.uniprot.org/uniprotkb/P53157/entry","name":"MPC1","description":"Mitochondrial pyruvate carrier 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14154","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-304","complexName":"MCL1-PMAIP1 complex","organismName":"Homo sapiens; 9606","description":"Pro-apoptotic complex. BH3 domain-containing PMAIP1 interacts with and inhibits anti-apoptotic MCL-1.","predictedComplex":false,"interactors":[{"ac":"EBI-1003422","identifier":"Q07820","identifierLink":"https://www.uniprot.org/uniprotkb/Q07820/entry","name":"MCL1","description":"Induced myeloid leukemia cell differentiation protein Mcl-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11256","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-707392","identifier":"Q13794","identifierLink":"https://www.uniprot.org/uniprotkb/Q13794/entry","name":"PMAIP1","description":"Phorbol-12-myristate-13-acetate-induced protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14299","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-305","complexName":"MCL1:PMAIP1 complex","organismName":"Mus musculus; 10090","description":"Pro-apoptotic complex. BH3 domain-containing PMAIP1 interacts with and inhibits anti-apoptotic MCL-1.","predictedComplex":false,"interactors":[{"ac":"EBI-707292","identifier":"P97287","identifierLink":"https://www.uniprot.org/uniprotkb/P97287/entry","name":"Mcl1","description":"Induced myeloid leukemia cell differentiation protein Mcl-1 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11256","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-709183","identifier":"Q9JM54","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JM54/entry","name":"Pmaip1","description":"Phorbol-12-myristate-13-acetate-induced protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14299","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-306","complexName":"MCL1:PMAIP1 complex","organismName":"Rattus norvegicus; 10116","description":"Pro-apoptotic complex. BH3 domain-containing PMAIP1 interacts with and inhibits anti-apoptotic MCL-1.","predictedComplex":false,"interactors":[{"ac":"EBI-11358076","identifier":"Q5U777","identifierLink":"https://www.uniprot.org/uniprotkb/Q5U777/entry","name":"Pmaip1","description":"Phorbol-12-myristate-13-acetate-induced protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR14299","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-78982","identifier":"Q9Z1P3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z1P3/entry","name":"Mcl1","description":"Induced myeloid leukemia cell differentiation protein Mcl-1 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11256","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-307","complexName":"Endoplasmic Reticulum Membrane Complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for transfer of phosphatidylserine (PS) from the endoplasmic reticulum to mitochondria. Complex is tethered to the ER and mitochondria through Tom5 (P80967).","predictedComplex":false,"interactors":[{"ac":"EBI-21744","identifier":"P25574","identifierLink":"https://www.uniprot.org/uniprotkb/P25574/entry","name":"EMC1","description":"ER membrane protein complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21573","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2345238","identifier":"Q12431","identifierLink":"https://www.uniprot.org/uniprotkb/Q12431/entry","name":"EMC6","description":"ER membrane protein complex subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR20994","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-24977","identifier":"P40540","identifierLink":"https://www.uniprot.org/uniprotkb/P40540/entry","name":"EMC5","description":"ER membrane protein complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28144","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25568","identifier":"P47133","identifierLink":"https://www.uniprot.org/uniprotkb/P47133/entry","name":"EMC2","description":"ER membrane protein complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12760","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27005","identifier":"P36039","identifierLink":"https://www.uniprot.org/uniprotkb/P36039/entry","name":"EMC3","description":"ER membrane protein complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13116","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3731930","identifier":"P53073","identifierLink":"https://www.uniprot.org/uniprotkb/P53073/entry","name":"EMC4","description":"ER membrane protein complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19315","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-308","complexName":"UV DNA damage recognition complex DBB1-DBB2","organismName":"Homo sapiens; 9606","description":"Mediates the initial detection of UV light-induced cyclobutane pyrimidine photodimers as part of the nucleotide excision repair (NER) process. Performs a 3D search mechanism, examining sites on DNA in discrete steps before binding as long-lived, non-motile dimers at sites of damage. The complex then constitutively associates with Cullin4A or 4B and RBX1 to form an E3 ligase (CPX-477/CPX-648).","predictedComplex":false,"interactors":[{"ac":"EBI-1176171","identifier":"Q92466","identifierLink":"https://www.uniprot.org/uniprotkb/Q92466/entry","name":"DDB2","description":"DNA damage-binding protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15169","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-309","complexName":"BIK:BCL-w complex","organismName":"Homo sapiens; 9606","description":"Binding of BCL2L2 inhibits the pro-apoptotic activity of BIK.","predictedComplex":false,"interactors":[{"ac":"EBI-700794","identifier":"Q13323","identifierLink":"https://www.uniprot.org/uniprotkb/Q13323/entry","name":"BIK","description":"Bcl-2-interacting killer","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15018","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-707714","identifier":"Q92843","identifierLink":"https://www.uniprot.org/uniprotkb/Q92843/entry","name":"BCL2L2","description":"Bcl-2-like protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11256","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-310","complexName":"BIK:BCL-w complex","organismName":"Mus musculus; 10090","description":"Binding of BCL2L2 inhibits the pro-apoptotic activity of BIK.","predictedComplex":false,"interactors":[{"ac":"EBI-11421662","identifier":"O70337","identifierLink":"https://www.uniprot.org/uniprotkb/O70337/entry","name":"Bik","description":"Bcl-2-interacting killer","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15018","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11421686","identifier":"P70345","identifierLink":"https://www.uniprot.org/uniprotkb/P70345/entry","name":"Bcl2l2","description":"Bcl-2-like protein 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11256","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-311","complexName":"BIK:BCL-w complex","organismName":"Rattus norvegicus; 10116","description":"Binding of BCL2L2 inhibits the pro-apoptotic activity of BIK.","predictedComplex":false,"interactors":[{"ac":"EBI-11421741","identifier":"A6HT97","identifierLink":"https://www.uniprot.org/uniprotkb/A6HT97/entry","name":"Bik","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-79061","identifier":"O88996","identifierLink":"https://www.uniprot.org/uniprotkb/O88996/entry","name":"Bcl2l2","description":"Bcl-2-like protein 2","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11256","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-312","complexName":"Amiloride-sensitive sodium channel complex, delta-alpha-beta-gamma","organismName":"Homo sapiens; 9606","description":"Inward cation channel with high sodium selectivity but also permeable to lithium. Activated under low extracellular sodium concentrations and low extracellular pH and self-inhibited by high extracellular sodium concentrations. Activation is dependent on proteolytic cleavage of alpha and gamma subunits, post-translational modifications (such as glycosylation of beta subunit and palmitoylation) and possibly cyclic nucleotides that lift self-inhibition. Regulated by hormones such as aldosterone and vasopressin and inhibited by the diuretic amiloride. Although the channel activity itself is not voltage-gated, ameloride-sensitivity may be voltage-dependent. Channel gating and conductance are comparatively slow. \r\n\r\nPlays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid (ASL) homeostasis, which is important for proper clearance of mucus and pathogens. Mutations leading to a loss of ASL homeostatis are a trigger for cystic fibrosis. The inward sodium transport may trigger action potentials in neurons by gradually depolarizing membrane potentials. In nephrons may also be activated by shear stress potentially changing the conformation of the bulky extracellular loop or the transmembrane domains and thereby increasing channel opening times. May also play a role in salt and sour taste perception. \r\n\r\nFound in the apical membrane of many epithelial cell types, especially in the Aldosterone Sensitive Distal Nephron (ASDN), kidney, colon, lung and sweat glands but also in heart, liver, pancreas, skeletal muscle and blood leukocytes. Also expressed in vascular endothelia where their mechanical properties and function differ from epithelial sodium channels (ENaCs) in other tissues: vascular endothelia are ‘leaky’, allowing passive sodium transport through the membrane. Here, ENaCs are activated by increased external sodium concentrations that enhances the sodium influx into the cell. May stabilize F-actin through strengthening of the inter-subunits causing swelling or stiffening of endothelia and which can ultimately lead to hypertension.","predictedComplex":false,"interactors":[{"ac":"EBI-2547114","identifier":"P51172","identifierLink":"https://www.uniprot.org/uniprotkb/P51172/entry","name":"SCNN1D","description":"Epithelial sodium channel subunit delta","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11690","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2547187","identifier":"P51168","identifierLink":"https://www.uniprot.org/uniprotkb/P51168/entry","name":"SCNN1B","description":"Epithelial sodium channel subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11690","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2547354","identifier":"P51170","identifierLink":"https://www.uniprot.org/uniprotkb/P51170/entry","name":"SCNN1G","description":"Epithelial sodium channel subunit gamma","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11690","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7845444","identifier":"P37088","identifierLink":"https://www.uniprot.org/uniprotkb/P37088/entry","name":"SCNN1A","description":"Epithelial sodium channel subunit alpha","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11690","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-313","complexName":"Amiloride-sensitive sodium channel complex, delta-beta-gamma","organismName":"Homo sapiens; 9606","description":"Inward cation channel with high sodium selectivity but also permeable to lithium. Activated under low extracellular sodium concentrations and low extracellular pH and self-inhibited by high extracellular sodium concentrations. Activation is dependent on proteolytic cleavage of alpha and gamma subunits, post-translational modifications (such as glycosylation of beta subunit and palmitoylation) and possibly cyclic nucleotides that lift self-inhibition. Regulated by hormones such as aldosterone and vasopressin and inhibited by the diuretic amiloride. Although the channel activity itself is not voltage-gated, ameloride-sensitivity may be voltage-dependent. Channel gating and conductance are comparatively slow. \r\n\r\nPlays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid (ASL) homeostasis, which is important for proper clearance of mucus and pathogens. Mutations leading to a loss of ASL homeostatis are a trigger for cystic fibrosis. The inward sodium transport may trigger action potentials in neurons by gradually depolarizing membrane potentials. In nephrons may also be activated by shear stress potentially changing the conformation of the bulky extracellular loop or the transmembrane domains and thereby increasing channel opening times. May also play a role in salt and sour taste perception. \r\n\r\nFound in the apical membrane of many epithelial cell types, especially in the Aldosterone Sensitive Distal Nephron (ASDN), kidney, colon, lung and sweat glands but also in heart, liver, pancreas, skeletal muscle and blood leukocytes. Also expressed in vascular endothelia where their mechanical properties and function differ from epithelial sodium channels (ENaCs) in other tissues: vascular endothelia are ‘leaky’, allowing passive sodium transport through the membrane. Here, ENaCs are activated by increased external sodium concentrations that enhances the sodium influx into the cell. May stabilize F-actin through strengthening of the inter-subunits","predictedComplex":false,"interactors":[{"ac":"EBI-2547114","identifier":"P51172","identifierLink":"https://www.uniprot.org/uniprotkb/P51172/entry","name":"SCNN1D","description":"Epithelial sodium channel subunit delta","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11690","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2547187","identifier":"P51168","identifierLink":"https://www.uniprot.org/uniprotkb/P51168/entry","name":"SCNN1B","description":"Epithelial sodium channel subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11690","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2547354","identifier":"P51170","identifierLink":"https://www.uniprot.org/uniprotkb/P51170/entry","name":"SCNN1G","description":"Epithelial sodium channel subunit gamma","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11690","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-314","complexName":"Amiloride-sensitive sodium channel complex, alpha-beta-gamma","organismName":"Rattus norvegicus; 10116","description":"Inward cation channel with high sodium selectivity but also permeable to lithium. Activated under low extracellular sodium concentrations and self-inhibited by high extracellular sodium concentrations. Activation is dependent on proteolytic cleavage of alpha and gamma subunits, post-translational modifications (such as glycosylation of beta subunit and palmitoylation) and possibly cyclic nucleotides that lift self-inhibition. Regulated by hormones such as aldosterone and vasopressin and inhibited by the diuretic amiloride. Although the channel activity itself is not voltage-gated, ameloride-sensitivity may be voltage-dependent. Channel gating and conductance are comparatively slow. \r\n\r\nPlays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid (ASL) homeostasis, which is important for proper clearance of mucus and pathogens. Mutations leading to a loss of ASL homeostatis are a trigger for cystic fibrosis. The inward sodium transport may trigger action potentials in neurons by gradually depolarizing membrane potentials. In nephrons may also be activated by shear stress potentially changing the conformation of the bulky extracellular loop or the transmembrane domains and thereby increasing channel opening times. May also play a role in salt and sour taste perception. \r\n\r\nFound in the apical membrane of many epithelial cell types, especially in the Aldosterone Sensitive Distal Nephron (ASDN), kidney, colon, lung and sweat glands but also in heart, liver, pancreas, skeletal muscle and blood leukocytes. Also expressed in vascular endothelia where their mechanical properties and function differ from epithelial sodium channels (ENaCs) in other tissues: vascular endothelia are ‘leaky’, allowing passive sodium transport through the membrane. Here, ENaCs are activated by increased external sodium concentrations that enhances the sodium influx into the cell. May stabilize F-actin through strengthening of the inter-subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-11422003","identifier":"P37089","identifierLink":"https://www.uniprot.org/uniprotkb/P37089/entry","name":"Scnn1a","description":"Epithelial sodium channel subunit alpha","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11690","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11422032","identifier":"P37090","identifierLink":"https://www.uniprot.org/uniprotkb/P37090/entry","name":"Scnn1b","description":"Epithelial sodium channel subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11690","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11422068","identifier":"P37091","identifierLink":"https://www.uniprot.org/uniprotkb/P37091/entry","name":"Scnn1g","description":"Epithelial sodium channel subunit gamma","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11690","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-315","complexName":"Amiloride-sensitive sodium channel complex, alpha-beta-gamma","organismName":"Mus musculus; 10090","description":"Inward cation channel with high sodium selectivity but also permeable to lithium. Activated under low extracellular sodium concentrations and self-inhibited by high extracellular sodium concentrations. Activation is dependent on proteolytic cleavage of alpha and gamma subunits, post-translational modifications (such as glycosylation of beta subunit and palmitoylation) and possibly cyclic nucleotides that lift self-inhibition. Regulated by hormones such as aldosterone and vasopressin and inhibited by the diuretic amiloride. Although the channel activity itself is not voltage-gated, ameloride-sensitivity may be voltage-dependent. Channel gating and conductance are comparatively slow. \r\n\r\nPlays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid (ASL) homeostasis, which is important for proper clearance of mucus and pathogens. Mutations leading to a loss of ASL homeostatis are a trigger for cystic fibrosis. The inward sodium transport may trigger action potentials in neurons by gradually depolarizing membrane potentials. In nephrons may also be activated by shear stress potentially changing the conformation of the bulky extracellular loop or the transmembrane domains and thereby increasing channel opening times. May also play a role in salt and sour taste perception. \r\n\r\nFound in the apical membrane of many epithelial cell types, especially in the Aldosterone Sensitive Distal Nephron (ASDN), kidney, colon, lung and sweat glands but also in heart, liver, pancreas, skeletal muscle and blood leukocytes. Also expressed in vascular endothelia where their mechanical properties and function differ from epithelial sodium channels (ENaCs) in other tissues: vascular endothelia are ‘leaky’, allowing passive sodium transport through the membrane. Here, ENaCs are activated by increased external sodium concentrations that enhances the sodium influx into the cell. May stabilize F-actin through strengthening of the inter-subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-11424565","identifier":"Q61180","identifierLink":"https://www.uniprot.org/uniprotkb/Q61180/entry","name":"Scnn1a","description":"Epithelial sodium channel subunit alpha","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11690","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11424593","identifier":"Q9WU38","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WU38/entry","name":"Scnn1b","description":"Epithelial sodium channel subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11690","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11424624","identifier":"Q9WU39","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WU39/entry","name":"Scnn1g","description":"Epithelial sodium channel subunit gamma","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11690","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-316","complexName":"beta1-catenin - LEF1 complex","organismName":"Homo sapiens; 9606","description":"Transcription factor complex that activates Wnt responsive genes. Binds DNA in a sequence-specific manner. Repressed by TLE1 (Q04724), TLE2 (Q04725), TLE3 (Q04726) and TLE4 (Q04727).","predictedComplex":false,"interactors":[{"ac":"EBI-491549","identifier":"P35222","identifierLink":"https://www.uniprot.org/uniprotkb/P35222/entry","name":"CTNNB1","description":"Catenin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45976","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-926131","identifier":"Q9UJU2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UJU2/entry","name":"LEF1","description":"Lymphoid enhancer-binding factor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10373","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-317","complexName":"Formate hydrogenlyase-H/Hydrogenase-3 complex","organismName":"Escherichia coli (strain K12); 83333","description":"Role in the mixed-acid fermentation that takes place under anaerobic conditions, ultimately producing molecular hydrogen. Consists of two enzymatic activities: a formate dehydrogenase‐H (encoded by fdhF) for producing 2H+, 2 electrons and CO2 from formate and HycE for synthesizing molecular hydrogen (H2) from 2H+ and 2 electrons. HycE catalyzes production of H2 even at high partial pressures of H2.","predictedComplex":false,"interactors":[{"ac":"EBI-1117285","identifier":"P16432","identifierLink":"https://www.uniprot.org/uniprotkb/P16432/entry","name":"hycF","description":"Formate hydrogenlyase subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10849","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1121603","identifier":"P07658","identifierLink":"https://www.uniprot.org/uniprotkb/P07658/entry","name":"fdhF","description":"Formate dehydrogenase H","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11420781","identifier":"P0AAK1","identifierLink":"https://www.uniprot.org/uniprotkb/P0AAK1/entry","name":"hycB","description":"Formate hydrogenlyase subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11425617","identifier":"P16430","identifierLink":"https://www.uniprot.org/uniprotkb/P16430/entry","name":"hycD","description":"Formate hydrogenlyase subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43359","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11426020","identifier":"CHEBI:60539","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60539","name":"mo(=o)-bis(molybdopterin guanine dinucleotide)(4-)","description":"Mo(=O)-bis(molybdopterin guanine dinucleotide)(4-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":"minValue: 7, maxValue: 7","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2296617","identifier":"CHEBI:49786","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49786","name":"nickel(2+)","description":"Nickel(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-541977","identifier":"P16433","identifierLink":"https://www.uniprot.org/uniprotkb/P16433/entry","name":"hycG","description":"Formate hydrogenlyase subunit 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42989","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-552702","identifier":"P16431","identifierLink":"https://www.uniprot.org/uniprotkb/P16431/entry","name":"hycE","description":"Formate hydrogenlyase subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43485","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-556705","identifier":"P16429","identifierLink":"https://www.uniprot.org/uniprotkb/P16429/entry","name":"hycC","description":"Formate hydrogenlyase subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42682","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-318","complexName":"beta1-catenin - LEF1 complex","organismName":"Mus musculus; 10090","description":"Transcription factor complex that activates Wnt responsive genes. Binds DNA in a sequence-specific manner. Repressed by TLE1 (Q62440), TLE2 (Q9WVB2), TLE3 (Q08122) and TLE4 (Q62441).","predictedComplex":false,"interactors":[{"ac":"EBI-397872","identifier":"Q02248","identifierLink":"https://www.uniprot.org/uniprotkb/Q02248/entry","name":"Ctnnb1","description":"Catenin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45976","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-984464","identifier":"P27782","identifierLink":"https://www.uniprot.org/uniprotkb/P27782/entry","name":"Lef1","description":"Lymphoid enhancer-binding factor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10373","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-319","complexName":"Trimethylamine-N-oxide reductase TorAC complex","organismName":"Escherichia coli (strain K12); 83333","description":"Reduces trimethylamine-N-oxide (TMAO) to trimethylamine, enabling its use under anaerobic conditions as an electron acceptor for the oxidation of organic substrates and the production of energy. TorAC is also present under aerobic conditions, when production of alkaline trimethylamine may balance the acidification of the cell caused by generation of acetic acid caused by glycerol utilization.","predictedComplex":false,"interactors":[{"ac":"EBI-11426020","identifier":"CHEBI:60539","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60539","name":"mo(=o)-bis(molybdopterin guanine dinucleotide)(4-)","description":"Mo(=O)-bis(molybdopterin guanine dinucleotide)(4-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-553710","identifier":"P33226","identifierLink":"https://www.uniprot.org/uniprotkb/P33226/entry","name":"torC","description":"Cytochrome c-type protein TorC","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-557008","identifier":"P33225","identifierLink":"https://www.uniprot.org/uniprotkb/P33225/entry","name":"torA","description":"Trimethylamine-N-oxide reductase 1","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 5, maxValue: 5","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-320","complexName":"DmaABC DMSO reductase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Terminal reductase required for the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS) and that of a broad array of S- and N-oxide compounds during anaerobic growth. Induced in the presence of fumarate. The expression of the enzyme is dependent on molybdenum.","predictedComplex":false,"interactors":[{"ac":"EBI-1120825","identifier":"P18776","identifierLink":"https://www.uniprot.org/uniprotkb/P18776/entry","name":"dmsB","description":"Anaerobic dimethyl sulfoxide reductase chain B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11426020","identifier":"CHEBI:60539","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60539","name":"mo(=o)-bis(molybdopterin guanine dinucleotide)(4-)","description":"Mo(=O)-bis(molybdopterin guanine dinucleotide)(4-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-11464414","identifier":"P18777","identifierLink":"https://www.uniprot.org/uniprotkb/P18777/entry","name":"dmsC","description":"Anaerobic dimethyl sulfoxide reductase chain C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR38095","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-4411104","identifier":"P18775","identifierLink":"https://www.uniprot.org/uniprotkb/P18775/entry","name":"dmsA","description":"Dimethyl sulfoxide reductase DmsA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-321","complexName":"Positive transcription elongation factor B, CDK9-cyclinT2a complex","organismName":"Homo sapiens; 9606","description":"A serine kinase complex that phosphorylates elongation pausing factors such as DSIF (CPX-891) and NELF (CPX-6267) and Ser-2 and Ser-5 of RNA polymerase II (RNA Pol II), thus positively regulating productive mRNA elongation through the gene body after promoter-proximal pausing of RNA Pol II. Involved in cotranscriptional histone modification, mRNA processing mRNA export and myocyte differentiation. Potential target of anticancer drugs. \r\n\r\nBinds to the transactivation domain of the HIV-2 and SIV (not HIV-1) nuclear transcriptional activator, Tat, thereby increasing Tat's affinity for the transactivating response RNA element (TAR RNA) leading to RNA Pol II activation and transcription of viral genes.","predictedComplex":false,"interactors":[{"ac":"EBI-1383449","identifier":"P50750","identifierLink":"https://www.uniprot.org/uniprotkb/P50750/entry","name":"CDK9","description":"Cyclin-dependent kinase 9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9077112","identifier":"O60583-2","identifierLink":"https://www.uniprot.org/uniprotkb/O60583-2/entry","name":"CCNT2","description":"Cyclin-T2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-322","complexName":"Positive transcription elongation factor B, CDK9-cyclinT2b complex","organismName":"Homo sapiens; 9606","description":"A serine kinase complex that phosphorylates elongation pausing factors such as DSIF (CPX-891) and NELF (CPX-6267) and Ser- 2 and Ser-5 of RNA polymerase II (RNA Pol II), thus positively regulating productive mRNA elongation through the gene body after promoter-proximal pausing of RNA Pol II. Involved in cotranscriptional histone modification, mRNA processing mRNA export and myocyte differentiation. Potential target of anticancer drugs. \r\n\r\nBinds to the transactivation domain of the HIV-2 and SIV (not HIV-1) nuclear transcriptional activator, Tat, thereby increasing Tat's affinity for the transactivating response RNA element (TAR RNA) leading to RNA Pol II activation and transcription of viral genes.","predictedComplex":false,"interactors":[{"ac":"EBI-1383449","identifier":"P50750","identifierLink":"https://www.uniprot.org/uniprotkb/P50750/entry","name":"CDK9","description":"Cyclin-dependent kinase 9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9077118","identifier":"O60583-1","identifierLink":"https://www.uniprot.org/uniprotkb/O60583-1/entry","name":"CCNT2","description":"Cyclin-T2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-323","complexName":"Positive transcription elongation factor B, CDK9-cyclinT2a complex","organismName":"Mus musculus; 10090","description":"A serine kinase complex that phosphorylates elongation pausing factors (e.g. DSIF - DRB sensitivity-inducing factor and NELF - negative elongation factor) and Ser- 2 and Ser-5 of RNA polymerase II (RNA Pol II), thus positively regulating productive mRNA elongation through the gene body after promoter-proximal pausing of RNA Pol II. Involved in cotranscriptional histone modification, mRNA processing mRNA export and myocyte differentiation.","predictedComplex":false,"interactors":[{"ac":"EBI-15480846","identifier":"Q7TQK0-2","identifierLink":"https://www.uniprot.org/uniprotkb/Q7TQK0-2/entry","name":"Ccnt2","description":"Cyclin-T2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-2654963","identifier":"Q99J95","identifierLink":"https://www.uniprot.org/uniprotkb/Q99J95/entry","name":"Cdk9","description":"Cyclin-dependent kinase 9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-324","complexName":"Positive transcription elongation factor B, CDK9-cyclinT2b complex","organismName":"Mus musculus; 10090","description":"A serine kinase complex that phosphorylates elongation pausing factors (e.g. DSIF - DRB sensitivity-inducing factor and NELF - negative elongation factor) and Ser-2  and Ser-5 of RNA polymerase II (RNA Pol II), thus positively regulating productive mRNA elongation through the gene body after promoter-proximal pausing of RNA Pol II. Involved in cotranscriptional histone modification, mRNA processing mRNA export and myocyte differentiation.","predictedComplex":false,"interactors":[{"ac":"EBI-25746326","identifier":"Q7TQK0-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q7TQK0-1/entry","name":"Ccnt2","description":"Cyclin-T2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-2654963","identifier":"Q99J95","identifierLink":"https://www.uniprot.org/uniprotkb/Q99J95/entry","name":"Cdk9","description":"Cyclin-dependent kinase 9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-325","complexName":"Glutathione hydrolase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Glutathione hydrolase/Glutamine Amidotransferase II complex responsible for glutathione degradation. Both DUG2 and DUG3 are depressed under sulfur limitation conditions. Although neither protein alone can cleave glutathione, the complex degrades glutathione by cleaving of the gamma-glutamyl linkage. DUG3 has the GATase activity, while DUG2 probably acts as a scaffold protein, bringing two DUG3 proteins together.","predictedComplex":false,"interactors":[{"ac":"EBI-21176","identifier":"P38149","identifierLink":"https://www.uniprot.org/uniprotkb/P38149/entry","name":"DUG2","description":"Probable di- and tripeptidase DUG2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43270","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29079","identifier":"P53871","identifierLink":"https://www.uniprot.org/uniprotkb/P53871/entry","name":"DUG3","description":"Probable glutamine amidotransferase DUG3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43187","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-326","complexName":"Cyclin M-CDK10 complex","organismName":"Homo sapiens; 9606","description":"Cyclin-dependent protein kinase. Acts as a cell cycle regulator in some cells and as a tumor suppressor in others. Inhibits the transcriptional activity of Ets2 (P15036) by positively controlling its degradation by the proteasome, through the phosphorylation of Ser-220 and Ser-225.","predictedComplex":false,"interactors":[{"ac":"EBI-11507283","identifier":"Q15131-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q15131-1/entry","name":"CDK10","description":"Cyclin-dependent kinase 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-3925043","identifier":"Q8N1B3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N1B3/entry","name":"CCNQ","description":"Cyclin-Q","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-327","complexName":"Cyclin M-CDK10 complex","organismName":"Mus musculus; 10090","description":"Cyclin-dependent protein kinase. Acts as a cell cycle regulator in some cells and as a tumor suppressor in others. Inhibits the transcriptional activity of Ets2 (P15037) by positively controlling its degradation by the proteasome, through the phosphorylation of Ser-220 and Ser-225.","predictedComplex":false,"interactors":[{"ac":"EBI-11507809","identifier":"Q3UMM4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3UMM4/entry","name":"Cdk10","description":"Cyclin-dependent kinase 10","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11507831","identifier":"Q8QZR8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8QZR8/entry","name":"Ccnq","description":"Cyclin-Q","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-328","complexName":"Atg12-Atg5-Atg16l1 complex","organismName":"Mus musculus; 10090","description":"Essential for autophagy during nutrient deprivation, a catabolic process that sequesters undesired cellular material into autophagosomes for delivery to lysosomes for degradation. Required for the elongation of isolation membranes (phagophores).\r\n\r\nActs as an E3-like enzyme to recruit the E2-like protein Atg3, conjugated to LC3-I, to the endoplasmic reticulum-derived  omegasome. Atg3 binds to and is activated by Atg12, facilitating conjugation of the LC3 to phosphatidylethanolamine, thus converting LC3-I to LC3-II. Therefore, the site of Atg12-Atg5-Atg16l1 complex recruitment determines the site of LC3-II formation. The LC3 family is required for phagophore expansion, closure, and cargo recruitment.","predictedComplex":false,"interactors":[{"ac":"EBI-2911788","identifier":"Q9CQY1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQY1/entry","name":"Atg12","description":"Ubiquitin-like protein ATG12","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13385","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2911848","identifier":"Q99J83","identifierLink":"https://www.uniprot.org/uniprotkb/Q99J83/entry","name":"Atg5","description":"Autophagy protein 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-769195","identifier":"Q8C0J2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C0J2/entry","name":"Atg16l1","description":"Autophagy-related protein 16-1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR19878","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-329","complexName":"ESCRT-III complex","organismName":"Homo sapiens; 9606","description":"The ESCRT machinery, consisting of ESCRT-0, -I, -II (CPX-2506.), -III (this complex) and -IV (VPS4A/B complex, CPX-338) has been implicated in membrane scission steps, transforming a single, continuous bilayer into two distinct bilayers, either from within the neck of a vesicle budding away from the cytoplasm or from within a membrane tubule, while segregating cargo throughout the process. Membrane fission processes include: a) the sorting of multivesicular bodies (MVB) in the endocytic pathway; cargoes destined for inclusion into the MVB pathway are covalently modified with ubiquitin, recognized by ubiquitin-binding domains in the early ESCRTs (ESCRT-0, -I, and -II) and sequestered into endosomal microdomains that bud into the endosome as intralumenal vesicles aided by ESCRT-III, b) downregulation of cell-surface receptors, c) repair of plasma membrane wounds, d) abscission of the cellular bridge during cytokineses, d) nuclear envelope sealing by annular fusion and e) budding of virions (especially HIV-1) from the plasma membrane. The ESCRT machinery seems to play an indirect role in the proper functioning of cellular polarity and migration, the miRNA machinery and gene expression regulation. \r\n\r\nESCRT-0 binds to and clusters ubiquitinated cargo for delivery into MVBs, and recruits clathrin, ubiquitin ligases, and deubiquitinating enzymes.. ESCRT-0 recruits ESCRT-I which engages ESCRT-II to nucleate ESCRT-III polymerization. VPS4A/B complex, also known as ESCRT-IV, disassembles ESCRT-III to recycle its subunits. The ESCRT-III complex facilitates changes in membrane architecture by oligomerizing to form spiral, filament-like tubules, accumulation of which is associated with membrane constriction and fission. Disassembly of ESCRT-III by VPS4A/B may be a required step for fission. \r\n\r\nCHMP1A, CHMP1B and CHMP5 are sometimes regarded as ESCRT-III accessory proteins rather than full complex members, suggesting that multiple variants with different core components and/or associated auxiliary factors may exist within the same cell and be active in different processes.","predictedComplex":false,"interactors":[{"ac":"EBI-1049648","identifier":"Q96FZ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q96FZ7/entry","name":"CHMP6","description":"Charged multivesicular body protein 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1057156","identifier":"Q9HD42","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HD42/entry","name":"CHMP1A","description":"Charged multivesicular body protein 1a","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1221015","identifier":"Q96CF2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96CF2/entry","name":"CHMP4C","description":"Charged multivesicular body protein 4c","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2118090","identifier":"Q7LBR1","identifierLink":"https://www.uniprot.org/uniprotkb/Q7LBR1/entry","name":"CHMP1B","description":"Charged multivesicular body protein 1b","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2118119","identifier":"Q9Y3E7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3E7/entry","name":"CHMP3","description":"Charged multivesicular body protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2692789","identifier":"O43633","identifierLink":"https://www.uniprot.org/uniprotkb/O43633/entry","name":"CHMP2A","description":"Charged multivesicular body protein 2a","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-718324","identifier":"Q9UQN3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UQN3/entry","name":"CHMP2B","description":"Charged multivesicular body protein 2b","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-747981","identifier":"Q9BY43","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BY43/entry","name":"CHMP4A","description":"Charged multivesicular body protein 4a","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749253","identifier":"Q8WUX9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WUX9/entry","name":"CHMP7","description":"Charged multivesicular body protein 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749627","identifier":"Q9H444","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H444/entry","name":"CHMP4B","description":"Charged multivesicular body protein 4b","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-751303","identifier":"Q9NZZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZZ3/entry","name":"CHMP5","description":"Charged multivesicular body protein 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-330","complexName":"Cyclin C-CDK3 complex","organismName":"Homo sapiens; 9606","description":"Cyclin-dependent protein kinase complex. Phosphorylates Rb at Ser-807 and Ser-811, resulting in activation of E2F transcription factors which causes induction of transcription and transition from G0 to G1 of the cell cycle. However, most laboratory mouse strains are naturally deficient in CDK3 suggesting this activity is redundant to that of CDK1 and CDK2. Cyclin-C-CDK3  also phosphorylates the intracellular domain of NOTCH1 leading to its SCF-Fbw7-dependent ubiquitination and proteasome-driven degradation, thus potentially playing a role in self-renewal and differentiation of multiple cell types.","predictedComplex":false,"interactors":[{"ac":"EBI-1245761","identifier":"Q00526","identifierLink":"https://www.uniprot.org/uniprotkb/Q00526/entry","name":"CDK3","description":"Cyclin-dependent kinase 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395261","identifier":"P24863","identifierLink":"https://www.uniprot.org/uniprotkb/P24863/entry","name":"CCNC","description":"Cyclin-C","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-331","complexName":"Cyclin C-CDK3 complex","organismName":"Mus musculus; 10090","description":"Cyclin-dependent protein kinase complex. Phosphorylates Rb at Ser-800 and Ser-804, resulting in activation of E2F transcription factors which causes induction of transcription and transition from G0 to G1 of the cell cycle. However, most laboratory mouse strains are naturally deficient in Cdk3 suggesting this activity is redundant to that of Cdk1 and Cdk2. Cyclin-C-Cdk3  also phosphorylates the intracellular domain of Notch1 leading to its SCF-Fbw7-dependent ubiquitination and proteasome-driven degradation, thus potentially playing a role in self-renewal and differentiation of multiple cell types.","predictedComplex":false,"interactors":[{"ac":"EBI-11510117","identifier":"Q80YP0","identifierLink":"https://www.uniprot.org/uniprotkb/Q80YP0/entry","name":"Cdk3","description":"Cyclin-dependent kinase 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9847822","identifier":"Q62447","identifierLink":"https://www.uniprot.org/uniprotkb/Q62447/entry","name":"Ccnc","description":"Cyclin-C","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-332","complexName":"ESCRT-III complex, variant Chmp1b1","organismName":"Mus musculus; 10090","description":"The ESCRT machinery has been implicated in membrane scission steps, transforming a single, continuous bilayer into two distinct bilayers, either from within the neck of a vesicle budding away from the cytoplasm or from within a membrane tubule, while segregating cargo throughout the process. Membrane fission processes include: a) the sorting of multivesicular bodies (MVB) in the endocytic pathway; cargoes destined for inclusion into the MVB pathway are covalently modified with ubiquitin, recognized by ubiquitin-binding domains in the early ESCRTs (ESCRT-0, -I, and -II) and sequestered into endosomal microdomains that bud into the endosome as intralumenal vesicles aided by ESCRT-III, b) downregulation of cell-surface receptors, c) repair of plasma membrane wounds, d) abscission of the cellular bridge during cytokineses, d) nuclear envelope sealing by annular fusion and e) budding of virions from the plasma membrane. The ESCRT machinery seems to play an indirect role in the proper functioning of cellular polarity and migration, the miRNA machinery and gene expression regulation. \r\n\r\nESCRT-0 recruits ESCRT-I which engages ESCRT-II to nucleate ESCRT-III polymerization. VPS4A/B complex, also known as ESCRT-IV, disassembles ESCRT-III to recycle its subunits. The ESCRT-III complex facilitates changes in membrane architecture by oligomerizing to form spiral, filament-like tubules, accumulation of which is associated with membrane constriction and fission. Disassembly of ESCRT-III by VPS4A/B may be a required step for fission. \r\n\r\nCHMP1A, CHMP1B and CHMP5 are sometimes regarded as ESCRT-III accessory proteins rather than full complex members, suggesting that multiple variants with different core components and/or associated auxiliary factors may exist within the same cell and be active in different processes.","predictedComplex":false,"interactors":[{"ac":"EBI-11116446","identifier":"Q9D7F7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D7F7/entry","name":"Chmp4c","description":"Charged multivesicular body protein 4c","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11116518","identifier":"P0C0A3","identifierLink":"https://www.uniprot.org/uniprotkb/P0C0A3/entry","name":"Chmp6","description":"Charged multivesicular body protein 6","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11513819","identifier":"Q921W0","identifierLink":"https://www.uniprot.org/uniprotkb/Q921W0/entry","name":"Chmp1a","description":"Charged multivesicular body protein 1a","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11513855","identifier":"Q9D7S9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D7S9/entry","name":"Chmp5","description":"Charged multivesicular body protein 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11513882","identifier":"Q8R1T1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R1T1/entry","name":"Chmp7","description":"Charged multivesicular body protein 7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2554069","identifier":"Q9CQ10","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQ10/entry","name":"Chmp3","description":"Charged multivesicular body protein 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-643463","identifier":"Q99LU0","identifierLink":"https://www.uniprot.org/uniprotkb/Q99LU0/entry","name":"Chmp1b1","description":"Charged multivesicular body protein 1B1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8322817","identifier":"Q9D8B3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D8B3/entry","name":"Chmp4b","description":"Charged multivesicular body protein 4b","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8586095","identifier":"Q9DB34","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DB34/entry","name":"Chmp2a","description":"Charged multivesicular body protein 2a","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8586771","identifier":"Q8BJF9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BJF9/entry","name":"Chmp2b","description":"Charged multivesicular body protein 2b","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-333","complexName":"ESCRT-III complex, variant Chmp1b2","organismName":"Mus musculus; 10090","description":"The ESCRT machinery has been implicated in membrane scission steps, transforming a single, continuous bilayer into two distinct bilayers, either from within the neck of a vesicle budding away from the cytoplasm or from within a membrane tubule, while segregating cargo throughout the process. Membrane fission processes include: a) the sorting of multivesicular bodies (MVB) in the endocytic pathway; cargoes destined for inclusion into the MVB pathway are covalently modified with ubiquitin, recognized by ubiquitin-binding domains in the early ESCRTs (ESCRT-0, -I, and -II) and sequestered into endosomal microdomains that bud into the endosome as intralumenal vesicles aided by ESCRT-III, b) downregulation of cell-surface receptors, c) repair of plasma membrane wounds, d) abscission of the cellular bridge during cytokineses, d) nuclear envelope sealing by annular fusion and e) budding of virions from the plasma membrane. The ESCRT machinery seems to play an indirect role in the proper functioning of cellular polarity and migration, the miRNA machinery and gene expression regulation. \r\n\r\nESCRT-0 recruits ESCRT-I which engages ESCRT-II to nucleate ESCRT-III polymerization. VPS4A/B complex, also known as ESCRT-IV, disassembles ESCRT-III to recycle its subunits. The ESCRT-III complex facilitates changes in membrane architecture by oligomerizing to form spiral, filament-like tubules, accumulation of which is associated with membrane constriction and fission. Disassembly of ESCRT-III by VPS4A/B may be a required step for fission. \r\n\r\nCHMP1A, CHMP1B and CHMP5 are sometimes regarded as ESCRT-III accessory proteins rather than full complex members, suggesting that multiple variants with different core components and/or associated auxiliary factors may exist within the same cell and be active in different processes.","predictedComplex":false,"interactors":[{"ac":"EBI-11116446","identifier":"Q9D7F7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D7F7/entry","name":"Chmp4c","description":"Charged multivesicular body protein 4c","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11116518","identifier":"P0C0A3","identifierLink":"https://www.uniprot.org/uniprotkb/P0C0A3/entry","name":"Chmp6","description":"Charged multivesicular body protein 6","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11513819","identifier":"Q921W0","identifierLink":"https://www.uniprot.org/uniprotkb/Q921W0/entry","name":"Chmp1a","description":"Charged multivesicular body protein 1a","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11513855","identifier":"Q9D7S9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D7S9/entry","name":"Chmp5","description":"Charged multivesicular body protein 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11513882","identifier":"Q8R1T1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R1T1/entry","name":"Chmp7","description":"Charged multivesicular body protein 7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11515489","identifier":"Q9CQD4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQD4/entry","name":"Chmp1b2","description":"Charged multivesicular body protein 1B2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2554069","identifier":"Q9CQ10","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQ10/entry","name":"Chmp3","description":"Charged multivesicular body protein 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8322817","identifier":"Q9D8B3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D8B3/entry","name":"Chmp4b","description":"Charged multivesicular body protein 4b","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8586095","identifier":"Q9DB34","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DB34/entry","name":"Chmp2a","description":"Charged multivesicular body protein 2a","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8586771","identifier":"Q8BJF9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BJF9/entry","name":"Chmp2b","description":"Charged multivesicular body protein 2b","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-334","complexName":"VPS4 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"An AAA-ATPase that is probably the main energy-providing system for the membrane deformation and abscission function of the ESCRT machinery consisting of ESCRT-0 (CPX-1622), -I (CPX-940), -II (CPX-1623), -III (CPX-1624) and -IV (this complex) . Required for the dissociation and recycling of ESCRT-III complex subunits from vesicle and plasma membranes as well as the midbody during the final stages of cytokinesis where it causes constriction of the ESCRT-III polymer and fission of the associated membrane neck. Multiple disassembly reactions are performed until ESCRT-III dissociation has been completed. \r\n\r\nVPS4 ATPase activity is regulated by a) ESCRT-III interactions with VPS4 which enhance ATP hydrolysis by relieving autoinhibition of the AAA domain and b) binding of the VTA1 homodimers (Q06263) which both promotes VPS4 oligomerization and enhances ATP hydrolysis. Binding of ESCRT-III subunits DID2 (P69771) or VPS60 (Q03390) to the amino-terminal of VTA1 relieves autoinhibition within VTA1 to further enhance stimulation of VPS4 ATP hydrolysis. Binding of IST1 (P53843) to VPS4 negatively regulates VPS4 activity by blocking binding to the ESCRT machinery.","predictedComplex":false,"interactors":[{"ac":"EBI-20475","identifier":"P52917","identifierLink":"https://www.uniprot.org/uniprotkb/P52917/entry","name":"VPS4","description":"Vacuolar protein sorting-associated protein 4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23074","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-335","complexName":"CLB1-CDC28 kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Cyclin-dependent protein kinase complex required for the control of the cell cycle at the G2/M (mitosis) transition. Mitotic cyclin-CDKs (M-CDKs) regulate accurate chromosome segregation through mitosis.","predictedComplex":false,"interactors":[{"ac":"EBI-4253","identifier":"P00546","identifierLink":"https://www.uniprot.org/uniprotkb/P00546/entry","name":"CDC28","description":"Cyclin-dependent kinase 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4508","identifier":"P24868","identifierLink":"https://www.uniprot.org/uniprotkb/P24868/entry","name":"CLB1","description":"G2/mitotic-specific cyclin-1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-336","complexName":"CLB3-CDC28 kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Cyclin-dependent protein kinase complex required for the control of the cell cycle at the G2/M (mitosis) transition. Mitotic cyclin-CDKs (M-CDKs) regulate accurate chromosome segregation through mitosis.","predictedComplex":false,"interactors":[{"ac":"EBI-4253","identifier":"P00546","identifierLink":"https://www.uniprot.org/uniprotkb/P00546/entry","name":"CDC28","description":"Cyclin-dependent kinase 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4522","identifier":"P24870","identifierLink":"https://www.uniprot.org/uniprotkb/P24870/entry","name":"CLB3","description":"G2/mitotic-specific cyclin-3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-337","complexName":"CLB4-CDC28 kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Cyclin-dependent protein kinase complex required for the control of the cell cycle at the G2/M (mitosis) transition. Mitotic cyclin-CDKs (M-CDKs) regulate accurate chromosome segregation through mitosis.","predictedComplex":false,"interactors":[{"ac":"EBI-4253","identifier":"P00546","identifierLink":"https://www.uniprot.org/uniprotkb/P00546/entry","name":"CDC28","description":"Cyclin-dependent kinase 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4528","identifier":"P24871","identifierLink":"https://www.uniprot.org/uniprotkb/P24871/entry","name":"CLB4","description":"G2/mitotic-specific cyclin-4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-338","complexName":"VPS4A/B complex","organismName":"Homo sapiens; 9606","description":"An AAA-ATPase that is probably the main energy-providing system for the membrane deformation and abscission function of the ESCRT machinery. Required for the dissociation and recycling of ESCRT-III complex (CPX-329) subunits from vesicle and plasma membranes as well as the midbody during the final stages of cytokinesis where it causes constriction of the ESCRT-III polymer and fission of the associated membrane neck. Multiple disassembly reactions are performed until ESCRT-III dissociation has been completed. \r\n\r\nVPS4 ATPase activity is regulated by a) ESCRT-III interactions with VPS4 which enhance ATP hydrolysis by relieving autoinhibition of the AAA domain and b) binding of the VTA1 homodimers (Q9NP79) which both promotes VPS4 oligomerization and enhances ATP hydrolysis. Binding of ESCRT-III subunits CHMP1B (Q7LBR1) or CHMP5 (Q9NZZ3) to the amino-terminal of VTA1 relieves autoinhibition within VTA1 to further enhance stimulation of VPS4 ATP hydrolysis. Binding of IST1 (P53990) to VPS4 negatively regulates VPS4 activity by blocking binding to the ESCRT machinery.","predictedComplex":false,"interactors":[{"ac":"EBI-1171942","identifier":"Q9UN37","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UN37/entry","name":"VPS4A","description":"Vacuolar protein sorting-associated protein 4A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23074","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2514459","identifier":"O75351","identifierLink":"https://www.uniprot.org/uniprotkb/O75351/entry","name":"VPS4B","description":"Vacuolar protein sorting-associated protein 4B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23074","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-339","complexName":"CLB6-CDC28 kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Cyclin-dependent protein kinase complex required for the control of the cell cycle during S-phase where it is required to activate DNA replication.","predictedComplex":false,"interactors":[{"ac":"EBI-2049771","identifier":"P32943","identifierLink":"https://www.uniprot.org/uniprotkb/P32943/entry","name":"CLB6","description":"S-phase entry cyclin-6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4253","identifier":"P00546","identifierLink":"https://www.uniprot.org/uniprotkb/P00546/entry","name":"CDC28","description":"Cyclin-dependent kinase 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-340","complexName":"VPS4A/B complex","organismName":"Mus musculus; 10090","description":"An AAA-ATPase that is probably the main energy-providing system for the membrane deformation and abscission function of the ESCRT machinery. Required for the dissociation and recycling of ESCRT-III complex (CPX-332/CPX-333) subunits from vesicle and plasma membranes as well as the midbody during the final stages of cytokinesis where it causes constriction of the ESCRT-III polymer and fission of the associated membrane neck. Multiple disassembly reactions are performed until ESCRT-III dissociation has been completed. \r\n\r\nVPS4 ATPase activity is regulated by a) ESCRT-III interactions with VPS4 which enhance ATP hydrolysis by relieving autoinhibition of the AAA domain and b) binding of the VTA1 homodimers (Q9CR26) which both promotes VPS4 oligomerization and enhances ATP hydrolysis. Binding of ESCRT-III subunits CHMP1B (Q99LU0/Q9CQD4) or CHMP5 (Q9D7S9) to the amino-terminal of VTA1 relieves autoinhibition within VTA1 to further enhance stimulation of VPS4 ATP hydrolysis. Binding of IST1 (Q9CX00) to VPS4 negatively regulates VPS4 activity by blocking binding to the ESCRT machinery.","predictedComplex":false,"interactors":[{"ac":"EBI-8314109","identifier":"Q8VEJ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VEJ9/entry","name":"Vps4a","description":"Vacuolar protein sorting-associated protein 4A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23074","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8376721","identifier":"P46467","identifierLink":"https://www.uniprot.org/uniprotkb/P46467/entry","name":"Vps4b","description":"Vacuolar protein sorting-associated protein 4B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23074","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-341","complexName":"Cyclin L1-CDK11A(p110) complex","organismName":"Homo sapiens; 9606","description":"Cyclin-dependent protein kinase complex. Role in pre-mRNA splicing and transcription regulation, possibly through phosphorylation of the splicing factor SFRS7 (Q16629). Phosphorylated by CHK2 (O96017), a key mediator in the response to DNA damage, however the phosphorylation appears to occur in a DNA damage-independent manner and is not required for kinase activity but does promote pre-mRNA splicing.","predictedComplex":false,"interactors":[{"ac":"EBI-11579223","identifier":"Q9UQ88-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UQ88-1/entry","name":"CDK11A","description":"Cyclin-dependent kinase 11A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2836773","identifier":"Q9UK58","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK58/entry","name":"CCNL1","description":"Cyclin-L1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-342","complexName":"CLN2-CDC28 kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Cyclin-dependent protein kinase complex required for the control of the cell cycle at the G1/S (start) transition, controlling the trigger of post-Start processes such as spindle pole body duplication, and the initiation of DNA replication. CKS1 is required for activity of CLN-CDC28 complexes. The protein may also play a role in complex stability and substrate recognition.","predictedComplex":false,"interactors":[{"ac":"EBI-4253","identifier":"P00546","identifierLink":"https://www.uniprot.org/uniprotkb/P00546/entry","name":"CDC28","description":"Cyclin-dependent kinase 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4483","identifier":"P20438","identifierLink":"https://www.uniprot.org/uniprotkb/P20438/entry","name":"CLN2","description":"G1/S-specific cyclin CLN2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4746","identifier":"P20486","identifierLink":"https://www.uniprot.org/uniprotkb/P20486/entry","name":"CKS1","description":"Cyclin-dependent kinases regulatory subunit","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23415","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-343","complexName":"Cyclin L2-CDK11A(p110) complex","organismName":"Homo sapiens; 9606","description":"Cyclin-dependent protein kinase complex. Role in pre-mRNA splicing and transcription regulation, possibly through phosphorylation of the splicing factor SFRS7 (Q16629). Phosphorylated by CHK2 (O96017), a key mediator in the response to DNA damage, however the phosphorylation appears to occur in a DNA damage-independent manner and is not required for kinase activity but does promote pre-mRNA splicing.","predictedComplex":false,"interactors":[{"ac":"EBI-1045974","identifier":"Q96S94","identifierLink":"https://www.uniprot.org/uniprotkb/Q96S94/entry","name":"CCNL2","description":"Cyclin-L2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11579223","identifier":"Q9UQ88-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UQ88-1/entry","name":"CDK11A","description":"Cyclin-dependent kinase 11A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-344","complexName":"Cyclin L1-CDK11A(p58) complex","organismName":"Homo sapiens; 9606","description":"Cyclin-dependent protein kinase complex. Appears to be involved in early events in the establishment of the centromere protection machinery and is required for centrosome maturation and centriole duplication, including sister chromatid cohesion. Also plays a role in apoptosis, apparently by phosphorylating and down-regulating members of the BCL-2 family of proteins. The p58 isoform of CDK11A is expressed during G2 and M phases, upon activation of an internal ribosome entry site present in the CDK11 mRNA.","predictedComplex":false,"interactors":[{"ac":"EBI-11580640","identifier":"Q9UQ88-10","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UQ88-10/entry","name":"CDK11A","description":"Cyclin-dependent kinase 11A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2836773","identifier":"Q9UK58","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK58/entry","name":"CCNL1","description":"Cyclin-L1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-345","complexName":"Cyclin L2-CDK11B(p58) complex","organismName":"Homo sapiens; 9606","description":"Cyclin-dependent protein kinase complex. Appears to be involved in early events in the establishment of the centromere protection machinery and is required for centrosome maturation and centriole duplication, including sister chromatid cohesion. Also plays a role in apoptosis, apparently by phosphorylating and down-regulating members of the BCL-2 family of proteins. The p58 isoform of CDK11B is expressed during G2 and M phases, upon activation of an internal ribosome entry site present in the CDK11 mRNA.","predictedComplex":false,"interactors":[{"ac":"EBI-1018806","identifier":"P21127-12","identifierLink":"https://www.uniprot.org/uniprotkb/P21127-12/entry","name":"CDK11B","description":"Cyclin-dependent kinase 11B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-1045974","identifier":"Q96S94","identifierLink":"https://www.uniprot.org/uniprotkb/Q96S94/entry","name":"CCNL2","description":"Cyclin-L2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-346","complexName":"Cyclin L1-CDK11B(p58) complex","organismName":"Homo sapiens; 9606","description":"Cyclin-dependent protein kinase complex. Appears to be involved in early events in the establishment of the centromere protection machinery and is required for centrosome maturation and centriole duplication, including sister chromatid cohesion. Also plays a role in apoptosis, apparently by phosphorylating and down-regulating members of the BCL-2 family of proteins. The p58 isoform of CDK11B (P21127-12) is expressed during G2 and M phases, upon activation of an internal ribosome entry site present in the CDK11 mRNA.","predictedComplex":false,"interactors":[{"ac":"EBI-1018806","identifier":"P21127-12","identifierLink":"https://www.uniprot.org/uniprotkb/P21127-12/entry","name":"CDK11B","description":"Cyclin-dependent kinase 11B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2836773","identifier":"Q9UK58","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK58/entry","name":"CCNL1","description":"Cyclin-L1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-347","complexName":"Cyclin L2-CDK11A(p58) complex","organismName":"Homo sapiens; 9606","description":"Cyclin-dependent protein kinase complex. Appears to be involved in early events in the establishment of the centromere protection machinery and is required for centrosome maturation and centriole duplication, including sister chromatid cohesion. Also plays a role in apoptosis, apparently by phosphorylating and down-regulating members of the BCL-2 family of proteins. The p58 isoform of CDK11A is expressed during G2 and M phases, upon activation of an internal ribosome entry site present in the CDK11 mRNA.","predictedComplex":false,"interactors":[{"ac":"EBI-1045974","identifier":"Q96S94","identifierLink":"https://www.uniprot.org/uniprotkb/Q96S94/entry","name":"CCNL2","description":"Cyclin-L2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11580640","identifier":"Q9UQ88-10","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UQ88-10/entry","name":"CDK11A","description":"Cyclin-dependent kinase 11A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-348","complexName":"Cyclin L1-CDK11B(p110) complex","organismName":"Homo sapiens; 9606","description":"Cyclin-dependent protein kinase complex. Role in pre-mRNA splicing and transcription regulation, possibly through phosphorylation of the splicing factor SFRS7 (Q16629). Phosphorylated by CHK2 (O96017), a key mediator in the response to DNA damage, however the phosphorylation appears to occur in a DNA damage-independent manner and is not required for kinase activity but does promote pre-mRNA splicing.","predictedComplex":false,"interactors":[{"ac":"EBI-20769085","identifier":"P21127-1","identifierLink":"https://www.uniprot.org/uniprotkb/P21127-1/entry","name":"CDK11B","description":"Cyclin-dependent kinase 11B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2836773","identifier":"Q9UK58","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK58/entry","name":"CCNL1","description":"Cyclin-L1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-349","complexName":"Cyclin L2-CDK11B(p110) complex","organismName":"Homo sapiens; 9606","description":"Cyclin-dependent protein kinase complex. Role in pre-mRNA splicing and transcription regulation, possibly through phosphorylation of the splicing factor SFRS7 (Q16629). Phosphorylated by CHK2 (O96017), a key mediator in the response to DNA damage, however the phosphorylation appears to occur in a DNA damage-independent manner and is not required for kinase activity but does promote pre-mRNA splicing.","predictedComplex":false,"interactors":[{"ac":"EBI-1045974","identifier":"Q96S94","identifierLink":"https://www.uniprot.org/uniprotkb/Q96S94/entry","name":"CCNL2","description":"Cyclin-L2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20769085","identifier":"P21127-1","identifierLink":"https://www.uniprot.org/uniprotkb/P21127-1/entry","name":"CDK11B","description":"Cyclin-dependent kinase 11B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-350","complexName":"Cyclin L2-CDK11B(p110) complex","organismName":"Mus musculus; 10090","description":"Cyclin-dependent protein kinase complex. Role in pre-mRNA splicing and transcription regulation, possibly through phosphorylation of the splicing factor SFRS7 (Q8BL97). Phosphorylated by CHK2 (Q9Z265), a key mediator in the response to DNA damage, however the phosphorylation appears to occur in a DNA damage-independent manner and is not required for kinase activity but does promote pre-mRNA splicing.","predictedComplex":false,"interactors":[{"ac":"EBI-11581772","identifier":"P24788-1","identifierLink":"https://www.uniprot.org/uniprotkb/P24788-1/entry","name":"Cdk11b","description":"Cyclin-dependent kinase 11B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-8458011","identifier":"Q9JJA7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JJA7/entry","name":"Ccnl2","description":"Cyclin-L2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-351","complexName":"Cyclin L1-CDK11B(p110) complex","organismName":"Mus musculus; 10090","description":"Cyclin-dependent protein kinase complex. Role in pre-mRNA splicing and transcription regulation, possibly through phosphorylation of the splicing factor SFRS7 (Q8BL97). Phosphorylated by CHK2 (Q9Z265), a key mediator in the response to DNA damage, however the phosphorylation appears to occur in a DNA damage-independent manner and is not required for kinase activity but does promote pre-mRNA splicing.","predictedComplex":false,"interactors":[{"ac":"EBI-11581772","identifier":"P24788-1","identifierLink":"https://www.uniprot.org/uniprotkb/P24788-1/entry","name":"Cdk11b","description":"Cyclin-dependent kinase 11B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-8458542","identifier":"Q52KE7","identifierLink":"https://www.uniprot.org/uniprotkb/Q52KE7/entry","name":"Ccnl1","description":"Cyclin-L1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-352","complexName":"Cyclin L1-CDK11B(p58) complex","organismName":"Mus musculus; 10090","description":"Cyclin-dependent protein kinase complex. Appears to be involved in early events in the establishment of the centromere protection machinery and is required for centrosome maturation and centriole duplication, including sister chromatid cohesion. Also plays a role in apoptosis, apparently by phosphorylating and down-regulating members of the BCL-2 family of proteins. The p58 isoform of CDK11B is expressed during G2 and M phases, upon activation of an internal ribosome entry site present in the CDK11 mRNA.","predictedComplex":false,"interactors":[{"ac":"EBI-11581787","identifier":"P24788-2","identifierLink":"https://www.uniprot.org/uniprotkb/P24788-2/entry","name":"Cdk11b","description":"Cyclin-dependent kinase 11B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-8458542","identifier":"Q52KE7","identifierLink":"https://www.uniprot.org/uniprotkb/Q52KE7/entry","name":"Ccnl1","description":"Cyclin-L1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-353","complexName":"Cyclin L2-CDK11B(p58) complex","organismName":"Mus musculus; 10090","description":"Cyclin-dependent protein kinase complex. Appears to be involved in early events in the establishment of the centromere protection machinery and is required for centrosome maturation and centriole duplication, including sister chromatid cohesion. Also plays a role in apoptosis, apparently by phosphorylating and down-regulating members of the BCL-2 family of proteins. The p58 isoform of CDK11B is expressed during G2 and M phases, upon activation of an internal ribosome entry site present in the CDK11 mRNA.","predictedComplex":false,"interactors":[{"ac":"EBI-11581787","identifier":"P24788-2","identifierLink":"https://www.uniprot.org/uniprotkb/P24788-2/entry","name":"Cdk11b","description":"Cyclin-dependent kinase 11B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-8458011","identifier":"Q9JJA7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JJA7/entry","name":"Ccnl2","description":"Cyclin-L2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-354","complexName":"ATG12-ATG5-ATG16L2 complex","organismName":"Homo sapiens; 9606","description":"No known role is ascribed to this complex. Unlike the closely related ATG12-ATG5-ATG16L1 complex (CPX-200), it does not appear to be required for autophagy.\r\n\r\nAssumed to act as an E3-like enzyme to recruit the E2-like protein ATG3, conjugated to LC3-I, to the endoplasmic reticulum-derived  omegasome. ATG3 binds to and is activated by ATG12, facilitating conjugation of the LC3 to phosphatidylethanolamine, thus converting LC3-I to LC3-II. Therefore, the site of ATG12-ATG5-ATG16L2 complex recruitment determines the site of LC3-II formation.","predictedComplex":false,"interactors":[{"ac":"EBI-1047414","identifier":"Q9H1Y0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H1Y0/entry","name":"ATG5","description":"Autophagy protein 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2946815","identifier":"Q8NAA4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NAA4/entry","name":"ATG16L2","description":"Protein Atg16l2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19878","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-746742","identifier":"O94817","identifierLink":"https://www.uniprot.org/uniprotkb/O94817/entry","name":"ATG12","description":"Ubiquitin-like protein ATG12","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13385","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-355","complexName":"Atg12-Atg5-Atg16l2 complex","organismName":"Mus musculus; 10090","description":"No known role is ascribed to this complex. Unlike the closely related Atg12-Atg5-Atg16l1 complex (CPX-328), it does not appear to be required for autophagy.\r\n\r\nAssumed to act as an E3-like enzyme to recruit the E2-like protein ATG3, conjugated to LC3-I, to the endoplasmic reticulum-derived  omegasome. Atg3 binds to and is activated by Atg12, facilitating conjugation of the LC3 to phosphatidylethanolamine, thus converting LC3-I to LC3-II. Therefore, the site of  Atg12-Atg5-Atg16l2 complex recruitment determines the site of LC3-II formation.","predictedComplex":false,"interactors":[{"ac":"EBI-11615265","identifier":"Q6KAU8","identifierLink":"https://www.uniprot.org/uniprotkb/Q6KAU8/entry","name":"Atg16l2","description":"Protein Atg16l2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR19878","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2911788","identifier":"Q9CQY1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQY1/entry","name":"Atg12","description":"Ubiquitin-like protein ATG12","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13385","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2911848","identifier":"Q99J83","identifierLink":"https://www.uniprot.org/uniprotkb/Q99J83/entry","name":"Atg5","description":"Autophagy protein 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-356","complexName":"ATG5-ATG12 complex","organismName":"Homo sapiens; 9606","description":"Essential for autophagy during nutrient deprivation, a catabolic process that sequesters undesired cellular material into autophagosomes for delivery to lysosomes for degradation. Required for the elongation of isolation membranes (phagophores) in complex with ATG16L1/ATG16L2 (CPX-200/CPX-354) or lysosomal fusion in complex with TECPR1 (CPX-358).\r\n \r\nActs as an E3-like enzyme to recruit the E2-like protein ATG3, conjugated to LC3-I, to the endoplasmic reticulum-derived omegasome. ATG3 binds to and is activated by ATG12, facilitating conjugation of the LC3 to phosphatidylethanolamine, thus converting LC3-I to LC3-II. Therefore, the site of ATG12–ATG5-ATG16L1 complex recruitment determines the site of LC3-II formation. The LC3 family is required for phagophore expansion, closure, and cargo recruitment.\r\n\r\nNegatively regulates the innate antiviral immune response by blocking the type I IFN production pathway through direct association with RARRES3 (Q9UL19) and MAVS (Q7Z434). Plays a role in translation or delivery of incoming viral RNA to the translation apparatus.","predictedComplex":false,"interactors":[{"ac":"EBI-1047414","identifier":"Q9H1Y0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H1Y0/entry","name":"ATG5","description":"Autophagy protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-746742","identifier":"O94817","identifierLink":"https://www.uniprot.org/uniprotkb/O94817/entry","name":"ATG12","description":"Ubiquitin-like protein ATG12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13385","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-357","complexName":"Atg5-Atg12 complex","organismName":"Mus musculus; 10090","description":"Essential for autophagy during nutrient deprivation, a catabolic process that sequesters undesired cellular material into autophagosomes for delivery to lysosomes for degradation. Required for the elongation of isolation membranes (phagophores) in complex with Atg16l1/Atg16l2 (CPX-328/CPX-355) or lysosomal fusion in complex with Tecpr1 (CPX-360).\r\n \r\nActs as an E3-like enzyme to recruit the E2-like protein Atg3, conjugated to LC3-I, to the endoplasmic reticulum-derived omegasome. Atg3 binds to and is activated by Atg12, facilitating conjugation of the LC3 to phosphatidylethanolamine, thus converting LC3-I to LC3-II. Therefore, the site of Atg12-Atg5-Atg16l1 complex recruitment determines the site of LC3-II formation. The LC3 family is required for phagophore expansion, closure, and cargo recruitment.","predictedComplex":false,"interactors":[{"ac":"EBI-2911788","identifier":"Q9CQY1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQY1/entry","name":"Atg12","description":"Ubiquitin-like protein ATG12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13385","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2911848","identifier":"Q99J83","identifierLink":"https://www.uniprot.org/uniprotkb/Q99J83/entry","name":"Atg5","description":"Autophagy protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-358","complexName":"ATG5-ATG12-TECPR1 complex","organismName":"Homo sapiens; 9606","description":"Essential for autophagy during nutrient deprivation, a catabolic process that sequesters undesired cellular material into autophagosomes for delivery to lysosomes for degradation. Once autophagosome formation is completed, the autophagosome docks lysosomes in order to degrade cellular cargoes by fusion. At this point, the surrounding acidic condition drives ATG5 to change its binding partner from ATG16L1 to TECPR1. Binding of the ATG12-ATG5 conjugate to a region of TECPR1 frees an auto-inhibition of the PH domain within this protein. This domain is then freed to attach to a phosphatidylinositol 3-phosphate molecule of the autophagosomal membrane, thus tethering the autophagosome to a lysosome. These 2 vesicles will then undergo SNARE-mediated fusion to form an autolysosome.","predictedComplex":false,"interactors":[{"ac":"EBI-1047414","identifier":"Q9H1Y0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H1Y0/entry","name":"ATG5","description":"Autophagy protein 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2946676","identifier":"Q7Z6L1","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z6L1/entry","name":"TECPR1","description":"Tectonin beta-propeller repeat-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23250","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-746742","identifier":"O94817","identifierLink":"https://www.uniprot.org/uniprotkb/O94817/entry","name":"ATG12","description":"Ubiquitin-like protein ATG12","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13385","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-359","complexName":"Cyclin K-CDK13 complex","organismName":"Homo sapiens; 9606","description":"Cyclin-dependent protein kinase complex which appears to regulate expression of genes associated with growth signaling pathways. Phosphorylates the C-terminal domain (CTD) of RNA polymerase II (POLR2A). Preferentially phosphorylates  Ser-2 and Ser-5 in CTD repeats with a preference for Ser-7 pre-phosphorylations at a C-terminal position.","predictedComplex":false,"interactors":[{"ac":"EBI-739806","identifier":"O75909","identifierLink":"https://www.uniprot.org/uniprotkb/O75909/entry","name":"CCNK","description":"Cyclin-K","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968626","identifier":"Q14004","identifierLink":"https://www.uniprot.org/uniprotkb/Q14004/entry","name":"CDK13","description":"Cyclin-dependent kinase 13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-360","complexName":"ATG5-ATG12-TECPR1 complex","organismName":"Mus musculus; 10090","description":"Essential for autophagy during nutrient deprivation, a catabolic process that sequesters undesired cellular material into autophagosomes for delivery to lysosomes for degradation. Once autophagosome formation is completed, the autophagosome docks lysosomes in order to degrade cellular cargoes by fusion. At this point, the surrounding acidic condition drives Atg5 to change its binding partner from Atg16l1 to Tecpr1. Binding of the Atg12-Atg5 conjugate to a region of Tecpr1 frees an auto-inhibition of the PH domain within this protein. This domain is then freed to attach to a  phosphatidylinositol 3-phosphate molecule of the autophagosomal membrane, thus tethering the autophagosome to a lysosome. These 2 vesicles will then undergo SNARE-mediated fusion to form an autolysosome.","predictedComplex":false,"interactors":[{"ac":"EBI-11614745","identifier":"Q80VP0","identifierLink":"https://www.uniprot.org/uniprotkb/Q80VP0/entry","name":"Tecpr1","description":"Tectonin beta-propeller repeat-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23250","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2911788","identifier":"Q9CQY1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQY1/entry","name":"Atg12","description":"Ubiquitin-like protein ATG12","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13385","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2911848","identifier":"Q99J83","identifierLink":"https://www.uniprot.org/uniprotkb/Q99J83/entry","name":"Atg5","description":"Autophagy protein 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-361","complexName":"ATG2-ATG18 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Essential for autophagy during nutrient deprivation, a catabolic process that sequesters undesired cellular material into autophagosomes for delivery to lysosomes for degradation. Contributes to nutrition homeostasis and damage control in eukaryotic cells. Functions at a late step of autophagosome formation for efficient completion of sequestration, probably through facilitating recruitment of ATG8-phosphatidylethanolamine (PE) to the preautophagosomal structure (PAS) and/or its protection from deconjugation by ATG4.","predictedComplex":false,"interactors":[{"ac":"EBI-22968","identifier":"P43601","identifierLink":"https://www.uniprot.org/uniprotkb/P43601/entry","name":"ATG18","description":"Autophagy-related protein 18","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11227","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29212","identifier":"P53855","identifierLink":"https://www.uniprot.org/uniprotkb/P53855/entry","name":"ATG2","description":"Autophagy-related protein 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13190","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-362","complexName":"Heparanase complex","organismName":"Homo sapiens; 9606","description":"An endo-beta-D-glucuronidase of the glycoside hydrolase 79 (GH79) family complex that cleaves the extracellular matrix heparan sulfate proteoglycans (HSPGs) into HS side chains and core proteoglycans. Selectively cleaves the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit of HSPGs carrying either a 3-O-sulfo, a 6-O-sulfo or a 2-O-sulfo group, but not linkages between a glucuronic acid unit and a 2-O-sulfated iduronic acid moiety. HS sulfation serves as a molecular signal that directs heparanase to cleave only certain glycan sites and acts as mechanistic handles by which the enzyme can prize open the substrate HS helix and more effectively access the trisaccharide cleavage site via heparanase-binding induced distortion of the substrate helix. \r\n\r\nPresent in a variety of cellular locations where it performs an essential housekeeping role in catabolic processing of internalized HSPGs and at the cell surface or released into the ECM where it participates in ECM degradation and remodeling. \r\n\r\nHSPGs ensure that bioactive molecules such as growth factors, chemokines, lipoproteins, and enzymes are localized to the cell surface and ECM and function in the control of normal and pathological processes. These include morphogenesis, osteogenesis, hair follicle inner root sheath differentiation and hair homeostasis, wound healing, shedding of syndecans, inflammation, pre-eclampsia, autoimmunity, cell proliferation and migration associated with metastasis, endothelial invasion and angiogenesis. Cleavage of HSPGs is likely to release these regulators that can alter the functional state of tissues and provide a mechanism by which cells can respond rapidly to changes in the extracellular environment. The proliferative advantages conferred by heparanase lead to its up-regulation in tumors in a variety of tissues, and its over-expression correlates strongly with metastasis and worsened clinical prognoses. \r\n\r\nAlso acts as pro-coagulant by increasing the generation of activation factor X in the presence of tissue factor and activation factor VII. Increases cell adhesion to the extracellular matrix (ECM) independent of its enzymatic activity.\r\n\r\nHPSE is the only mammalian gene so far identified to have heparanase activity.","predictedComplex":false,"interactors":[{"ac":"EBI-11600831","identifier":"Q9Y251-PRO_0000042262","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y251-PRO_0000042262/entry","name":"HPSE","description":"Heparanase 50 kDa subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-11600845","identifier":"Q9Y251-PRO_0000042260","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y251-PRO_0000042260/entry","name":"HPSE","description":"Heparanase 8 kDa subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-363","complexName":"Heparanase complex","organismName":"Mus musculus; 10090","description":"An endo-beta-D-glucuronidase of the glycoside hydrolase 79 (GH79) family complex that cleaves the extracellular matrix heparan sulfate proteoglycans (HSPGs) into HS side chains and core proteoglycans. Selectively cleaves the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit of HSPGs carrying either a 3-O-sulfo, a 6-O-sulfo or a 2-O-sulfo group, but not linkages between a glucuronic acid unit and a 2-O-sulfated iduronic acid moiety. HS sulfation serves as a molecular signal that directs heparanase to cleave only certain glycan sites and acts as mechanistic handles by which the enzyme can prize open the substrate HS helix and more effectively access the trisaccharide cleavage site via heparanase-binding induced distortion of the substrate helix. \r\n\r\nPresent in a variety of cellular locations where it performs an essential housekeeping role in catabolic processing of internalized HSPGs and at the cell surface or released into the ECM where it participates in ECM degradation and remodeling. \r\n\r\nHSPGs ensure that bioactive molecules such as growth factors, chemokines, lipoproteins, and enzymes are localized to the cell surface and ECM and function in the control of normal and pathological processes. These include morphogenesis, osteogenesis, hair follicle inner root sheath differentiation and hair homeostasis, wound healing, shedding of syndecans, inflammation, pre-eclampsia, autoimmunity, cell proliferation and migration associated with metastasis, endothelial invasion and angiogenesis. Cleavage of HSPGs is likely to release these regulators that can alter the functional state of tissues and provide a mechanism by which cells can respond rapidly to changes in the extracellular environment. The proliferative advantages conferred by heparanase lead to its up-regulation in tumors in a variety of tissues, and its over-expression correlates strongly with metastasis and worsened clinical prognoses. \r\n\r\nAlso acts as pro-coagulant by increasing the generation of activation factor X in the presence of tissue factor and activation factor VII. Increases cell adhesion to the extracellular matrix (ECM) independent of its enzymatic activity.\r\n\r\nHPSE is the only mammalian gene so far identified to have heparanase activity.","predictedComplex":false,"interactors":[{"ac":"EBI-11603242","identifier":"Q6YGZ1-PRO_0000042263","identifierLink":"https://www.uniprot.org/uniprotkb/Q6YGZ1-PRO_0000042263/entry","name":"Hpse","description":"Heparanase 8 kDa subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-11603248","identifier":"Q6YGZ1-PRO_0000042265","identifierLink":"https://www.uniprot.org/uniprotkb/Q6YGZ1-PRO_0000042265/entry","name":"Hpse","description":"Heparanase 50 kDa subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-364","complexName":"Cyclin Y-CDK14 complex","organismName":"Homo sapiens; 9606","description":"Cyclin-dependent protein kinase complex which acts as a cell-cycle regulator of Wnt signaling pathway during G2/M phase. CDK14 can be recruited to the plasma membrane via the N-terminal myristoylation site of cyclin Y where it can then phosphorylate LRP6 (O75581) at Ser-1490, a transmembrane receptor that initiates Wnt/Beta-catenin signaling, leading to the activation of the Wnt signaling pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-1043945","identifier":"O94921","identifierLink":"https://www.uniprot.org/uniprotkb/O94921/entry","name":"CDK14","description":"Cyclin-dependent kinase 14","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1049189","identifier":"Q8ND76","identifierLink":"https://www.uniprot.org/uniprotkb/Q8ND76/entry","name":"CCNY","description":"Cyclin-Y","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14248","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-365","complexName":"GARP tethering complex","organismName":"Caenorhabditis elegans; 6239","description":"Tethering complex required for retrograde traffic from both the early and late endosomes to the Golgi during vesicle trafficking. Links the vesicle through differential SNARE interactions to the Golgi, leading to membrane fusion between late Golgi and endosomal vesicles.","predictedComplex":false,"interactors":[{"ac":"EBI-313277","identifier":"O01839","identifierLink":"https://www.uniprot.org/uniprotkb/O01839/entry","name":"vps-51","description":"Vacuolar protein sorting-associated protein 51 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR15954","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-318981","identifier":"G5EFV8","identifierLink":"https://www.uniprot.org/uniprotkb/G5EFV8/entry","name":"vps-52","description":"Vacuolar protein sorting-associated protein 52 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR14190","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6394890","identifier":"P34561","identifierLink":"https://www.uniprot.org/uniprotkb/P34561/entry","name":"vps-53","description":"Vacuolar protein sorting-associated protein 53 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12820","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6395200","identifier":"Q22639","identifierLink":"https://www.uniprot.org/uniprotkb/Q22639/entry","name":"vps-54","description":"Vacuolar protein sorting-associated protein 54","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12965","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-366","complexName":"Cyclin K-Cdk13 complex","organismName":"Mus musculus; 10090","description":"Cyclin-dependent protein kinase complex which appears to regulate expression of genes associated with growth signaling pathways. Phosphorylates the C-terminal domain (CTD) of RNA polymerase II (Polr2a). Preferentially phosphorylates  Ser-2 and Ser-5 in CTD repeats with a preference for Ser-7 pre-phosphorylations at a C-terminal position.","predictedComplex":false,"interactors":[{"ac":"EBI-8357367","identifier":"O88874","identifierLink":"https://www.uniprot.org/uniprotkb/O88874/entry","name":"Ccnk","description":"Cyclin-K","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8412666","identifier":"Q69ZA1","identifierLink":"https://www.uniprot.org/uniprotkb/Q69ZA1/entry","name":"Cdk13","description":"Cyclin-dependent kinase 13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-367","complexName":"Cyclin Y-Cdk14 complex","organismName":"Mus musculus; 10090","description":"Cyclin-dependent protein kinase complex which acts as a cell-cycle regulator of Wnt signaling pathway during G2/M phase. Cdk14 can be recruited to the plasma membrane via the N-terminal myristoylation site of cyclin Y where it can then phosphorylate Lrp6 (O88572) at Ser-1490, a transmembrane receptor that initiates Wnt/Beta-catenin signaling, leading to the activation of the Wnt signaling pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-7052935","identifier":"O35495","identifierLink":"https://www.uniprot.org/uniprotkb/O35495/entry","name":"Cdk14","description":"Cyclin-dependent kinase 14","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-772904","identifier":"Q8BGU5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BGU5/entry","name":"Ccny","description":"Cyclin-Y","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14248","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-368","complexName":"Polycomb Repressive Complex 2","organismName":"Caenorhabditis elegans; 6239","description":"Chromatin repressor complex that di- and tri-methylates lysine 27 of histone H3 in the early embryo and adult germline to transcriptionally repress target genes. In the germline, silencing occurs on the X chromosomes in hermaphrodites thus controlling germline development.","predictedComplex":false,"interactors":[{"ac":"EBI-11615731","identifier":"O17514","identifierLink":"https://www.uniprot.org/uniprotkb/O17514/entry","name":"mes-2","description":"Histone-lysine N-methyltransferase mes-2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45747","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-314965","identifier":"Q9GYS1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9GYS1/entry","name":"mes-6","description":"Polycomb protein mes-6","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10253","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-322965","identifier":"Q10665","identifierLink":"https://www.uniprot.org/uniprotkb/Q10665/entry","name":"mes-3","description":"Polycomb protein mes-3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]}]},{"complexAC":"CPX-369","complexName":"Ribonucleoside-diphosphate reductase RR1 complex, RRM2B variant","organismName":"Homo sapiens; 9606","description":"Catalyzes the reduction of ribonucleotides to the corresponding deoxyribonucleotides, an essential step in the de novo synthesis of monomeric precursors for DNA replication and repair, while reducing either glutaredoxin (P35754/Q9NS18) or thioredoxin (P10599). The RRM1 subunit binds 2 Mg2+ ions and RRM2B contains a ferric iron-tyrosyl free radical center. The enzyme is allosterically regulated, stimulated by ATP and inhibited by dATP binding to the activity site on the RRM1 subunit. Plays a pivotal role in cell survival by supplying nucleotides in a p53-dependent manner for mitochondrial DNA synthesis and to the DNA repair machinery in cells arrested at G0/G1 or G2/M.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-717006","identifier":"P23921","identifierLink":"https://www.uniprot.org/uniprotkb/P23921/entry","name":"RRM1","description":"Ribonucleoside-diphosphate reductase large subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11573","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9009083","identifier":"Q7LG56","identifierLink":"https://www.uniprot.org/uniprotkb/Q7LG56/entry","name":"RRM2B","description":"Ribonucleoside-diphosphate reductase subunit M2 B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23409","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-370","complexName":"Ribonucleoside-diphosphate reductase RR1 complex, RRM2 variant","organismName":"Mus musculus; 10090","description":"Catalyzes the reduction of ribonucleotides to the corresponding deoxyribonucleotides, an essential step in the de novo synthesis of monomeric precursors for DNA replication and repair, while reducing either glutaredoxin (Q9QUH0/Q923X4) or thioredoxin (P10639). Supplies nucleotides for DNA replication during G1/S phase. The RRM1 subunit binds 2 Mg2+ ions and RRM2 contains a ferric iron-tyrosyl free radical center. The enzyme is allosterically regulated: stimulated by ATP and inhibited by dATP binding to the activity site on the RRM1 subunit.  Possibly suppressed by DNA damage which primarily activates related RRM1-RRM2B complex (CPX-371) during G0/G1 and G2/M transitions.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-642122","identifier":"P11157","identifierLink":"https://www.uniprot.org/uniprotkb/P11157/entry","name":"Rrm2","description":"Ribonucleoside-diphosphate reductase subunit M2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23409","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8419105","identifier":"P07742","identifierLink":"https://www.uniprot.org/uniprotkb/P07742/entry","name":"Rrm1","description":"Ribonucleoside-diphosphate reductase large subunit","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11573","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-371","complexName":"Ribonucleoside-diphosphate reductase RR1 complex, RRM2B variant","organismName":"Mus musculus; 10090","description":"Catalyzes the reduction of ribonucleotides to the corresponding deoxyribonucleotides, an essential step in the de novo synthesis of monomeric precursors for DNA replication and repair, while reducing either glutaredoxin (Q9QUH0/Q923X4) or thioredoxin (P10639). The RRM1 subunit binds 2 Mg2+ ions and Rrm2b contains a ferric iron-tyrosyl free radical center. The enzyme is allosterically regulated: stimulated by ATP and inhibited by dATP binding to the activity site on the RRM1 subunit. Plays a pivotal role in cell survival by supplying nucleotides in a p53-dependent manner for mitochondrial DNA synthesis and to the DNA repair machinery in cells arrested at G0/G1 or G2/M.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-11618354","identifier":"Q6PEE3","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PEE3/entry","name":"Rrm2b","description":"Ribonucleoside-diphosphate reductase subunit M2 B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23409","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8419105","identifier":"P07742","identifierLink":"https://www.uniprot.org/uniprotkb/P07742/entry","name":"Rrm1","description":"Ribonucleoside-diphosphate reductase large subunit","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11573","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-372","complexName":"Zyg-9/Tac-1 complex","organismName":"Caenorhabditis elegans; 6239","description":"Microtubule stabilizing complex that functions during the early stages of embryonic development to regulate microtubule assembly throughout the cell cycle. Specifically, the complex is required for the formation and growth of astral microtubules and spindle microtubles during mitotic spindle assembly.\r\n\r\nThought to function in a partially redundant manner with the Tac-1/Zyg-8 complex to regulate microtubule assembly and processes during interphase, mitosis and meiosis in one-cell stage embryos.\r\n\r\nThe complex directly binds to centosomes throughout the cell cycle and the kinetochore of metaphase and early anaphase chromosomes. At anaphase, the complex is required for mitotic spindle positioning in one-cell stage embryos.","predictedComplex":false,"interactors":[{"ac":"EBI-320102","identifier":"G5EEM5","identifierLink":"https://www.uniprot.org/uniprotkb/G5EEM5/entry","name":"zyg-9","description":"Zygote defective protein 9","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12609","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-320612","identifier":"G5ECG0","identifierLink":"https://www.uniprot.org/uniprotkb/G5ECG0/entry","name":"tac-1","description":"Transforming acid coiled-coil-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]}]},{"complexAC":"CPX-373","complexName":"ULK1-ATG13-RB1CC1-ATG101 autophagy initiation complex","organismName":"Homo sapiens; 9606","description":"Serine/threonine-protein kinase complex required for pre-autophagosomal structure assembly in response to starvation. Ultimately facilitates sequestration of cytoplasmic proteins and organelles for bulk degradation via autophagy and mitophagy, respectively. \r\n\r\nUnder glucose starvation conditions activated through phosphorylation of ULK1 on Ser-317 by AMPK complex. Under amino acid starvation conditions ULK1 and ATG13 are phosphorylated by mTORC1. Activated ULK1 represses mTORC1 kinase activity via phosphorylation of RPTOR (Q8N122, subunit of mTORC1 complex) and phosphorylates ATG13, RB1CC1 and itself. \r\n\r\nUnder nutrient-rich conditions inhibited through phosphorylation of ATG13 and ULK1 on Ser-683 and Ser-758 by RPTOR and AMPK complex, leading to cell proliferation and cell mass increase.","predictedComplex":false,"interactors":[{"ac":"EBI-1047793","identifier":"Q8TDY2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TDY2/entry","name":"RB1CC1","description":"RB1-inducible coiled-coil protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2798775","identifier":"O75143","identifierLink":"https://www.uniprot.org/uniprotkb/O75143/entry","name":"ATG13","description":"Autophagy-related protein 13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13430","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2946739","identifier":"Q9BSB4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BSB4/entry","name":"ATG101","description":"Autophagy-related protein 101","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13292","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-908831","identifier":"O75385","identifierLink":"https://www.uniprot.org/uniprotkb/O75385/entry","name":"ULK1","description":"Serine/threonine-protein kinase ULK1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24348","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-374","complexName":"Zyg-8/Tac-1 complex","organismName":"Caenorhabditis elegans; 6239","description":"Microtubule stabilizing complex that functions during the early stages of embryonic development to regulate microtubule assembly throughout the cell cycle.\r\n\r\nThought to function in a partially redundant manner with the Zyg-9/Tac-1 complex to regulate microtubule assembly and processes during interphase, mitosis and meiosis in one-cell stage embyos.","predictedComplex":false,"interactors":[{"ac":"EBI-320612","identifier":"G5ECG0","identifierLink":"https://www.uniprot.org/uniprotkb/G5ECG0/entry","name":"tac-1","description":"Transforming acid coiled-coil-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-331795","identifier":"Q95QC4","identifierLink":"https://www.uniprot.org/uniprotkb/Q95QC4/entry","name":"zyg-8","description":"Serine/threonine-protein kinase zyg-8","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR44167","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-375","complexName":"brc-1/brd-1 E3 ubiquitin ligase complex","organismName":"Caenorhabditis elegans; 6239","description":"E3 ubiquitin ligase containing complex that mediates the formation of 'Lys-6'-linked polyubiquitin chains and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability, initiating homologous recombination at stalled replication forks.\r\n\r\nThe E3-ubiquitin ligase is responsible for ubiquitination at DNA-damage sites in response to ionizing radiation. The complex associates with the E2-ubiquitin-conjugating enzyme, let-70, to form an active E3-ubiquitin ligase on chromatin in response to DNA damage.","predictedComplex":false,"interactors":[{"ac":"EBI-3895480","identifier":"Q21209","identifierLink":"https://www.uniprot.org/uniprotkb/Q21209/entry","name":"brd-1","description":"BRCA1-associated RING domain protein 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24171","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3895496","identifier":"B6VQ60","identifierLink":"https://www.uniprot.org/uniprotkb/B6VQ60/entry","name":"brc-1","description":"Breast cancer type 1 susceptibility protein homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13763","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6940","complexName":"IgG2 - Ig lambda 3 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgG occurs predominantly in secreted form and is responsible for longlasting humoral immunity.","predictedComplex":false,"interactors":[{"ac":"EBI-1044662","identifier":"P01859","identifierLink":"https://www.uniprot.org/uniprotkb/P01859/entry","name":"IGHG2","description":"Immunoglobulin heavy constant gamma 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21503142","identifier":"P0DOY3","identifierLink":"https://www.uniprot.org/uniprotkb/P0DOY3/entry","name":"IGLC3","description":"Immunoglobulin lambda constant 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6941","complexName":"IgG2 - Ig lambda 6 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgG occurs predominantly in secreted form and is responsible for longlasting humoral immunity.","predictedComplex":false,"interactors":[{"ac":"EBI-1044662","identifier":"P01859","identifierLink":"https://www.uniprot.org/uniprotkb/P01859/entry","name":"IGHG2","description":"Immunoglobulin heavy constant gamma 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6151653","identifier":"P0CF74","identifierLink":"https://www.uniprot.org/uniprotkb/P0CF74/entry","name":"IGLC6","description":"Immunoglobulin lambda constant 6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6942","complexName":"IgG2 - Ig lambda 7 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgG occurs predominantly in secreted form and is responsible for longlasting humoral immunity.","predictedComplex":false,"interactors":[{"ac":"EBI-1044662","identifier":"P01859","identifierLink":"https://www.uniprot.org/uniprotkb/P01859/entry","name":"IGHG2","description":"Immunoglobulin heavy constant gamma 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6677450","identifier":"A0M8Q6","identifierLink":"https://www.uniprot.org/uniprotkb/A0M8Q6/entry","name":"IGLC7","description":"Immunoglobulin lambda constant 7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6943","complexName":"IgG3 - Ig kappa immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgG occurs predominantly in secreted form and is responsible for longlasting humoral immunity.","predictedComplex":false,"interactors":[{"ac":"EBI-1054530","identifier":"P01834","identifierLink":"https://www.uniprot.org/uniprotkb/P01834/entry","name":"IGKC","description":"Immunoglobulin kappa constant","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355805","identifier":"P01860","identifierLink":"https://www.uniprot.org/uniprotkb/P01860/entry","name":"IGHG3","description":"Immunoglobulin heavy constant gamma 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6944","complexName":"IgG3 - Ig lambda 1 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgG occurs predominantly in secreted form and is responsible for longlasting humoral immunity.","predictedComplex":false,"interactors":[{"ac":"EBI-1221063","identifier":"P0CG04","identifierLink":"https://www.uniprot.org/uniprotkb/P0CG04/entry","name":"IGLC1","description":"Immunoglobulin lambda constant 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355805","identifier":"P01860","identifierLink":"https://www.uniprot.org/uniprotkb/P01860/entry","name":"IGHG3","description":"Immunoglobulin heavy constant gamma 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6945","complexName":"IgG3 - Ig lambda 2 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgG occurs predominantly in secreted form and is responsible for longlasting humoral immunity.","predictedComplex":false,"interactors":[{"ac":"EBI-355805","identifier":"P01860","identifierLink":"https://www.uniprot.org/uniprotkb/P01860/entry","name":"IGHG3","description":"Immunoglobulin heavy constant gamma 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6151637","identifier":"P0CG05","identifierLink":"https://www.uniprot.org/uniprotkb/P0CG05/entry","name":"IGLC2","description":"Immunoglobulin lambda constant 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6946","complexName":"IgG3 - Ig lambda 3 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgG occurs predominantly in secreted form and is responsible for longlasting humoral immunity.","predictedComplex":false,"interactors":[{"ac":"EBI-21503142","identifier":"P0DOY3","identifierLink":"https://www.uniprot.org/uniprotkb/P0DOY3/entry","name":"IGLC3","description":"Immunoglobulin lambda constant 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355805","identifier":"P01860","identifierLink":"https://www.uniprot.org/uniprotkb/P01860/entry","name":"IGHG3","description":"Immunoglobulin heavy constant gamma 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6947","complexName":"IgG3 - Ig lambda 6 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgG occurs predominantly in secreted form and is responsible for longlasting humoral immunity.","predictedComplex":false,"interactors":[{"ac":"EBI-355805","identifier":"P01860","identifierLink":"https://www.uniprot.org/uniprotkb/P01860/entry","name":"IGHG3","description":"Immunoglobulin heavy constant gamma 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6151653","identifier":"P0CF74","identifierLink":"https://www.uniprot.org/uniprotkb/P0CF74/entry","name":"IGLC6","description":"Immunoglobulin lambda constant 6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6948","complexName":"IgG3 - Ig lambda 7 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgG occurs predominantly in secreted form and is responsible for longlasting humoral immunity.","predictedComplex":false,"interactors":[{"ac":"EBI-355805","identifier":"P01860","identifierLink":"https://www.uniprot.org/uniprotkb/P01860/entry","name":"IGHG3","description":"Immunoglobulin heavy constant gamma 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6677450","identifier":"A0M8Q6","identifierLink":"https://www.uniprot.org/uniprotkb/A0M8Q6/entry","name":"IGLC7","description":"Immunoglobulin lambda constant 7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6949","complexName":"IgG4 - Ig kappa immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgG occurs predominantly in secreted form and is responsible for longlasting humoral immunity.","predictedComplex":false,"interactors":[{"ac":"EBI-1054530","identifier":"P01834","identifierLink":"https://www.uniprot.org/uniprotkb/P01834/entry","name":"IGKC","description":"Immunoglobulin kappa constant","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7211518","identifier":"P01861","identifierLink":"https://www.uniprot.org/uniprotkb/P01861/entry","name":"IGHG4","description":"Immunoglobulin heavy constant gamma 4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6950","complexName":"IgG4 - Ig lambda 1 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgG occurs predominantly in secreted form and is responsible for longlasting humoral immunity.","predictedComplex":false,"interactors":[{"ac":"EBI-1221063","identifier":"P0CG04","identifierLink":"https://www.uniprot.org/uniprotkb/P0CG04/entry","name":"IGLC1","description":"Immunoglobulin lambda constant 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7211518","identifier":"P01861","identifierLink":"https://www.uniprot.org/uniprotkb/P01861/entry","name":"IGHG4","description":"Immunoglobulin heavy constant gamma 4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6951","complexName":"IgG4 - Ig lambda 2 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgG occurs predominantly in secreted form and is responsible for longlasting humoral immunity.","predictedComplex":false,"interactors":[{"ac":"EBI-6151637","identifier":"P0CG05","identifierLink":"https://www.uniprot.org/uniprotkb/P0CG05/entry","name":"IGLC2","description":"Immunoglobulin lambda constant 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-7211518","identifier":"P01861","identifierLink":"https://www.uniprot.org/uniprotkb/P01861/entry","name":"IGHG4","description":"Immunoglobulin heavy constant gamma 4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6952","complexName":"IgG4 - Ig lambda 3 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgG occurs predominantly in secreted form and is responsible for longlasting humoral immunity.","predictedComplex":false,"interactors":[{"ac":"EBI-21503142","identifier":"P0DOY3","identifierLink":"https://www.uniprot.org/uniprotkb/P0DOY3/entry","name":"IGLC3","description":"Immunoglobulin lambda constant 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7211518","identifier":"P01861","identifierLink":"https://www.uniprot.org/uniprotkb/P01861/entry","name":"IGHG4","description":"Immunoglobulin heavy constant gamma 4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6953","complexName":"IgG4 - Ig lambda 6 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgG occurs predominantly in secreted form and is responsible for longlasting humoral immunity.","predictedComplex":false,"interactors":[{"ac":"EBI-6151653","identifier":"P0CF74","identifierLink":"https://www.uniprot.org/uniprotkb/P0CF74/entry","name":"IGLC6","description":"Immunoglobulin lambda constant 6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7211518","identifier":"P01861","identifierLink":"https://www.uniprot.org/uniprotkb/P01861/entry","name":"IGHG4","description":"Immunoglobulin heavy constant gamma 4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6954","complexName":"IgG4 - Ig lambda 7 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgG occurs predominantly in secreted form and is responsible for longlasting humoral immunity.","predictedComplex":false,"interactors":[{"ac":"EBI-6677450","identifier":"A0M8Q6","identifierLink":"https://www.uniprot.org/uniprotkb/A0M8Q6/entry","name":"IGLC7","description":"Immunoglobulin lambda constant 7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7211518","identifier":"P01861","identifierLink":"https://www.uniprot.org/uniprotkb/P01861/entry","name":"IGHG4","description":"Immunoglobulin heavy constant gamma 4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6955","complexName":"IgA1 - Ig kappa immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgA is the major immunoglobulin class in body secretions such as saliva and breast milk and protects mucosal surfaces from toxins, virus and bacteria by direct neutralization or by prevention of binding to the mucosal surface. Predominantly a monomer in serum, secretory IgA, is a dimer (sometimes trimer and tetramer) associated with a J-chain (P01591) and another polypeptide chain, the secretory component polymeric Ig receptor, PIGR (P01833-PRO_0000014901).","predictedComplex":false,"interactors":[{"ac":"EBI-1054530","identifier":"P01834","identifierLink":"https://www.uniprot.org/uniprotkb/P01834/entry","name":"IGKC","description":"Immunoglobulin kappa constant","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727651","identifier":"P01876","identifierLink":"https://www.uniprot.org/uniprotkb/P01876/entry","name":"IGHA1","description":"Immunoglobulin heavy constant alpha 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6956","complexName":"IgA1 - Ig lambda 1 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgA is the major immunoglobulin class in body secretions such as saliva and breast milk and protects mucosal surfaces from toxins, virus and bacteria by direct neutralization or by prevention of binding to the mucosal surface. Predominantly a monomer in serum, secretory IgA, is a dimer (sometimes trimer and tetramer) associated with a J-chain (P01591) and another polypeptide chain, the secretory component polymeric Ig receptor, PIGR (P01833-PRO_0000014901).","predictedComplex":false,"interactors":[{"ac":"EBI-1221063","identifier":"P0CG04","identifierLink":"https://www.uniprot.org/uniprotkb/P0CG04/entry","name":"IGLC1","description":"Immunoglobulin lambda constant 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727651","identifier":"P01876","identifierLink":"https://www.uniprot.org/uniprotkb/P01876/entry","name":"IGHA1","description":"Immunoglobulin heavy constant alpha 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6957","complexName":"GRX5 iron-sulfur cluster assembly homodimer complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Reversibly binds Fe-S clusters and appears to play a role in Fe-S cluster assembly and trafficking. May also participate in the maturation of [4Fe-4S]2+ cluster-containing proteins in a glutathione-independent manner, possibly as a carrier protein to mediate the transfer of preassembled [4Fe-4S]2+ cluster to target proteins. Active in the mitchondria.","predictedComplex":false,"interactors":[{"ac":"EBI-10824516","identifier":"CHEBI:16856","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16856","name":"glutathione","description":"glutathione","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-29427","identifier":"Q02784","identifierLink":"https://www.uniprot.org/uniprotkb/Q02784/entry","name":"GRX5","description":"Monothiol glutaredoxin-5, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10293","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880384","identifier":"CHEBI:30408","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30408","name":"fe-s cluster","description":"iron-sulfur cluster","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-6958","complexName":"IgA1 - Ig lambda 2 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\nIgA is the major immunoglobulin class in body secretions such as saliva and breast milk and protects mucosal surfaces from toxins, virus and bacteria by direct neutralization or by prevention of binding to the mucosal surface. Predominantly a monomer in serum, secretory IgA, is a dimer (sometimes trimer and tetramer) associated with a J-chain (P01591) and another polypeptide chain, the secretory component polymeric Ig receptor, PIGR (P01833-PRO_0000014901).","predictedComplex":false,"interactors":[{"ac":"EBI-6151637","identifier":"P0CG05","identifierLink":"https://www.uniprot.org/uniprotkb/P0CG05/entry","name":"IGLC2","description":"Immunoglobulin lambda constant 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-727651","identifier":"P01876","identifierLink":"https://www.uniprot.org/uniprotkb/P01876/entry","name":"IGHA1","description":"Immunoglobulin heavy constant alpha 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6959","complexName":"IgA1 - Ig lambda 3 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\nIgA is the major immunoglobulin class in body secretions such as saliva and breast milk and protects mucosal surfaces from toxins, virus and bacteria by direct neutralization or by prevention of binding to the mucosal surface. Predominantly a monomer in serum, secretory IgA, is a dimer (sometimes trimer and tetramer) associated with a J-chain (P01591) and another polypeptide chain, the secretory component polymeric Ig receptor, PIGR (P01833-PRO_0000014901).","predictedComplex":false,"interactors":[{"ac":"EBI-21503142","identifier":"P0DOY3","identifierLink":"https://www.uniprot.org/uniprotkb/P0DOY3/entry","name":"IGLC3","description":"Immunoglobulin lambda constant 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727651","identifier":"P01876","identifierLink":"https://www.uniprot.org/uniprotkb/P01876/entry","name":"IGHA1","description":"Immunoglobulin heavy constant alpha 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6960","complexName":"IgA1 - Ig lambda 6 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgA is the major immunoglobulin class in body secretions such as saliva and breast milk and protects mucosal surfaces from toxins, virus and bacteria by direct neutralization or by prevention of binding to the mucosal surface. Predominantly a monomer in serum, secretory IgA, is a dimer (sometimes trimer and tetramer) associated with a J-chain (P01591) and another polypeptide chain, the secretory component polymeric Ig receptor, PIGR (P01833-PRO_0000014901).","predictedComplex":false,"interactors":[{"ac":"EBI-6151653","identifier":"P0CF74","identifierLink":"https://www.uniprot.org/uniprotkb/P0CF74/entry","name":"IGLC6","description":"Immunoglobulin lambda constant 6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727651","identifier":"P01876","identifierLink":"https://www.uniprot.org/uniprotkb/P01876/entry","name":"IGHA1","description":"Immunoglobulin heavy constant alpha 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6961","complexName":"IgA1 - Ig lambda 7 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\nIgA is the major immunoglobulin class in body secretions such as saliva and breast milk and protects mucosal surfaces from toxins, virus and bacteria by direct neutralization or by prevention of binding to the mucosal surface. Predominantly a monomer in serum, secretory IgA, is a dimer (sometimes trimer and tetramer) associated with a J-chain (P01591) and another polypeptide chain, the secretory component polymeric Ig receptor, PIGR (P01833-PRO_0000014901).","predictedComplex":false,"interactors":[{"ac":"EBI-6677450","identifier":"A0M8Q6","identifierLink":"https://www.uniprot.org/uniprotkb/A0M8Q6/entry","name":"IGLC7","description":"Immunoglobulin lambda constant 7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727651","identifier":"P01876","identifierLink":"https://www.uniprot.org/uniprotkb/P01876/entry","name":"IGHA1","description":"Immunoglobulin heavy constant alpha 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6962","complexName":"IgA2 - Ig kappa immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgA is the major immunoglobulin class in body secretions such as saliva and breast milk and protects mucosal surfaces from toxins, virus and bacteria by direct neutralization or by prevention of binding to the mucosal surface. Predominantly a monomer in serum, secretory IgA, is a dimer (sometimes trimer and tetramer) associated with a J-chain (P01591) and another polypeptide chain, the secretory component polymeric Ig receptor, PIGR (P01833-PRO_0000014901).","predictedComplex":false,"interactors":[{"ac":"EBI-1044357","identifier":"P01877","identifierLink":"https://www.uniprot.org/uniprotkb/P01877/entry","name":"IGHA2","description":"Immunoglobulin heavy constant alpha 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1054530","identifier":"P01834","identifierLink":"https://www.uniprot.org/uniprotkb/P01834/entry","name":"IGKC","description":"Immunoglobulin kappa constant","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6963","complexName":"IgA2 - Ig lambda 1 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\nIgA is the major immunoglobulin class in body secretions such as saliva and breast milk and protects mucosal surfaces from toxins, virus and bacteria by direct neutralization or by prevention of binding to the mucosal surface. Predominantly a monomer in serum, secretory IgA, is a dimer (sometimes trimer and tetramer) associated with a J-chain (P01591) and another polypeptide chain, the secretory component polymeric Ig receptor, PIGR (P01833-PRO_0000014901).","predictedComplex":false,"interactors":[{"ac":"EBI-1044357","identifier":"P01877","identifierLink":"https://www.uniprot.org/uniprotkb/P01877/entry","name":"IGHA2","description":"Immunoglobulin heavy constant alpha 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1221063","identifier":"P0CG04","identifierLink":"https://www.uniprot.org/uniprotkb/P0CG04/entry","name":"IGLC1","description":"Immunoglobulin lambda constant 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6964","complexName":"IgA2 - Ig lambda 2 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgA is the major immunoglobulin class in body secretions such as saliva and breast milk and protects mucosal surfaces from toxins, virus and bacteria by direct neutralization or by prevention of binding to the mucosal surface. Predominantly a monomer in serum, secretory IgA, is a dimer (sometimes trimer and tetramer) associated with a J-chain (P01591) and another polypeptide chain, the secretory component polymeric Ig receptor, PIGR (P01833-PRO_0000014901).","predictedComplex":false,"interactors":[{"ac":"EBI-1044357","identifier":"P01877","identifierLink":"https://www.uniprot.org/uniprotkb/P01877/entry","name":"IGHA2","description":"Immunoglobulin heavy constant alpha 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6151637","identifier":"P0CG05","identifierLink":"https://www.uniprot.org/uniprotkb/P0CG05/entry","name":"IGLC2","description":"Immunoglobulin lambda constant 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6965","complexName":"IgA2 - Ig lambda 3 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgA is the major immunoglobulin class in body secretions such as saliva and breast milk and protects mucosal surfaces from toxins, virus and bacteria by direct neutralization or by prevention of binding to the mucosal surface. Predominantly a monomer in serum, secretory IgA, is a dimer (sometimes trimer and tetramer) associated with a J-chain (P01591) and another polypeptide chain, the secretory component polymeric Ig receptor, PIGR (P01833-PRO_0000014901).","predictedComplex":false,"interactors":[{"ac":"EBI-1044357","identifier":"P01877","identifierLink":"https://www.uniprot.org/uniprotkb/P01877/entry","name":"IGHA2","description":"Immunoglobulin heavy constant alpha 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21503142","identifier":"P0DOY3","identifierLink":"https://www.uniprot.org/uniprotkb/P0DOY3/entry","name":"IGLC3","description":"Immunoglobulin lambda constant 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6966","complexName":"IgA2 - Ig lambda 6 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgA is the major immunoglobulin class in body secretions such as saliva and breast milk and protects mucosal surfaces from toxins, virus and bacteria by direct neutralization or by prevention of binding to the mucosal surface. Predominantly a monomer in serum, secretory IgA, is a dimer (sometimes trimer and tetramer) associated with a J-chain (P01591) and another polypeptide chain, the secretory component polymeric Ig receptor, PIGR (P01833-PRO_0000014901).","predictedComplex":false,"interactors":[{"ac":"EBI-1044357","identifier":"P01877","identifierLink":"https://www.uniprot.org/uniprotkb/P01877/entry","name":"IGHA2","description":"Immunoglobulin heavy constant alpha 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6151653","identifier":"P0CF74","identifierLink":"https://www.uniprot.org/uniprotkb/P0CF74/entry","name":"IGLC6","description":"Immunoglobulin lambda constant 6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6967","complexName":"IgA2 - Ig lambda 7 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgA is the major immunoglobulin class in body secretions such as saliva and breast milk and protects mucosal surfaces from toxins, virus and bacteria by direct neutralization or by prevention of binding to the mucosal surface. Predominantly a monomer in serum, secretory IgA, is a dimer (sometimes trimer and tetramer) associated with a J-chain (P01591) and another polypeptide chain, the secretory component polymeric Ig receptor, PIGR (P01833-PRO_0000014901).","predictedComplex":false,"interactors":[{"ac":"EBI-1044357","identifier":"P01877","identifierLink":"https://www.uniprot.org/uniprotkb/P01877/entry","name":"IGHA2","description":"Immunoglobulin heavy constant alpha 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6677450","identifier":"A0M8Q6","identifierLink":"https://www.uniprot.org/uniprotkb/A0M8Q6/entry","name":"IGLC7","description":"Immunoglobulin lambda constant 7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6969","complexName":"IgE - Ig kappa immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgE is associated with hypersensitivity, allergies and a response to parasitic worms. Binds with extremely high affinity to FcERI/MS4A2 (Q01362) which is expressed on mast cells, basophils, Langerhans cells and eosinophils, up-regulating the FceR on these cells.","predictedComplex":false,"interactors":[{"ac":"EBI-1054530","identifier":"P01834","identifierLink":"https://www.uniprot.org/uniprotkb/P01834/entry","name":"IGKC","description":"Immunoglobulin kappa constant","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27068775","identifier":"P01854","identifierLink":"https://www.uniprot.org/uniprotkb/P01854/entry","name":"IGHE","description":"Immunoglobulin heavy constant epsilon","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6970","complexName":"IgE - Ig lambda 1 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgE is associated with hypersensitivity, allergies and a response to parasitic worms. Binds with extremely high affinity to FcERI/MS4A2 (Q01362) which is expressed on mast cells, basophils, Langerhans cells and eosinophils, up-regulating the FceR on these cells.","predictedComplex":false,"interactors":[{"ac":"EBI-1221063","identifier":"P0CG04","identifierLink":"https://www.uniprot.org/uniprotkb/P0CG04/entry","name":"IGLC1","description":"Immunoglobulin lambda constant 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27068775","identifier":"P01854","identifierLink":"https://www.uniprot.org/uniprotkb/P01854/entry","name":"IGHE","description":"Immunoglobulin heavy constant epsilon","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6971","complexName":"IgE - Ig lambda 2 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgE is associated with hypersensitivity, allergies and a response to parasitic worms. Binds with extremely high affinity to FcERI/MS4A2 (Q01362) which is expressed on mast cells, basophils, Langerhans cells and eosinophils, up-regulating the FceR on these cells.","predictedComplex":false,"interactors":[{"ac":"EBI-27068775","identifier":"P01854","identifierLink":"https://www.uniprot.org/uniprotkb/P01854/entry","name":"IGHE","description":"Immunoglobulin heavy constant epsilon","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6151637","identifier":"P0CG05","identifierLink":"https://www.uniprot.org/uniprotkb/P0CG05/entry","name":"IGLC2","description":"Immunoglobulin lambda constant 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6972","complexName":"IgE - Ig lambda 3 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgE is associated with hypersensitivity, allergies and a response to parasitic worms. Binds with extremely high affinity to FcERI/MS4A2 (Q01362) which is expressed on mast cells, basophils, Langerhans cells and eosinophils, up-regulating the FceR on these cells.","predictedComplex":false,"interactors":[{"ac":"EBI-21503142","identifier":"P0DOY3","identifierLink":"https://www.uniprot.org/uniprotkb/P0DOY3/entry","name":"IGLC3","description":"Immunoglobulin lambda constant 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27068775","identifier":"P01854","identifierLink":"https://www.uniprot.org/uniprotkb/P01854/entry","name":"IGHE","description":"Immunoglobulin heavy constant epsilon","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6973","complexName":"IgE - Ig lambda 6 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgE is associated with hypersensitivity, allergies and a response to parasitic worms. Binds with extremely high affinity to FcERI/MS4A2 (Q01362) which is expressed on mast cells, basophils, Langerhans cells and eosinophils, up-regulating the FceR on these cells.","predictedComplex":false,"interactors":[{"ac":"EBI-27068775","identifier":"P01854","identifierLink":"https://www.uniprot.org/uniprotkb/P01854/entry","name":"IGHE","description":"Immunoglobulin heavy constant epsilon","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6151653","identifier":"P0CF74","identifierLink":"https://www.uniprot.org/uniprotkb/P0CF74/entry","name":"IGLC6","description":"Immunoglobulin lambda constant 6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6974","complexName":"IgE - Ig lambda 7 immunoglobulin complex, constant regions","organismName":"Homo sapiens; 9606","description":"Membrane-bound or secreted glycoprotein produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulin-secreting plasma cells. Secreted immunoglobulins (also known as antibodies) mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. \r\n\r\nIgE is associated with hypersensitivity, allergies and a response to parasitic worms. Binds with extremely high affinity to FcERI/MS4A2 (Q01362) which is expressed on mast cells, basophils, Langerhans cells and eosinophils, up-regulating the FceR on these cells.","predictedComplex":false,"interactors":[{"ac":"EBI-27068775","identifier":"P01854","identifierLink":"https://www.uniprot.org/uniprotkb/P01854/entry","name":"IGHE","description":"Immunoglobulin heavy constant epsilon","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6677450","identifier":"A0M8Q6","identifierLink":"https://www.uniprot.org/uniprotkb/A0M8Q6/entry","name":"IGLC7","description":"Immunoglobulin lambda constant 7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7002","complexName":"bZIP transcription factor complex, BATF-BATF","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-749503","identifier":"Q16520","identifierLink":"https://www.uniprot.org/uniprotkb/Q16520/entry","name":"BATF","description":"Basic leucine zipper transcriptional factor ATF-like","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7003","complexName":"bZIP transcription factor complex, BATF-JUNB","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site. Regulates the expression of Th17-related genes.","predictedComplex":false,"interactors":[{"ac":"EBI-748062","identifier":"P17275","identifierLink":"https://www.uniprot.org/uniprotkb/P17275/entry","name":"JUNB","description":"Transcription factor JunB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749503","identifier":"Q16520","identifierLink":"https://www.uniprot.org/uniprotkb/Q16520/entry","name":"BATF","description":"Basic leucine zipper transcriptional factor ATF-like","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7004","complexName":"bZIP transcription factor complex, BATF-DDIT3","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-742651","identifier":"P35638","identifierLink":"https://www.uniprot.org/uniprotkb/P35638/entry","name":"DDIT3","description":"DNA damage-inducible transcript 3 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16833","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749503","identifier":"Q16520","identifierLink":"https://www.uniprot.org/uniprotkb/Q16520/entry","name":"BATF","description":"Basic leucine zipper transcriptional factor ATF-like","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7005","complexName":"bZIP transcription factor complex, BATF-JUN","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-749503","identifier":"Q16520","identifierLink":"https://www.uniprot.org/uniprotkb/Q16520/entry","name":"BATF","description":"Basic leucine zipper transcriptional factor ATF-like","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-852823","identifier":"P05412","identifierLink":"https://www.uniprot.org/uniprotkb/P05412/entry","name":"JUN","description":"Transcription factor Jun","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7006","complexName":"bZIP transcription factor complex, BATF-CEBPA","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-1172054","identifier":"P49715","identifierLink":"https://www.uniprot.org/uniprotkb/P49715/entry","name":"CEBPA","description":"CCAAT/enhancer-binding protein alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749503","identifier":"Q16520","identifierLink":"https://www.uniprot.org/uniprotkb/Q16520/entry","name":"BATF","description":"Basic leucine zipper transcriptional factor ATF-like","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7007","complexName":"bZIP transcription factor complex, BATF-CEBPB","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-749503","identifier":"Q16520","identifierLink":"https://www.uniprot.org/uniprotkb/Q16520/entry","name":"BATF","description":"Basic leucine zipper transcriptional factor ATF-like","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-969696","identifier":"P17676","identifierLink":"https://www.uniprot.org/uniprotkb/P17676/entry","name":"CEBPB","description":"CCAAT/enhancer-binding protein beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7008","complexName":"bZIP transcription factor complex, BATF-CEBPG","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-740209","identifier":"P53567","identifierLink":"https://www.uniprot.org/uniprotkb/P53567/entry","name":"CEBPG","description":"CCAAT/enhancer-binding protein gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749503","identifier":"Q16520","identifierLink":"https://www.uniprot.org/uniprotkb/Q16520/entry","name":"BATF","description":"Basic leucine zipper transcriptional factor ATF-like","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7009","complexName":"bZIP transcription factor complex, BATF-CEBPD","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-749503","identifier":"Q16520","identifierLink":"https://www.uniprot.org/uniprotkb/Q16520/entry","name":"BATF","description":"Basic leucine zipper transcriptional factor ATF-like","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7962058","identifier":"P49716","identifierLink":"https://www.uniprot.org/uniprotkb/P49716/entry","name":"CEBPD","description":"CCAAT/enhancer-binding protein delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7010","complexName":"bZIP transcription factor complex, BATF-CEBPE","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-3907048","identifier":"Q15744","identifierLink":"https://www.uniprot.org/uniprotkb/Q15744/entry","name":"CEBPE","description":"CCAAT/enhancer-binding protein epsilon","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749503","identifier":"Q16520","identifierLink":"https://www.uniprot.org/uniprotkb/Q16520/entry","name":"BATF","description":"Basic leucine zipper transcriptional factor ATF-like","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7011","complexName":"bZIP transcription factor complex, BATF-HLF","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-2798854","identifier":"Q16534","identifierLink":"https://www.uniprot.org/uniprotkb/Q16534/entry","name":"HLF","description":"Hepatic leukemia factor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11988","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749503","identifier":"Q16520","identifierLink":"https://www.uniprot.org/uniprotkb/Q16520/entry","name":"BATF","description":"Basic leucine zipper transcriptional factor ATF-like","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7012","complexName":"bZIP transcription factor complex, BACH1-BATF","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-1263541","identifier":"O14867","identifierLink":"https://www.uniprot.org/uniprotkb/O14867/entry","name":"BACH1","description":"Transcription regulator protein BACH1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749503","identifier":"Q16520","identifierLink":"https://www.uniprot.org/uniprotkb/Q16520/entry","name":"BATF","description":"Basic leucine zipper transcriptional factor ATF-like","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7013","complexName":"bZIP transcription factor complex, BATF-JUND","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-2682803","identifier":"P17535","identifierLink":"https://www.uniprot.org/uniprotkb/P17535/entry","name":"JUND","description":"Transcription factor JunD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749503","identifier":"Q16520","identifierLink":"https://www.uniprot.org/uniprotkb/Q16520/entry","name":"BATF","description":"Basic leucine zipper transcriptional factor ATF-like","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7014","complexName":"bZIP transcription factor complex, BATF-DBP","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-3908088","identifier":"Q10586","identifierLink":"https://www.uniprot.org/uniprotkb/Q10586/entry","name":"DBP","description":"D site-binding protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11988","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749503","identifier":"Q16520","identifierLink":"https://www.uniprot.org/uniprotkb/Q16520/entry","name":"BATF","description":"Basic leucine zipper transcriptional factor ATF-like","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7015","complexName":"bZIP transcription factor complex, BATF-NFE2L1","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-28952014","identifier":"Q14494-PRO_0000443103","identifierLink":"https://www.uniprot.org/uniprotkb/Q14494-PRO_0000443103/entry","name":"NFE2L1","description":"Transcription factor NRF1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-749503","identifier":"Q16520","identifierLink":"https://www.uniprot.org/uniprotkb/Q16520/entry","name":"BATF","description":"Basic leucine zipper transcriptional factor ATF-like","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7017","complexName":"bZIP transcription factor complex, BATF-NFIL3","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-3951858","identifier":"Q16649","identifierLink":"https://www.uniprot.org/uniprotkb/Q16649/entry","name":"NFIL3","description":"Nuclear factor interleukin-3-regulated protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15284","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749503","identifier":"Q16520","identifierLink":"https://www.uniprot.org/uniprotkb/Q16520/entry","name":"BATF","description":"Basic leucine zipper transcriptional factor ATF-like","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7018","complexName":"bZIP transcription factor complex, BATF-BATF3","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-10312707","identifier":"Q9NR55","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NR55/entry","name":"BATF3","description":"Basic leucine zipper transcriptional factor ATF-like 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749503","identifier":"Q16520","identifierLink":"https://www.uniprot.org/uniprotkb/Q16520/entry","name":"BATF","description":"Basic leucine zipper transcriptional factor ATF-like","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7020","complexName":"PAT intramembrane chaperone complex","organismName":"Homo sapiens; 9606","description":"Intramembrane chaperone that minimizes the misfolding of multi-spanning membrane protein in the endoplasmic reticulum. The complex protects transmembrane domains (TMDs) during assembly by  engaging nascent TMDs that contain unshielded hydrophilic side chains within the lipid bilayer. The protein is released upon correct folding. Acts as part of an ER translocon that functions co-translationally with SEC61 channel-forming translocon complex during biogenesis of multi-pass membrane proteins, along with the GEL multi-spanning membrane protein insertion complex (CPX-5606) and the BOS complex.","predictedComplex":false,"interactors":[{"ac":"EBI-6309120","identifier":"Q9Y284","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y284/entry","name":"WDR83OS","description":"PAT complex subunit Asterix","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13193","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-720151","identifier":"Q96A33","identifierLink":"https://www.uniprot.org/uniprotkb/Q96A33/entry","name":"CCDC47","description":"PAT complex subunit CCDC47","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12883","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7041","complexName":"SARS-CoV-2 Cap(0)-replication and transcription complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","description":"Cap(0)-Replication and transcription complex (RTC) of the SARS-CoV-2 coronavirus. The nsp12 nucleotidyltransferase (NiRAN) domain of the RTC (CPX-6442) possesses guanylyltransferase activity which catalyzes the formation of the cap core structure (GpppA) on the nascent mRNA. nsp9 and nsp12 NiRAN domain recruit the nsp14 ExoN domain of the exoribonuclease proof-reading complex, nsp14-nsp10 (CPX-5692), into the Cap(0)-RTC, forming the N7-CCC (co-transcriptional capping complex) to yield cap(0) (7MeGpppA) at the 5' end of pre-mRNA. \r\n\r\nRNA polymerase has been known to possess a “backtrack” feature, in which the productive elongation and translocation complexes are in the same conformation to facilitate reversible backward motion during RNA synthesis. The SARS-CoV-2 Cap(0)-RTC structure suggests it has the same function here.","predictedComplex":false,"interactors":[{"ac":"EBI-25475877","identifier":"P0DTD1-PRO_0000449627","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTD1-PRO_0000449627/entry","name":"rep","description":"Viral protein genome-linked nsp9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]},{"ac":"EBI-25564924","identifier":"CPX-5692","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-5692","name":"SARS-CoV-2 3'-5' exoribonuclease proof-reading complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]},{"ac":"EBI-26617590","identifier":"CPX-6442","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-6442","name":"SARS-CoV-2 replication and transcription complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]}]},{"complexAC":"CPX-7042","complexName":"SARS-CoV-2 uncleaved Spike protein complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","description":"Spike protein complex of the SARS-CoV-2 coronavirus that binds to human receptor ACE2 (Q9BYF1). May also bind CLEC4M/DC-SIGNR (Q9H2X3) (by homology from SARS-CoV-S (CPX-5694)). Cell entry via binding of Spike to the ACE2 receptor (CPX-5683) relies on two proteolytic cleavage events facilitated by host proteases, such as furin (P09958) and TMPRSS2 (O15393): the first cleavage occurs at the S1/S2 site, the second at the S2' site. Cleavage at the S1/S2 site can occur prior to exit from an infected cell or once bound to ACE2 on the surface of a new host cell. Cleavage at the S2' site occurs only on the surface of the new host cell. While furin is active in the Golgi and on the plasma membrane and can cleave Spike at both cleavage sites, TMPRSS2 only facilitates S2' cleavage on the plasma membrane. \r\n\r\nWhile cleaved Spike (CPX-5682) greatly enhances viral entry into the host cell, it is not strictly required for infection and not all Spike complexes on the viral surface are cleaved. Alternatively, virions can enter the cell via the endosomal pathway and the use of an alternative protease, e.g. cathepsin L (P07711). Some variants of Spike carry mutations in the furin cleavage site that increases the proportion of cleaved Spike complexes which is linked to a higher infectivity of these variants.","predictedComplex":false,"interactors":[{"ac":"EBI-25474821","identifier":"P0DTC2","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTC2/entry","name":"S","description":"Spike glycoprotein","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]}]},{"complexAC":"CPX-7043","complexName":"SARS-CoV-2 post-fusion S2 Spike complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","description":"Post-fusion Spike protein complex of the SARS-CoV-2 coronavirus consisting of three chains of the S2 domain. Cell entry via binding of Spike to the ACE2 receptor (CPX-5683) relies on two proteolytic cleavage events facilitated by host proteases, such as furin (P09958) and TMPRSS2 (O15393): the first cleavage occurs at the S1/S2 site, the second at the S2' site. Cleavage at the S1/S2 site can occur prior to exit from an infected cell or once bound to ACE2 on the surface of a new host cell. Cleavage at the S2' site occurs only on the surface of the new host cell. While furin is active in the Golgi and on the plasma membrane and can cleave Spike at both cleavage sites, TMPRSS2 only facilitates S2' cleavage on the plasma membrane. \r\n\r\nWhile cleaved Spike (CPX-5682) greatly enhances viral entry into the host cell, it is not strictly required for infection and not all Spike complexes on the viral surface are cleaved (CPX-7042). Alternatively, virions can enter the cell via the endosomal pathway and the use of an alternative protease, e.g. cathepsin L (P07711). Some variants of Spike carry mutations in the furin cleavage site that increases the proportion of cleaved Spike complexes which is linked to a higher infectivity of these variants.","predictedComplex":false,"interactors":[{"ac":"EBI-25490326","identifier":"P0DTC2-PRO_0000449648","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTC2-PRO_0000449648/entry","name":"S","description":"Spike protein S2","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]}]},{"complexAC":"CPX-7061","complexName":"bZIP transcription factor complex, BATF2-JUNB","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-742695","identifier":"Q8N1L9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N1L9/entry","name":"BATF2","description":"Basic leucine zipper transcriptional factor ATF-like 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-748062","identifier":"P17275","identifierLink":"https://www.uniprot.org/uniprotkb/P17275/entry","name":"JUNB","description":"Transcription factor JunB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7062","complexName":"Histone-lysine N-methyltransferase complex, KMT2B variant","organismName":"Homo sapiens; 9606","description":"Histone lysine methyltransferase complex which methylates lysine-4 on the histone H3 tail at important regulatory regions in the genome and thus modulates chromatin structures and DNA accessibility. Distinct H3K4 methylation states are recognized by chromatin reader modules leading to specific transcription outcomes.","predictedComplex":false,"interactors":[{"ac":"EBI-396176","identifier":"P51610","identifierLink":"https://www.uniprot.org/uniprotkb/P51610/entry","name":"HCFC1","description":"Host cell factor 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46003","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-540797","identifier":"Q9UBL3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UBL3/entry","name":"ASH2L","description":"Set1/Ash2 histone methyltransferase complex subunit ASH2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10598","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-540834","identifier":"P61964","identifierLink":"https://www.uniprot.org/uniprotkb/P61964/entry","name":"WDR5","description":"WD repeat-containing protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-592728","identifier":"Q9Y5Z7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5Z7/entry","name":"HCFC2","description":"Host cell factor 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46003","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-592789","identifier":"O00255","identifierLink":"https://www.uniprot.org/uniprotkb/O00255/entry","name":"MEN1","description":"Menin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12693","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-592823","identifier":"Q15291","identifierLink":"https://www.uniprot.org/uniprotkb/Q15291/entry","name":"RBBP5","description":"Retinoblastoma-binding protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744973","identifier":"Q9C005","identifierLink":"https://www.uniprot.org/uniprotkb/Q9C005/entry","name":"DPY30","description":"Protein dpy-30 homolog","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-765774","identifier":"Q9UMN6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UMN6/entry","name":"KMT2B","description":"Histone-lysine N-methyltransferase 2B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45838","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-7063","complexName":"bZIP transcription factor complex, BATF2-JUN","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-742695","identifier":"Q8N1L9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N1L9/entry","name":"BATF2","description":"Basic leucine zipper transcriptional factor ATF-like 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-852823","identifier":"P05412","identifierLink":"https://www.uniprot.org/uniprotkb/P05412/entry","name":"JUN","description":"Transcription factor Jun","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7064","complexName":"bZIP transcription factor complex, BATF2-DDIT3","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-742651","identifier":"P35638","identifierLink":"https://www.uniprot.org/uniprotkb/P35638/entry","name":"DDIT3","description":"DNA damage-inducible transcript 3 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16833","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742695","identifier":"Q8N1L9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N1L9/entry","name":"BATF2","description":"Basic leucine zipper transcriptional factor ATF-like 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7065","complexName":"bZIP transcription factor complex, BATF2-CEBPA","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-1172054","identifier":"P49715","identifierLink":"https://www.uniprot.org/uniprotkb/P49715/entry","name":"CEBPA","description":"CCAAT/enhancer-binding protein alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742695","identifier":"Q8N1L9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N1L9/entry","name":"BATF2","description":"Basic leucine zipper transcriptional factor ATF-like 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7066","complexName":"bZIP transcription factor complex, BATF2-CEBPG","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-740209","identifier":"P53567","identifierLink":"https://www.uniprot.org/uniprotkb/P53567/entry","name":"CEBPG","description":"CCAAT/enhancer-binding protein gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742695","identifier":"Q8N1L9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N1L9/entry","name":"BATF2","description":"Basic leucine zipper transcriptional factor ATF-like 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7067","complexName":"bZIP transcription factor complex, BATF2-CEBPE","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-3907048","identifier":"Q15744","identifierLink":"https://www.uniprot.org/uniprotkb/Q15744/entry","name":"CEBPE","description":"CCAAT/enhancer-binding protein epsilon","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742695","identifier":"Q8N1L9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N1L9/entry","name":"BATF2","description":"Basic leucine zipper transcriptional factor ATF-like 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7068","complexName":"bZIP transcription factor complex, BATF2-DBP","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-3908088","identifier":"Q10586","identifierLink":"https://www.uniprot.org/uniprotkb/Q10586/entry","name":"DBP","description":"D site-binding protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11988","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742695","identifier":"Q8N1L9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N1L9/entry","name":"BATF2","description":"Basic leucine zipper transcriptional factor ATF-like 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7081","complexName":"bZIP transcription factor complex, BATF2-HLF","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-2798854","identifier":"Q16534","identifierLink":"https://www.uniprot.org/uniprotkb/Q16534/entry","name":"HLF","description":"Hepatic leukemia factor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11988","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742695","identifier":"Q8N1L9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N1L9/entry","name":"BATF2","description":"Basic leucine zipper transcriptional factor ATF-like 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7083","complexName":"SARS-CoV-2 dimeric Cap(0)-replication and transcription complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","description":"Dimeric Cap(0)-Replication and transcription complex (RTC), dCap(0)-RTC, of the SARS-CoV-2 coronavirus formed by 2 copies of the Cap(0)-RTC (CPX-7041). The nsp12 nucleotidyltransferase (NiRAN) domain of the RTC (CPX-6442) possesses guanylyltransferase activity which catalyzes the formation of the cap core structure (GpppA) on the nascent mRNA. nsp9 and nsp12 NiRAN domain recruit the nsp14 ExoN domain of the exoribonuclease proof-reading complex, nsp14-nsp10 (CPX-5692), into the Cap(0)-RTC, forming the N7-CCC (co-transcriptional capping complex) to yield cap(0) (7MeGpppA) at the 5' end of pre-mRNA. \r\n\r\nRNA polymerase has been known to possess a “backtrack” feature, in which the productive elongation and translocation complexes are in the same conformation to facilitate reversible backward motion during RNA synthesis. The SARS-CoV-2 Cap(0)-RTC structure suggests it has the same function here.","predictedComplex":false,"interactors":[{"ac":"EBI-27089100","identifier":"CPX-7041","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-7041","name":"SARS-CoV-2 Cap(0)-replication and transcription complex","description":null,"stochiometry":"minValue: 2, maxValue: 2","interactorType":"stable complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]}]},{"complexAC":"CPX-7085","complexName":"bZIP transcription factor complex, BATF2-MAFF","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-721128","identifier":"Q9ULX9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ULX9/entry","name":"MAFF","description":"Transcription factor MafF","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742695","identifier":"Q8N1L9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N1L9/entry","name":"BATF2","description":"Basic leucine zipper transcriptional factor ATF-like 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7088","complexName":"SARS-CoV uncleaved Spike protein complex","organismName":"Severe acute respiratory syndrome coronavirus; 694009","description":"Spike protein complex of the SARS-CoV coronavirus that binds to human receptor ACE2 (Q9BYF1) and CLEC4M/DC-SIGNR (Q9H2X3). Cell entry via binding of Spike to the ACE2 receptor (CPX-5695) relies on two proteolytic cleavage events facilitated by host proteases, such as furin (P09958) and TMPRSS2 (O15393): the first cleavage occurs at the S1/S2 site, the second at the S2' site. Cleavage at the S1/S2 site can occur prior to exit from an infected cell or once bound to ACE2 on the surface of a new host cell. Cleavage at the S2' site occurs only on the surface of the new host cell. While furin is active in the Golgi and on the plasma membrane and can cleave Spike at both cleavage sites, TMPRSS2 only facilitates S2' cleavage on the plasma membrane. \r\n\r\nWhile cleaved Spike (CPX-5694) greatly enhances viral entry into the host cell, it is not strictly required for infection and not all Spike complexes on the viral surface are cleaved. Contrary to the activity of Spike in related SARS-CoV-2 (CPX-5682), owing to a different furin cleavage site, cleavage and activation of SARS-CoV Spike by furin and TMPRSS2 is less efficient. It is therefore thought that SARS-CoV virions may rely more heavily on the less efficient cell entry process via endosomes and the use of an alternative protease, e.g. cathepsin L (P07711).","predictedComplex":false,"interactors":[{"ac":"EBI-15582614","identifier":"P59594","identifierLink":"https://www.uniprot.org/uniprotkb/P59594/entry","name":"S","description":"Spike glycoprotein","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus; 694009","xrefs":[]}]},{"complexAC":"CPX-7089","complexName":"MERS-CoV uncleaved Spike protein complex","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","description":"Spike protein complex of the MERS coronavirus that binds to human receptor DPP4 (P27487). Cell entry via binding of Spike to the DPP4 receptor (CPX-5768) relies on two proteolytic cleavage events facilitated by host proteases, such as furin (P09958) and TMPRSS2 (O15393): the first cleavage occurs at the S1/S2 site, the second at the S2' site. Cleavage at the S1/S2 site can occur prior to exit from an infected cell or once bound to DPP4 on the surface of a new host cell. Cleavage at the S2' site occurs only on the surface of the new host cell. While furin is active in the Golgi and on the plasma membrane and can cleave Spike at both cleavage sites, TMPRSS2 only facilitates S2' cleavage on the plasma membrane. \r\n\r\nWhile cleaved Spike (CPX-5766) greatly enhances viral entry into the host cell, it is not strictly required for infection and not all Spike complexes on the viral surface are cleaved. Alternatively, virions can enter the cell via the endosomal pathway and the use of an alternative protease, e.g. cathepsin L (P07711). Some variants of Spike carry mutations in the furin cleavage site that increases the proportion of cleaved Spike complexes which is linked to a higher infectivity of these variants.","predictedComplex":false,"interactors":[{"ac":"EBI-25474996","identifier":"K9N5Q8","identifierLink":"https://www.uniprot.org/uniprotkb/K9N5Q8/entry","name":"S","description":"Spike glycoprotein","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","xrefs":[]}]},{"complexAC":"CPX-7090","complexName":"MERS-CoV uncleaved Spike protein complex","organismName":"Human betacoronavirus 2c EMC/2012; 1235996","description":"Spike protein complex of the MERS coronavirus that binds to human receptor DPP4 (P27487). Cell entry via binding of Spike to the DPP4 receptor (CPX-5768) relies on two proteolytic cleavage events facilitated by host proteases, such as furin (P09958) and TMPRSS2 (O15393): the first cleavage occurs at the S1/S2 site, the second at the S2' site. Cleavage at the S1/S2 site can occur prior to exit from an infected cell or once bound to DPP4 on the surface of a new host cell. Cleavage at the S2' site occurs only on the surface of the new host cell. While furin is active in the Golgi and on the plasma membrane and can cleave Spike at both cleavage sites, TMPRSS2 only facilitates S2' cleavage on the plasma membrane. \r\n\r\nWhile cleaved Spike (CPX-5767) greatly enhances viral entry into the host cell, it is not strictly required for infection and not all Spike complexes on the viral surface are cleaved. Alternatively, virions can enter the cell via the endosomal pathway and the use of an alternative protease, e.g. cathepsin L (P07711). Some variants of Spike carry mutations in the furin cleavage site that increases the proportion of cleaved Spike complexes which is linked to a higher infectivity of these variants.","predictedComplex":false,"interactors":[{"ac":"EBI-16040613","identifier":"K0BRG7","identifierLink":"https://www.uniprot.org/uniprotkb/K0BRG7/entry","name":"S","description":"Spike glycoprotein","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Human betacoronavirus 2c EMC/2012; 1235996","xrefs":[]}]},{"complexAC":"CPX-7091","complexName":"Histone-lysine N-methyltransferase complex, KMT2C variant","organismName":"Homo sapiens; 9606","description":"Histone lysine methyltransferase complex which methylates lysine-4 on the histone H3 tail at important regulatory regions in the genome and thus modulates chromatin structures and DNA accessibility. Distinct H3K4 methylation states are recognized by chromatin reader modules leading to specific transcription outcomes.","predictedComplex":false,"interactors":[{"ac":"EBI-1042997","identifier":"Q8NEZ4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NEZ4/entry","name":"KMT2C","description":"Histone-lysine N-methyltransferase 2C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2372223","identifier":"Q9BTK6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BTK6/entry","name":"PAGR1","description":"PAXIP1-associated glutamate-rich protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28467","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4292203","identifier":"O15550","identifierLink":"https://www.uniprot.org/uniprotkb/O15550/entry","name":"KDM6A","description":"Lysine-specific demethylase 6A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14017","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-540797","identifier":"Q9UBL3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UBL3/entry","name":"ASH2L","description":"Set1/Ash2 histone methyltransferase complex subunit ASH2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10598","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-540834","identifier":"P61964","identifierLink":"https://www.uniprot.org/uniprotkb/P61964/entry","name":"WDR5","description":"WD repeat-containing protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-592823","identifier":"Q15291","identifierLink":"https://www.uniprot.org/uniprotkb/Q15291/entry","name":"RBBP5","description":"Retinoblastoma-binding protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743225","identifier":"Q6ZW49","identifierLink":"https://www.uniprot.org/uniprotkb/Q6ZW49/entry","name":"PAXIP1","description":"PAX-interacting protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23196","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744973","identifier":"Q9C005","identifierLink":"https://www.uniprot.org/uniprotkb/Q9C005/entry","name":"DPY30","description":"Protein dpy-30 homolog","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-78670","identifier":"Q14686","identifierLink":"https://www.uniprot.org/uniprotkb/Q14686/entry","name":"NCOA6","description":"Nuclear receptor coactivator 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15690","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-7092","complexName":"bZIP transcription factor complex, BATF3-BATF3","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. BATF3 has been implicated in the differentiation of CD8+ thymic conventional dendritic cells in the immune system but this may be as a heterodimer with other transcription factors.","predictedComplex":false,"interactors":[{"ac":"EBI-10312707","identifier":"Q9NR55","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NR55/entry","name":"BATF3","description":"Basic leucine zipper transcriptional factor ATF-like 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7093","complexName":"bZIP transcription factor complex, BACH2-BATF3","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-10312707","identifier":"Q9NR55","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NR55/entry","name":"BATF3","description":"Basic leucine zipper transcriptional factor ATF-like 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1642333","identifier":"Q9BYV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BYV9/entry","name":"BACH2","description":"Transcription regulator protein BACH2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7095","complexName":"bZIP transcription factor complex, BATF3-CEBPA","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-10312707","identifier":"Q9NR55","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NR55/entry","name":"BATF3","description":"Basic leucine zipper transcriptional factor ATF-like 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1172054","identifier":"P49715","identifierLink":"https://www.uniprot.org/uniprotkb/P49715/entry","name":"CEBPA","description":"CCAAT/enhancer-binding protein alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7096","complexName":"bZIP transcription factor complex, BATF3-CEBPB","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-10312707","identifier":"Q9NR55","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NR55/entry","name":"BATF3","description":"Basic leucine zipper transcriptional factor ATF-like 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-969696","identifier":"P17676","identifierLink":"https://www.uniprot.org/uniprotkb/P17676/entry","name":"CEBPB","description":"CCAAT/enhancer-binding protein beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7097","complexName":"bZIP transcription factor complex, BATF3-CEBPG","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-10312707","identifier":"Q9NR55","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NR55/entry","name":"BATF3","description":"Basic leucine zipper transcriptional factor ATF-like 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-740209","identifier":"P53567","identifierLink":"https://www.uniprot.org/uniprotkb/P53567/entry","name":"CEBPG","description":"CCAAT/enhancer-binding protein gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7098","complexName":"bZIP transcription factor complex, BATF3-CEBPD","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-10312707","identifier":"Q9NR55","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NR55/entry","name":"BATF3","description":"Basic leucine zipper transcriptional factor ATF-like 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7962058","identifier":"P49716","identifierLink":"https://www.uniprot.org/uniprotkb/P49716/entry","name":"CEBPD","description":"CCAAT/enhancer-binding protein delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7099","complexName":"bZIP transcription factor complex, BATF3-CEBPE","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-10312707","identifier":"Q9NR55","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NR55/entry","name":"BATF3","description":"Basic leucine zipper transcriptional factor ATF-like 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3907048","identifier":"Q15744","identifierLink":"https://www.uniprot.org/uniprotkb/Q15744/entry","name":"CEBPE","description":"CCAAT/enhancer-binding protein epsilon","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7100","complexName":"bZIP transcription factor complex, BATF3-JUN","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site. \r\nBATF3-JUN dimers directly bind to the MYC promoter, contributing to high MYC protein levels in classical Hodgkin lymphoma and anaplastic large cell lymphoma.","predictedComplex":false,"interactors":[{"ac":"EBI-10312707","identifier":"Q9NR55","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NR55/entry","name":"BATF3","description":"Basic leucine zipper transcriptional factor ATF-like 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-852823","identifier":"P05412","identifierLink":"https://www.uniprot.org/uniprotkb/P05412/entry","name":"JUN","description":"Transcription factor Jun","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7101","complexName":"bZIP transcription factor complex, BATF3-JUNB","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. 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Promotes ER-associated protein degradation (ERAD) of the activated IP3 receptor and of 3-hydroxy-3-methylglutaryl-CoA reductase (P04035). May also regulate sterol regulatory element-binding proteins (SREBPs) thus playing a role in cholesterol homeostasis. Also identifed in mitochondria-associated endoplasmic reticulum membranes (MAMs), tethering sites between ER and mitochondria which play a key role in the membrane scrambling and function, and may drive mitochondria-ER crosstalk.","predictedComplex":false,"interactors":[{"ac":"EBI-359299","identifier":"O75477","identifierLink":"https://www.uniprot.org/uniprotkb/O75477/entry","name":"ERLIN1","description":"Erlin-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4400770","identifier":"O94905","identifierLink":"https://www.uniprot.org/uniprotkb/O94905/entry","name":"ERLIN2","description":"Erlin-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7142","complexName":"Hydride transfer complex","organismName":"Homo sapiens; 9606","description":"Catalyzes a metabolic cycle that transfers a hydride anion (H−) from NADH to NADP+, thus regenerating NAD+ and supplying NADPH. Cytosolic PC appears to supply oxaloacetate for NAD+ regeneration via MDH1, which also produces malate that is then converted back to pyruvate by cytosolic ME1, transferring the hydride ion from NADH to NADP+. This cycle overcomes mitochondrial dysfunction and confers fitness to cells under hypoxic conditions but by-passes senescence which prevents cells bearing oncogenic mutations from expanding.","predictedComplex":false,"interactors":[{"ac":"EBI-11958484","identifier":"P48163","identifierLink":"https://www.uniprot.org/uniprotkb/P48163/entry","name":"ME1","description":"NADP-dependent malic enzyme","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23406","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2211322","identifier":"P11498","identifierLink":"https://www.uniprot.org/uniprotkb/P11498/entry","name":"PC","description":"Pyruvate carboxylase, mitochondrial","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43778","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-709625","identifier":"P40925","identifierLink":"https://www.uniprot.org/uniprotkb/P40925/entry","name":"MDH1","description":"Malate dehydrogenase, cytoplasmic","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23382","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7143","complexName":"ESCRT-0 complex, STAM2 variant","organismName":"Homo sapiens; 9606","description":"The ESCRT machinery, consisting of ESCRT-0  (this complex), -I, -II (CPX-2506), -III (CPX-329) and -IV (VPS4A/B complex, CPX-338)  has been implicated in membrane scission steps, transforming a single, continuous bilayer into two distinct bilayers, either from within the neck of a vesicle budding away from the cytoplasm or from within a membrane tubule, while segregating cargo throughout the process. Membrane fission processes include: a) the sorting of multivesicular bodies (MVB) in the endocytic pathway; cargoes destined for inclusion into the MVB pathway are covalently modified with ubiquitin, recognized by ubiquitin-binding domains in the early ESCRTs (ESCRT-0, -I, and -II) and sequestered into endosomal microdomains that bud into the endosome as intralumenal vesicles aided by ESCRT-III, b) downregulation of cell-surface receptors, c) repair of plasma membrane wounds, d) abscission of the cellular bridge during cytokineses, d) nuclear envelope sealing by annular fusion and e) budding of virions (especially HIV-1) from the plasma membrane. The ESCRT machinery seems to play an indirect role in the proper functioning of cellular polarity and migration, the miRNA machinery and gene expression regulation. ESCRT-0 binds to and clusters ubiquitinated cargo for delivery into MVBs, and recruits clathrin, ubiquitin ligases, and deubiquitinating enzymes. ESCRT-0 recruits ESCRT-I which engages ESCRT-II to nucleate ESCRT-III polymerization. VPS4A/B complex, also known as ESCRT-IV, disassembles ESCRT-III to recycle its subunits. The ESCRT-III complex facilitates changes in membrane architecture by oligomerizing to form spiral, filament-like tubules, accumulation of which is associated with membrane constriction and fission. Disassembly of ESCRT-III by VPS4A/B may be a required step for fission.","predictedComplex":false,"interactors":[{"ac":"EBI-373258","identifier":"O75886","identifierLink":"https://www.uniprot.org/uniprotkb/O75886/entry","name":"STAM2","description":"Signal transducing adapter molecule 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45929","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-740220","identifier":"O14964","identifierLink":"https://www.uniprot.org/uniprotkb/O14964/entry","name":"HGS","description":"Hepatocyte growth factor-regulated tyrosine kinase substrate","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46275","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7146","complexName":"ESCRT-I complex, VPS37A-MVB12B variant","organismName":"Homo sapiens; 9606","description":"The ESCRT machinery, consisting of ESCRT-0  (this complex), -I, -II (CPX-2506), -III (CPX-329) and -IV (VPS4A/B complex, CPX-338)  has been implicated in membrane scission steps, transforming a single, continuous bilayer into two distinct bilayers, either from within the neck of a vesicle budding away from the cytoplasm or from within a membrane tubule, while segregating cargo throughout the process. Membrane fission processes include: a) the sorting of multivesicular bodies (MVB) in the endocytic pathway; cargoes destined for inclusion into the MVB pathway are covalently modified with ubiquitin, recognized by ubiquitin-binding domains in the early ESCRTs (ESCRT-0, -I, and -II) and sequestered into endosomal microdomains that bud into the endosome as intralumenal vesicles aided by ESCRT-III, b) downregulation of cell-surface receptors, c) repair of plasma membrane wounds, d) abscission of the cellular bridge during cytokineses, d) nuclear envelope sealing by annular fusion and e) budding of virions (especially HIV-1) from the plasma membrane. The ESCRT machinery seems to play an indirect role in the proper functioning of cellular polarity and migration, the miRNA machinery and gene expression regulation. ESCRT-0 binds to and clusters ubiquitinated cargo for delivery into MVBs, and recruits clathrin, ubiquitin ligases, and deubiquitinating enzymes. ESCRT-0 recruits ESCRT-I which engages ESCRT-II to nucleate ESCRT-III polymerization. VPS4A/B complex, also known as ESCRT-IV, disassembles ESCRT-III to recycle its subunits. The ESCRT-III complex facilitates changes in membrane architecture by oligomerizing to form spiral, filament-like tubules, accumulation of which is associated with membrane constriction and fission. Disassembly of ESCRT-III by VPS4A/B may be a required step for fission.","predictedComplex":false,"interactors":[{"ac":"EBI-27106929","identifier":"Q9H7P6-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H7P6-1/entry","name":"MVB12B","description":"Multivesicular body subunit 12B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2850578","identifier":"Q8NEZ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NEZ2/entry","name":"VPS37A","description":"Vacuolar protein sorting-associated protein 37A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-346882","identifier":"Q99816","identifierLink":"https://www.uniprot.org/uniprotkb/Q99816/entry","name":"TSG101","description":"Tumor susceptibility gene 101 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23306","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727424","identifier":"Q9UK41","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK41/entry","name":"VPS28","description":"Vacuolar protein sorting-associated protein 28 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7147","complexName":"ESCRT-I complex, VPS37C-MVB12A variant","organismName":"Homo sapiens; 9606","description":"The ESCRT machinery, consisting of ESCRT-0  (this complex), -I, -II (CPX-2506), -III (CPX-329) and -IV (VPS4A/B complex, CPX-338)  has been implicated in membrane scission steps, transforming a single, continuous bilayer into two distinct bilayers, either from within the neck of a vesicle budding away from the cytoplasm or from within a membrane tubule, while segregating cargo throughout the process. Membrane fission processes include: a) the sorting of multivesicular bodies (MVB) in the endocytic pathway; cargoes destined for inclusion into the MVB pathway are covalently modified with ubiquitin, recognized by ubiquitin-binding domains in the early ESCRTs (ESCRT-0, -I, and -II) and sequestered into endosomal microdomains that bud into the endosome as intralumenal vesicles aided by ESCRT-III, b) downregulation of cell-surface receptors, c) repair of plasma membrane wounds, d) abscission of the cellular bridge during cytokineses, d) nuclear envelope sealing by annular fusion and e) budding of virions (especially HIV-1) from the plasma membrane. The ESCRT machinery seems to play an indirect role in the proper functioning of cellular polarity and migration, the miRNA machinery and gene expression regulation. ESCRT-0 binds to and clusters ubiquitinated cargo for delivery into MVBs, and recruits clathrin, ubiquitin ligases, and deubiquitinating enzymes. ESCRT-0 recruits ESCRT-I which engages ESCRT-II to nucleate ESCRT-III polymerization. VPS4A/B complex, also known as ESCRT-IV, disassembles ESCRT-III to recycle its subunits. The ESCRT-III complex facilitates changes in membrane architecture by oligomerizing to form spiral, filament-like tubules, accumulation of which is associated with membrane constriction and fission. Disassembly of ESCRT-III by VPS4A/B may be a required step for fission.","predictedComplex":false,"interactors":[{"ac":"EBI-2559305","identifier":"A5D8V6","identifierLink":"https://www.uniprot.org/uniprotkb/A5D8V6/entry","name":"VPS37C","description":"Vacuolar protein sorting-associated protein 37C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-346882","identifier":"Q99816","identifierLink":"https://www.uniprot.org/uniprotkb/Q99816/entry","name":"TSG101","description":"Tumor susceptibility gene 101 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23306","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4290865","identifier":"Q96EY5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96EY5/entry","name":"MVB12A","description":"Multivesicular body subunit 12A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31612","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727424","identifier":"Q9UK41","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK41/entry","name":"VPS28","description":"Vacuolar protein sorting-associated protein 28 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7148","complexName":"ESCRT-I complex, VPS37D-MVB12A variant","organismName":"Homo sapiens; 9606","description":"The ESCRT machinery, consisting of ESCRT-0  (this complex), -I, -II (CPX-2506), -III (CPX-329) and -IV (VPS4A/B complex, CPX-338)  has been implicated in membrane scission steps, transforming a single, continuous bilayer into two distinct bilayers, either from within the neck of a vesicle budding away from the cytoplasm or from within a membrane tubule, while segregating cargo throughout the process. Membrane fission processes include: a) the sorting of multivesicular bodies (MVB) in the endocytic pathway; cargoes destined for inclusion into the MVB pathway are covalently modified with ubiquitin, recognized by ubiquitin-binding domains in the early ESCRTs (ESCRT-0, -I, and -II) and sequestered into endosomal microdomains that bud into the endosome as intralumenal vesicles aided by ESCRT-III, b) downregulation of cell-surface receptors, c) repair of plasma membrane wounds, d) abscission of the cellular bridge during cytokineses, d) nuclear envelope sealing by annular fusion and e) budding of virions (especially HIV-1) from the plasma membrane. The ESCRT machinery seems to play an indirect role in the proper functioning of cellular polarity and migration, the miRNA machinery and gene expression regulation. ESCRT-0 binds to and clusters ubiquitinated cargo for delivery into MVBs, and recruits clathrin, ubiquitin ligases, and deubiquitinating enzymes. ESCRT-0 recruits ESCRT-I which engages ESCRT-II to nucleate ESCRT-III polymerization. VPS4A/B complex, also known as ESCRT-IV, disassembles ESCRT-III to recycle its subunits. The ESCRT-III complex facilitates changes in membrane architecture by oligomerizing to form spiral, filament-like tubules, accumulation of which is associated with membrane constriction and fission. Disassembly of ESCRT-III by VPS4A/B may be a required step for fission.","predictedComplex":false,"interactors":[{"ac":"EBI-346882","identifier":"Q99816","identifierLink":"https://www.uniprot.org/uniprotkb/Q99816/entry","name":"TSG101","description":"Tumor susceptibility gene 101 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23306","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4290865","identifier":"Q96EY5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96EY5/entry","name":"MVB12A","description":"Multivesicular body subunit 12A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31612","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727424","identifier":"Q9UK41","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK41/entry","name":"VPS28","description":"Vacuolar protein sorting-associated protein 28 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7604353","identifier":"Q86XT2","identifierLink":"https://www.uniprot.org/uniprotkb/Q86XT2/entry","name":"VPS37D","description":"Vacuolar protein sorting-associated protein 37D","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7162","complexName":"ESCRT-I complex, VPS37A-MVB12A variant","organismName":"Homo sapiens; 9606","description":"The ESCRT machinery, consisting of ESCRT-0  (this complex), -I, -II (CPX-2506), -III (CPX-329) and -IV (VPS4A/B complex, CPX-338)  has been implicated in membrane scission steps, transforming a single, continuous bilayer into two distinct bilayers, either from within the neck of a vesicle budding away from the cytoplasm or from within a membrane tubule, while segregating cargo throughout the process. Membrane fission processes include: a) the sorting of multivesicular bodies (MVB) in the endocytic pathway; cargoes destined for inclusion into the MVB pathway are covalently modified with ubiquitin, recognized by ubiquitin-binding domains in the early ESCRTs (ESCRT-0, -I, and -II) and sequestered into endosomal microdomains that bud into the endosome as intralumenal vesicles aided by ESCRT-III, b) downregulation of cell-surface receptors, c) repair of plasma membrane wounds, d) abscission of the cellular bridge during cytokineses, d) nuclear envelope sealing by annular fusion and e) budding of virions (especially HIV-1) from the plasma membrane. The ESCRT machinery seems to play an indirect role in the proper functioning of cellular polarity and migration, the miRNA machinery and gene expression regulation. ESCRT-0 binds to and clusters ubiquitinated cargo for delivery into MVBs, and recruits clathrin, ubiquitin ligases, and deubiquitinating enzymes. ESCRT-0 recruits ESCRT-I which engages ESCRT-II to nucleate ESCRT-III polymerization. VPS4A/B complex, also known as ESCRT-IV, disassembles ESCRT-III to recycle its subunits. The ESCRT-III complex facilitates changes in membrane architecture by oligomerizing to form spiral, filament-like tubules, accumulation of which is associated with membrane constriction and fission. Disassembly of ESCRT-III by VPS4A/B may be a required step for fission.","predictedComplex":false,"interactors":[{"ac":"EBI-2850578","identifier":"Q8NEZ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NEZ2/entry","name":"VPS37A","description":"Vacuolar protein sorting-associated protein 37A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-346882","identifier":"Q99816","identifierLink":"https://www.uniprot.org/uniprotkb/Q99816/entry","name":"TSG101","description":"Tumor susceptibility gene 101 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23306","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4290865","identifier":"Q96EY5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96EY5/entry","name":"MVB12A","description":"Multivesicular body subunit 12A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31612","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727424","identifier":"Q9UK41","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK41/entry","name":"VPS28","description":"Vacuolar protein sorting-associated protein 28 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7164","complexName":"ESCRT-I complex, VPS37B-MVB12B variant","organismName":"Homo sapiens; 9606","description":"The ESCRT machinery, consisting of ESCRT-0  (this complex), -I, -II (CPX-2506), -III (CPX-329) and -IV (VPS4A/B complex, CPX-338)  has been implicated in membrane scission steps, transforming a single, continuous bilayer into two distinct bilayers, either from within the neck of a vesicle budding away from the cytoplasm or from within a membrane tubule, while segregating cargo throughout the process. Membrane fission processes include: a) the sorting of multivesicular bodies (MVB) in the endocytic pathway; cargoes destined for inclusion into the MVB pathway are covalently modified with ubiquitin, recognized by ubiquitin-binding domains in the early ESCRTs (ESCRT-0, -I, and -II) and sequestered into endosomal microdomains that bud into the endosome as intralumenal vesicles aided by ESCRT-III, b) downregulation of cell-surface receptors, c) repair of plasma membrane wounds, d) abscission of the cellular bridge during cytokineses, d) nuclear envelope sealing by annular fusion and e) budding of virions (especially HIV-1) from the plasma membrane. The ESCRT machinery seems to play an indirect role in the proper functioning of cellular polarity and migration, the miRNA machinery and gene expression regulation. ESCRT-0 binds to and clusters ubiquitinated cargo for delivery into MVBs, and recruits clathrin, ubiquitin ligases, and deubiquitinating enzymes. ESCRT-0 recruits ESCRT-I which engages ESCRT-II to nucleate ESCRT-III polymerization. VPS4A/B complex, also known as ESCRT-IV, disassembles ESCRT-III to recycle its subunits. The ESCRT-III complex facilitates changes in membrane architecture by oligomerizing to form spiral, filament-like tubules, accumulation of which is associated with membrane constriction and fission. Disassembly of ESCRT-III by VPS4A/B may be a required step for fission.","predictedComplex":false,"interactors":[{"ac":"EBI-27106929","identifier":"Q9H7P6-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H7P6-1/entry","name":"MVB12B","description":"Multivesicular body subunit 12B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-346882","identifier":"Q99816","identifierLink":"https://www.uniprot.org/uniprotkb/Q99816/entry","name":"TSG101","description":"Tumor susceptibility gene 101 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23306","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4400866","identifier":"Q9H9H4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H9H4/entry","name":"VPS37B","description":"Vacuolar protein sorting-associated protein 37B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727424","identifier":"Q9UK41","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK41/entry","name":"VPS28","description":"Vacuolar protein sorting-associated protein 28 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7165","complexName":"bZIP transcription factor complex, BACH1-MAFF","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site. Acts as a transcriptional repressor binding to the MARE (Maf recognition element) site in gene promoters, thus repressing the expression of NFE2L2 (Q16236) target genes which play a key role in the response to oxidative stress. Represses the transcription of heme oxygenase 1 (P09601) under low heme conditions. When free heme levels rise, activated NFE2L2 partners with MAF proteins to enable transactivation of HMOX1. Heme binds to BACH1 and heme-bound BACH1 undergoes nuclear export and ubiquitin-dependent degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-1263541","identifier":"O14867","identifierLink":"https://www.uniprot.org/uniprotkb/O14867/entry","name":"BACH1","description":"Transcription regulator protein BACH1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-721128","identifier":"Q9ULX9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ULX9/entry","name":"MAFF","description":"Transcription factor MafF","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7166","complexName":"ESCRT-I complex, VPS37C-MVB12B variant","organismName":"Homo sapiens; 9606","description":"The ESCRT machinery, consisting of ESCRT-0  (this complex), -I, -II (CPX-2506), -III (CPX-329) and -IV (VPS4A/B complex, CPX-338)  has been implicated in membrane scission steps, transforming a single, continuous bilayer into two distinct bilayers, either from within the neck of a vesicle budding away from the cytoplasm or from within a membrane tubule, while segregating cargo throughout the process. Membrane fission processes include: a) the sorting of multivesicular bodies (MVB) in the endocytic pathway; cargoes destined for inclusion into the MVB pathway are covalently modified with ubiquitin, recognized by ubiquitin-binding domains in the early ESCRTs (ESCRT-0, -I, and -II) and sequestered into endosomal microdomains that bud into the endosome as intralumenal vesicles aided by ESCRT-III, b) downregulation of cell-surface receptors, c) repair of plasma membrane wounds, d) abscission of the cellular bridge during cytokineses, d) nuclear envelope sealing by annular fusion and e) budding of virions (especially HIV-1) from the plasma membrane. The ESCRT machinery seems to play an indirect role in the proper functioning of cellular polarity and migration, the miRNA machinery and gene expression regulation. ESCRT-0 binds to and clusters ubiquitinated cargo for delivery into MVBs, and recruits clathrin, ubiquitin ligases, and deubiquitinating enzymes. ESCRT-0 recruits ESCRT-I which engages ESCRT-II to nucleate ESCRT-III polymerization. VPS4A/B complex, also known as ESCRT-IV, disassembles ESCRT-III to recycle its subunits. The ESCRT-III complex facilitates changes in membrane architecture by oligomerizing to form spiral, filament-like tubules, accumulation of which is associated with membrane constriction and fission. Disassembly of ESCRT-III by VPS4A/B may be a required step for fission.","predictedComplex":false,"interactors":[{"ac":"EBI-2559305","identifier":"A5D8V6","identifierLink":"https://www.uniprot.org/uniprotkb/A5D8V6/entry","name":"VPS37C","description":"Vacuolar protein sorting-associated protein 37C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27106929","identifier":"Q9H7P6-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H7P6-1/entry","name":"MVB12B","description":"Multivesicular body subunit 12B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-346882","identifier":"Q99816","identifierLink":"https://www.uniprot.org/uniprotkb/Q99816/entry","name":"TSG101","description":"Tumor susceptibility gene 101 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23306","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727424","identifier":"Q9UK41","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK41/entry","name":"VPS28","description":"Vacuolar protein sorting-associated protein 28 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7167","complexName":"ESCRT-I complex, VPS37D-MVB12B variant","organismName":"Homo sapiens; 9606","description":"The ESCRT machinery, consisting of ESCRT-0  (this complex), -I, -II (CPX-2506), -III (CPX-329) and -IV (VPS4A/B complex, CPX-338)  has been implicated in membrane scission steps, transforming a single, continuous bilayer into two distinct bilayers, either from within the neck of a vesicle budding away from the cytoplasm or from within a membrane tubule, while segregating cargo throughout the process. Membrane fission processes include: a) the sorting of multivesicular bodies (MVB) in the endocytic pathway; cargoes destined for inclusion into the MVB pathway are covalently modified with ubiquitin, recognized by ubiquitin-binding domains in the early ESCRTs (ESCRT-0, -I, and -II) and sequestered into endosomal microdomains that bud into the endosome as intralumenal vesicles aided by ESCRT-III, b) downregulation of cell-surface receptors, c) repair of plasma membrane wounds, d) abscission of the cellular bridge during cytokineses, d) nuclear envelope sealing by annular fusion and e) budding of virions (especially HIV-1) from the plasma membrane. The ESCRT machinery seems to play an indirect role in the proper functioning of cellular polarity and migration, the miRNA machinery and gene expression regulation. ESCRT-0 binds to and clusters ubiquitinated cargo for delivery into MVBs, and recruits clathrin, ubiquitin ligases, and deubiquitinating enzymes. ESCRT-0 recruits ESCRT-I which engages ESCRT-II to nucleate ESCRT-III polymerization. VPS4A/B complex, also known as ESCRT-IV, disassembles ESCRT-III to recycle its subunits. The ESCRT-III complex facilitates changes in membrane architecture by oligomerizing to form spiral, filament-like tubules, accumulation of which is associated with membrane constriction and fission. Disassembly of ESCRT-III by VPS4A/B may be a required step for fission.","predictedComplex":false,"interactors":[{"ac":"EBI-27106929","identifier":"Q9H7P6-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H7P6-1/entry","name":"MVB12B","description":"Multivesicular body subunit 12B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-346882","identifier":"Q99816","identifierLink":"https://www.uniprot.org/uniprotkb/Q99816/entry","name":"TSG101","description":"Tumor susceptibility gene 101 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23306","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727424","identifier":"Q9UK41","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK41/entry","name":"VPS28","description":"Vacuolar protein sorting-associated protein 28 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7604353","identifier":"Q86XT2","identifierLink":"https://www.uniprot.org/uniprotkb/Q86XT2/entry","name":"VPS37D","description":"Vacuolar protein sorting-associated protein 37D","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3262","complexName":"Kv4.3-KChIP1 channel complex","organismName":"Mus musculus; 10090","description":"Member of the transient outward (A-type), rapidly inactivating voltage-gated potassium channels, also called the D member of the Shal-related voltage-gated potassium channels. A transmembrane channel specific for potassium and sensitive to voltage changes in the cell's membrane potential, composed of alpha and beta subunits. Alpha subunit (Kv4.3), is a potassium voltage-gated channel subfamily D member 3 protein, encoded by the Kcnd3 gene. Beta subunit is an auxiliary, regulatory subunit, called Kv channel-interacting protein 1 (KChIP1) that modulates channels density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent manner. During action potentials, the channel plays a crucial role in returning the depolarized cell to a resting state (repolarisation phase). It contributes to the cardiac transient outward current I(TO) in the heart and the somatodendritic A-type current  I(SA) in neurons.These currents operate at subthreshold membrane potentials to control the excitability of neurons and cardiac myocytes.","predictedComplex":false,"interactors":[{"ac":"EBI-8328087","identifier":"Q9Z0V1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0V1/entry","name":"Kcnd3","description":"A-type voltage-gated potassium channel KCND3","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11537","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9843856","identifier":"Q9JJ57","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JJ57/entry","name":"Kcnip1","description":"A-type potassium channel modulatory protein KCNIP1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23055","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3265","complexName":"Ribosome quality control complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A 60S-ribosomal subunit-associated complex involved in ubiquitin proteasome mediated degradation of  polypeptides whose translation is stalled on the ribosome. The abnormal stalled ribosome is recognized and ubiquitinated at one or more specific residues by the E3 ubiquitin ligase HEL2 (Q05580) . Ribosome ubiquitination induces subunit dissociation by the RQT complex (CPX-6643). Dissociation of the 40S subunits allows binding of 60S ribosome-nascent chains to RQC2, which recruits the LTN1 E3 ubiquitin ligase.  LTN1 ubiquitinates the nascent polypeptide chains, targeting them for degradation. RQC2 attaches C-terminal alanyl/threonyl sequences to stalled polypeptides. The ATPase CDC48 and cofactors UFD1 and NPL4 unfold ubiquitinated polypeptides, then extracts the peptidyl-tRNA from the 60S, thereby recruiting it to the 26S proteasome for degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-12193","identifier":"P33755","identifierLink":"https://www.uniprot.org/uniprotkb/P33755/entry","name":"NPL4","description":"Nuclear protein localization protein 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12710","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19997","identifier":"P53044","identifierLink":"https://www.uniprot.org/uniprotkb/P53044/entry","name":"UFD1","description":"Ubiquitin fusion degradation protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12555","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32961","identifier":"Q05468","identifierLink":"https://www.uniprot.org/uniprotkb/Q05468/entry","name":"RQC1","description":"Ribosome quality control complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-33283","identifier":"Q12532","identifierLink":"https://www.uniprot.org/uniprotkb/Q12532/entry","name":"RQC2","description":"Ribosome quality control complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3773151","identifier":"Q04781","identifierLink":"https://www.uniprot.org/uniprotkb/Q04781/entry","name":"RKR1","description":"E3 ubiquitin-protein ligase listerin","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12389","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4308","identifier":"P25694","identifierLink":"https://www.uniprot.org/uniprotkb/P25694/entry","name":"CDC48","description":"Cell division control protein 48","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3268","complexName":"Cyclin-dependent protein kinase-activating kinase complex","organismName":"Mus musculus; 10090","description":"Cyclin-dependent kinase (CDK) activation minimally depends on two events: binding to a cyclin and phosphorylation of a conserved Thr residue in the activation (T) loop. CAK activates the cyclin-associated kinases CDK1 (P11440), CDK2 (P97377), CDK4 (P30285) and CDK6 Q64261) by threonine phosphorylation, thus regulating cell cycle progression. CAK activity is itself regulated throughout the cell cycle by T-loop phosphorylation of CDK7 on Thr-170. Phosphorylation of Ser-164 during mitosis inactivates the enzyme. \r\nIn the transcription cycle, CAK serine phosphorylates the carboxyl-terminal domain (CTD) of RNA polymerase II (POLR2A, P08775) and other proteins, as part of the general transcription factor TFIIH. Phosphorylation of POLR2A in complex with DNA promotes transcription initiation by triggering dissociation from DNA. CAK also phosphorylates CDK9 (P-TEFb, Q99J95), which releases POLR2A from the promoter and and enables elongation of the transcripts.","predictedComplex":false,"interactors":[{"ac":"EBI-6260998","identifier":"P51949","identifierLink":"https://www.uniprot.org/uniprotkb/P51949/entry","name":"Mnat1","description":"CDK-activating kinase assembly factor MAT1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12683","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6261044","identifier":"Q03147","identifierLink":"https://www.uniprot.org/uniprotkb/Q03147/entry","name":"Cdk7","description":"Cyclin-dependent kinase 7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8419314","identifier":"Q61458","identifierLink":"https://www.uniprot.org/uniprotkb/Q61458/entry","name":"Ccnh","description":"Cyclin-H","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3269","complexName":"IkappaB kinase complex","organismName":"Homo sapiens; 9606","description":"Phosphorylates inhibitory-kappaB (I-kappaB) proteins and a range of other substrates, many found in the NF-kappaB signalling cascade thereby both positively and negatively regulating the NF-kappaB signalling pathway. Also active in the insulin signalling pathway, mTOR pathway and other tumorigenesis promoting pathways. \r\n\r\nThe activation of IKBKB and presence of NEMO are required for the canonical NF-kappaB pathway triggered by proinflammatory stimuli while the activation of CHUK is required for the alternative NF-kappaB pathway triggered by a multitude of ligands. \r\n\r\nThe kinase subunits are activated by phosphorylation on Ser-177 and Ser-181 of IKBKB/IKKB and Ser-176 and Ser-180 of CHUK/IKKA. Kinase subunits may cis-autophosphorylate, trans-autophosphorylate or be phosphorylated by other kinases (the identity of which is not certain).","predictedComplex":false,"interactors":[{"ac":"EBI-81249","identifier":"O15111","identifierLink":"https://www.uniprot.org/uniprotkb/O15111/entry","name":"CHUK","description":"Inhibitor of nuclear factor kappa-B kinase subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22969","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-81266","identifier":"O14920","identifierLink":"https://www.uniprot.org/uniprotkb/O14920/entry","name":"IKBKB","description":"Inhibitor of nuclear factor kappa-B kinase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22969","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-81279","identifier":"Q9Y6K9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6K9/entry","name":"IKBKG","description":"NF-kappa-B essential modulator","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3270","complexName":"IkappaB kinase complex","organismName":"Mus musculus; 10090","description":"Phosphorylates inhibitory-kappaB (I-kappaB) proteins and a range of other substrates, many found in the NF-kappaB signalling cascade thereby both positively and negatively regulating the NF-kappaB signalling pathway. Also active in the insulin signalling pathway, mTOR pathway and other tumorigenesis promoting pathways. \r\n\r\nThe activation of IKBKB and presence of NEMO are required for the canonical NF-kappaB pathway triggered by proinflammatory stimuli while the activation of CHUK is required for the alternative NF-kappaB pathway triggered by a multitude of ligands. \r\n\r\nThe kinase subunits are activated by phosphorylation on Ser-177 and Ser-181 of Ikbkb/Ikkb and Ser-176 and Ser-180 of Chuk/Ikka. Kinase subunits may cis-autophosphorylate, trans-autophosphorylate or be phosphorylated by other kinases (the identity of which is not certain).","predictedComplex":false,"interactors":[{"ac":"EBI-447960","identifier":"O88351","identifierLink":"https://www.uniprot.org/uniprotkb/O88351/entry","name":"Ikbkb","description":"Inhibitor of nuclear factor kappa-B kinase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22969","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-646245","identifier":"Q60680","identifierLink":"https://www.uniprot.org/uniprotkb/Q60680/entry","name":"Chuk","description":"Inhibitor of nuclear factor kappa-B kinase subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22969","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-998011","identifier":"O88522","identifierLink":"https://www.uniprot.org/uniprotkb/O88522/entry","name":"Ikbkg","description":"NF-kappa-B essential modulator","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR31553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3271","complexName":"KCNQ1-KCNE1 I(Ks) channel complex","organismName":"Homo sapiens; 9606","description":"A voltage-gated K+ channel that produces the delayed rectifier, slow K+ current (IKs) in cardiac myocytes. IKs is a major repolarization current in the heart that responds rapidly and robustly to sympathetic nervous system stimulation. \r\n\r\nBinding of beta subunit MinK (KCNE1) modifies the gating properties of the channel: it increases the single channel conductance, slows the rate of activation and removes (or greatly slows) inactivation of KCNQ1 alpha subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-359667","identifier":"P51787","identifierLink":"https://www.uniprot.org/uniprotkb/P51787/entry","name":"KCNQ1","description":"Potassium voltage-gated channel subfamily KQT member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11537","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7043557","identifier":"P15382","identifierLink":"https://www.uniprot.org/uniprotkb/P15382/entry","name":"KCNE1","description":"Potassium voltage-gated channel subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15282","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3272","complexName":"CENP-A recruiting complex","organismName":"Homo sapiens; 9606","description":"Orchestrates the deposition of CENP-A, the centromere-specific histone H3 variant which is required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. The redistribution of CENP-A nucleosomes between the two new DNA strands is necessary to maintain the epigenetic mark of the centromere and leads to the dilution of CENP-A nucleosomes. The Mis18 complex localizes to centromeres just prior to the pre-nucleosomal HJURP/CENP-A/H4 complex and is absolutely required for the CENP-A-specific chaperone, Holliday junction recognition protein (HJURP, Q8NCD3) to reach the centromeres. CDK phosphorylation of MISBP1 during G2 and mitosis, prior to the metaphase-to-anaphase transition, negatively regulates complex assembly. Plk1 phosphorylation activates Mis18 complex recruitment to the centromeres during G1.","predictedComplex":false,"interactors":[{"ac":"EBI-1104552","identifier":"Q9NYP9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NYP9/entry","name":"MIS18A","description":"Protein Mis18-alpha","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16431","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-536879","identifier":"O43482","identifierLink":"https://www.uniprot.org/uniprotkb/O43482/entry","name":"OIP5","description":"Protein Mis18-beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16431","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9870821","identifier":"Q6P0N0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P0N0/entry","name":"MIS18BP1","description":"Mis18-binding protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16124","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3273","complexName":"CENP-A recruiting complex","organismName":"Mus musculus; 10090","description":"Orchestrates the deposition of CENP-A, the centromere-specific histone H3 variant which is required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. The redistribution of CENP-A nucleosomes between the two new DNA strands is necessary to maintain the epigenetic mark of the centromere and leads to the dilution of CENP-A nucleosomes. The Mis18 complex localizes to centromeres just prior to the pre-nucleosomal HJURP/CENP-A/H4 complex and is absolutely required for the CENP-A-specific chaperone, Holliday junction recognition protein (HJURP, Q6PG16) to reach the centromeres. CDK phosphorylation of MISBP1 during G2 and mitosis, prior to the metaphase-to-anaphase transition, negatively regulates complex assembly. Plk1 phosphorylation activates Mis18 complex recruitment to the centromeres during G1.","predictedComplex":false,"interactors":[{"ac":"EBI-9874001","identifier":"A2AQ14","identifierLink":"https://www.uniprot.org/uniprotkb/A2AQ14/entry","name":"Oip5","description":"Protein Mis18-beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16431","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9874022","identifier":"Q9CZJ6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CZJ6/entry","name":"Mis18a","description":"Protein Mis18-alpha","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16431","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9874042","identifier":"Q80WQ8","identifierLink":"https://www.uniprot.org/uniprotkb/Q80WQ8/entry","name":"Mis18bp1","description":"Mis18-binding protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16124","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3274","complexName":"KCNQ1-KCNE1 I(Ks) channel complex","organismName":"Mus musculus; 10090","description":"A voltage-gated K+ channel that produces the delayed rectifier, slow K+ current (IKs) in cardiac myocytes. IKS is a major repolarization current in the heart that responds rapidly and robustly to sympathetic nervous system stimulation. \r\n\r\nBinding of beta subunit MinK (KCNE1) modifies the gating properties of the channel: it increases the single channel conductance, slows the rate of activation and removes (or greatly slows) inactivation of KCNQ1 alpha subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-9688385","identifier":"P23299","identifierLink":"https://www.uniprot.org/uniprotkb/P23299/entry","name":"Kcne1","description":"Potassium voltage-gated channel subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15282","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9869724","identifier":"P97414","identifierLink":"https://www.uniprot.org/uniprotkb/P97414/entry","name":"Kcnq1","description":"Potassium voltage-gated channel subfamily KQT member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11537","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3275","complexName":"I(KACh) inward rectifier potassium channel complex","organismName":"Bos taurus; 9913","description":"The GIRK1-GIRK4, or I(KACh) potassium channel is a member of the G protein-coupled inward rectifier potassium channels. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. I(KACh) is expressed in cardiac muscle, specifically the sinoatrial node and atria. Regulation of I(KACh) via G protein-coupled receptor signaling underlies the control of heart rate. I(KACh) channel couples to the muscarinic M2 and adenosine A1 receptors. Binding of acetylcholine or adenosine to its respective receptor activates I(KACh), which plays a crucial role in regulating the heartbeat.","predictedComplex":false,"interactors":[{"ac":"EBI-9973944","identifier":"F1MYR9","identifierLink":"https://www.uniprot.org/uniprotkb/F1MYR9/entry","name":"KCNJ5","description":"G protein-activated inward rectifier potassium channel 4","stochiometry":null,"interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR11767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9973959","identifier":"E1BNE9","identifierLink":"https://www.uniprot.org/uniprotkb/E1BNE9/entry","name":"KCNJ3","description":"G protein-activated inward rectifier potassium channel 1","stochiometry":null,"interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR11767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3276","complexName":"I(KACh) inward rectifier potassium channel complex","organismName":"Rattus norvegicus; 10116","description":"The GIRK1-GIRK4, or I(KACh) potassium channel is a member of the G protein-coupled inward rectifier potassium channels. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. I(KACh) is expressed in cardiac muscle, specifically the sinoatrial node and atria. Regulation of I(KACh) via G protein-coupled receptor signaling underlies the control of heart rate. I(KACh) channel couples to the muscarinic M2 and adenosine A1 receptors. Binding of acetylcholine or adenosine to its respective receptor activates I(KACh), which plays a crucial role in regulating the heartbeat.","predictedComplex":false,"interactors":[{"ac":"EBI-7250981","identifier":"P63251","identifierLink":"https://www.uniprot.org/uniprotkb/P63251/entry","name":"Kcnj3","description":"G protein-activated inward rectifier potassium channel 1","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9973587","identifier":"P48548","identifierLink":"https://www.uniprot.org/uniprotkb/P48548/entry","name":"Kcnj5","description":"G protein-activated inward rectifier potassium channel 4","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3277","complexName":"I(KACh) inward rectifier potassium channel complex","organismName":"Mus musculus; 10090","description":"The GIRK1-GIRK4, or I(KACh) potassium channel is a member of the G protein-coupled inward rectifier potassium channels. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. I(KACh) is expressed in cardiac muscle, specifically the sinoatrial node and atria. Regulation of I(KACh) via G protein-coupled receptor signaling underlies the control of heart rate. I(KACh) channel couples to the muscarinic M2 and adenosine A1 receptors. Binding of acetylcholine or adenosine to its respective receptor activates I(KACh), which plays a crucial role in regulating the heartbeat.","predictedComplex":false,"interactors":[{"ac":"EBI-9020861","identifier":"P63250","identifierLink":"https://www.uniprot.org/uniprotkb/P63250/entry","name":"Kcnj3","description":"G protein-activated inward rectifier potassium channel 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9975502","identifier":"P48545","identifierLink":"https://www.uniprot.org/uniprotkb/P48545/entry","name":"Kcnj5","description":"G protein-activated inward rectifier potassium channel 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3278","complexName":"I(KACh) inward rectifier potassium channel complex","organismName":"Homo sapiens; 9606","description":"The GIRK1-GIRK4, or I(KACh) potassium channel is a member of the G protein-coupled inward rectifier potassium channels. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. I(KACh) is expressed in cardiac muscle, specifically the sinoatrial node and atria. Regulation of I(KACh) via G protein-coupled receptor signaling underlies the control of heart rate. I(KACh) channel couples to the muscarinic M2 and adenosine A1 receptors. Binding of acetylcholine or adenosine to its respective receptor activates I(KACh), which plays a crucial role in regulating the heartbeat.","predictedComplex":false,"interactors":[{"ac":"EBI-9975563","identifier":"P48544","identifierLink":"https://www.uniprot.org/uniprotkb/P48544/entry","name":"KCNJ5","description":"G protein-activated inward rectifier potassium channel 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9975595","identifier":"P48549","identifierLink":"https://www.uniprot.org/uniprotkb/P48549/entry","name":"KCNJ3","description":"G protein-activated inward rectifier potassium channel 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3279","complexName":"INAC inner membrane assembly complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Inner membrane assembly complex (INAC) promotes the biogenesis of mitochondrial F1Fo-ATP synthase by facilitating assembly of the peripheral stalk. Loss of INAC function causes dissociation of the F1-domain from the membrane-integral Fo-portion.","predictedComplex":false,"interactors":[{"ac":"EBI-25429","identifier":"P40576","identifierLink":"https://www.uniprot.org/uniprotkb/P40576/entry","name":"INA22","description":"Inner membrane assembly complex subunit 22","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-7668387","identifier":"Q02888","identifierLink":"https://www.uniprot.org/uniprotkb/Q02888/entry","name":"INA17","description":"Inner membrane assembly complex subunit 17","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-3280","complexName":"Cardiac Troponin complex","organismName":"Homo sapiens; 9606","description":"Regulates contraction-relaxation cycles in response to changes in intracellular calcium. Together with tropomyosin, cTn is generally located along polymerised actin, which forms the backbone of the cardiomyocyte thin filament. At resting levels of intracellular calcium, the cTn complex keeps  tropomyosin in a position that prevents force-producing interactions between myosin heads and actin. When the muscle cell is stimulated to contract by an action potential, calcium channels open in the sarcoplasmic membrane and release calcium into the sarcoplasm. Some of this calcium binds to specific sites in the N-domain of TnC, triggering a series of protein structural changes and tropomyosin is rolled away from myosin-binding sites on actin, allowing myosin to attach to the thin filament and produce force and/or shorten the sarcomere of the cardiomyocyte.","predictedComplex":false,"interactors":[{"ac":"EBI-3906339","identifier":"P63316","identifierLink":"https://www.uniprot.org/uniprotkb/P63316/entry","name":"TNNC1","description":"Troponin C, slow skeletal and cardiac muscles","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23064","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-704146","identifier":"P19429","identifierLink":"https://www.uniprot.org/uniprotkb/P19429/entry","name":"TNNI3","description":"Troponin I, cardiac muscle","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13738","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8485957","identifier":"P45379","identifierLink":"https://www.uniprot.org/uniprotkb/P45379/entry","name":"TNNT2","description":"Troponin T, cardiac muscle","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11521","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3281","complexName":"Mitochondrial proton-transporting ATP synthase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Acts to convert the energy of oxidation-reduction reactions of the electron transport chain (respiration) to the phosphorylation of ADP. The synthesis of ATP is coupled to the respiratory chain via the proton potential. The ATP synthase is a molecular motor composed of two separable parts: F1 and F0. The F1 portion contains the catalytic sites for ATP synthesis and protrudes into the mitochondrial matrix. F0 forms a proton turbine that is embedded in the inner membrane and connected to the rotor of F1. The flux of protons flowing down a potential gradient powers the rotation of the rotor driving the synthesis of ATP. Thus, the flow of protons though F0 is coupled to the synthesis of ATP.","predictedComplex":false,"interactors":[{"ac":"EBI-2045988","identifier":"P81450","identifierLink":"https://www.uniprot.org/uniprotkb/P81450/entry","name":"ATP18","description":"ATP synthase subunit J, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28060","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2095699","identifier":"P81449","identifierLink":"https://www.uniprot.org/uniprotkb/P81449/entry","name":"TIM11","description":"ATP synthase subunit e, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-2347197","identifier":"P00854","identifierLink":"https://www.uniprot.org/uniprotkb/P00854/entry","name":"ATP6","description":"ATP synthase subunit a","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11410","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3071","identifier":"Q12349","identifierLink":"https://www.uniprot.org/uniprotkb/Q12349/entry","name":"ATP14","description":"ATP synthase subunit H, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28207","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3212","identifier":"P30902","identifierLink":"https://www.uniprot.org/uniprotkb/P30902/entry","name":"ATP7","description":"ATP synthase subunit d, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12700","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3219","identifier":"P00856","identifierLink":"https://www.uniprot.org/uniprotkb/P00856/entry","name":"ATP8","description":"ATP synthase protein 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR36101","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3234","identifier":"P07251","identifierLink":"https://www.uniprot.org/uniprotkb/P07251/entry","name":"ATP1","description":"ATP synthase subunit alpha, mitochondrial","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR48082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3242","identifier":"P00830","identifierLink":"https://www.uniprot.org/uniprotkb/P00830/entry","name":"ATP2","description":"ATP synthase subunit beta, mitochondrial","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15184","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3257","identifier":"P21306","identifierLink":"https://www.uniprot.org/uniprotkb/P21306/entry","name":"ATP15","description":"ATP synthase subunit epsilon, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12448","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3264","identifier":"P05626","identifierLink":"https://www.uniprot.org/uniprotkb/P05626/entry","name":"ATP4","description":"ATP synthase subunit 4, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12733","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3271","identifier":"P38077","identifierLink":"https://www.uniprot.org/uniprotkb/P38077/entry","name":"ATP3","description":"ATP synthase subunit gamma, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11693","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3285","identifier":"Q06405","identifierLink":"https://www.uniprot.org/uniprotkb/Q06405/entry","name":"ATP17","description":"ATP synthase subunit f, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28161","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3292","identifier":"Q12233","identifierLink":"https://www.uniprot.org/uniprotkb/Q12233/entry","name":"ATP20","description":"ATP synthase subunit g, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12386","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3299","identifier":"P09457","identifierLink":"https://www.uniprot.org/uniprotkb/P09457/entry","name":"ATP5","description":"ATP synthase subunit 5, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11910","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3667566","identifier":"P81451","identifierLink":"https://www.uniprot.org/uniprotkb/P81451/entry","name":"ATP19","description":"ATP synthase subunit K, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28074","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7926894","identifier":"Q12165","identifierLink":"https://www.uniprot.org/uniprotkb/Q12165/entry","name":"ATP16","description":"ATP synthase subunit delta, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13822","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9016907","identifier":"P61829","identifierLink":"https://www.uniprot.org/uniprotkb/P61829/entry","name":"OLI1","description":"ATP synthase subunit 9, mitochondrial","stochiometry":"minValue: 10, maxValue: 10","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3282","complexName":"Syndecan-1-syntenin-1-ALIX complex","organismName":"Homo sapiens; 9606","description":"Exosome complex that is assembled in the multivesicular body (MVB) membrane and chaperoned to the exosome by the ESCRT-III machinery. A potential regulator of membrane trafficking and heparan sulphate-assisted signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-2855248","identifier":"P18827","identifierLink":"https://www.uniprot.org/uniprotkb/P18827/entry","name":"SDC1","description":"Syndecan-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10915","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-310624","identifier":"Q8WUM4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WUM4/entry","name":"PDCD6IP","description":"Programmed cell death 6-interacting protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23030","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727004","identifier":"O00560","identifierLink":"https://www.uniprot.org/uniprotkb/O00560/entry","name":"SDCBP","description":"Syntenin-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12345","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3283","complexName":"Syndecan-1-syntenin-1-ALIX complex","organismName":"Mus musculus; 10090","description":"Exosome complex that is assembled in the multivesicular body (MVB) membrane and chaperoned to the exosome by the ESCRT-III machinery. A potential regulator of membrane trafficking and heparan sulphate-assisted signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-538265","identifier":"O08992","identifierLink":"https://www.uniprot.org/uniprotkb/O08992/entry","name":"Sdcbp","description":"Syntenin-1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12345","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-641897","identifier":"Q9WU78","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WU78/entry","name":"Pdcd6ip","description":"Programmed cell death 6-interacting protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23030","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9985816","identifier":"P18828","identifierLink":"https://www.uniprot.org/uniprotkb/P18828/entry","name":"Sdc1","description":"Syndecan-1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10915","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3284","complexName":"Ribonuclease MRP complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Site-specific endonuclease, closely related to RNAse P complex (CPX-1873). Most protein subunits are common between the two complexes, only SNM1 and RNP1 are unique to MRP, as well as the RNA component NME1. RNAse MRP is involved in rRNA processing in the nucleolus, but during exit from mitosis it also localizes to specialized cytoplasmic P bodies and participates in cleaving CLB2 mRNA. The RNA subunit NME1 is a catalytically active ribozyme that is capable of both recognizing and cleaving substrates,  Despite its name (Mitochondrial RNA Processing) the nucleolar complex is not involved in processing mitochondrial RNA.","predictedComplex":false,"interactors":[{"ac":"EBI-13621","identifier":"P41812","identifierLink":"https://www.uniprot.org/uniprotkb/P41812/entry","name":"POP1","description":"Ribonucleases P/MRP protein subunit POP1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22731","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13638","identifier":"P53833","identifierLink":"https://www.uniprot.org/uniprotkb/P53833/entry","name":"POP3","description":"Ribonucleases P/MRP protein subunit POP3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28272","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13646","identifier":"P38336","identifierLink":"https://www.uniprot.org/uniprotkb/P38336/entry","name":"POP4","description":"RNases MRP/P 32.9 kDa subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13348","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13654","identifier":"P28005","identifierLink":"https://www.uniprot.org/uniprotkb/P28005/entry","name":"POP5","description":"Ribonuclease P/MRP protein subunit POP5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR48414","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13662","identifier":"P53218","identifierLink":"https://www.uniprot.org/uniprotkb/P53218/entry","name":"POP6","description":"Ribonucleases P/MRP protein subunit POP6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-13670","identifier":"P38291","identifierLink":"https://www.uniprot.org/uniprotkb/P38291/entry","name":"POP7","description":"Ribonucleases P/MRP protein subunit POP7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28256","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13678","identifier":"P38208","identifierLink":"https://www.uniprot.org/uniprotkb/P38208/entry","name":"POP8","description":"Ribonucleases P/MRP protein subunit POP8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28173","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15622","identifier":"P40993","identifierLink":"https://www.uniprot.org/uniprotkb/P40993/entry","name":"SNM1","description":"Ribonuclease MRP protein subunit SNM1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15968","identifier":"P38786","identifierLink":"https://www.uniprot.org/uniprotkb/P38786/entry","name":"RPP1","description":"Ribonuclease P/MRP protein subunit RPP1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2864202","identifier":"URS000006F31F_559292","identifierLink":"http://rnacentral.org/rna/URS000006F31F_559292","name":"nme1_yeast_rna","description":"NME1 RNA component of RNase MRP","stochiometry":"minValue: 1, maxValue: 1","interactorType":"ribonucleic acid","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-29955","identifier":"Q12530","identifierLink":"https://www.uniprot.org/uniprotkb/Q12530/entry","name":"RMP1","description":"Ribonuclease MRP protein subunit RMP1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR37792","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3285","complexName":"HSP90B-CDC37 chaperone complex","organismName":"Homo sapiens; 9606","description":"A protein kinase chaperone complex required for the proper folding, maturation and stabilization of target proteins (mostly signalling protein kinases, some steroid hormone receptors), usually during or immediately after completion of translation. The highly conserved, phosphorylated CDC37-Ser13 is essential for complex assembly and target protein binding. CDC37-Ser13 is phosphorylated by Casein kinase II (CK2), which in turn is a target of CDC37 creating a positive feedback loop. CDC37-Ser13 is de-phosphorylated by PP5 (P53041). Target proteins are recognised by the CDC37 subunit. HSP90 does not bind any particular motif but rather associates with intrinsically unstable kinases. Complex binding also prevents rapid ubiquitin-dependent proteosomal degradation of target proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-295634","identifier":"Q16543","identifierLink":"https://www.uniprot.org/uniprotkb/Q16543/entry","name":"CDC37","description":"Hsp90 co-chaperone Cdc37","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352572","identifier":"P08238","identifierLink":"https://www.uniprot.org/uniprotkb/P08238/entry","name":"HSP90AB1","description":"Heat shock protein HSP 90-beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11528","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3286","complexName":"SMAD3-SMAD4 complex","organismName":"Mus musculus; 10090","description":"A transcription factor complex which binds to the promoters of target genes and recruits co-activators and histone acetyltransferases, such as p300, CBP and P300/CBP-associated factor, facilitating transcription. In response to TGF-beta/activin-family protein binding, TGF-beta type II receptors phosphorylate TGF-beta type I receptors (Alk4, 5 and 7) which in turn phosphorylates Smad3 on Ser-423 and Ser-425. This enables binding to Smad4 to form heteromeric Smad complexes that enter the nucleus to initiate gene transcription. \r\nBecause of their relatively low DNA-binding affinity, Smad complexes interact with a wide variety of DNA-binding proteins. Crosstalk with other signalling pathways and interaction with other DNA-binding cofactors define the specific binding patterns of Smads; in addition, interaction with coactivators/corepressors modulates their transcriptional activity.","predictedComplex":false,"interactors":[{"ac":"EBI-2337983","identifier":"Q8BUN5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BUN5/entry","name":"Smad3","description":"Mothers against decapentaplegic homolog 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13703","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5259270","identifier":"P97471","identifierLink":"https://www.uniprot.org/uniprotkb/P97471/entry","name":"Smad4","description":"Mothers against decapentaplegic homolog 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13703","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3287","complexName":"HSP90B-CDC37 chaperone complex","organismName":"Mus musculus; 10090","description":"A protein kinase chaperone complex required for the proper folding, maturation and stabilization of target proteins (mostly signalling protein kinases, some steroid hormone receptors), usually during or immediately after completion of translation. The highly conserved, phosphorylated CDC37-Ser13 is essential for complex assembly and target protein binding. CDC37-Ser13 is phosphorylated by Casein kinase II (CK2), which in turn is a target of CDC37 creating a positive feedback loop. CDC37-Ser13 is de-phosphorylated by PP5 (P53041). Target proteins are recognised by the CDC37 subunit. HSP90 does not bind any particular motif but rather associates with intrinsically unstable kinases. Complex binding also prevents rapid ubiquitin-dependent proteosomal degradation of target proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-2906727","identifier":"Q61081","identifierLink":"https://www.uniprot.org/uniprotkb/Q61081/entry","name":"Cdc37","description":"Hsp90 co-chaperone Cdc37","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-492813","identifier":"P11499","identifierLink":"https://www.uniprot.org/uniprotkb/P11499/entry","name":"Hsp90ab1","description":"Heat shock protein HSP 90-beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11528","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3288","complexName":"HSP90A-CDC37 chaperone complex","organismName":"Homo sapiens; 9606","description":"A chaperone complex required for the proper folding, maturation and stabilization of target proteins (mostly signalling protein kinases, some steroid hormone receptors), usually during or immediately after completion of translation. The complex prevents the aggregation and degradation of protein kinases while maintaining the proper structure of their domains, recognizing and binding the extended kinase domain formed by reorganisation of the client protein to enable replacement of a hydrolyzed ADP with a new ATP molecule.  The highly conserved, phosphorylated CDC37 Ser-13 is essential for complex assembly and target protein binding.\r\n\r\nCDC37 Ser-13 is phosphorylated by Casein kinase II (CK2), which in turn is a target of CDC37 creating a positive feedback loop. CDC37 Ser-13 is de-phosphorylated by PP5 (P53041). Target proteins are recognised by the CDC37 subunit. The complex  associates with intrinsically unstable kinases, recognizing and folding both nascent kinase polypeptides emerging from ribosomes and mature kinases to maintain their activity and stability. Complex binding also prevents rapid ubiquitin-dependent proteosomal degradation of target proteins.kinases to maintain their activity and stability Complex binding also prevents rapid ubiquitin-dependent proteosomal degradation of target proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-295634","identifier":"Q16543","identifierLink":"https://www.uniprot.org/uniprotkb/Q16543/entry","name":"CDC37","description":"Hsp90 co-chaperone Cdc37","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-296047","identifier":"P07900","identifierLink":"https://www.uniprot.org/uniprotkb/P07900/entry","name":"HSP90AA1","description":"Heat shock protein HSP 90-alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11528","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3289","complexName":"HSP90A-CDC37 chaperone complex","organismName":"Mus musculus; 10090","description":"A protein kinase chaperone complex required for the proper folding, maturation and stabilization of target proteins (mostly signalling protein kinases, some steroid hormone receptors), usually during or immediately after completion of translation. The complex prevents the aggregation and degradation of protein kinases while maintaining the proper structure of their domains, recognizing and binding the extended kinase domain formed by reorganisation of the client protein to enable replacement of a hydrolyzed ADP with a new ATP molecule.  The highly conserved, phosphorylated CDC37 Ser-13 is essential for complex assembly and target protein binding.\r\n\r\nCDC37 Ser-13 is phosphorylated by Casein kinase II (CK2), which in turn is a target of CDC37 creating a positive feedback loop. CDC37 Ser-13 is de-phosphorylated by PP5 (P53041). Target proteins are recognised by the CDC37 subunit. The complex  associates with intrinsically unstable kinases, recognizing and folding both nascent kinase polypeptides emerging from ribosomes and mature kinases to maintain their activity and stability. Complex binding also prevents rapid ubiquitin-dependent proteosomal degradation of target proteins.kinases to maintain their activity and stability Complex binding also prevents rapid ubiquitin-dependent proteosomal degradation of target proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-2906727","identifier":"Q61081","identifierLink":"https://www.uniprot.org/uniprotkb/Q61081/entry","name":"Cdc37","description":"Hsp90 co-chaperone Cdc37","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-78930","identifier":"P07901","identifierLink":"https://www.uniprot.org/uniprotkb/P07901/entry","name":"Hsp90aa1","description":"Heat shock protein HSP 90-alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11528","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3290","complexName":"Interleukin-23 complex","organismName":"Homo sapiens; 9606","description":"Cytokine complex that activates and stimulates proliferation of a wide range of lymphocytes, in particular memory T cells and Th17 cells, upon binding to its receptor subunits IL12RB1 (P42701) and IL23R (Q5VWK5). Formation of the ligand-receptor complex (CPX-383) and tyrosine phosphorylation of the IL23R subunit initiates the JAK-STAT signaling cascade which ultimately activates transcription of interferon-gamma or Interleukin-17. Produced by antigen-presenting cells in response to Interleukin-18. Associated with the pathogenesis of autoimmune inflammations, including rheumatoid and Lyme arthritis, multiple sclerosis, psoriasis, and inflammatory bowel disease as well as mycobacterial diseases of varying severity, primarily bacillus Calmette-Guerin and Salmonella infections.","predictedComplex":false,"interactors":[{"ac":"EBI-11665075","identifier":"P29460-PRO_0000010930","identifierLink":"https://www.uniprot.org/uniprotkb/P29460-PRO_0000010930/entry","name":"IL12B","description":"Interleukin-12 subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-11665249","identifier":"Q9NPF7-PRO_0000259488","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPF7-PRO_0000259488/entry","name":"IL23A","description":"Interleukin-23 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-3291","complexName":"SCF E3 ubiquitin ligase complex, FBXL3 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXL3 target proteins include circadian rhythm proteins CRY1 (Q16526) and CRY2 (Q49AN0), thus maintaining circadian clock oscillations, and  MYC (P01106) which controls cell proliferation.","predictedComplex":false,"interactors":[{"ac":"EBI-2557269","identifier":"Q9UKT7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UKT7/entry","name":"FBXL3","description":"F-box/LRR-repeat protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3292","complexName":"SCF E3 ubiquitin ligase complex, FBXL2 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXL2 target proteins include the chromosomal passenger complex (CPX-116) AURKB (Q96GD4),  CCND2 (P30279) and CCND3 (P30281), activators of the G1 phase CDKs and the transcription factor FOXM1 (Q08050), the downstream targets of which include several cell cycle regulators. The complex also acts as a crucial, pan-reactive inhibitor of TRAF function by mediating their ubiquitination and degradation in epithelia and human monocytes. FBXL2 can be modified by O-GlcNAcylation, which suppresses FOXM1 degradation and contributes to gastric cancer pathogenesis","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724253","identifier":"Q9UKC9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UKC9/entry","name":"FBXL2","description":"F-box/LRR-repeat protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13382","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3293","complexName":"Interleukin-23 complex","organismName":"Mus musculus; 10090","description":"Cytokine complex that activates and stimulates proliferation of a wide range of lymphocytes, in particular memory T cells and Th17 cells, upon binding to its receptor subunits Il12rb1 (Q60837) and Il23r (Q8K4B4). Formation of the ligand-receptor complex (CPX-389) and tyrosine phosphorylation of the Il23r subunit initiates the JAK-STAT signaling cascade which ultimately activates transcription of interferon-gamma or Interleukin-17. Produced by antigen-presenting cells in response to Interleukin-18.","predictedComplex":false,"interactors":[{"ac":"EBI-11682058","identifier":"P43432-PRO_0000010933","identifierLink":"https://www.uniprot.org/uniprotkb/P43432-PRO_0000010933/entry","name":"Il12b","description":"Interleukin-12 subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-11682079","identifier":"Q9EQ14-PRO_0000259489","identifierLink":"https://www.uniprot.org/uniprotkb/Q9EQ14-PRO_0000259489/entry","name":"Il23a","description":"Interleukin-23 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-3294","complexName":"PAN2-PAN3 mRNA deadenylation complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A poly(A)-specific 3' exoribonuclease required to regulate Poly(A) tails added to mRNA co-transcriptionally and  which are required for the export of mature mRNAs to the cytoplasm  The complex is responsible for the  poly(A) trimming of the tail length to a transcript specific size which regulates  translation repression and mRNA decay.The complex is non-essential, but its deletion results in increased poly(A)-tail length.","predictedComplex":false,"interactors":[{"ac":"EBI-12887","identifier":"P53010","identifierLink":"https://www.uniprot.org/uniprotkb/P53010/entry","name":"PAN2","description":"PAN2-PAN3 deadenylation complex catalytic subunit PAN2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15728","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12895","identifier":"P36102","identifierLink":"https://www.uniprot.org/uniprotkb/P36102/entry","name":"PAN3","description":"PAN2-PAN3 deadenylation complex subunit PAN3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12272","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3295","complexName":"SCF E3 ubiquitin ligase complex, SKP2 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-SKP2 target proteins include phosphorylated CDKN1B/p27kip (P46527) and thus the complex plays a role in regulation of G1/S transition.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456291","identifier":"Q13309","identifierLink":"https://www.uniprot.org/uniprotkb/Q13309/entry","name":"SKP2","description":"S-phase kinase-associated protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3296","complexName":"Fucose-binding lectin II complex","organismName":"Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1); 208964","description":"Fucose-binding lectin responsible for adhesion of Pseudomonas aeruginosa to the lung mucins. P. aeruginosa infection is a major cause of morbidity and mortality in cystic fibrosis patients. It colonises patients with chronic lung diseases, particularly those on assisted ventilation, and especially cystic fibrosis patients. Adheres to surfaces, forms biofilms and secretes hydrolytic enzymes and toxic compounds.","predictedComplex":false,"interactors":[{"ac":"EBI-9992817","identifier":"Q9HYN5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HYN5/entry","name":"lecB","description":null,"stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1); 208964","xrefs":[]}]},{"complexAC":"CPX-3297","complexName":"FUN30 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Important roles in heterochromatin silencing and DNA repair. Remodels chromatin at the 5-prime end of genes by sliding promoter-proximal nucleosomes.","predictedComplex":false,"interactors":[{"ac":"EBI-20621","identifier":"P31380","identifierLink":"https://www.uniprot.org/uniprotkb/P31380/entry","name":"FUN30","description":"ATP-dependent helicase FUN30","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3298","complexName":"Telomerase holoenzyme complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Telomerase is a ribonucleoprotein complex that is essential for maintenance of telomeres. It is a reverse transcriptase that elongates the single-stranded G-rich 3' protruding ends of chromosomal DNA using TLC1 RNA as a template. Est1 and TLC1 are sufficient for telomerase activity in vitro, but in vivo all 4 subunits are required. Although telomerase activity can be detected throughout the cell cycle, telomeres are only elongated in late S-phase. Telomerase is known to interact with other complexes, including CDC13 complex (via EST1), Yku70/80 complex (CPX-1732) (via TLC1) and Sm heteroheptameric complex (via TLC1).","predictedComplex":false,"interactors":[{"ac":"EBI-2213511","identifier":"URS0000348061_559292","identifierLink":"http://rnacentral.org/rna/URS0000348061_559292","name":"tlc1_yeast_rna","description":"Yeast integral telomerase RNA template component, TLC1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"ribonucleic acid","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-3764464","identifier":"Q06163","identifierLink":"https://www.uniprot.org/uniprotkb/Q06163/entry","name":"EST2","description":"Telomerase reverse transcriptase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12066","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6684","identifier":"P17214","identifierLink":"https://www.uniprot.org/uniprotkb/P17214/entry","name":"EST1","description":"Telomere elongation protein EST1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15696","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6691","identifier":"Q03096","identifierLink":"https://www.uniprot.org/uniprotkb/Q03096/entry","name":"EST3","description":"Telomere replication protein EST3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-3299","complexName":"FtsBL complex","organismName":"Escherichia coli (strain K12); 83333","description":"Hypothesized to be structural proteins that contribute to the stabilization of the Z-ring. May be a multi-valent tethering structural element of the divisome.","predictedComplex":false,"interactors":[{"ac":"EBI-1113953","identifier":"P0A6S5","identifierLink":"https://www.uniprot.org/uniprotkb/P0A6S5/entry","name":"ftsB","description":"Cell division protein FtsB","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR37485","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1119082","identifier":"P0AEN4","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEN4/entry","name":"ftsL","description":"Cell division protein FtsL","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR37479","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3300","complexName":"Collagen type V trimer variant 1","organismName":"Bos taurus; 9913","description":"Form the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite.","predictedComplex":false,"interactors":[{"ac":"EBI-9998695","identifier":"G3MZI7","identifierLink":"https://www.uniprot.org/uniprotkb/G3MZI7/entry","name":"COL5A1","description":null,"stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9998735","identifier":"F1N2Y2","identifierLink":"https://www.uniprot.org/uniprotkb/F1N2Y2/entry","name":"COL5A2","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[]}]},{"complexAC":"CPX-1","complexName":"SMAD2-SMAD3-SMAD4 complex","organismName":"Homo sapiens; 9606","description":"A transcription factor complex which binds to the promoters of target genes and recruits co-activators and histone acetyltransferases, such as p300, CBP and P300/CBP-associated factor, facilitating transcription. In response to TGF-beta/activin-family protein binding, TGF-beta type II receptors phosphorylate TGF-beta type I receptors (ALK4, 5 and 7) which in turn phosphorylates SMAD2 on two Ser-465 and Ser-467, and SMAD3 on Ser-423 and Ser-425. This enables binding to SMAD4 to form heteromeric SMAD complexes that enter the nucleus to initiate gene transcription.\r\nBecause of their relatively low DNA-binding affinity, SMAD complexes interact with a wide variety of DNA-binding proteins. Crosstalk with other signalling pathways and interaction with other DNA-binding cofactors define the specific binding patterns of SMADs; in addition, interaction with coactivators/corepressors modulates their transcriptional activity.","predictedComplex":false,"interactors":[{"ac":"EBI-1040141","identifier":"Q15796","identifierLink":"https://www.uniprot.org/uniprotkb/Q15796/entry","name":"SMAD2","description":"Mothers against decapentaplegic homolog 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13703","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347161","identifier":"P84022","identifierLink":"https://www.uniprot.org/uniprotkb/P84022/entry","name":"SMAD3","description":"Mothers against decapentaplegic homolog 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13703","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347263","identifier":"Q13485","identifierLink":"https://www.uniprot.org/uniprotkb/Q13485/entry","name":"SMAD4","description":"Mothers against decapentaplegic homolog 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13703","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-4","complexName":"Collagen type V trimer variant 2","organismName":"Bos taurus; 9913","description":"Form the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite.","predictedComplex":false,"interactors":[{"ac":"EBI-10040910","identifier":"F1MJQ6","identifierLink":"https://www.uniprot.org/uniprotkb/F1MJQ6/entry","name":"COL5A3","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9998695","identifier":"G3MZI7","identifierLink":"https://www.uniprot.org/uniprotkb/G3MZI7/entry","name":"COL5A1","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9998735","identifier":"F1N2Y2","identifierLink":"https://www.uniprot.org/uniprotkb/F1N2Y2/entry","name":"COL5A2","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[]}]},{"complexAC":"CPX-5","complexName":"Collagen type V trimer variant 3","organismName":"Bos taurus; 9913","description":"Form the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite.","predictedComplex":false,"interactors":[{"ac":"EBI-9998695","identifier":"G3MZI7","identifierLink":"https://www.uniprot.org/uniprotkb/G3MZI7/entry","name":"COL5A1","description":null,"stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6","complexName":"bZIP transcription factor complex, Atf4-Creb1","organismName":"Mus musculus; 10090","description":"Transcription factor complex which binds to a specific DNA site to regulate transcription. This complex binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'). Involved in the ER stress response pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-2291098","identifier":"Q01147","identifierLink":"https://www.uniprot.org/uniprotkb/Q01147/entry","name":"Creb1","description":"Cyclic AMP-responsive element-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45879","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-77383","identifier":"Q06507","identifierLink":"https://www.uniprot.org/uniprotkb/Q06507/entry","name":"Atf4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7","complexName":"bZIP transcription factor complex, Atf1-Atf4","organismName":"Mus musculus; 10090","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-77383","identifier":"Q06507","identifierLink":"https://www.uniprot.org/uniprotkb/Q06507/entry","name":"Atf4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9987643","identifier":"P81269","identifierLink":"https://www.uniprot.org/uniprotkb/P81269/entry","name":"Atf1","description":"Cyclic AMP-dependent transcription factor ATF-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45879","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8","complexName":"bZIP transcription factor complex, ATF4-CREB1","organismName":"Homo sapiens; 9606","description":"Transcription factor complex that binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3') of the GRP78 (HSPA5) promoter. Involved in the ER stress response pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-492498","identifier":"P18848","identifierLink":"https://www.uniprot.org/uniprotkb/P18848/entry","name":"ATF4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-711855","identifier":"P16220","identifierLink":"https://www.uniprot.org/uniprotkb/P16220/entry","name":"CREB1","description":"Cyclic AMP-responsive element-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45879","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9","complexName":"bZIP transcription factor complex, ATF1-ATF4","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-492498","identifier":"P18848","identifierLink":"https://www.uniprot.org/uniprotkb/P18848/entry","name":"ATF4","description":"Cyclic AMP-dependent transcription factor ATF-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-852794","identifier":"P18846","identifierLink":"https://www.uniprot.org/uniprotkb/P18846/entry","name":"ATF1","description":"Cyclic AMP-dependent transcription factor ATF-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45879","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10","complexName":"SMAD2-SMAD3-SMAD4 complex","organismName":"Mus musculus; 10090","description":"A transcription factor complex which binds to the promoters of target genes and recruits co-activators and histone acetyltransferases, such as p300, CBP and P300/CBP-associated factor, facilitating transcription. In response to TGF-beta/activin-family protein binding, TGF-beta type II receptors phosphorylate TGF-beta type I receptors (ALK4, 5 and 7) which in turn phosphorylates SMAD2 on two Ser-465 and Ser-467. and Smad3 on Ser-423 and Ser-425. This enables binding to SMAD4 to form heteromeric Smad complexes that enter the nucleus to initiate gene transcription.\r\nBecause of their relatively low DNA-binding affinity, Smad complexes interact with a wide variety of DNA-binding proteins. Crosstalk with other signaling pathways and interaction with other DNA-binding cofactors define the specific binding patterns of Smads; in addition, interaction with coactivators/corepressors modulates their transcriptional activity.","predictedComplex":false,"interactors":[{"ac":"EBI-2337932","identifier":"Q62432","identifierLink":"https://www.uniprot.org/uniprotkb/Q62432/entry","name":"Smad2","description":"Mothers against decapentaplegic homolog 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13703","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2337983","identifier":"Q8BUN5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BUN5/entry","name":"Smad3","description":"Mothers against decapentaplegic homolog 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13703","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5259270","identifier":"P97471","identifierLink":"https://www.uniprot.org/uniprotkb/P97471/entry","name":"Smad4","description":"Mothers against decapentaplegic homolog 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13703","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-11","complexName":"SMAD2 homotrimer","organismName":"Homo sapiens; 9606","description":"In the absence of Smad4, R-Smad phosphorylation results in homotrimerization, however, this complex does not appear to import into the nucleus and is assumed to be transcriptionally inactive.","predictedComplex":false,"interactors":[{"ac":"EBI-1040141","identifier":"Q15796","identifierLink":"https://www.uniprot.org/uniprotkb/Q15796/entry","name":"SMAD2","description":"Mothers against decapentaplegic homolog 2","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13703","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-12","complexName":"SMAD3 homotrimer","organismName":"Homo sapiens; 9606","description":"In the absence of Smad4, R-Smad phosphorylation results in homotrimerization, however, this complex does not appear to import into the nucleus and is assumed to be transcriptionally inactive.","predictedComplex":false,"interactors":[{"ac":"EBI-347161","identifier":"P84022","identifierLink":"https://www.uniprot.org/uniprotkb/P84022/entry","name":"SMAD3","description":"Mothers against decapentaplegic homolog 3","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13703","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-13","complexName":"SMAD2 homotrimer","organismName":"Mus musculus; 10090","description":"In the absence of Smad4, R-Smad phosphorylation results in homotrimerization, however, this complex does not appear to import into the nucleus and is assumed to be transcriptionally inactive.","predictedComplex":false,"interactors":[{"ac":"EBI-2337932","identifier":"Q62432","identifierLink":"https://www.uniprot.org/uniprotkb/Q62432/entry","name":"Smad2","description":"Mothers against decapentaplegic homolog 2","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13703","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-14","complexName":"SMAD3 homotrimer","organismName":"Mus musculus; 10090","description":"In the absence of Smad4, R-Smad phosphorylation results in homotrimerization, however, this complex does not appear to import into the nucleus and is assumed to be transcriptionally inactive.","predictedComplex":false,"interactors":[{"ac":"EBI-2337983","identifier":"Q8BUN5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BUN5/entry","name":"Smad3","description":"Mothers against decapentaplegic homolog 3","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13703","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-15","complexName":"CST complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"RPA-like (replication protein A) complex, that has high affinity for telomeric ssDNA. The complex is assembled during late S-G2 and is involved in capping, and thus protecting, single stranded telomeric DNA and preventing chromosomal damage by inhibiting telomerase activity. Plays a role in the regulation of the synthesis of C strand via its interaction with polymerase alpha primase.","predictedComplex":false,"interactors":[{"ac":"EBI-18427","identifier":"P38960","identifierLink":"https://www.uniprot.org/uniprotkb/P38960/entry","name":"STN1","description":"Protein STN1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-35131","identifier":"Q07921","identifierLink":"https://www.uniprot.org/uniprotkb/Q07921/entry","name":"TEN1","description":"Telomere length regulation protein TEN1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-4187","identifier":"P32797","identifierLink":"https://www.uniprot.org/uniprotkb/P32797/entry","name":"CDC13","description":"Cell division control protein 13","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14513","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-16","complexName":"Cardiac troponin complex","organismName":"Mus musculus; 10090","description":"Regulates contraction-relaxation cycles in response to changes in intracellular calcium. Together with tropomyosin, cTn is generally located along polymerised actin, which forms the backbone of the cardiomyocyte thin filament. At resting levels of intracellular calcium, the cTn complex keeps  tropomyosin in a position that prevents force-producing interactions between myosin heads and actin. When the muscle cell is stimulated to contract by an action potential, calcium channels open in the sarcoplasmic membrane and release calcium into the sarcoplasm. Some of this calcium binds to specific sites in the N-domain of TnC, triggering a series of protein structural changes and tropomyosin is rolled away from myosin-binding sites on actin, allowing myosin to attach to the thin filament and produce force and/or shorten the sarcomere of the cardiomyocyte.","predictedComplex":false,"interactors":[{"ac":"EBI-299247","identifier":"P19123","identifierLink":"https://www.uniprot.org/uniprotkb/P19123/entry","name":"Tnnc1","description":"Troponin C, slow skeletal and cardiac muscles","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23064","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-299254","identifier":"P48787","identifierLink":"https://www.uniprot.org/uniprotkb/P48787/entry","name":"Tnni3","description":"Troponin I, cardiac muscle","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13738","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7037406","identifier":"P50752","identifierLink":"https://www.uniprot.org/uniprotkb/P50752/entry","name":"Tnnt2","description":"Troponin T, cardiac muscle","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11521","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-17","complexName":"Telomerase catalytic core complex","organismName":"Homo sapiens; 9606","description":"A ribonucleoprotein complex essential for the replication of chromosome termini in most eukaryotes. Catalytic component of the telomerase holoenzyme complex whose main activity is the elongation of telomeres. Acts as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and release of product once the template boundary has been reached or nascent product translocation followed by further extension. Overexpressed telomerase results in telomere lengthening which may lead to cell immortalization and cancer cell pathogenesis.","predictedComplex":false,"interactors":[{"ac":"EBI-1772203","identifier":"O14746","identifierLink":"https://www.uniprot.org/uniprotkb/O14746/entry","name":"TERT","description":"Telomerase reverse transcriptase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12066","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1772365","identifier":"URS00004A7003_9606","identifierLink":"http://rnacentral.org/rna/URS00004A7003_9606","name":"terc_human_rna","description":"Human telomerase RNA","stochiometry":"minValue: 2, maxValue: 2","interactorType":"ribonucleic acid","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-19","complexName":"Telomerase catalytic core complex","organismName":"Mus musculus; 10090","description":"A ribonucleoprotein complex essential for the replication of chromosome termini in most eukaryotes. Catalytic component of the teleromerase holoenzyme complex whose main activity is the elongation of telomeres. Acts as a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme. Catalyzes the RNA-dependent extension of 3'-chromosomal termini with the 6-nucleotide telomeric repeat unit, 5'-TTAGGG-3'. The catalytic cycle involves primer binding, primer extension and either release of product once the template boundary has been reached or nascent product translocation followed by further extension. Overexpressed telomerase results in telomere lengthening which may lead to cell immortalization and cancer cell pathogenesis.","predictedComplex":false,"interactors":[{"ac":"EBI-10046300","identifier":"URS00004A29D0_10090","identifierLink":"http://rnacentral.org/rna/URS00004A29D0_10090","name":"terc_mouse_rna","description":"Mouse telomerase RNA","stochiometry":"minValue: 2, maxValue: 2","interactorType":"ribonucleic acid","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-9662790","identifier":"O70372","identifierLink":"https://www.uniprot.org/uniprotkb/O70372/entry","name":"Tert","description":"Telomerase reverse transcriptase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12066","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-20","complexName":"TERT-RMRP complex","organismName":"Homo sapiens; 9606","description":"A ribonucleoprotein complex that has RNA-directed RNA polymerase (RdRP) activity and produces double-stranded RNAs that can be processed into small interfering RNA in a DICER (Q9UPY3)-dependent manner.","predictedComplex":false,"interactors":[{"ac":"EBI-1772203","identifier":"O14746","identifierLink":"https://www.uniprot.org/uniprotkb/O14746/entry","name":"TERT","description":"Telomerase reverse transcriptase","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12066","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9875627","identifier":"URS000075C8FA_9606","identifierLink":"http://rnacentral.org/rna/URS000075C8FA_9606","name":"rmrp_human_rna","description":"RNA component of mitochondrial RNA processing endoribonuclease","stochiometry":null,"interactorType":"small nucleolar rna","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-21","complexName":"Replication protein A complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Single-stranded DNA binding protein complex involved in all processes that involve single-stranded (ss)DNA by binding to and protecting exposed ssDNA from nucleases. Forms a physical platform to recruit other factors to the DNA including those involved in DNA damage signaling, DNA repair, and DNA replication.  RPA protects against inappropriate telomere recombination, and upon telomere uncapping, prevents cell proliferation by a checkpoint-independent pathway. RPA prevents degradation of ssDNA and prevents formation of secondary structures.","predictedComplex":false,"interactors":[{"ac":"EBI-14971","identifier":"P22336","identifierLink":"https://www.uniprot.org/uniprotkb/P22336/entry","name":"RFA1","description":"Replication factor A protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23273","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14976","identifier":"P26754","identifierLink":"https://www.uniprot.org/uniprotkb/P26754/entry","name":"RFA2","description":"Replication factor A protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13989","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14981","identifier":"P26755","identifierLink":"https://www.uniprot.org/uniprotkb/P26755/entry","name":"RFA3","description":"Replication factor A protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-22","complexName":"TERT-RMRP complex","organismName":"Mus musculus; 10090","description":"A ribonucleoprotein complex that has RNA-directed RNA polymerase (RdRP) activity and produces double-stranded RNAs that can be processed into small interfering RNA in a Dicer (Q8R418)-dependent manner.","predictedComplex":false,"interactors":[{"ac":"EBI-10046842","identifier":"URS00003E65A4_10090","identifierLink":"http://rnacentral.org/rna/URS00003E65A4_10090","name":"rmrp_mouse_rna","description":"RNA component of mitochondrial RNA processing endoribonuclease","stochiometry":null,"interactorType":"small nucleolar rna","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-9662790","identifier":"O70372","identifierLink":"https://www.uniprot.org/uniprotkb/O70372/entry","name":"Tert","description":"Telomerase reverse transcriptase","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12066","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-23","complexName":"U1 small nuclear ribonucleoprotein complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Non-coding RNA containing complex that is involved in mRNA splicing. U1 snRNP binds to the 5-prime splice site contributing to the formation of the Commitment complex (CPX-1418)  during spliceosome assembly. The spliceosome is a highly dynamic structure, assembled by sequential binding and release of the small nuclear RNAs and protein factors which removes intronic sequence from pre-mRNA. After assembly of the precatalytic spliceosome, U1 is released during the activation of the spliceosome.","predictedComplex":false,"interactors":[{"ac":"EBI-10054789","identifier":"URS000012D749_559292","identifierLink":"http://rnacentral.org/rna/URS000012D749_559292","name":"snr19_u1_yeast","description":"SNR19","stochiometry":null,"interactorType":"small nuclear rna","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-11835","identifier":"Q00539","identifierLink":"https://www.uniprot.org/uniprotkb/Q00539/entry","name":"NAM8","description":"Protein NAM8","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47640","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16359","identifier":"Q12330","identifierLink":"https://www.uniprot.org/uniprotkb/Q12330/entry","name":"SME1","description":"Small nuclear ribonucleoprotein E","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11193","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-235","identifier":"Q06217","identifierLink":"https://www.uniprot.org/uniprotkb/Q06217/entry","name":"SMD2","description":"Small nuclear ribonucleoprotein Sm D2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12777","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-432","identifier":"P40018","identifierLink":"https://www.uniprot.org/uniprotkb/P40018/entry","name":"SMB1","description":"Small nuclear ribonucleoprotein-associated protein B","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-529","identifier":"P43321","identifierLink":"https://www.uniprot.org/uniprotkb/P43321/entry","name":"SMD3","description":"Small nuclear ribonucleoprotein Sm D3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-585","identifier":"Q02260","identifierLink":"https://www.uniprot.org/uniprotkb/Q02260/entry","name":"SMD1","description":"Small nuclear ribonucleoprotein Sm D1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-612","identifier":"P39682","identifierLink":"https://www.uniprot.org/uniprotkb/P39682/entry","name":"PRP39","description":"Pre-mRNA-processing factor 39","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR17204","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-627","identifier":"Q03782","identifierLink":"https://www.uniprot.org/uniprotkb/Q03782/entry","name":"SNU56","description":"56 kDa U1 small nuclear ribonucleoprotein component","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-637","identifier":"P40204","identifierLink":"https://www.uniprot.org/uniprotkb/P40204/entry","name":"SMX2","description":"Small nuclear ribonucleoprotein G","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-673","identifier":"Q07508","identifierLink":"https://www.uniprot.org/uniprotkb/Q07508/entry","name":"LUC7","description":"Protein LUC7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-680","identifier":"P32605","identifierLink":"https://www.uniprot.org/uniprotkb/P32605/entry","name":"MUD1","description":"U1 small nuclear ribonucleoprotein A","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10501","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-701","identifier":"P33203","identifierLink":"https://www.uniprot.org/uniprotkb/P33203/entry","name":"PRP40","description":"Pre-mRNA-processing protein PRP40","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11864","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724","identifier":"Q00916","identifierLink":"https://www.uniprot.org/uniprotkb/Q00916/entry","name":"SNP1","description":"U1 small nuclear ribonucleoprotein 70 kDa homolog","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13952","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-736","identifier":"P53207","identifierLink":"https://www.uniprot.org/uniprotkb/P53207/entry","name":"SNU71","description":"U1 small nuclear ribonucleoprotein component SNU71","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-754","identifier":"Q05900","identifierLink":"https://www.uniprot.org/uniprotkb/Q05900/entry","name":"YHC1","description":"U1 small nuclear ribonucleoprotein C","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31148","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-770","identifier":"P54999","identifierLink":"https://www.uniprot.org/uniprotkb/P54999/entry","name":"SMX3","description":"Small nuclear ribonucleoprotein F","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-802","identifier":"Q03776","identifierLink":"https://www.uniprot.org/uniprotkb/Q03776/entry","name":"PRP42","description":"U1 small nuclear ribonucleoprotein component PRP42","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR17204","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-24","complexName":"U6 small nuclear ribonucleoprotein complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Non-coding RNA containing complex that is involved in mRNA splicing. Instead of the Sm ring found in the other spliceosomal snRNPs, it contains an Sm-like ring.  The spliceosome is a highly dynamic structure, assembled by sequential binding and release of the small nuclear RNAs and protein factors which removes intronic sequence from pre-mRNA. U6 is part of the activated spliceosome and is involved in the first transestherification step of splicing. After splicing is complete, the spliceosome disassembles and free U6 snRNP forms. It then reassociates with U4 (CPX-31) to form U4/U6 snRNP (CPX-32).","predictedComplex":false,"interactors":[{"ac":"EBI-10227","identifier":"P57743","identifierLink":"https://www.uniprot.org/uniprotkb/P57743/entry","name":"LSM3","description":"LSM complex subunit LSM3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13110","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10236","identifier":"P40089","identifierLink":"https://www.uniprot.org/uniprotkb/P40089/entry","name":"LSM5","description":"LSM complex subunit LSM5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR20971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10824938","identifier":"URS00006184A9_559292","identifierLink":"http://rnacentral.org/rna/URS00006184A9_559292","name":"snru6_yeast","description":"small nuclear RNA U6 Yeast","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small nuclear rna","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-141","identifier":"P53905","identifierLink":"https://www.uniprot.org/uniprotkb/P53905/entry","name":"LSM7","description":"LSM complex subunit LSM7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-180","identifier":"P38203","identifierLink":"https://www.uniprot.org/uniprotkb/P38203/entry","name":"LSM2","description":"LSM complex subunit LSM2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-188","identifier":"P40070","identifierLink":"https://www.uniprot.org/uniprotkb/P40070/entry","name":"LSM4","description":"LSM complex subunit LSM4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-196","identifier":"Q06406","identifierLink":"https://www.uniprot.org/uniprotkb/Q06406/entry","name":"LSM6","description":"LSM complex subunit LSM6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-212","identifier":"P49960","identifierLink":"https://www.uniprot.org/uniprotkb/P49960/entry","name":"PRP24","description":"U4/U6 snRNA-associated-splicing factor PRP24","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24012","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-313","identifier":"P47093","identifierLink":"https://www.uniprot.org/uniprotkb/P47093/entry","name":"LSM8","description":"LSM2-LSM8 complex subunit LSM8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25","complexName":"U4/U6.U5 tri-small nuclear ribonucleoprotein complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Non-coding RNA containing complex that is involved in mRNA splicing. The U4/U6 x U5 tri-snRNP complex binds to the pre-spliceosome complex to form the pre-activation complex. The spliceosome is a highly dynamic structure, assembled by sequential binding and release of the small nuclear RNAs and protein factors which removes intronic sequence from pre-mRNA.","predictedComplex":false,"interactors":[{"ac":"EBI-10054797","identifier":"URS00001143F5_559292","identifierLink":"http://rnacentral.org/rna/URS00001143F5_559292","name":"snr14_u4_yeast","description":"SNR14","stochiometry":null,"interactorType":"small nuclear rna","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-10054803","identifier":"URS000053F313_559292","identifierLink":"http://rnacentral.org/rna/URS000053F313_559292","name":"snr7l_yeast_ncrna","description":"SNR7-L","stochiometry":null,"interactorType":"small nuclear rna","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-10227","identifier":"P57743","identifierLink":"https://www.uniprot.org/uniprotkb/P57743/entry","name":"LSM3","description":"LSM complex subunit LSM3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 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559292","xrefs":[]},{"ac":"EBI-12032","identifier":"P39990","identifierLink":"https://www.uniprot.org/uniprotkb/P39990/entry","name":"SNU13","description":"13 kDa ribonucleoprotein-associated protein","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13858","identifier":"P23394","identifierLink":"https://www.uniprot.org/uniprotkb/P23394/entry","name":"PRP28","description":"Pre-mRNA-splicing ATP-dependent RNA helicase PRP28","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47958","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-141","identifier":"P53905","identifierLink":"https://www.uniprot.org/uniprotkb/P53905/entry","name":"LSM7","description":"LSM complex subunit LSM7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16359","identifier":"Q12330","identifierLink":"https://www.uniprot.org/uniprotkb/Q12330/entry","name":"SME1","description":"Small nuclear ribonucleoprotein E","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11193","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-166","identifier":"Q06819","identifierLink":"https://www.uniprot.org/uniprotkb/Q06819/entry","name":"DIB1","description":"Spliceosomal protein DIB1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12052","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-180","identifier":"P38203","identifierLink":"https://www.uniprot.org/uniprotkb/P38203/entry","name":"LSM2","description":"LSM complex subunit LSM2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-188","identifier":"P40070","identifierLink":"https://www.uniprot.org/uniprotkb/P40070/entry","name":"LSM4","description":"LSM complex subunit LSM4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-196","identifier":"Q06406","identifierLink":"https://www.uniprot.org/uniprotkb/Q06406/entry","name":"LSM6","description":"LSM complex subunit LSM6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2085586","identifier":"P43589","identifierLink":"https://www.uniprot.org/uniprotkb/P43589/entry","name":"SAD1","description":"Pre-mRNA-splicing factor SAD1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21646","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-219","identifier":"P20053","identifierLink":"https://www.uniprot.org/uniprotkb/P20053/entry","name":"PRP4","description":"U4/U6 small nuclear ribonucleoprotein PRP4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19846","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-227","identifier":"P19735","identifierLink":"https://www.uniprot.org/uniprotkb/P19735/entry","name":"PRP6","description":"Pre-mRNA-splicing factor 6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11246","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-235","identifier":"Q06217","identifierLink":"https://www.uniprot.org/uniprotkb/Q06217/entry","name":"SMD2","description":"Small nuclear ribonucleoprotein Sm D2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12777","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-243","identifier":"P36048","identifierLink":"https://www.uniprot.org/uniprotkb/P36048/entry","name":"SNU114","description":"Pre-mRNA-splicing factor SNU114","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR42908","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-252","identifier":"Q12368","identifierLink":"https://www.uniprot.org/uniprotkb/Q12368/entry","name":"SNU23","description":"23 kDa U4/U6.U5 small nuclear ribonucleoprotein component","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45986","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-260","identifier":"Q12420","identifierLink":"https://www.uniprot.org/uniprotkb/Q12420/entry","name":"SNU66","description":"66 kDa U4/U6.U5 small nuclear ribonucleoprotein component","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14152","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-313","identifier":"P47093","identifierLink":"https://www.uniprot.org/uniprotkb/P47093/entry","name":"LSM8","description":"LSM2-LSM8 complex subunit LSM8","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347","identifier":"P49704","identifierLink":"https://www.uniprot.org/uniprotkb/P49704/entry","name":"PRP31","description":"Pre-mRNA-processing factor 31","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13904","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-421","identifier":"Q03338","identifierLink":"https://www.uniprot.org/uniprotkb/Q03338/entry","name":"PRP3","description":"U4/U6 small nuclear ribonucleoprotein PRP3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14212","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-432","identifier":"P40018","identifierLink":"https://www.uniprot.org/uniprotkb/P40018/entry","name":"SMB1","description":"Small nuclear ribonucleoprotein-associated protein B","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-443","identifier":"P38282","identifierLink":"https://www.uniprot.org/uniprotkb/P38282/entry","name":"SPP381","description":"Pre-mRNA-splicing factor SPP381","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-465","identifier":"P33334","identifierLink":"https://www.uniprot.org/uniprotkb/P33334/entry","name":"PRP8","description":"Pre-mRNA-splicing factor 8","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11140","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-529","identifier":"P43321","identifierLink":"https://www.uniprot.org/uniprotkb/P43321/entry","name":"SMD3","description":"Small nuclear ribonucleoprotein Sm D3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-585","identifier":"Q02260","identifierLink":"https://www.uniprot.org/uniprotkb/Q02260/entry","name":"SMD1","description":"Small nuclear ribonucleoprotein Sm D1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-637","identifier":"P40204","identifierLink":"https://www.uniprot.org/uniprotkb/P40204/entry","name":"SMX2","description":"Small nuclear ribonucleoprotein G","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-770","identifier":"P54999","identifierLink":"https://www.uniprot.org/uniprotkb/P54999/entry","name":"SMX3","description":"Small nuclear ribonucleoprotein F","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-841","identifier":"Q00723","identifierLink":"https://www.uniprot.org/uniprotkb/Q00723/entry","name":"PRP38","description":"Pre-mRNA-splicing factor 38","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23142","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-861","identifier":"P32639","identifierLink":"https://www.uniprot.org/uniprotkb/P32639/entry","name":"BRR2","description":"Pre-mRNA-splicing helicase BRR2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 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U2 snRNP binds to the intron branch site of the commitment complex (CPX-1418) to form the pre-spliceosome in an ATP dependent step.   The spliceosome is a highly dynamic structure, assembled by sequential binding and release of the small nuclear RNAs and protein factors which removes intronic sequence from pre-mRNA. During formation of the activated spliceosome, U2 will replace the dissociating U4 (CPX-31) to form base pairs with U6 (CPX-24). Prior to the first catalytic reaction, the SF3a (CPX-1648) and SF3b (CPX-1647) sub-complexes dissociate from the spliceosome, presumably making the branch site accessible to lariat formation.","predictedComplex":false,"interactors":[{"ac":"EBI-10860871","identifier":"URS000023C730_559292","identifierLink":"http://rnacentral.org/rna/URS000023C730_559292","name":"lsr1_snr20_u2 yeast","description":"small nuclear RNA U2 yeast","stochiometry":null,"interactorType":"small nuclear rna","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-16359","identifier":"Q12330","identifierLink":"https://www.uniprot.org/uniprotkb/Q12330/entry","name":"SME1","description":"Small nuclear ribonucleoprotein E","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11193","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-235","identifier":"Q06217","identifierLink":"https://www.uniprot.org/uniprotkb/Q06217/entry","name":"SMD2","description":"Small nuclear ribonucleoprotein Sm D2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 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559292","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-585","identifier":"Q02260","identifierLink":"https://www.uniprot.org/uniprotkb/Q02260/entry","name":"SMD1","description":"Small nuclear ribonucleoprotein Sm D1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-594","identifier":"Q08963","identifierLink":"https://www.uniprot.org/uniprotkb/Q08963/entry","name":"LEA1","description":"U2 small nuclear ribonucleoprotein A'","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10552","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603","identifier":"P32524","identifierLink":"https://www.uniprot.org/uniprotkb/P32524/entry","name":"PRP21","description":"Pre-mRNA-splicing factor PRP21","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 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559292","xrefs":[]},{"ac":"EBI-8579","identifier":"Q99181","identifierLink":"https://www.uniprot.org/uniprotkb/Q99181/entry","name":"HSH49","description":"Protein HSH49","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-970846","identifier":"P0C074","identifierLink":"https://www.uniprot.org/uniprotkb/P0C074/entry","name":"YSF3","description":"RDS3 complex subunit 10","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR20978","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-28","complexName":"p-aminobenzoyl-glutamate hydrolase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the cleavage of the folate breakdown product p-aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. Reduced derivatives of folic acid are required for biosynthesis of DNA, RNA, amino acids, and other important cellular components.","predictedComplex":false,"interactors":[{"ac":"EBI-1123629","identifier":"P76052","identifierLink":"https://www.uniprot.org/uniprotkb/P76052/entry","name":"abgB","description":"p-aminobenzoyl-glutamate hydrolase subunit B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30575","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9155452","identifier":"P77357","identifierLink":"https://www.uniprot.org/uniprotkb/P77357/entry","name":"abgA","description":"p-aminobenzoyl-glutamate hydrolase subunit A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30575","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-29","complexName":"U5 small nuclear ribonucleoprotein complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Non-coding RNA containing complex that is involved in mRNA splicing. U5 snRNP is delivered to the forming spliceosome as part of the U4/U6 x U5 tri-snRNP complex (CPX-25).  The spliceosome is a highly dynamic structure, assembled by sequential binding and release of the small nuclear RNAs and protein factors which removes intronic sequence from pre-mRNA. During spliceosome activation several subunits dissociate, but U5 is necessary for both trans-esterification steps during splicing.","predictedComplex":false,"interactors":[{"ac":"EBI-10054803","identifier":"URS000053F313_559292","identifierLink":"http://rnacentral.org/rna/URS000053F313_559292","name":"snr7l_yeast_ncrna","description":"SNR7-L","stochiometry":null,"interactorType":"small nuclear rna","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-10825220","identifier":"URS0000514318_559292","identifierLink":"http://rnacentral.org/rna/URS0000514318_559292","name":"snr7s_u5_yeast","description":"small nuclear RNA U5 Yeast","stochiometry":null,"interactorType":"small nuclear rna","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-13858","identifier":"P23394","identifierLink":"https://www.uniprot.org/uniprotkb/P23394/entry","name":"PRP28","description":"Pre-mRNA-splicing ATP-dependent RNA helicase PRP28","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 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AAR2 is mutually exclusive with BRR2, which is present in the form of U5 localized at the spliceosome.  The spliceosome is a highly dynamic structure, assembled by sequential binding and release of the small nuclear RNAs and protein factors which removes intronic sequence from pre-mRNA.","predictedComplex":false,"interactors":[{"ac":"EBI-10054803","identifier":"URS000053F313_559292","identifierLink":"http://rnacentral.org/rna/URS000053F313_559292","name":"snr7l_yeast_ncrna","description":"SNR7-L","stochiometry":null,"interactorType":"small nuclear rna","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-10825220","identifier":"URS0000514318_559292","identifierLink":"http://rnacentral.org/rna/URS0000514318_559292","name":"snr7s_u5_yeast","description":"small nuclear RNA U5 Yeast","stochiometry":null,"interactorType":"small nuclear rna","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-16359","identifier":"Q12330","identifierLink":"https://www.uniprot.org/uniprotkb/Q12330/entry","name":"SME1","description":"Small nuclear ribonucleoprotein E","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 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U4 is found in a complex with U6 snRNP (the U4/6 snRNP complex, CPX-32), which is an intermediate in the assembly of the spliceosome. The spliceosome is a highly dynamic structure, assembled by sequential binding and release of the small nuclear RNAs and protein factors which removes intronic sequence from pre-mRNA. U4 dissociates from the spliceosome during the activation step. The U4/6 complex is then re-assembled in each cycle. Its function seems to be to deliver U6 to the spliceosome.","predictedComplex":false,"interactors":[{"ac":"EBI-10054797","identifier":"URS00001143F5_559292","identifierLink":"http://rnacentral.org/rna/URS00001143F5_559292","name":"snr14_u4_yeast","description":"SNR14","stochiometry":null,"interactorType":"small nuclear rna","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-12032","identifier":"P39990","identifierLink":"https://www.uniprot.org/uniprotkb/P39990/entry","name":"SNU13","description":"13 kDa ribonucleoprotein-associated protein","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16359","identifier":"Q12330","identifierLink":"https://www.uniprot.org/uniprotkb/Q12330/entry","name":"SME1","description":"Small nuclear ribonucleoprotein E","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11193","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-219","identifier":"P20053","identifierLink":"https://www.uniprot.org/uniprotkb/P20053/entry","name":"PRP4","description":"U4/U6 small nuclear ribonucleoprotein PRP4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19846","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-235","identifier":"Q06217","identifierLink":"https://www.uniprot.org/uniprotkb/Q06217/entry","name":"SMD2","description":"Small nuclear ribonucleoprotein Sm D2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12777","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-421","identifier":"Q03338","identifierLink":"https://www.uniprot.org/uniprotkb/Q03338/entry","name":"PRP3","description":"U4/U6 small nuclear ribonucleoprotein PRP3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14212","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-432","identifier":"P40018","identifierLink":"https://www.uniprot.org/uniprotkb/P40018/entry","name":"SMB1","description":"Small nuclear ribonucleoprotein-associated protein B","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-529","identifier":"P43321","identifierLink":"https://www.uniprot.org/uniprotkb/P43321/entry","name":"SMD3","description":"Small nuclear ribonucleoprotein Sm D3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-585","identifier":"Q02260","identifierLink":"https://www.uniprot.org/uniprotkb/Q02260/entry","name":"SMD1","description":"Small nuclear ribonucleoprotein Sm D1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-637","identifier":"P40204","identifierLink":"https://www.uniprot.org/uniprotkb/P40204/entry","name":"SMX2","description":"Small nuclear ribonucleoprotein G","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-770","identifier":"P54999","identifierLink":"https://www.uniprot.org/uniprotkb/P54999/entry","name":"SMX3","description":"Small nuclear ribonucleoprotein F","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-32","complexName":"U4/U6 small nuclear ribonucleoprotein complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Non-coding RNA containing complex that is involved in mRNA splicing. Intermediate complex in the assembly of U4/U6 x U5 tri-snRNP complex (CPX-25) and the precatalytic spliceosome. Its main function is to deliver U6 (CPX-24) to the spliceosome, a highly dynamic structure, assembled by sequential binding and release of the small nuclear RNAs and protein factors which removes intronic sequence from pre-mRNA.","predictedComplex":false,"interactors":[{"ac":"EBI-10054797","identifier":"URS00001143F5_559292","identifierLink":"http://rnacentral.org/rna/URS00001143F5_559292","name":"snr14_u4_yeast","description":"SNR14","stochiometry":null,"interactorType":"small nuclear rna","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-10227","identifier":"P57743","identifierLink":"https://www.uniprot.org/uniprotkb/P57743/entry","name":"LSM3","description":"LSM complex subunit LSM3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13110","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10236","identifier":"P40089","identifierLink":"https://www.uniprot.org/uniprotkb/P40089/entry","name":"LSM5","description":"LSM complex subunit LSM5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 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559292","xrefs":[{"identifier":"PTHR12777","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-313","identifier":"P47093","identifierLink":"https://www.uniprot.org/uniprotkb/P47093/entry","name":"LSM8","description":"LSM2-LSM8 complex subunit LSM8","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347","identifier":"P49704","identifierLink":"https://www.uniprot.org/uniprotkb/P49704/entry","name":"PRP31","description":"Pre-mRNA-processing factor 31","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13904","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-421","identifier":"Q03338","identifierLink":"https://www.uniprot.org/uniprotkb/Q03338/entry","name":"PRP3","description":"U4/U6 small nuclear ribonucleoprotein PRP3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 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Binding of the ligand AMP in response to atrial distension (high blood volume)  plays a major role in the regulation of blood pressure and salt-fluid volume homeostasis. Binding of ANP to ANPR-A dimer activates the receptor and stimulates its guanylate cyclase activity, thereby elevating intracellular cGMP levels. cGMP, in return mediates the hormonal actions through cGMP-regulated ion channels, protein kinases and phosphodiesterases. The end result is a reduction in blood volume and, therefore, a reduction in cardiac output and systemic blood pressure.","predictedComplex":false,"interactors":[{"ac":"EBI-7945470","identifier":"P18910","identifierLink":"https://www.uniprot.org/uniprotkb/P18910/entry","name":"Npr1","description":"Atrial natriuretic peptide receptor 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11920","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-34","complexName":"ANPR-A receptor complex","organismName":"Mus musculus; 10090","description":"Dimeric receptor complex expressed in the atrium. Binding of the ligand AMP in response to atrial distension (high blood volume)  plays a major role in the regulation of blood pressure and salt-fluid volume homeostasis. Binding of ANP to ANPR-A dimer activates the receptor and stimulates its guanylate cyclase activity, thereby elevating intracellular cGMP levels. cGMP, in return mediates the hormonal actions through cGMP-regulated ion channels, protein kinases and phosphodiesterases. The end result is a reduction in blood volume and, therefore, a reduction in cardiac output and systemic blood pressure.","predictedComplex":false,"interactors":[{"ac":"EBI-10093306","identifier":"P18293","identifierLink":"https://www.uniprot.org/uniprotkb/P18293/entry","name":"Npr1","description":"Atrial natriuretic peptide receptor 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11920","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-35","complexName":"ANPR-A receptor complex","organismName":"Homo sapiens; 9606","description":"Dimeric receptor complex expressed in the atrium. Binding of the ligand AMP in response to atrial distension (high blood volume)  plays a major role in the regulation of blood pressure and salt-fluid volume homeostasis. Binding of atrial natriuretic peptide ANP to ANPR-A dimer activates the receptor and stimulates its guanylate cyclase activity, thereby elevating intracellular cGMP levels. cGMP, in return mediates the hormonal actions through cGMP-regulated ion channels, protein kinases and phosphodiesterases. The end result is a reduction in blood volume and, therefore, a reduction in cardiac output and systemic blood pressure.","predictedComplex":false,"interactors":[{"ac":"EBI-2558784","identifier":"P16066","identifierLink":"https://www.uniprot.org/uniprotkb/P16066/entry","name":"NPR1","description":"Atrial natriuretic peptide receptor 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11920","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-36","complexName":"Kelch-containing Formin Regulatory Complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Regulates BNR1 (P40450)-mediated actin cable formation, polarized cell growth, and cytokinesis. Localizes to the bud neck and cortex and binds to the FH2 domain of the formin, displacing BNR1 from the growing ends of actin filaments to control actin cable architecture. Actin cables serve as linear tracks for myosin V-based transport of secretory vesicles, organelles, and daughter-specific transcripts to the bud, as well as guiding astral microtubule plus ends to the cell cortex to position and orient the mitotic spindle","predictedComplex":false,"interactors":[{"ac":"EBI-20747","identifier":"P27637","identifierLink":"https://www.uniprot.org/uniprotkb/P27637/entry","name":"BUD14","description":"Bud site selection protein 14","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47775","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9619","identifier":"P38853","identifierLink":"https://www.uniprot.org/uniprotkb/P38853/entry","name":"KEL1","description":"Kelch repeat-containing protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23244","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9630","identifier":"P50090","identifierLink":"https://www.uniprot.org/uniprotkb/P50090/entry","name":"KEL2","description":"Kelch repeat-containing protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23244","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-37","complexName":"Calprotectin heterotetramer","organismName":"Homo sapiens; 9606","description":"A Ca(2+), Mn(2+) and Zn(2+)-binding complex used by the innate immune system in a metal-withholding strategy that limits Mn(2+) and Zn(2+) availability at sites of infection. Calprotectin is expressed and released by neutrophils and epithelial cells, and exhibits broad-spectrum antimicrobial activity attributed to its metal-binding properties. Upon neutrophil activation or endothelial adhesion of monocytes, Calprotectin becomes secreted via a microtubule-mediated pathway and can thus serve as a marker for the influx of mononuclear phagocytes into the site of inflammation. Calprotectin is an endogenous ligand of toll-like receptor 4 (TLR4) and of the receptor for advanced glycation end products (RAGE) initiating signal transduction through NF-kappa-B pathways.","predictedComplex":false,"interactors":[{"ac":"EBI-1055001","identifier":"P06702","identifierLink":"https://www.uniprot.org/uniprotkb/P06702/entry","name":"S100A9","description":"Protein S100-A9","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 0, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-355281","identifier":"P05109","identifierLink":"https://www.uniprot.org/uniprotkb/P05109/entry","name":"S100A8","description":"Protein S100-A8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-39","complexName":"Calprotectin heterodimer","organismName":"Homo sapiens; 9606","description":"A Ca(2+), Mn(2+) and Zn(2+)-binding complex used by the innate immune system in a metal-withholding strategy that limits Mn(2+) and Zn(2+) availability at sites of infection. 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Calprotectin is an endogenous ligand of toll-like receptor 4 (TLR4) and of the receptor for advanced glycation end products (RAGE) initiating signal transduction through NF-kappa-B pathways.","predictedComplex":false,"interactors":[{"ac":"EBI-1055001","identifier":"P06702","identifierLink":"https://www.uniprot.org/uniprotkb/P06702/entry","name":"S100A9","description":"Protein S100-A9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 0, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-355281","identifier":"P05109","identifierLink":"https://www.uniprot.org/uniprotkb/P05109/entry","name":"S100A8","description":"Protein S100-A8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-40","complexName":"Calprotectin heterotetramer","organismName":"Mus musculus; 10090","description":"A Ca(2+), Mn(2+) and Zn(2+)-binding complex used by the innate immune system in a metal-withholding strategy that limits Mn(2+) and Zn(2+) availability at sites of infection. 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Calprotectin is an endogenous ligand of toll-like receptor 4 (TLR4) and of the receptor for advanced glycation end products (RAGE) initiating signal transduction through NF-kappa-B pathways.","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 0, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2105477","identifier":"P27005","identifierLink":"https://www.uniprot.org/uniprotkb/P27005/entry","name":"S100a8","description":"Protein S100-A8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2105496","identifier":"P31725","identifierLink":"https://www.uniprot.org/uniprotkb/P31725/entry","name":"S100a9","description":"Protein S100-A9","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-41","complexName":"Calprotectin heterodimer","organismName":"Mus musculus; 10090","description":"A Ca(2+), Mn(2+) and Zn(2+)-binding complex used by the innate immune system in a metal-withholding strategy that limits Mn(2+) and Zn(2+) availability at sites of infection. Calprotectin is expressed and released by neutrophils and epithelial cells, and exhibits broad-spectrum antimicrobial activity attributed to its metal-binding properties. Upon neutrophil activation or endothelial adhesion of monocytes, Calprotectin becomes secreted via a microtubule-mediated pathway and can thus serve as a marker for the influx of mononuclear phagocytes into the site of inflammation. Calprotectin is an endogenous ligand of toll-like receptor 4 (TLR4) and of the receptor for advanced glycation end products (RAGE) initiating signal transduction through NF-kappa-B pathways.","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 0, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2105477","identifier":"P27005","identifierLink":"https://www.uniprot.org/uniprotkb/P27005/entry","name":"S100a8","description":"Protein S100-A8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2105496","identifier":"P31725","identifierLink":"https://www.uniprot.org/uniprotkb/P31725/entry","name":"S100a9","description":"Protein S100-A9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-42","complexName":"S100A8 complex","organismName":"Homo sapiens; 9606","description":"Homodimer, stabilised by Ca2+ binding. Binds to toll-like receptor 4 (TLR4).","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-355281","identifier":"P05109","identifierLink":"https://www.uniprot.org/uniprotkb/P05109/entry","name":"S100A8","description":"Protein S100-A8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-43","complexName":"Sm complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Essential role in pre-mRNA splicing. Form a heteroheptameric complex on binding to a conserved Sm site [consensus AU(4-6)G] found in single-stranded regions of U1, U2, U4 and U5 snRNAs. U1, U2, U4 and U5 snRNAs are produced in the nucleus by RNA polymerase II and exported to the cytoplasm, where the Sm proteins bind to them and promote the hypermethylation of the N7-monomethyl guanosine cap at their 5-prime-ends, to produce the 2,2,7-trimethyl guanosine cap structure.","predictedComplex":false,"interactors":[{"ac":"EBI-16359","identifier":"Q12330","identifierLink":"https://www.uniprot.org/uniprotkb/Q12330/entry","name":"SME1","description":"Small nuclear ribonucleoprotein E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11193","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-235","identifier":"Q06217","identifierLink":"https://www.uniprot.org/uniprotkb/Q06217/entry","name":"SMD2","description":"Small nuclear ribonucleoprotein Sm D2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12777","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-432","identifier":"P40018","identifierLink":"https://www.uniprot.org/uniprotkb/P40018/entry","name":"SMB1","description":"Small nuclear ribonucleoprotein-associated protein B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-529","identifier":"P43321","identifierLink":"https://www.uniprot.org/uniprotkb/P43321/entry","name":"SMD3","description":"Small nuclear ribonucleoprotein Sm D3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-585","identifier":"Q02260","identifierLink":"https://www.uniprot.org/uniprotkb/Q02260/entry","name":"SMD1","description":"Small nuclear ribonucleoprotein Sm D1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-637","identifier":"P40204","identifierLink":"https://www.uniprot.org/uniprotkb/P40204/entry","name":"SMX2","description":"Small nuclear ribonucleoprotein G","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-770","identifier":"P54999","identifierLink":"https://www.uniprot.org/uniprotkb/P54999/entry","name":"SMX3","description":"Small nuclear ribonucleoprotein F","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-44","complexName":"LSM2-8 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"The hetero-heptameric complex of seven Lsm proteins (Lsm2-8) affects the processing of small stable RNAs (including tRNAs, rRNAs) and pre-mRNAs in the nucleus. The complex is part of the U6 snRNA, where it binds to the U6 RNA and contributes to  stabilizing the U6 snRNA and chaperoning it through the splicing process. The Lsm2-8 complex is thought to pre-exist in the cell and bind to U6 as a complex.","predictedComplex":false,"interactors":[{"ac":"EBI-10227","identifier":"P57743","identifierLink":"https://www.uniprot.org/uniprotkb/P57743/entry","name":"LSM3","description":"LSM complex subunit LSM3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13110","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10236","identifier":"P40089","identifierLink":"https://www.uniprot.org/uniprotkb/P40089/entry","name":"LSM5","description":"LSM complex subunit LSM5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR20971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-141","identifier":"P53905","identifierLink":"https://www.uniprot.org/uniprotkb/P53905/entry","name":"LSM7","description":"LSM complex subunit LSM7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-180","identifier":"P38203","identifierLink":"https://www.uniprot.org/uniprotkb/P38203/entry","name":"LSM2","description":"LSM complex subunit LSM2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-188","identifier":"P40070","identifierLink":"https://www.uniprot.org/uniprotkb/P40070/entry","name":"LSM4","description":"LSM complex subunit LSM4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-196","identifier":"Q06406","identifierLink":"https://www.uniprot.org/uniprotkb/Q06406/entry","name":"LSM6","description":"LSM complex subunit LSM6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-313","identifier":"P47093","identifierLink":"https://www.uniprot.org/uniprotkb/P47093/entry","name":"LSM8","description":"LSM2-LSM8 complex subunit LSM8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-45","complexName":"LSM1-7 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Lsm1-7 is a complex conserved in all eukaryotes and has similar function to the homohexamer Hfq in bacteria. It is an important part of cytoplasmic mRNA degradation. It preferentially binds oligo-adenylated (but not poly-A) mRNAs at their 3' end and promotes decapping at the 5' end thereby directing the mRNA for degradation through the 5' to 3' pathway. Lsm1-7 in yeast can be isolated as part of the Lsm1-7-Pat1 complex.","predictedComplex":false,"interactors":[{"ac":"EBI-10227","identifier":"P57743","identifierLink":"https://www.uniprot.org/uniprotkb/P57743/entry","name":"LSM3","description":"LSM complex subunit LSM3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13110","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10236","identifier":"P40089","identifierLink":"https://www.uniprot.org/uniprotkb/P40089/entry","name":"LSM5","description":"LSM complex subunit LSM5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR20971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-141","identifier":"P53905","identifierLink":"https://www.uniprot.org/uniprotkb/P53905/entry","name":"LSM7","description":"LSM complex subunit LSM7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-174","identifier":"P47017","identifierLink":"https://www.uniprot.org/uniprotkb/P47017/entry","name":"LSM1","description":"LSM1-LSM7 complex subunit LSM1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-180","identifier":"P38203","identifierLink":"https://www.uniprot.org/uniprotkb/P38203/entry","name":"LSM2","description":"LSM complex subunit LSM2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-188","identifier":"P40070","identifierLink":"https://www.uniprot.org/uniprotkb/P40070/entry","name":"LSM4","description":"LSM complex subunit LSM4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-196","identifier":"Q06406","identifierLink":"https://www.uniprot.org/uniprotkb/Q06406/entry","name":"LSM6","description":"LSM complex subunit LSM6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-46","complexName":"LSM2-7 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Sml2-7 proteins form a complex that is found associated with snR5 and pre-Rnase P in yeast nucleoli. The function of this complex is unclear.","predictedComplex":false,"interactors":[{"ac":"EBI-10227","identifier":"P57743","identifierLink":"https://www.uniprot.org/uniprotkb/P57743/entry","name":"LSM3","description":"LSM complex subunit LSM3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13110","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10236","identifier":"P40089","identifierLink":"https://www.uniprot.org/uniprotkb/P40089/entry","name":"LSM5","description":"LSM complex subunit LSM5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR20971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-141","identifier":"P53905","identifierLink":"https://www.uniprot.org/uniprotkb/P53905/entry","name":"LSM7","description":"LSM complex subunit LSM7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-180","identifier":"P38203","identifierLink":"https://www.uniprot.org/uniprotkb/P38203/entry","name":"LSM2","description":"LSM complex subunit LSM2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-188","identifier":"P40070","identifierLink":"https://www.uniprot.org/uniprotkb/P40070/entry","name":"LSM4","description":"LSM complex subunit LSM4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-196","identifier":"Q06406","identifierLink":"https://www.uniprot.org/uniprotkb/Q06406/entry","name":"LSM6","description":"LSM complex subunit LSM6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-47","complexName":"S100A8 complex","organismName":"Mus musculus; 10090","description":"Homodimer, stabilised by Ca2+ binding. Binds to toll-like receptor 4 (TLR4).","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2105477","identifier":"P27005","identifierLink":"https://www.uniprot.org/uniprotkb/P27005/entry","name":"S100a8","description":"Protein S100-A8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-48","complexName":"S100A9 complex","organismName":"Homo sapiens; 9606","description":"Homodimer, stabilised by Ca2+ binding. Binds to toll-like receptor 4 (TLR4) and the receptor for advanced glycation end products (RAGE) initiating signal transduction through NF-kappa-B pathways. S100A9 transports arachidonic acid between the cytosol and the NADPH oxidase complex at the plasma membrane in neutrophils as part of an inflammatory signal cascade leading to an oxidative burst. S100A9 complexes with microtubules increasing cell motility.","predictedComplex":false,"interactors":[{"ac":"EBI-1055001","identifier":"P06702","identifierLink":"https://www.uniprot.org/uniprotkb/P06702/entry","name":"S100A9","description":"Protein S100-A9","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-49","complexName":"S100A9 complex","organismName":"Mus musculus; 10090","description":"Homodimer, stabilised by Ca2+ binding. Binds to toll-like receptor 4 (TLR4) and the receptor for advanced glycation end products (RAGE) initiating signal transduction through NF-kappa-B pathways. S100A9 transports arachidonic acid between the cytosol and the NADPH oxidase complex at the plasma membrane in neutrophils as part of an inflammatory signal cascade  leading to an oxidative burst. S100A9 complexes with microtubules increasing cell motility.","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2105496","identifier":"P31725","identifierLink":"https://www.uniprot.org/uniprotkb/P31725/entry","name":"S100a9","description":"Protein S100-A9","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-50","complexName":"Collagen type XXIII trimer","organismName":"Rattus norvegicus; 10116","description":"Type II orientated transmembrane collagen.","predictedComplex":false,"interactors":[{"ac":"EBI-10095843","identifier":"Q810Y4","identifierLink":"https://www.uniprot.org/uniprotkb/Q810Y4/entry","name":"Col23a1","description":"Collagen alpha-1(XXIII) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-51","complexName":"Cardiac phospholamban complex","organismName":"Homo sapiens; 9606","description":"The cardiac PLN complex is a homopentamer  found in the sarcoplasmic reticulum (SR) membrane of the cardiomyocytes and acts as a regulator of intracellular calcium levels. Cardiac PLN is a main determinant of muscle contraction and relaxation. In the unphosphorylated form PLN  inhibits the sarco(endo)plasmic reticulum calcium ATPase (SERCA), a membrane protein responsible for the pumping most of the calcium from the cytoplasm to the SR, thereby causing a relaxation of myofibrils.","predictedComplex":false,"interactors":[{"ac":"EBI-692836","identifier":"P26678","identifierLink":"https://www.uniprot.org/uniprotkb/P26678/entry","name":"PLN","description":"Phospholamban","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21194","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-52","complexName":"iNOS-S100A8/A9 complex","organismName":"Homo sapiens; 9606","description":"Stimulus-inducible, S-nitrosylase complex which S-nitrosylates cysteine residues in target proteins, a principal mechanism of nitric oxide (NO)-mediated signal transduction. S100A9 acts both as an adaptor linking NOS2 to its target via protein-protein interaction and as a transnitrosylase that transfers the nitric oxide moiety from NOS2 to its target, via its own S-nitrosylated Cys-3. S100A8 interacts with the target and dictates site-specificity of the S-nitrosylase complex by [I/L]-X-C-X2-[D/E] motif recognition. S100A8 binding induces a conformational change in the target protein and restricts transfer of NO from S100A9 to the motif-associated cysteine. Stimulated by oxidised LDL (CHEBI:60151) and interferon-gamma.","predictedComplex":false,"interactors":[{"ac":"EBI-1055001","identifier":"P06702","identifierLink":"https://www.uniprot.org/uniprotkb/P06702/entry","name":"S100A9","description":"Protein S100-A9","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355281","identifier":"P05109","identifierLink":"https://www.uniprot.org/uniprotkb/P05109/entry","name":"S100A8","description":"Protein S100-A8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6662224","identifier":"P35228","identifierLink":"https://www.uniprot.org/uniprotkb/P35228/entry","name":"NOS2","description":"Nitric oxide synthase, inducible","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19384","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-53","complexName":"iNOS-S100A8/A9 complex","organismName":"Mus musculus; 10090","description":"Stimulus-inducible, S-nitrosylase complex which S-nitrosylates cysteine residues in target proteins, a principal mechanism of nitric oxide (NO)-mediated signal transduction. S100A9 acts both as an adaptor linking NOS2 to its target via protein-protein interaction and as a transnitrosylase that transfers the nitric oxide moiety from NOS2 to its target, via its own S-nitrosylated Cys-3. S100A8 interacts with the target and dictates site-specificity of the S-nitrosylase complex by [I/L]-X-C-X2-[D/E] motif recognition. S100A8 binding induces a conformational change in the target protein and restricts transfer of NO from S100A9 to the motif-associated cysteine. Stimulated by oxidised LDL (CHEBI:60151) and interferon-gamma.","predictedComplex":false,"interactors":[{"ac":"EBI-2105477","identifier":"P27005","identifierLink":"https://www.uniprot.org/uniprotkb/P27005/entry","name":"S100a8","description":"Protein S100-A8","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2105496","identifier":"P31725","identifierLink":"https://www.uniprot.org/uniprotkb/P31725/entry","name":"S100a9","description":"Protein S100-A9","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-298897","identifier":"P29477","identifierLink":"https://www.uniprot.org/uniprotkb/P29477/entry","name":"Nos2","description":"Nitric oxide synthase, inducible","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR19384","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-54","complexName":"SMAD1-SMAD4 complex","organismName":"Homo sapiens; 9606","description":"A transcription factor complex which binds to the promoters of target genes and recruits co-activators and histone acetyltransferases, such as p300, CBP and P300/CBP-associated factor, facilitating transcription. In response to TGF-beta/activin-family protein binding, primarily  BMP (bone morphogenetic proteins), TGF-beta type II receptors phosphorylate TGF-beta type I receptors (ALK1, 2, 3 and 6) which in turn phosphorylates SMAD1 on Ser-463 and Ser-465. This enables binding to SMAD4 to form heteromeric SMAD complexes that enter the nucleus to initiate gene transcription.\r\nBecause of their relatively low DNA-binding affinity, SMAD complexes interact with a wide variety of DNA-binding proteins. Crosstalk with other signalling pathways and interaction with other DNA-binding cofactors define the specific binding patterns of SMADs; in addition, interaction with coactivators/corepressors modulates their transcriptional activity.","predictedComplex":false,"interactors":[{"ac":"EBI-1567153","identifier":"Q15797","identifierLink":"https://www.uniprot.org/uniprotkb/Q15797/entry","name":"SMAD1","description":"Mothers against decapentaplegic homolog 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13703","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347263","identifier":"Q13485","identifierLink":"https://www.uniprot.org/uniprotkb/Q13485/entry","name":"SMAD4","description":"Mothers against decapentaplegic homolog 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13703","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-55","complexName":"Cardiac phospholamban complex","organismName":"Mus musculus; 10090","description":"The cardiac PLN complex is a homopentamer  found in the sarcoplasmic reticulum (SR) membrane of the cardiomyocytes and acts as a regulator of intracellular calcium levels. Therefore, cardiac PLN is a main determinant of muscle contraction and relaxation. In the unphosphorylated form PLN  inhibits the sarco(endo)plasmic reticulum calcium ATPase (SERCA), a membrane protein responsible for the pumping most of the calcium from the cytoplasm to the SR, thereby causing a relaxation of myofibrils.","predictedComplex":false,"interactors":[{"ac":"EBI-10148373","identifier":"P61014","identifierLink":"https://www.uniprot.org/uniprotkb/P61014/entry","name":"Pln","description":"Phospholamban","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21194","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-56","complexName":"GLI1-SUFU complex","organismName":"Homo sapiens; 9606","description":"Transcriptional modulator complex, the formation of which regulates the activity of GLI transcription factors. Role as a negative regulator of the hedgehog-signalling network and plays a fundamental role in the control of development, cell proliferation and differentiation.","predictedComplex":false,"interactors":[{"ac":"EBI-308084","identifier":"P08151","identifierLink":"https://www.uniprot.org/uniprotkb/P08151/entry","name":"GLI1","description":"Zinc finger protein GLI1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45718","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-740595","identifier":"Q9UMX1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UMX1/entry","name":"SUFU","description":"Suppressor of fused homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10928","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-57","complexName":"Sodium:potassium-exchanging ATPase complex, FXYD2 variant","organismName":"Sus scrofa; 9823","description":"An ATPase-dependent transmembrane transport complex capable of generating electrochemical gradients by exchanging three intracellular sodium ions for two extracellular potassium ions during each cycle of ATP hydrolysis.  Na+/K+ pumps can also generate an inward current of protons.  \r\n\r\nEach transport cycle comprises a sequence of conformational transitions that permit extracellular K+ ions to access the binding sites in phosphorylated pumps and cytoplasmic Na+ ions to access the sites after dephosphorylation . Binding of the third Na+ ion triggers autophosphorylation, and binding of the second K+ ion prompts auto-dephosphorylation. This coupling of alternating ion access to ATP hydrolysis ensures forward, energetically uphill, progress of the Na+/K+ transport cycle. The larger pumped Na+ efflux than K+ influx constitutes outward current, a direction tending to make the membrane potential more negative. However, because each step in the cycle is reversible , if the normally transported intracellular Na+ and extracellular K+ are both scarce, the cycle can run backward, thus synthesizing ATP and generating inward, depolarizing current.","predictedComplex":false,"interactors":[{"ac":"EBI-9014004","identifier":"Q58K79","identifierLink":"https://www.uniprot.org/uniprotkb/Q58K79/entry","name":"FXYD2","description":"FXYD domain-containing ion transport regulator","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Sus scrofa; 9823","xrefs":[]},{"ac":"EBI-9014008","identifier":"P05027","identifierLink":"https://www.uniprot.org/uniprotkb/P05027/entry","name":"ATP1B1","description":"Sodium/potassium-transporting ATPase subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Sus scrofa; 9823","xrefs":[{"identifier":"PTHR11523","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9014019","identifier":"P05024","identifierLink":"https://www.uniprot.org/uniprotkb/P05024/entry","name":"ATP1A1","description":"Sodium/potassium-transporting ATPase subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Sus scrofa; 9823","xrefs":[{"identifier":"PTHR43294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-60","complexName":"bZIP transcription factor complex, Cebpa-Ddit3","organismName":"Rattus norvegicus; 10116","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site. Ddit3 binding to Cebpa inhibits Cebpa homodimerisation and therefore activation of transcription of Cebpa-specific genes. Induced in response to ER stress, nutrient deprivation and certain toxins. Induces cell cycle arrest and apoptosis in response to ER stress.","predictedComplex":false,"interactors":[{"ac":"EBI-10634485","identifier":"Q62857","identifierLink":"https://www.uniprot.org/uniprotkb/Q62857/entry","name":"Ddit3","description":"DNA damage-inducible transcript 3 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR16833","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1172084","identifier":"P05554","identifierLink":"https://www.uniprot.org/uniprotkb/P05554/entry","name":"Cebpa","description":"CCAAT/enhancer-binding protein alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-61","complexName":"NKX2-5 transcription factor complex","organismName":"Homo sapiens; 9606","description":"Nkx-2.5 is an evolutionary conserved transcription factor important for the specification and differentiation of cardiomyocytes during heart development and also required for spleen development. It binds DNA either as a monomer, homodimer, or heterodimer complex to activate or inhibit expression of genes.","predictedComplex":false,"interactors":[{"ac":"EBI-936601","identifier":"P52952","identifierLink":"https://www.uniprot.org/uniprotkb/P52952/entry","name":"NKX2-5","description":"Homeobox protein Nkx-2.5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24340","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-62","complexName":"bZIP transcription factor complex, Cebpb-Ddit3","organismName":"Rattus norvegicus; 10116","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.. Ddit3 binding to Cebpb inhibits Cebpb homodimerisation and therefore activation of transcription of Cebpb-specific genes. Induced in response to ER stress, nutrient deprivation and certain toxins. Induces cell cycle arrest and apoptosis in response to ER stress.","predictedComplex":false,"interactors":[{"ac":"EBI-10634485","identifier":"Q62857","identifierLink":"https://www.uniprot.org/uniprotkb/Q62857/entry","name":"Ddit3","description":"DNA damage-inducible transcript 3 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR16833","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5333201","identifier":"P21272","identifierLink":"https://www.uniprot.org/uniprotkb/P21272/entry","name":"Cebpb","description":"CCAAT/enhancer-binding protein beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-63","complexName":"bZIP transcription factor complex, Cebpb-Cebpb","organismName":"Rattus norvegicus; 10116","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site. This complex regulates the expression of genes involved in immune and inflammatory responses, binding to the regulatory regions of several acute-phase and cytokines genes and probably playing a role in the regulation of acute-phase reaction, inflammation and hemopoiesis.","predictedComplex":false,"interactors":[{"ac":"EBI-5333201","identifier":"P21272","identifierLink":"https://www.uniprot.org/uniprotkb/P21272/entry","name":"Cebpb","description":"CCAAT/enhancer-binding protein beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-64","complexName":"bZIP transcription factor complex, Cebpa-Cebpa","organismName":"Rattus norvegicus; 10116","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site. This complex regulates the expression of genes involved in immune and inflammatory responses, binding to the regulatory regions of several acute-phase and cytokines genes and probably playing a role in the regulation of acute-phase reaction, inflammation and hemopoiesis.","predictedComplex":false,"interactors":[{"ac":"EBI-1172084","identifier":"P05554","identifierLink":"https://www.uniprot.org/uniprotkb/P05554/entry","name":"Cebpa","description":"CCAAT/enhancer-binding protein alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-65","complexName":"bZIP transcription factor complex, Cebpa-Ddit3","organismName":"Mus musculus; 10090","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site. Ddit3 binding to Cebpa inhibits Cebpa homodimerisation and therefore activation of transcription of Cebpa-specific genes. Induced in response to ER stress, nutrient deprivation and certain toxins. Induces cell cycle arrest and apoptosis in response to ER stress.","predictedComplex":false,"interactors":[{"ac":"EBI-10636142","identifier":"P35639","identifierLink":"https://www.uniprot.org/uniprotkb/P35639/entry","name":"Ddit3","description":"DNA damage-inducible transcript 3 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16833","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2644207","identifier":"P53566","identifierLink":"https://www.uniprot.org/uniprotkb/P53566/entry","name":"Cebpa","description":"CCAAT/enhancer-binding protein alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-66","complexName":"bZIP transcription factor complex, Cebpb-Ddit3","organismName":"Mus musculus; 10090","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site. Ddit3 binding to Cebpb inhibits Cebpb homodimerisation and therefore activation of transcription of Cebpb-specific genes. Induced in response to ER stress, nutrient deprivation and certain toxins. Induces cell cycle arrest and apoptosis in response to ER stress","predictedComplex":false,"interactors":[{"ac":"EBI-1029979","identifier":"P28033","identifierLink":"https://www.uniprot.org/uniprotkb/P28033/entry","name":"Cebpb","description":"CCAAT/enhancer-binding protein beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10636142","identifier":"P35639","identifierLink":"https://www.uniprot.org/uniprotkb/P35639/entry","name":"Ddit3","description":"DNA damage-inducible transcript 3 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16833","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-67","complexName":"bZIP transcription factor complex, Cebpa-Cebpa","organismName":"Mus musculus; 10090","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site. This complex regulates the expression of genes involved in immune and inflammatory responses, binding to the regulatory regions of several acute-phase and cytokines genes and probably playing a role in the regulation of acute-phase reaction, inflammation and hemopoiesis.","predictedComplex":false,"interactors":[{"ac":"EBI-2644207","identifier":"P53566","identifierLink":"https://www.uniprot.org/uniprotkb/P53566/entry","name":"Cebpa","description":"CCAAT/enhancer-binding protein alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-68","complexName":"bZIP transcription factor complex, Cebpb-Cebpb","organismName":"Mus musculus; 10090","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site. This complex regulates the expression of genes involved in immune and inflammatory responses, binding to the regulatory regions of several acute-phase and cytokines genes and probably playing a role in the regulation of acute-phase reaction, inflammation and hemopoiesis.","predictedComplex":false,"interactors":[{"ac":"EBI-1029979","identifier":"P28033","identifierLink":"https://www.uniprot.org/uniprotkb/P28033/entry","name":"Cebpb","description":"CCAAT/enhancer-binding protein beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-69","complexName":"bZIP transcription factor complex, CEBPA-DDIT3","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.  DDIT3 binding to CEBPA inhibits CEBPA homodimerisation and therefore activation of transcription of CEBPA-specific genes. Induced in response to ER stress, nutrient deprivation and certain toxins. Induces cell cycle arrest and apoptosis in response to ER stress.","predictedComplex":false,"interactors":[{"ac":"EBI-1172054","identifier":"P49715","identifierLink":"https://www.uniprot.org/uniprotkb/P49715/entry","name":"CEBPA","description":"CCAAT/enhancer-binding protein alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742651","identifier":"P35638","identifierLink":"https://www.uniprot.org/uniprotkb/P35638/entry","name":"DDIT3","description":"DNA damage-inducible transcript 3 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16833","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-70","complexName":"bZIP transcription factor complex, CEBPB-DDIT3","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site. DDIT3 binding to CEBPB inhibits CEBPB homodimerisation and therefore activation of transcription of CEBPB-specific genes. Induced in response to ER stress, nutrient deprivation and certain toxins. Induces cell cycle arrest and apoptosis in response to ER stress.","predictedComplex":false,"interactors":[{"ac":"EBI-742651","identifier":"P35638","identifierLink":"https://www.uniprot.org/uniprotkb/P35638/entry","name":"DDIT3","description":"DNA damage-inducible transcript 3 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16833","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-969696","identifier":"P17676","identifierLink":"https://www.uniprot.org/uniprotkb/P17676/entry","name":"CEBPB","description":"CCAAT/enhancer-binding protein beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-71","complexName":"bZIP transcription factor complex, CEBPA-CEBPA","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site. This complex regulates the expression of genes involved in immune and inflammatory responses, binding to the regulatory regions of several acute-phase and cytokines genes and probably playing a role in the regulation of acute-phase reaction, inflammation and hemopoiesis.","predictedComplex":false,"interactors":[{"ac":"EBI-1172054","identifier":"P49715","identifierLink":"https://www.uniprot.org/uniprotkb/P49715/entry","name":"CEBPA","description":"CCAAT/enhancer-binding protein alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-72","complexName":"NKX2-5 homodimer complex","organismName":"Mus musculus; 10090","description":"Nkx-2.5 is an evolutionary conserved transcription factor important for the specification and differentiation of cardiomyocytes during heart development and also required for spleen development. It binds DNA either as a monomer, homodimer, or heterodimer complex to activate or inhibit expression of genes.","predictedComplex":false,"interactors":[{"ac":"EBI-297021","identifier":"P42582","identifierLink":"https://www.uniprot.org/uniprotkb/P42582/entry","name":"Nkx2-5","description":"Homeobox protein Nkx-2.5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24340","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2455","complexName":"Dystrophin glycoprotein complex, retinal inner limiting membrane variant","organismName":"Homo sapiens; 9606","description":"A plasma membrane transmembrane complex that links the actin cytoskeleton to the extracellular matrix. In the retina the complex is  required for correct electrical activity and retina formation and is present in the presynapse.","predictedComplex":false,"interactors":[{"ac":"EBI-20738802","identifier":"Q14118-PRO_0000021066","identifierLink":"https://www.uniprot.org/uniprotkb/Q14118-PRO_0000021066/entry","name":"DAG1","description":"Beta-dystroglycan","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-20738807","identifier":"Q14118-PRO_0000021065","identifierLink":"https://www.uniprot.org/uniprotkb/Q14118-PRO_0000021065/entry","name":"DAG1","description":"Alpha-dystroglycan","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-20811995","identifier":"Q14714","identifierLink":"https://www.uniprot.org/uniprotkb/Q14714/entry","name":"SSPN","description":"Sarcospan","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15260","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21503759","identifier":"Q9Y4J8-2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4J8-2/entry","name":"DTNA","description":"Dystrobrevin alpha","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-295843","identifier":"Q13884","identifierLink":"https://www.uniprot.org/uniprotkb/Q13884/entry","name":"SNTB1","description":"Beta-1-syntrophin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10554","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30876608","identifier":"P11532-7","identifierLink":"https://www.uniprot.org/uniprotkb/P11532-7/entry","name":"DMD","description":"Dystrophin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-3904504","identifier":"Q92629","identifierLink":"https://www.uniprot.org/uniprotkb/Q92629/entry","name":"SGCD","description":"Delta-sarcoglycan","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12939","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5357343","identifier":"Q13326","identifierLink":"https://www.uniprot.org/uniprotkb/Q13326/entry","name":"SGCG","description":"Gamma-sarcoglycan","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12939","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5663553","identifier":"Q16586","identifierLink":"https://www.uniprot.org/uniprotkb/Q16586/entry","name":"SGCA","description":"Alpha-sarcoglycan","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10132","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5663627","identifier":"Q16585","identifierLink":"https://www.uniprot.org/uniprotkb/Q16585/entry","name":"SGCB","description":"Beta-sarcoglycan","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21142","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-717191","identifier":"Q13424","identifierLink":"https://www.uniprot.org/uniprotkb/Q13424/entry","name":"SNTA1","description":"Alpha-1-syntrophin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10554","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2457","complexName":"ESCRT-I complex, Vps37B variant","organismName":"Drosophila melanogaster; 7227","description":"The ESCRT machinery, consisting of ESCRT-0 (CPX-2452), -I (this complex), -II (CPX-2458), -III (CPX-2459) and -IV (VPS4-VTA1 complex, CPX-2462) has been implicated in membrane scission steps, transforming a single, continuous bilayer into two distinct bilayers, either from within the neck of a vesicle budding away from the cytoplasm or from within a membrane tubule, while segregating cargo throughout the process. ESCRT-0 binds to and clusters ubiquitinated cargo for delivery into  multivesicular bodies, and recruits clathrin, ubiquitin ligases, and deubiquitinating enzymes. ESCRT-0 recruits ESCRT-I which engages ESCRT-II to nucleate ESCRT-III polymerization. VPS4-VTA1 complex, also known as ESCRT-IV, disassembles ESCRT-III to recycle its subunits. The ESCRT-III complex facilitates changes in membrane architecture by oligomerizing to form spiral, filament-like tubules, accumulation of which is associated with membrane constriction and fission. Disassembly of ESCRT-III by VPS4-VTA1 may be a required step for fission.","predictedComplex":false,"interactors":[{"ac":"EBI-119339","identifier":"Q9V359","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V359/entry","name":"Vps28","description":"Vacuolar protein sorting-associated protein 28 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-120427","identifier":"Q9VN88","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VN88/entry","name":"Vps37B","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1629520","identifier":"Q9VWY7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VWY7/entry","name":"Mvb12","description":"Multivesicular body subunit 12A","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR31612","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-82848","identifier":"Q9VVA7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVA7/entry","name":"TSG101","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23306","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2458","complexName":"ESCRT-II complex","organismName":"Drosophila melanogaster; 7227","description":"The ESCRT machinery, consisting of ESCRT-0 (CPX-2452), -I (CPX-2457/CPX-2460), -II (this complex), -III (CPX-2459) and -IV (VPS4-VTA1 complex, CPX-2462) has been implicated in membrane scission steps, transforming a single, continuous bilayer into two distinct bilayers, either from within the neck of a vesicle budding away from the cytoplasm or from within a membrane tubule, while segregating cargo throughout the process. ESCRT-0 binds to and clusters ubiquitinated cargo for delivery into  multivesicular bodies, and recruits clathrin, ubiquitin ligases, and deubiquitinating enzymes. ESCRT-0 recruits ESCRT-I which engages ESCRT-II to nucleate ESCRT-III polymerization. VPS4-VTA1 complex, also known as ESCRT-IV, disassembles ESCRT-III to recycle its subunits. The ESCRT-III complex facilitates changes in membrane architecture by oligomerizing to form spiral, filament-like tubules, accumulation of which is associated with membrane constriction and fission. Disassembly of ESCRT-III by VPS4-VTA1 may be a required step for fission.","predictedComplex":false,"interactors":[{"ac":"EBI-104459","identifier":"Q9VD72","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VD72/entry","name":"lsn","description":"Vacuolar-sorting protein SNF8","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12806","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-130446","identifier":"Q9VU87","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VU87/entry","name":"Vps36","description":"Vacuolar protein-sorting-associated protein 36","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13128","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-98834","identifier":"Q7JXV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q7JXV9/entry","name":"Vps25","description":"Vacuolar protein-sorting-associated protein 25","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13149","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2459","complexName":"ESCRT-III complex","organismName":"Drosophila melanogaster; 7227","description":"The ESCRT machinery, consisting of ESCRT-0 (CPX-2452), -I (CPX-2457/CPX-2460), -II (CPX-2458), -III (this complex) and -IV (VPS4-VTA1 complex, CPX-2462) has been implicated in membrane scission steps, transforming a single, continuous bilayer into two distinct bilayers, either from within the neck of a vesicle budding away from the cytoplasm or from within a membrane tubule, while segregating cargo throughout the process. ESCRT-0 binds to and clusters ubiquitinated cargo for delivery into  multivesicular bodies, and recruits clathrin, ubiquitin ligases, and deubiquitinating enzymes. ESCRT-0 recruits ESCRT-I which engages ESCRT-II to nucleate ESCRT-III polymerization. VPS4-VTA1 complex, also known as ESCRT-IV, disassembles ESCRT-III to recycle its subunits. The ESCRT-III complex facilitates changes in membrane architecture by oligomerizing to form spiral, filament-like tubules, accumulation of which is associated with membrane constriction and fission. Disassembly of ESCRT-III by VPS4-VTA1 may be a required step for fission.","predictedComplex":false,"interactors":[{"ac":"EBI-100740","identifier":"Q9VVI9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVI9/entry","name":"Vps60","description":"Charged multivesicular body protein 5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-114729","identifier":"Q9VN02","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VN02/entry","name":"Vps24","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-139825","identifier":"Q9VBI3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VBI3/entry","name":"Vps2","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-151577","identifier":"Q8T0Q4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8T0Q4/entry","name":"shrb","description":"Charged multivesicular body protein 4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-207475","identifier":"Q9W236","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W236/entry","name":"Vps20","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26720466","identifier":"Q9VRJ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VRJ5/entry","name":"CHMP2B","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30878909","identifier":"Q9Y124","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y124/entry","name":"BcDNA.GH08385","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3431917","identifier":"Q95SH2","identifierLink":"https://www.uniprot.org/uniprotkb/Q95SH2/entry","name":"Chmp1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2460","complexName":"ESCRT-I complex, Vps37A variant","organismName":"Drosophila melanogaster; 7227","description":"The ESCRT machinery, consisting of ESCRT-0 (CPX-2452), -I (this complex), -II (CPX-2458), -III (CPX-2459) and -IV (VPS4-VTA1 complex, CPX-2462) has been implicated in membrane scission steps, transforming a single, continuous bilayer into two distinct bilayers, either from within the neck of a vesicle budding away from the cytoplasm or from within a membrane tubule, while segregating cargo throughout the process. ESCRT-0 binds to and clusters ubiquitinated cargo for delivery into  multivesicular bodies, and recruits clathrin, ubiquitin ligases, and deubiquitinating enzymes. ESCRT-0 recruits ESCRT-I which engages ESCRT-II to nucleate ESCRT-III polymerization. VPS4-VTA1 complex, also known as ESCRT-IV, disassembles ESCRT-III to recycle its subunits. The ESCRT-III complex facilitates changes in membrane architecture by oligomerizing to form spiral, filament-like tubules, accumulation of which is associated with membrane constriction and fission. Disassembly of ESCRT-III by VPS4-VTA1 may be a required step for fission.","predictedComplex":false,"interactors":[{"ac":"EBI-119339","identifier":"Q9V359","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V359/entry","name":"Vps28","description":"Vacuolar protein sorting-associated protein 28 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-161858","identifier":"O77259","identifierLink":"https://www.uniprot.org/uniprotkb/O77259/entry","name":"Vsp37A","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1629520","identifier":"Q9VWY7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VWY7/entry","name":"Mvb12","description":"Multivesicular body subunit 12A","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR31612","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-82848","identifier":"Q9VVA7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVA7/entry","name":"TSG101","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23306","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2461","complexName":"Synaptonemal complex","organismName":"Homo sapiens; 9606","description":"Liquid crystalline structure that forms a large scaffold connecting homologous chromosomes from end to end during meiotic prophase I. Required for stabilising chromosome pairing and alignment, and for crossover events and chiasmata formation between homologous chromosome pairs. Mediates the lengthwise alignment of homologous chromsomes within 100 nm of each other with thread-like axial or lateral elements are paired together by transverse filaments formed by oligomerized SYCP1 proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-10283466","identifier":"A1L190","identifierLink":"https://www.uniprot.org/uniprotkb/A1L190/entry","name":"SYCE3","description":"Synaptonemal complex central element protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR36686","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11958386","identifier":"Q6PIF2","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PIF2/entry","name":"SYCE2","description":"Synaptonemal complex central element protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28398","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12090309","identifier":"Q9BXU0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BXU0/entry","name":"TEX12","description":"Testis-expressed protein 12","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR37349","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2555298","identifier":"Q15431","identifierLink":"https://www.uniprot.org/uniprotkb/Q15431/entry","name":"SYCP1","description":"Synaptonemal complex protein 1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46918","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2800702","identifier":"Q9BX26","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BX26/entry","name":"SYCP2","description":"Synaptonemal complex protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6872807","identifier":"Q8N0S2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N0S2/entry","name":"SYCE1","description":"Synaptonemal complex central element protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21731","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7574149","identifier":"Q8IZU3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IZU3/entry","name":"SYCP3","description":"Synaptonemal complex protein 3","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19368","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2462","complexName":"VPS4-VTA1 compex","organismName":"Drosophila melanogaster; 7227","description":"The ESCRT machinery, consisting of ESCRT-0 (CPX-2452), -I (CPX-2457/CPX-2460), -II (CPX-2458), -III (CPX-2459) and -IV (VPS4-VTA1 complex, this complex) has been implicated in membrane scission steps, transforming a single, continuous bilayer into two distinct bilayers, either from within the neck of a vesicle budding away from the cytoplasm or from within a membrane tubule, while segregating cargo throughout the process. ESCRT-0 binds to and clusters ubiquitinated cargo for delivery into  multivesicular bodies, and recruits clathrin, ubiquitin ligases, and deubiquitinating enzymes. ESCRT-0 recruits ESCRT-I which engages ESCRT-II to nucleate ESCRT-III polymerization. VPS4-VTA1 complex, also known as ESCRT-IV, disassembles ESCRT-III to recycle its subunits. The ESCRT-III complex facilitates changes in membrane architecture by oligomerizing to form spiral, filament-like tubules, accumulation of which is associated with membrane constriction and fission. Disassembly of ESCRT-III by VPS4-VTA1 may be a required step for fission.","predictedComplex":false,"interactors":[{"ac":"EBI-161914","identifier":"Q9Y162","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y162/entry","name":"Vps4","description":"vesicle-fusing ATPase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23074","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-167336","identifier":"Q9W0B3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W0B3/entry","name":"Vta1","description":"Vacuolar protein sorting-associated protein VTA1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46009","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2465","complexName":"Exocyst","organismName":"Drosophila melanogaster; 7227","description":"Recruited to sites of active exocytosis and membrane expansion, where it mediates the tethering of secretory vesicles to the plasma membrane in preparation for soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein receptor (SNARE)-mediated membrane fusion. The targeting of secretory vesicles to the plasma membrane involves direct interactions of the Exocyst with PI(4,5)P2. In addition, a number of small GTP-binding proteins interact with components of the exocyst and regulate the assembly, localization, and function of this complex.","predictedComplex":false,"interactors":[{"ac":"EBI-107639","identifier":"Q9VSJ8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VSJ8/entry","name":"Exo70","description":"Exocyst complex component 7","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12542","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-123769","identifier":"Q9V8K2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V8K2/entry","name":"Sec6","description":"Exocyst complex component 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21292","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-158567","identifier":"Q9VQQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VQQ9/entry","name":"Sec5","description":"Exocyst complex component 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13043","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-162086","identifier":"Q9VDE6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VDE6/entry","name":"Sec15","description":"Exocyst complex component 6","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12702","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-168923","identifier":"Q9VVG4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVG4/entry","name":"Sec3","description":"Exocyst complex component 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR16092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30878976","identifier":"Q7KRZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KRZ3/entry","name":"Exo84","description":"Exocyst complex component 8","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21426","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-86247","identifier":"Q9VNH6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VNH6/entry","name":"Sec8","description":"Exocyst complex component 4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14146","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-96207","identifier":"Q9XTM1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XTM1/entry","name":"Sec10","description":"Exocyst complex component 5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12100","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2466","complexName":"FACT complex","organismName":"Drosophila melanogaster; 7227","description":"An H2A-H2B histone chaperon complex that helps reorganize nucleosomes in an ATP-independent fashion. It is involved in various processes related to chromatin dynamics: DNA replication, DNA damage and repair, transcription initiation and elongation. Binds histone H2A-H2B dimers and possibly small amounts of H3H4. Facilitates RNA Polymerase II driven transcription through chromatin by destabilizing nucleosomal structure so that one of the H2A-H2B dimers is removed upon RNA Pol II passage. Subsequently brings back the histones and thereby maintains nucleosome integrity after RNA Pol II passage.","predictedComplex":false,"interactors":[{"ac":"EBI-170040","identifier":"Q05344","identifierLink":"https://www.uniprot.org/uniprotkb/Q05344/entry","name":"Ssrp","description":"FACT complex subunit Ssrp1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45849","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3405152","identifier":"Q8IRG6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IRG6/entry","name":"dre4","description":"FACT complex subunit spt16","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13980","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2467","complexName":"Crotoxin complex, aCA1/2/4-bCA1-CBb variant","organismName":"Crotalus durissus terrificus; 8732","description":"Class I, beta-neurotoxin, composed of an acidic, non-toxic and non-enzymatic subunit (CA), and a basic, weakly toxic, phospholipase A2 protein (CB). The neurotoxin causes paralysis by both pre- and postsynaptic blocking of acetylcholine signalling. The CA subunit increases the lethal potency of the uncomplexed CB subunit by enabling the toxin to reach the specific protein crotoxin receptor at the neuromuscular junction.","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-28965060","identifier":"P08878-PRO_0000022854","identifierLink":"https://www.uniprot.org/uniprotkb/P08878-PRO_0000022854/entry","name":"p08878-pro","description":"Crotoxin chain alpha CA1, CA2 and CA4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Crotalus durissus terrificus; 8732","xrefs":[]},{"ac":"EBI-28965072","identifier":"P08878-PRO_0000022858","identifierLink":"https://www.uniprot.org/uniprotkb/P08878-PRO_0000022858/entry","name":"p08878-pro","description":"Crotoxin chain gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Crotalus durissus terrificus; 8732","xrefs":[]},{"ac":"EBI-28965081","identifier":"P0CG56","identifierLink":"https://www.uniprot.org/uniprotkb/P0CG56/entry","name":"pa2bb","description":"Phospholipase A2 crotoxin basic subunit CBb","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Crotalus durissus terrificus; 8732","xrefs":[]},{"ac":"EBI-28966157","identifier":"P08878-PRO_0000420454","identifierLink":"https://www.uniprot.org/uniprotkb/P08878-PRO_0000420454/entry","name":"p08878-pro","description":"Crotoxin chain beta CA1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Crotalus durissus terrificus; 8732","xrefs":[]}]},{"complexAC":"CPX-2468","complexName":"Crotoxin complex, aCA3-bCA2/3/4-CBb variant","organismName":"Crotalus durissus terrificus; 8732","description":"Class I, beta-neurotoxin, composed of an acidic, non-toxic and non-enzymatic subunit (CA), and a basic, weakly toxic, phospholipase A2 protein (CB). The neurotoxin causes paralysis by both pre- and postsynaptic blocking of acetylcholine signalling. The CA subunit increases the lethal potency of the uncomplexed CB subunit by enabling the toxin to reach the specific protein crotoxin receptor at the neuromuscular junction.","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-28965064","identifier":"P08878-PRO_0000022856","identifierLink":"https://www.uniprot.org/uniprotkb/P08878-PRO_0000022856/entry","name":"p08878-pro","description":"Crotoxin chain beta CA2, CA3 and CA4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Crotalus durissus terrificus; 8732","xrefs":[]},{"ac":"EBI-28965072","identifier":"P08878-PRO_0000022858","identifierLink":"https://www.uniprot.org/uniprotkb/P08878-PRO_0000022858/entry","name":"p08878-pro","description":"Crotoxin chain gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Crotalus durissus terrificus; 8732","xrefs":[]},{"ac":"EBI-28965081","identifier":"P0CG56","identifierLink":"https://www.uniprot.org/uniprotkb/P0CG56/entry","name":"pa2bb","description":"Phospholipase A2 crotoxin basic subunit CBb","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Crotalus durissus terrificus; 8732","xrefs":[]},{"ac":"EBI-28997066","identifier":"P08878-PRO_0000420453","identifierLink":"https://www.uniprot.org/uniprotkb/P08878-PRO_0000420453/entry","name":"p08878-pro","description":"Crotoxin chain alpha CA3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Crotalus durissus terrificus; 8732","xrefs":[]}]},{"complexAC":"CPX-2469","complexName":"Multiaminoacyl-tRNA synthetase complex","organismName":"Homo sapiens; 9606","description":"Multi-enzyme complex which brings into close proximity 8 cytoplasmic aminoacyl-tRNA synthetases which catalyze ATP-dependent charging of tRNA with cognate amino acids for delivery to the A-site of the ribosome. The function of the assembly is uncertain but may support a processive pathway in which a tRNA cycles from an aminoacyl-tRNA synthetase in the complex  to the elongation factor EEF1A1 /2 (P68104/Q05639), then to the ribosome, and back to the multiaminoacyl-tRNA synthetase complex, without requiring a high affinity interaction between the aminoacyl-tRNA synthetase and EEF1A.","predictedComplex":false,"interactors":[{"ac":"EBI-1045802","identifier":"Q12904","identifierLink":"https://www.uniprot.org/uniprotkb/Q12904/entry","name":"AIMP1","description":"Aminoacyl tRNA synthase complex-interacting multifunctional protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11586","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1048486","identifier":"O43324","identifierLink":"https://www.uniprot.org/uniprotkb/O43324/entry","name":"EEF1E1","description":"Eukaryotic translation elongation factor 1 epsilon-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44490","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347462","identifier":"P47897","identifierLink":"https://www.uniprot.org/uniprotkb/P47897/entry","name":"QARS1","description":"Glutamine--tRNA ligase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355303","identifier":"P41252","identifierLink":"https://www.uniprot.org/uniprotkb/P41252/entry","name":"IARS1","description":"Isoleucine--tRNA ligase, cytoplasmic","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR42780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355315","identifier":"P07814","identifierLink":"https://www.uniprot.org/uniprotkb/P07814/entry","name":"EPRS1","description":"Bifunctional glutamate/proline--tRNA ligase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43382","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355482","identifier":"P54136","identifierLink":"https://www.uniprot.org/uniprotkb/P54136/entry","name":"RARS1","description":"Arginine--tRNA ligase, cytoplasmic","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11956","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355848","identifier":"P56192","identifierLink":"https://www.uniprot.org/uniprotkb/P56192/entry","name":"MARS1","description":"Methionine--tRNA ligase, cytoplasmic","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45765","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356077","identifier":"Q9P2J5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P2J5/entry","name":"LARS1","description":"Leucine--tRNA ligase, cytoplasmic","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45794","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356367","identifier":"Q15046","identifierLink":"https://www.uniprot.org/uniprotkb/Q15046/entry","name":"KARS1","description":"Lysine--tRNA ligase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR42918","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358730","identifier":"P14868","identifierLink":"https://www.uniprot.org/uniprotkb/P14868/entry","name":"DARS1","description":"Aspartate--tRNA ligase, cytoplasmic","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43450","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-745226","identifier":"Q13155","identifierLink":"https://www.uniprot.org/uniprotkb/Q13155/entry","name":"AIMP2","description":"Aminoacyl tRNA synthase complex-interacting multifunctional protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13438","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2470","complexName":"Vacuolar proton translocating ATPase complex, ATP6V0A1 variant","organismName":"Homo sapiens; 9606","description":"Translocates protons across a lipid bilayer via an ATP-driven rotary mechanism, thus acidifing the lumen of its resident organelle. Membrane-bound ion transporters/proton exchangers use the pH gradient to sequester metal ions to the vacuole and other cellular organelles. The combined action of the V-ATPase and membrane transporters plays a key role in maintaining cellular homoeostasis. The ATP6V0A1 variant localizes to synaptic vesicles in presynaptic neurons and to late endo/lysosomal compartments in non-neuronal tissues.","predictedComplex":false,"interactors":[{"ac":"EBI-1054757","identifier":"P38606","identifierLink":"https://www.uniprot.org/uniprotkb/P38606/entry","name":"ATP6V1A","description":"V-type proton ATPase catalytic subunit A","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18397230","identifier":"Q6P5S7","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P5S7/entry","name":"RNASEK","description":"Ribonuclease kappa","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31733","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2512037","identifier":"O75787","identifierLink":"https://www.uniprot.org/uniprotkb/O75787/entry","name":"ATP6AP2","description":"Renin receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2684998","identifier":"Q9Y5K8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5K8/entry","name":"ATP6V1D","description":"V-type proton ATPase subunit D","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11671","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27058934","identifier":"P15313","identifierLink":"https://www.uniprot.org/uniprotkb/P15313/entry","name":"atp6v1b_human","description":"V-type proton ATPase subunit B","stochiometry":"minValue: 3, maxValue: 3","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-27059051","identifier":"P21283","identifierLink":"https://www.uniprot.org/uniprotkb/P21283/entry","name":"atp6v1c_human","description":"V-type proton ATPase subunit C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-27061278","identifier":"Q96A05","identifierLink":"https://www.uniprot.org/uniprotkb/Q96A05/entry","name":"atp6v1e_human","description":"V-type proton ATPase subunit E","stochiometry":"minValue: 3, maxValue: 3","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-27061705","identifier":"O95670","identifierLink":"https://www.uniprot.org/uniprotkb/O95670/entry","name":"atp6v1g_human","description":"V-type proton ATPase subunit G","stochiometry":"minValue: 3, maxValue: 3","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-27062249","identifier":"Q8N8Y2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N8Y2/entry","name":"atp6v0d_human","description":"V-type proton ATPase V0 subunit d","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-27062250","identifier":"O15342","identifierLink":"https://www.uniprot.org/uniprotkb/O15342/entry","name":"atp6v0e_human","description":"V-type proton ATPase V0 subunit e","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2891238","identifier":"Q93050","identifierLink":"https://www.uniprot.org/uniprotkb/Q93050/entry","name":"ATP6V0A1","description":"V-type proton ATPase 116 kDa subunit a 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11629","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3904417","identifier":"Q99437","identifierLink":"https://www.uniprot.org/uniprotkb/Q99437/entry","name":"ATP6V0B","description":"V-type proton ATPase 21 kDa proteolipid subunit c''","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10263","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714667","identifier":"Q15904","identifierLink":"https://www.uniprot.org/uniprotkb/Q15904/entry","name":"ATP6AP1","description":"V-type proton ATPase subunit S1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12471","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714690","identifier":"Q16864","identifierLink":"https://www.uniprot.org/uniprotkb/Q16864/entry","name":"ATP6V1F","description":"V-type proton ATPase subunit F","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13861","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-721179","identifier":"P27449","identifierLink":"https://www.uniprot.org/uniprotkb/P27449/entry","name":"ATP6V0C","description":"V-type proton ATPase 16 kDa proteolipid subunit c","stochiometry":"minValue: 9, maxValue: 9","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10263","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724719","identifier":"Q9UI12","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UI12/entry","name":"ATP6V1H","description":"V-type proton ATPase subunit H","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10698","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2471","complexName":"bZIP transcription factor complex, BACH2-NFE2L3","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-10890629","identifier":"Q9Y4A8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4A8/entry","name":"NFE2L3","description":"Nuclear factor erythroid 2-related factor 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1642333","identifier":"Q9BYV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BYV9/entry","name":"BACH2","description":"Transcription regulator protein BACH2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2473","complexName":"bZIP transcription factor complex, BACH2-NFE2L1","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-1642333","identifier":"Q9BYV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BYV9/entry","name":"BACH2","description":"Transcription regulator protein BACH2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28952014","identifier":"Q14494-PRO_0000443103","identifierLink":"https://www.uniprot.org/uniprotkb/Q14494-PRO_0000443103/entry","name":"NFE2L1","description":"Transcription factor NRF1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-2474","complexName":"Actin-related protein 2/3 complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Assembles branched actin networks capable of generating protrusive force and resisting mechanical deformation by stimulating new filament growth from the side of existing actin filaments associated with regions of the plasma membrane. Purified Arp2/3 complex is inactive but stimulates rapid actin polymerization in the presence of activator proteins, the most potent type being the VCA (Verprolin, cofilin, acidic) domain-containing Wiskott-Aldrich syndrome protein (WASP) family members. The Arp2/3 complex appears to bind VCA and an existing actin filament in a cooperative manner. Upon activation, arp2 and act2 move into the side-by-side arrangement of consecutive actin subunits along the short pitch helical axis of an actin filament, mimicking a filamentous actin dimer and creating a template for new filament assembly.  The process appears to be ATP-dependent.","predictedComplex":false,"interactors":[{"ac":"EBI-443389","identifier":"Q9UUJ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UUJ1/entry","name":"arp2","description":"Actin-related protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-443398","identifier":"P78774","identifierLink":"https://www.uniprot.org/uniprotkb/P78774/entry","name":"arc1","description":"Actin-related protein 2/3 complex subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10709","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-443406","identifier":"P32390","identifierLink":"https://www.uniprot.org/uniprotkb/P32390/entry","name":"act2","description":"Actin-related protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-443412","identifier":"O14241","identifierLink":"https://www.uniprot.org/uniprotkb/O14241/entry","name":"arc2","description":"Actin-related protein 2/3 complex subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12058","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-443417","identifier":"Q9Y7J4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y7J4/entry","name":"arc3","description":"Actin-related protein 2/3 complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12391","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-443422","identifier":"Q92352","identifierLink":"https://www.uniprot.org/uniprotkb/Q92352/entry","name":"arc4","description":"Actin-related protein 2/3 complex subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR22629","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-443429","identifier":"Q10316","identifierLink":"https://www.uniprot.org/uniprotkb/Q10316/entry","name":"arc5","description":"Actin-related protein 2/3 complex subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2476","complexName":"GAIT complex","organismName":"Homo sapiens; 9606","description":"Inhibits translation of mRNAs encoding inflammatory proteins, in particular chemokine and chemokine receptors, in myeloid cells in response to Interferon gamma. Binds to the GAIT element present in the 3' untranslated region of its target mRNAs, and inhibits translation at least in part by repressing the translation initiation factor eIF4G (Q04637/P78344/O43432}. An interaction between eIF4G and RPL13A blocks the 43S preinitiation complex and prevents translation initiation.","predictedComplex":false,"interactors":[{"ac":"EBI-1024357","identifier":"O60506","identifierLink":"https://www.uniprot.org/uniprotkb/O60506/entry","name":"SYNCRIP","description":"Heterogeneous nuclear ribonucleoprotein Q","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21245","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-354056","identifier":"P04406","identifierLink":"https://www.uniprot.org/uniprotkb/P04406/entry","name":"GAPDH","description":"Glyceraldehyde-3-phosphate dehydrogenase","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10836","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355315","identifier":"P07814","identifierLink":"https://www.uniprot.org/uniprotkb/P07814/entry","name":"EPRS1","description":"Bifunctional glutamate/proline--tRNA ligase","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43382","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-720205","identifier":"P40429","identifierLink":"https://www.uniprot.org/uniprotkb/P40429/entry","name":"RPL13A","description":"Large ribosomal subunit protein uL13","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11545","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2477","complexName":"TREX-2 transcription-export complex, CETN2 variant","organismName":"Homo sapiens; 9606","description":"Required for mRNA nuclear export, linking transcription to nuclear export by chaperoning mature messenger ribonuclear particles from the nuclear interior to the nuclear pore complex (CPX-873)..","predictedComplex":false,"interactors":[{"ac":"EBI-1051701","identifier":"Q5JVF3","identifierLink":"https://www.uniprot.org/uniprotkb/Q5JVF3/entry","name":"PCID2","description":"PCI domain-containing protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12732","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1789926","identifier":"P41208","identifierLink":"https://www.uniprot.org/uniprotkb/P41208/entry","name":"CETN2","description":"Centrin-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-308480","identifier":"O60318","identifierLink":"https://www.uniprot.org/uniprotkb/O60318/entry","name":"MCM3AP","description":"Germinal-center associated nuclear protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12436","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-719226","identifier":"Q9NPA8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPA8/entry","name":"ENY2","description":"Transcription and mRNA export factor ENY2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12514","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-79819","identifier":"P60896","identifierLink":"https://www.uniprot.org/uniprotkb/P60896/entry","name":"SEM1","description":"26S proteasome complex subunit SEM1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-2478","complexName":"MPP10 complex","organismName":"Homo sapiens; 9606","description":"Required for early co-transcriptional events in ribosome biogenesis, acting as an RNA chaperone to initiate ribosome assembly. IMP3 protein directly associates with the first 70 nucleotides of the U3 snoRNA, with a stem-loop structure within the hinge region, and thereby directs the preassembled MPP10 complex to the U3 preprocessome. A sub-unit of the small subunit (SSU) processome, a 2.2 MDa ribonucleoprotein complex involved in the processing, assembly and maturation of nascent pre-ribosomal RNA to form the small ribosomal subunit.","predictedComplex":false,"interactors":[{"ac":"EBI-5235884","identifier":"O00566","identifierLink":"https://www.uniprot.org/uniprotkb/O00566/entry","name":"MPHOSPH10","description":"U3 small nucleolar ribonucleoprotein protein MPP10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR17039","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-747481","identifier":"Q9NV31","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NV31/entry","name":"IMP3","description":"U3 small nucleolar ribonucleoprotein protein IMP3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11831","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8641721","identifier":"Q96G21","identifierLink":"https://www.uniprot.org/uniprotkb/Q96G21/entry","name":"IMP4","description":"U3 small nucleolar ribonucleoprotein protein IMP4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22734","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2479","complexName":"bZIP transcription factor complex, BACH2-MAFB","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site. Acts as a transcriptional repressor binding to the MARE (Maf recognition element) site in gene promoters  during specific stages of B-cell development and in neuronal cells.","predictedComplex":false,"interactors":[{"ac":"EBI-1642333","identifier":"Q9BYV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BYV9/entry","name":"BACH2","description":"Transcription regulator protein BACH2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3649340","identifier":"Q9Y5Q3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5Q3/entry","name":"MAFB","description":"Transcription factor MafB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2480","complexName":"Polycomb repressive complex 1, RING1-PCGF2-CBX2-PHC3 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin-protein ligase that acts as a transcriptional repressor by mediating the monoubiquitination of Lys-119 of histone H2A, compacting chromatin, stalling RNA polymerase II and transcriptionally silencing genes critical for development.  CBX2 stably binds to mitotic chromosomes, recruiting the canonical PRC1 components and this may be involved in chromosomal segregation and instability. CBX2 may recognize H3K27me3 in the chromatin but this may not be the main driver of its interaction with chromatin.","predictedComplex":false,"interactors":[{"ac":"EBI-1223801","identifier":"Q8NDX5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NDX5/entry","name":"PHC3","description":"Polyhomeotic-like protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12247","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2129767","identifier":"P35227","identifierLink":"https://www.uniprot.org/uniprotkb/P35227/entry","name":"PCGF2","description":"Polycomb group RING finger protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10825","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-745934","identifier":"Q14781","identifierLink":"https://www.uniprot.org/uniprotkb/Q14781/entry","name":"CBX2","description":"Chromobox protein homolog 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46860","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752313","identifier":"Q06587","identifierLink":"https://www.uniprot.org/uniprotkb/Q06587/entry","name":"RING1","description":"E3 ubiquitin-protein ligase RING1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2482","complexName":"bZIP transcription factor complex, BACH2-MAFK","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site. Acts as a transcriptional repressor binding to the MARE (Maf recognition element) site in gene promoters  during specific stages of B-cell development and in neuronal cells.","predictedComplex":false,"interactors":[{"ac":"EBI-1642333","identifier":"Q9BYV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BYV9/entry","name":"BACH2","description":"Transcription regulator protein BACH2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2559512","identifier":"O60675","identifierLink":"https://www.uniprot.org/uniprotkb/O60675/entry","name":"MAFK","description":"Transcription factor MafK","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2483","complexName":"bZIP transcription factor complex, BACH2-MAF","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site. Acts as a transcriptional repressor binding to the MARE (Maf recognition element) site in gene promoters  during specific stages of B-cell development and in neuronal cells.","predictedComplex":false,"interactors":[{"ac":"EBI-1642333","identifier":"Q9BYV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BYV9/entry","name":"BACH2","description":"Transcription regulator protein BACH2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2805091","identifier":"O75444","identifierLink":"https://www.uniprot.org/uniprotkb/O75444/entry","name":"MAF","description":"Transcription factor Maf","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2484","complexName":"bZIP transcription factor complex, BACH2-MAFF","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site. Acts as a transcriptional repressor binding to the MARE (Maf recognition element) site in gene promoters  during specific stages of B-cell development and in neuronal cells.","predictedComplex":false,"interactors":[{"ac":"EBI-1642333","identifier":"Q9BYV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BYV9/entry","name":"BACH2","description":"Transcription regulator protein BACH2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-721128","identifier":"Q9ULX9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ULX9/entry","name":"MAFF","description":"Transcription factor MafF","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2485","complexName":"bZIP transcription factor complex, BACH2-MAFG","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site. Acts as a transcriptional repressor binding to the MARE (Maf recognition element) site in gene promoters  during specific stages of B-cell development and in neuronal cells.","predictedComplex":false,"interactors":[{"ac":"EBI-1642333","identifier":"Q9BYV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BYV9/entry","name":"BACH2","description":"Transcription regulator protein BACH2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-713514","identifier":"O15525","identifierLink":"https://www.uniprot.org/uniprotkb/O15525/entry","name":"MAFG","description":"Transcription factor MafG","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2486","complexName":"THUMPD3-TRM112 methyltransferase complex","organismName":"Homo sapiens; 9606","description":"S-adenosylmethionine-dependent methyltransferase which catalyzes methylation of the amino group at the C2 position of guanine-6 to form N2-methylguanosine (m2G6) in a wide range of G6-containing human cytoplasmic tRNAs. The complex recognizes the characteristic 3′-CCA of mature tRNAs. The m2G7 of tRNATrp is also introduced by THUMPD3-TRMT112.","predictedComplex":false,"interactors":[{"ac":"EBI-30813205","identifier":"CHEBI:59789","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:59789","name":"s-adenosyl-l-methionine zwitterion","description":"S-adenosyl-L-methionine zwitterion","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-373253","identifier":"Q9BV44","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BV44/entry","name":"THUMPD3","description":"tRNA (guanine(6)-N(2))-methyltransferase THUMP3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14911","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373326","identifier":"Q9UI30","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UI30/entry","name":"TRMT112","description":"Multifunctional methyltransferase subunit TRM112-like protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12773","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2487","complexName":"bZIP transcription factor complex, BACH2-BACH2","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. Active as a transcriptional repressor during specific stages of B-cell development and in neuronal cells. Modulates class-switch recombination during the differentiation of mature B cells to antibody-secreting plasma cells and it is also an important regulator of apoptotic responses to oxidative stress.","predictedComplex":false,"interactors":[{"ac":"EBI-1642333","identifier":"Q9BYV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BYV9/entry","name":"BACH2","description":"Transcription regulator protein BACH2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2488","complexName":"TREX transcription-export complex, DX39B variant","organismName":"Homo sapiens; 9606","description":"Selectively binds maturing mRNA at the messenger ribonucleoprotein complex 5'-end, splice junctions, and 3'-end and licenses mRNA for nuclear export by loading the global mRNA-export factor NXF1-NXT (CPX-725/CPX-2435) . Also acts to chaperone the nascent mRNA by inhibiting the formation of harmful DNA-RNA hybrids, (R-loops), thus protecting genome integrity. The THO subcomplex is recruited to the mRNP and delivers DDX39B, which clamps the mRNA. THO-DDX39B binds export adapters such as ALYREF and together they promote loading of  NXF1-NXT onto mRNA.. It  is predicted that the multiple variants of this complex may exist with different compositional rearrangements of its adapter subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-10198848","identifier":"Q9P127","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P127/entry","name":"LUZP4","description":"Leucine zipper protein 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22550","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1755078","identifier":"Q8NI27","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NI27/entry","name":"THOC2","description":"THO complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21597","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1765605","identifier":"Q96FV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q96FV9/entry","name":"THOC1","description":"THO complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13265","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1776152","identifier":"Q9BY77","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BY77/entry","name":"POLDIP3","description":"Polymerase delta-interacting protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19965","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2510823","identifier":"Q96J01","identifierLink":"https://www.uniprot.org/uniprotkb/Q96J01/entry","name":"THOC3","description":"THO complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22839","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2880668","identifier":"Q86W42","identifierLink":"https://www.uniprot.org/uniprotkb/Q86W42/entry","name":"THOC6","description":"THO complex subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347495","identifier":"P82979","identifierLink":"https://www.uniprot.org/uniprotkb/P82979/entry","name":"SARNP","description":"SAP domain-containing ribonucleoprotein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46551","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347640","identifier":"Q86V81","identifierLink":"https://www.uniprot.org/uniprotkb/Q86V81/entry","name":"ALYREF","description":"THO complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19965","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347794","identifier":"Q9Y3Y2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3Y2/entry","name":"CHTOP","description":"Chromatin target of PRMT1 protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48426","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348622","identifier":"Q13838","identifierLink":"https://www.uniprot.org/uniprotkb/Q13838/entry","name":"DDX39B","description":"Spliceosome RNA helicase DDX39B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47958","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5280316","identifier":"Q13769","identifierLink":"https://www.uniprot.org/uniprotkb/Q13769/entry","name":"THOC5","description":"THO complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6657994","identifier":"Q53F19","identifierLink":"https://www.uniprot.org/uniprotkb/Q53F19/entry","name":"NCBP3","description":"Nuclear cap-binding protein subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16291","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-711389","identifier":"P84090","identifierLink":"https://www.uniprot.org/uniprotkb/P84090/entry","name":"ERH","description":"Enhancer of rudimentary homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12373","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-716286","identifier":"Q6I9Y2","identifierLink":"https://www.uniprot.org/uniprotkb/Q6I9Y2/entry","name":"THOC7","description":"THO complex subunit 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23405","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724553","identifier":"Q96QD9","identifierLink":"https://www.uniprot.org/uniprotkb/Q96QD9/entry","name":"FYTTD1","description":"UAP56-interacting factor","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21038","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-748480","identifier":"O75152","identifierLink":"https://www.uniprot.org/uniprotkb/O75152/entry","name":"ZC3H11A","description":"Zinc finger CCCH domain-containing protein 11A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15725","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2489","complexName":"SCF E3 ubiquitin ligase complex, FBXL22 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXL22 target proteins include ACTN2 (P35609) and FLNC (Q14315) suggesting a role in sacomeric muscle contraction and sarcomeric structure","predictedComplex":false,"interactors":[{"ac":"EBI-24224082","identifier":"Q6P050","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P050/entry","name":"FBXL22","description":"F-box and leucine-rich protein 22","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2490","complexName":"Actin-related protein 2/3 complex, ARPC1A-ACTR3B-ARPC5 variant","organismName":"Homo sapiens; 9606","description":"Assembles branched actin networks capable of generating protrusive force and resisting mechanical deformation by stimulating new filament growth from the side of existing actin filaments associated with regions of the plasma membrane. Purified Arp2/3 complex is inactive but stimulates rapid actin polymerization in the presence of activator proteins, the most potent type being the VCA (Verprolin, cofilin, acidic) domain-containing Wiskott-Aldrich syndrome protein (WASP) family members. The Arp2/3 complex appears to bind VCA and an existing actin filament in a cooperative manner. Upon activation, ACTR2 and ACTR3B move into the side-by-side arrangement of consecutive actin subunits along the short pitch helical axis of an actin filament, mimicking a filamentous actin dimer and creating a template for new filament assembly.  The process appears to be ATP-dependent.","predictedComplex":false,"interactors":[{"ac":"EBI-1020827","identifier":"Q92747","identifierLink":"https://www.uniprot.org/uniprotkb/Q92747/entry","name":"ARPC1A","description":"Actin-related protein 2/3 complex subunit 1A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10709","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1047175","identifier":"Q9P1U1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P1U1/entry","name":"ACTR3B","description":"Actin-related protein 3B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-351829","identifier":"O15145","identifierLink":"https://www.uniprot.org/uniprotkb/O15145/entry","name":"ARPC3","description":"Actin-related protein 2/3 complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12391","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-351872","identifier":"P59998","identifierLink":"https://www.uniprot.org/uniprotkb/P59998/entry","name":"ARPC4","description":"Actin-related protein 2/3 complex subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22629","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352356","identifier":"O15144","identifierLink":"https://www.uniprot.org/uniprotkb/O15144/entry","name":"ARPC2","description":"Actin-related protein 2/3 complex subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12058","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352975","identifier":"O15511","identifierLink":"https://www.uniprot.org/uniprotkb/O15511/entry","name":"ARPC5","description":"Actin-related protein 2/3 complex subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353580","identifier":"P61160","identifierLink":"https://www.uniprot.org/uniprotkb/P61160/entry","name":"ACTR2","description":"Actin-related protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2491","complexName":"bZIP transcription factor complex, BACH1-FOS","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-1263541","identifier":"O14867","identifierLink":"https://www.uniprot.org/uniprotkb/O14867/entry","name":"BACH1","description":"Transcription regulator protein BACH1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-852851","identifier":"P01100","identifierLink":"https://www.uniprot.org/uniprotkb/P01100/entry","name":"FOS","description":"Protein c-Fos","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2492","complexName":"SCF E3 ubiquitin ligase complex, FBXL15 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXL15 target proteins include the E3 ubiquitin-protein ligase SMURF1 (Q9HCE7) which acts as a negative regulator of BMP signaling pathway. The complex thus plays a role in dorsal/ventral pattern formation and bone mass maintenance.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6144096","identifier":"Q9H469","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H469/entry","name":"FBXL15","description":"F-box/LRR-repeat protein 15","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13318","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2493","complexName":"bZIP transcription factor complex, BACH1-MAFK","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site. Acts as a transcriptional repressor binding to the MARE (Maf recognition element) site in gene promoters, thus repressing the expression of NFE2L2 (Q16236) target genes which play a key role in the response to oxidative stress. Represses the transcription of heme oxygenase 1 (P09601) under low heme conditions. When free heme levels rise, activated NFE2L2 partners with MAF proteins to enable transactivation of HMOX1. Heme binds to BACH1 and heme-bound BACH1 undergoes nuclear export and ubiquitin-dependent degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-1263541","identifier":"O14867","identifierLink":"https://www.uniprot.org/uniprotkb/O14867/entry","name":"BACH1","description":"Transcription regulator protein BACH1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2559512","identifier":"O60675","identifierLink":"https://www.uniprot.org/uniprotkb/O60675/entry","name":"MAFK","description":"Transcription factor MafK","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2494","complexName":"bZIP transcription factor complex, BACH1-CREB1","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-1263541","identifier":"O14867","identifierLink":"https://www.uniprot.org/uniprotkb/O14867/entry","name":"BACH1","description":"Transcription regulator protein BACH1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-711855","identifier":"P16220","identifierLink":"https://www.uniprot.org/uniprotkb/P16220/entry","name":"CREB1","description":"Cyclic AMP-responsive element-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45879","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2496","complexName":"bZIP transcription factor complex, BACH1-DDIT3","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.","predictedComplex":false,"interactors":[{"ac":"EBI-1263541","identifier":"O14867","identifierLink":"https://www.uniprot.org/uniprotkb/O14867/entry","name":"BACH1","description":"Transcription regulator protein BACH1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742651","identifier":"P35638","identifierLink":"https://www.uniprot.org/uniprotkb/P35638/entry","name":"DDIT3","description":"DNA damage-inducible transcript 3 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16833","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2497","complexName":"bZIP transcription factor complex, BACH1-MAFB","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site. Acts as a transcriptional repressor binding to the MARE (Maf recognition element) site in gene promoters, thus repressing the expression of NFE2L2 (Q16236) target genes which play a key role in the response to oxidative stress. Represses the transcription of heme oxygenase 1 (P09601) under low heme conditions. When free heme levels rise, activated NFE2L2 partners with MAF proteins to enable transactivation of HMOX1. Heme binds to BACH1 and heme-bound BACH1 undergoes nuclear export and ubiquitin-dependent degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-1263541","identifier":"O14867","identifierLink":"https://www.uniprot.org/uniprotkb/O14867/entry","name":"BACH1","description":"Transcription regulator protein BACH1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3649340","identifier":"Q9Y5Q3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5Q3/entry","name":"MAFB","description":"Transcription factor MafB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2498","complexName":"DNA fragmentation factor complex","organismName":"Homo sapiens; 9606","description":"Inhibits the catalytic activity of DFFB,  a caspase-activated endo-nuclease that cleaves naked and chromosomal DNA during   apoptotic cell death. During protein biosynthesis, DFFA acts as a specific chaperone, helping DFFB to adopt a catalytically competent structure. The complex then translocates into the nucleus, a process that requires cooperation of the nuclear localization signals found at the C-termini of these proteins. When apoptotic stimuli activate effector caspases such as caspase-3 (CPX-970), the DFFA is cleaved at residues 117 and 224, resulting in the dissociation of DFFB. Dissociated DFFB dimerizes, and cleaves chromosomal DNA.","predictedComplex":false,"interactors":[{"ac":"EBI-1053821","identifier":"O76075","identifierLink":"https://www.uniprot.org/uniprotkb/O76075/entry","name":"DFFB","description":"DNA fragmentation factor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727171","identifier":"O00273","identifierLink":"https://www.uniprot.org/uniprotkb/O00273/entry","name":"DFFA","description":"DNA fragmentation factor subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12306","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2499","complexName":"Erythrocyte spectrin complex","organismName":"Homo sapiens; 9606","description":"The major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. Crucial for maintaining the stability and structure of the cell membrane and the shape of a cell. Major function of the spectrin skeleton in erythrocytes is to provide mechanical support for the membrane bilayer and allow survival of the cells in circulation. Associates with the intracellular face of the plasma membrane by indirect interaction, through direct interactions with Protein 4.1 (P11171) and ankyrin, with the transmembrane ion transporter band 3 (P02730). Protein 4.2 (P16452) binds the spectrin tail region to the transmembrane protein glycophorin A (P02724).","predictedComplex":false,"interactors":[{"ac":"EBI-375617","identifier":"P02549","identifierLink":"https://www.uniprot.org/uniprotkb/P02549/entry","name":"SPTA1","description":"Spectrin alpha chain, erythrocytic 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11915","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-514908","identifier":"P11277","identifierLink":"https://www.uniprot.org/uniprotkb/P11277/entry","name":"SPTB","description":"Spectrin beta chain, erythrocytic","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11915","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2500","complexName":"bZIP transcription factor complex, BACH1-MAF","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site. Acts as a transcriptional repressor binding to the MARE (Maf recognition element) site in gene promoters, thus repressing the expression of NFE2L2 (Q16236) target genes which play a key role in the response to oxidative stress. Represses the transcription of heme oxygenase 1 (P09601) under low heme conditions. When free heme levels rise, activated NFE2L2 partners with MAF proteins to enable transactivation of HMOX1. Heme binds to BACH1 and heme-bound BACH1 undergoes nuclear export and ubiquitin-dependent degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-1263541","identifier":"O14867","identifierLink":"https://www.uniprot.org/uniprotkb/O14867/entry","name":"BACH1","description":"Transcription regulator protein BACH1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2805091","identifier":"O75444","identifierLink":"https://www.uniprot.org/uniprotkb/O75444/entry","name":"MAF","description":"Transcription factor Maf","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2501","complexName":"USH2 complex","organismName":"Mus musculus; 10090","description":"Required for cochlear stereociliary bundle development. essential for stereociliary diameter and differentiation in inner ear hair cells and for stereociliary rigidity and V-shaped three-row organization in outer ear hair cells. Form ankle links, thin fibers that connect the bases of neighboring stereocilia and only exist during development. Defects in the complex result in disorganization of the stereocilia bundle. The complex may also form in photo receptors although the presence of Pdzd7 has not been proven in that location.","predictedComplex":false,"interactors":[{"ac":"EBI-17171120","identifier":"Q8VHN7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VHN7/entry","name":"Adgrv1","description":"Adhesion G-protein coupled receptor V1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46682","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27123285","identifier":"Q2QI47","identifierLink":"https://www.uniprot.org/uniprotkb/Q2QI47/entry","name":"Ush2A","description":"Usherin","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10574","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27123347","identifier":"E9Q9W7","identifierLink":"https://www.uniprot.org/uniprotkb/E9Q9W7/entry","name":"Pdzd7","description":"PDZ domain-containing protein 7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23116","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7417603","identifier":"Q80VW5","identifierLink":"https://www.uniprot.org/uniprotkb/Q80VW5/entry","name":"Whrn","description":"Whirlin","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23116","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2502","complexName":"CD94-NKG2A natural killer receptor complex","organismName":"Homo sapiens; 9606","description":"C-type lectin inhibitory receptor present on natural killer (NK) cells and a subset of T cells. Binds the HLA-E class I histocompatibility antigen molecule, specifically the peptide-bound HLA-E-B2M heterotrimeric complex, resulting in a suppression of the activation of signaling processes and the inhibition of NK cell-mediated cytolysis. The interaction of CD94-NKG2A with HLA-E is a central mechanism by which NK cells indirectly monitor the expression of other MHC class I molecules within a target cell.","predictedComplex":false,"interactors":[{"ac":"EBI-9018174","identifier":"Q13241","identifierLink":"https://www.uniprot.org/uniprotkb/Q13241/entry","name":"KLRD1","description":"Natural killer cells antigen CD94","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9018187","identifier":"P26715","identifierLink":"https://www.uniprot.org/uniprotkb/P26715/entry","name":"KLRC1","description":"NKG2-A/NKG2-B type II integral membrane protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2503","complexName":"ISCA2-IBA57 mitochondrial iron-sulfur protein assembly complex","organismName":"Homo sapiens; 9606","description":"Binds a [2Fe-2S] cluster which may then be inserted into mitochondrial target proteins. Receives the  [2Fe-2S] cluster from GLRX5 complexes (CPX-6862, CPX-6863). The [2Fe-2S] cluster is extremely stable against oxidative degradation when bound to the ISCA2-IBA57 complex. The complex may also play a role in forming/repairing [4Fe-4S] clusters under aerobic cellular conditions by transferring one/two [2Fe-2S] clusters to mitochondrial target proteins which directly generate the [4Fe-4S] cluster.","predictedComplex":false,"interactors":[{"ac":"EBI-10258659","identifier":"Q86U28","identifierLink":"https://www.uniprot.org/uniprotkb/Q86U28/entry","name":"ISCA2","description":"Iron-sulfur cluster assembly 2 homolog, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43011","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10714899","identifier":"Q5T440","identifierLink":"https://www.uniprot.org/uniprotkb/Q5T440/entry","name":"IBA57","description":"Iron-sulfur cluster assembly factor IBA57, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22602","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11172266","identifier":"CHEBI:49601","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49601","name":"fe2s2 iron-sulfur cluster","description":"Fe2S2 iron-sulfur cluster","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2505","complexName":"ESCRT-I complex, VPS37B-MVB12A variant","organismName":"Homo sapiens; 9606","description":"The ESCRT machinery, consisting of ESCRT-0  (this complex), -I, -II (CPX-2506), -III (CPX-329) and -IV (VPS4A/B complex, CPX-338)  has been implicated in membrane scission steps, transforming a single, continuous bilayer into two distinct bilayers, either from within the neck of a vesicle budding away from the cytoplasm or from within a membrane tubule, while segregating cargo throughout the process. Membrane fission processes include: a) the sorting of multivesicular bodies (MVB) in the endocytic pathway; cargoes destined for inclusion into the MVB pathway are covalently modified with ubiquitin, recognized by ubiquitin-binding domains in the early ESCRTs (ESCRT-0, -I, and -II) and sequestered into endosomal microdomains that bud into the endosome as intralumenal vesicles aided by ESCRT-III, b) downregulation of cell-surface receptors, c) repair of plasma membrane wounds, d) abscission of the cellular bridge during cytokineses, d) nuclear envelope sealing by annular fusion and e) budding of virions (especially HIV-1) from the plasma membrane. The ESCRT machinery seems to play an indirect role in the proper functioning of cellular polarity and migration, the miRNA machinery and gene expression regulation. ESCRT-0 binds to and clusters ubiquitinated cargo for delivery into MVBs, and recruits clathrin, ubiquitin ligases, and deubiquitinating enzymes. ESCRT-0 recruits ESCRT-I which engages ESCRT-II to nucleate ESCRT-III polymerization. VPS4A/B complex, also known as ESCRT-IV, disassembles ESCRT-III to recycle its subunits. The ESCRT-III complex facilitates changes in membrane architecture by oligomerizing to form spiral, filament-like tubules, accumulation of which is associated with membrane constriction and fission. Disassembly of ESCRT-III by VPS4A/B may be a required step for fission.","predictedComplex":false,"interactors":[{"ac":"EBI-346882","identifier":"Q99816","identifierLink":"https://www.uniprot.org/uniprotkb/Q99816/entry","name":"TSG101","description":"Tumor susceptibility gene 101 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23306","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4290865","identifier":"Q96EY5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96EY5/entry","name":"MVB12A","description":"Multivesicular body subunit 12A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31612","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4400866","identifier":"Q9H9H4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H9H4/entry","name":"VPS37B","description":"Vacuolar protein sorting-associated protein 37B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727424","identifier":"Q9UK41","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK41/entry","name":"VPS28","description":"Vacuolar protein sorting-associated protein 28 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2506","complexName":"ESCRT-II complex","organismName":"Homo sapiens; 9606","description":"The ESCRT machinery, consisting of ESCRT-0, -I, -II (this complex), -III (CPX-329) and -IV (VPS4A/B complex, CPX-338)  has been implicated in membrane scission steps, transforming a single, continuous bilayer into two distinct bilayers, either from within the neck of a vesicle budding away from the cytoplasm or from within a membrane tubule, while segregating cargo throughout the process. Membrane fission processes include: a) the sorting of multivesicular bodies (MVB) in the endocytic pathway; cargoes destined for inclusion into the MVB pathway are covalently modified with ubiquitin, recognized by ubiquitin-binding domains in the early ESCRTs (ESCRT-0, -I, and -II) and sequestered into endosomal microdomains that bud into the endosome as intralumenal vesicles aided by ESCRT-III, b) downregulation of cell-surface receptors, c) repair of plasma membrane wounds, d) abscission of the cellular bridge during cytokineses, d) nuclear envelope sealing by annular fusion and e) budding of virions (especially HIV-1) from the plasma membrane. The ESCRT machinery seems to play an indirect role in the proper functioning of cellular polarity and migration, the miRNA machinery and gene expression regulation. ESCRT-0 binds to and clusters ubiquitinated cargo for delivery into MVBs, and recruits clathrin, ubiquitin ligases, and deubiquitinating enzymes. ESCRT-0 recruits ESCRT-I which engages ESCRT-II to nucleate ESCRT-III polymerization. VPS4A/B complex, also known as ESCRT-IV, disassembles ESCRT-III to recycle its subunits. The ESCRT-III complex facilitates changes in membrane architecture by oligomerizing to form spiral, filament-like tubules, accumulation of which is associated with membrane constriction and fission. Disassembly of ESCRT-III by VPS4A/B may be a required step for fission.","predictedComplex":false,"interactors":[{"ac":"EBI-4401822","identifier":"Q86VN1","identifierLink":"https://www.uniprot.org/uniprotkb/Q86VN1/entry","name":"VPS36","description":"Vacuolar protein-sorting-associated protein 36","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13128","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-741945","identifier":"Q9BRG1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BRG1/entry","name":"VPS25","description":"Vacuolar protein-sorting-associated protein 25","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13149","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-747719","identifier":"Q96H20","identifierLink":"https://www.uniprot.org/uniprotkb/Q96H20/entry","name":"SNF8","description":"Vacuolar-sorting protein SNF8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12806","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2508","complexName":"FlhDC transcription factor complex","organismName":"Escherichia coli (strain K12); 83333","description":"Trans-acting transcriptional activator that has been shown to bind to the flagellar regulon, which consists of at least 14 operons and more than 50 genes. Master regulator of flagellum biogenesis and swarming migration. Activates flagellum class II genes which encode the flagellar basal body, proteins of the export machinery, the flagellar sigma subunit fliA (P0AEM6), and its anti-sigma factor, flgM (P0AEM4).","predictedComplex":false,"interactors":[{"ac":"EBI-1125980","identifier":"P0A8S9","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8S9/entry","name":"flhD","description":"Flagellar transcriptional regulator FlhD","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-9018288","identifier":"P0ABY7","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABY7/entry","name":"flhC","description":"Flagellar transcriptional regulator FlhC","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2509","complexName":"RNA decapping complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. The activity of this complex is tightly regulated to prevent premature degradation of the transcript.","predictedComplex":false,"interactors":[{"ac":"EBI-3647323","identifier":"O13828","identifierLink":"https://www.uniprot.org/uniprotkb/O13828/entry","name":"dcp2","description":"mRNA decapping complex subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23114","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67092826","identifier":"Q10108","identifierLink":"https://www.uniprot.org/uniprotkb/Q10108/entry","name":"yaq9","description":"Uncharacterized protein C18G6.09c","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-7557105","identifier":"Q9P805","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P805/entry","name":"dcp1","description":"mRNA-decapping enzyme subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]}]},{"complexAC":"CPX-2510","complexName":"Adaptor complex AP-1","organismName":"Drosophila melanogaster; 7227","description":"Adaptor complex that orchestrates the formation of membrane coats that mediate cargo selection and vesicle budding, for example by linking clathrin to the membrane surface of trans-Golgi network vesicles. AP-1 is specific for trafficking between the trans-Golgi network and endosomes.","predictedComplex":false,"interactors":[{"ac":"EBI-30858763","identifier":"Q7KVR8","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KVR8/entry","name":"AP-1gamma","description":"AP-1 complex subunit gamma","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30858834","identifier":"B8A403","identifierLink":"https://www.uniprot.org/uniprotkb/B8A403/entry","name":"AP-1sigma","description":"AP complex subunit sigma","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3423007","identifier":"O62531","identifierLink":"https://www.uniprot.org/uniprotkb/O62531/entry","name":"AP-1mu","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-85346","identifier":"Q24253","identifierLink":"https://www.uniprot.org/uniprotkb/Q24253/entry","name":"AP-1-2beta","description":"AP complex subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2511","complexName":"Small ribosomal subunit processome","organismName":"Homo sapiens; 9606","description":"Mediates the early stages of maturation of the small ribosomal subunit by coupling RNA folding to subsequent RNA cleavage and processing steps. A 47S precursor transcript contains coding segments for the small ribosomal subunit (18S) and large ribosomal subunit (28S and 5.8S) and regulatory regions including the 5' external transcribed spacer (5' ETS). The SSU processome binds to the 5' ETS and cleaves the precursor transcript at site A1, which separates the 5′ ETS and 18S segments. and then drives the transition toward a pre-40S particle. Some proteins are then lost from the processome and additional proteins bind, including the DHX37 helicase which is required for the release of U3 snoRNP.","predictedComplex":false,"interactors":[{"ac":"EBI-11026509","identifier":"Q9Y2P8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2P8/entry","name":"RCL1","description":"RNA 3'-terminal phosphate cyclase-like protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11096","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2115327","identifier":"O43818","identifierLink":"https://www.uniprot.org/uniprotkb/O43818/entry","name":"RRP9","description":"U3 small nucleolar RNA-interacting protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19865","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2513630","identifier":"Q14692","identifierLink":"https://www.uniprot.org/uniprotkb/Q14692/entry","name":"BMS1","description":"Ribosome biogenesis protein BMS1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12858","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2514288","identifier":"Q9H6R4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H6R4/entry","name":"NOL6","description":"Nucleolar protein 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR17972","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2837286","identifier":"Q8NDD1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NDD1/entry","name":"FSAF1","description":"40S small subunit processome assembly factor 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28366","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2876697","identifier":"Q9Y3A2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3A2/entry","name":"UTP11","description":"Probable U3 small nucleolar RNA-associated protein 11","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12838","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356062","identifier":"O75691","identifierLink":"https://www.uniprot.org/uniprotkb/O75691/entry","name":"UTP20","description":"Small subunit processome component 20 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR17695","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358318","identifier":"P22087","identifierLink":"https://www.uniprot.org/uniprotkb/P22087/entry","name":"FBL","description":"rRNA 2'-O-methyltransferase fibrillarin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10335","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372428","identifier":"Q9NY61","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NY61/entry","name":"AATF","description":"Protein AATF","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15565","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395469","identifier":"Q9Y2X3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2X3/entry","name":"NOP58","description":"Nucleolar protein 58","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395927","identifier":"Q9BVI4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BVI4/entry","name":"NOC4L","description":"Nucleolar complex protein 4 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12455","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-396034","identifier":"O00567","identifierLink":"https://www.uniprot.org/uniprotkb/O00567/entry","name":"NOP56","description":"Nucleolar protein 56","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-473284","identifier":"Q9BVJ6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BVJ6/entry","name":"UTP14A","description":"U3 small nucleolar RNA-associated protein 14 homolog A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14150","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5454840","identifier":"P78316","identifierLink":"https://www.uniprot.org/uniprotkb/P78316/entry","name":"NOP14","description":"Nucleolar protein 14","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23183","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5455734","identifier":"Q9Y324","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y324/entry","name":"FCF1","description":"rRNA-processing protein FCF1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5666736","identifier":"Q5QJE6","identifierLink":"https://www.uniprot.org/uniprotkb/Q5QJE6/entry","name":"DNTTIP2","description":"Deoxynucleotidyltransferase terminal-interacting protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21686","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712228","identifier":"P55769","identifierLink":"https://www.uniprot.org/uniprotkb/P55769/entry","name":"SNU13","description":"NHP2-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712787","identifier":"Q9NRX1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NRX1/entry","name":"PNO1","description":"RNA-binding protein PNO1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12826","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714067","identifier":"Q9NQZ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NQZ2/entry","name":"UTP3","description":"Something about silencing protein 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13237","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-718638","identifier":"Q92979","identifierLink":"https://www.uniprot.org/uniprotkb/Q92979/entry","name":"EMG1","description":"Ribosomal RNA small subunit methyltransferase NEP1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12636","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7223720","identifier":"Q9Y3A4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3A4/entry","name":"RRP7A","description":"Ribosomal RNA-processing protein 7 homolog A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 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SCF-FBXL4 acts to restrain basal mitophagy, the mitochondrial quality control mechanism that removes dysfunctional or excessive mitochondria by autophagy.","predictedComplex":false,"interactors":[{"ac":"EBI-2869903","identifier":"Q9UKA2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UKA2/entry","name":"FBXL4","description":"F-box/LRR-repeat protein 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13318","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2513","complexName":"RAG guanosine triphosphatase complex, RAGA-RAGD variant","organismName":"Homo sapiens; 9606","description":"GTPase which is tethered to lysosomal membranes through its association with the Ragulator complex (CPX-4741). High amino acid levels drive GTP binding and the resulting active complex binds to RPTOR (Q8N122) thus recruiting the mTORC1 complex (CPX-503) to the lysosomal surface. Amino acid deprivation induces the conversion of the complex to is inactive GDP-bound state. GATOR1 (CPX-6226) functions as a GTPase activating protein (GAP) complex and stimulates RRAGA GTPase activity to turn it into its inactive GDP-bound form.","predictedComplex":false,"interactors":[{"ac":"EBI-25820308","identifier":"CHEBI:37565","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:37565","name":"gtp(4-)","description":"GTP(4-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-37001918","identifier":"CHEBI:58189","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58189","name":"gdp(3-)","description":"GDP(3-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-752376","identifier":"Q7L523","identifierLink":"https://www.uniprot.org/uniprotkb/Q7L523/entry","name":"RRAGA","description":"Ras-related GTP-binding protein A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11259","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-992949","identifier":"Q9NQL2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NQL2/entry","name":"RRAGD","description":"Ras-related GTP-binding protein D","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11259","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2514","complexName":"RAG guanosine triphosphatase complex, RAGB-RAGC variant","organismName":"Homo sapiens; 9606","description":"GTPase which is tethered to lysosomal membranes through its association with the Ragulator complex (CPX-4741). High amino acid levels drive GTP binding and the resulting active complex binds to RPTOR (Q8N122) thus recruiting the mTORC1 complex (CPX-503) to the lysosomal surface. Amino acid deprivation induces the conversion of the complex to its inactive GDP-bound state. GATOR1 (CPX-6226) functions as a GTPase activating protein (GAP) complex and stimulates RRAGB GTPase activity to turn it into its inactive GDP-bound form.","predictedComplex":false,"interactors":[{"ac":"EBI-25820308","identifier":"CHEBI:37565","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:37565","name":"gtp(4-)","description":"GTP(4-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-37001918","identifier":"CHEBI:58189","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58189","name":"gdp(3-)","description":"GDP(3-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-752390","identifier":"Q9HB90","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HB90/entry","name":"RRAGC","description":"Ras-related GTP-binding protein C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11259","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-993049","identifier":"Q5VZM2","identifierLink":"https://www.uniprot.org/uniprotkb/Q5VZM2/entry","name":"RRAGB","description":"Ras-related GTP-binding protein B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11259","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2515","complexName":"MXI1-MAX transcriptional repressor complex","organismName":"Homo sapiens; 9606","description":"Transcriptional repressor which recognizes an E box hexanucleotide DNA consensus sequence 5'-CACGTG-3'  located within gene promoters. Antagonises transcriptional activation by MYC family members by competing for available MAX to form heterodimers, competiing with other heterodimers for E-box-binding sites, and also potentially directly repressing bound genes. MXD family members contain a short conserved amino acid sequence, which directly interacts with the SIN3A (CPX-3321.CPX-3323) or SIN3B (CPX-3322) histone deacetylase co-repressor complexes which mediate gene silencing.","predictedComplex":false,"interactors":[{"ac":"EBI-751711","identifier":"P61244","identifierLink":"https://www.uniprot.org/uniprotkb/P61244/entry","name":"MAX","description":"Protein max","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10328","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752241","identifier":"P50539","identifierLink":"https://www.uniprot.org/uniprotkb/P50539/entry","name":"MXI1","description":"Max-interacting protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11969","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2516","complexName":"SCF E3 ubiquitin ligase complex, FBXL6 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXL6 target proteins include the molecular chaperone HSP90AA1 (P07900). Ubiquitinaton at Lys-63 stabilizes this protein which in turn activates the cell cycle regulator MYC (P01106). May also play role in the quality control of neosynthesized mitochondrial proteins in coordination with the ribosome quality control complex (CPX-2656).","predictedComplex":false,"interactors":[{"ac":"EBI-2322696","identifier":"Q8N531","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N531/entry","name":"FBXL6","description":"F-box/LRR-repeat protein 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2517","complexName":"MXD3-MAX transcriptional repressor complex","organismName":"Homo sapiens; 9606","description":"Transcriptional repressor which recognizes an E box hexanucleotide DNA consensus sequence 5'-CACGTG-3'  located within gene promoters. Antagonises transcriptional activation by MYC family members by competing for available MAX to form heterodimers, competiing with other heterodimers for E-box-binding sites, and also potentially directly repressing bound genes. MXD family members contain a short conserved amino acid sequence, which directly interacts with the SIN3A (CPX-3321.CPX-3323) or SIN3B (CPX-3322) histone deacetylase co-repressor complexes which mediate gene silencing.","predictedComplex":false,"interactors":[{"ac":"EBI-741574","identifier":"Q9BW11","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BW11/entry","name":"MXD3","description":"Max dimerization protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11969","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-751711","identifier":"P61244","identifierLink":"https://www.uniprot.org/uniprotkb/P61244/entry","name":"MAX","description":"Protein max","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10328","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2518","complexName":"MNT-MAX transcriptional repressor complex","organismName":"Homo sapiens; 9606","description":"Transcriptional repressor which recognizes an E box hexanucleotide DNA consensus sequence 5'-CACGTG-3'  located within gene promoters. Antagonises transcriptional activation by MYC family members by competing for available MAX to form heterodimers, competiing with other heterodimers for E-box-binding sites, and also potentially directly repressing bound genes. MXD family members contain a short conserved amino acid sequence, which directly interacts with the SIN3A (CPX-3321.CPX-3323) or SIN3B (CPX-3322) histone deacetylase co-repressor complexes which mediate gene silencing.","predictedComplex":false,"interactors":[{"ac":"EBI-7959025","identifier":"Q99583","identifierLink":"https://www.uniprot.org/uniprotkb/Q99583/entry","name":"MNT","description":"Max-binding protein MNT","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11969","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2519","complexName":"MXD1-MLX transcriptional repressor complex","organismName":"Homo sapiens; 9606","description":"Transcriptional repressor which recognizes an E box hexanucleotide DNA consensus sequence 5'-CACGTG-3'  located within gene promoters. MXD family members contain a short conserved amino acid sequence, which directly interacts with the SIN3A (CPX-3321.CPX-3323) or SIN3B (CPX-3322) histone deacetylase co-repressor complexes which mediate gene silencing.","predictedComplex":false,"interactors":[{"ac":"EBI-741109","identifier":"Q9UH92","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UH92/entry","name":"MLX","description":"Max-like protein X","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15741","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8833637","identifier":"Q05195","identifierLink":"https://www.uniprot.org/uniprotkb/Q05195/entry","name":"MXD1","description":"Max dimerization protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11969","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2520","complexName":"MXD4-MLX transcriptional repressor complex","organismName":"Homo sapiens; 9606","description":"Transcriptional repressor which recognizes an E box hexanucleotide DNA consensus sequence 5'-CACGTG-3'  located within gene promoters. 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Involved in the regulation of the cell cycle, chromatin modification, activation and inhibition of transcription initiation, control of transcription elongation, RNA export, nuclear RNA surveillance, and DNA damage repair in the nucleus. The CNOT4 ubiquitin ligase only weakly associates with the complex but is required for optimal deadenylation activity by the full CCR4-NOT complex.","predictedComplex":false,"interactors":[{"ac":"EBI-1046635","identifier":"Q96LI5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96LI5/entry","name":"CNOT6L","description":"CCR4-NOT transcription complex subunit 6-like","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12121","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1054261","identifier":"Q9H9A5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H9A5/entry","name":"CNOT10","description":"CCR4-NOT transcription complex subunit 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12979","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1222758","identifier":"A5YKK6","identifierLink":"https://www.uniprot.org/uniprotkb/A5YKK6/entry","name":"CNOT1","description":"CCR4-NOT transcription complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13162","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2104458","identifier":"Q9C0C2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9C0C2/entry","name":"TNKS1BP1","description":"182 kDa tankyrase-1-binding protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22042","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2105113","identifier":"Q9UIV1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UIV1/entry","name":"CNOT7","description":"CCR4-NOT transcription complex subunit 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10797","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2129291","identifier":"O95628","identifierLink":"https://www.uniprot.org/uniprotkb/O95628/entry","name":"CNOT4","description":"CCR4-NOT transcription complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12603","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2562014","identifier":"Q9UKZ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UKZ1/entry","name":"CNOT11","description":"CCR4-NOT transcription complex subunit 11","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15975","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357079","identifier":"Q92600","identifierLink":"https://www.uniprot.org/uniprotkb/Q92600/entry","name":"CNOT9","description":"CCR4-NOT transcription complex subunit 9","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12262","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743033","identifier":"Q9NZN8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZN8/entry","name":"CNOT2","description":"CCR4-NOT transcription complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23326","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743073","identifier":"O75175","identifierLink":"https://www.uniprot.org/uniprotkb/O75175/entry","name":"CNOT3","description":"CCR4-NOT transcription complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23326","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9097897","identifier":"CHEBI:60240","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60240","name":"divalent metal cation","description":"divalent metal cation","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2523","complexName":"COPII vesicle coat complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Mediates formation of the membrane vesicles that export newly synthesised proteins from the endoplasmic reticulum. Upon exchange of GDP for GTP (catalysed by SEC12), SAR1 exposes an N-terminal amphipathic helix that inserts into the outer ER membrane leaflet, promoting curvature. SAR1 recruits SEC23/24 to the membrane to form the inner layer of the COPII coat. SEC24 binds transport cargo while SEC23 interacts with SAR1 and recruits the outer COPII components (SEC13/31) that form a cage around the vesicle by self-assembling into a polyhedron. SEC16 may also be required for proper COPII coat assembly but its role has not been clearly defined.","predictedComplex":false,"interactors":[{"ac":"EBI-16472","identifier":"P20606","identifierLink":"https://www.uniprot.org/uniprotkb/P20606/entry","name":"SAR1","description":"Small COPII coat GTPase SAR1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16529","identifier":"Q04491","identifierLink":"https://www.uniprot.org/uniprotkb/Q04491/entry","name":"SEC13","description":"Protein transport protein SEC13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11024","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16584","identifier":"P15303","identifierLink":"https://www.uniprot.org/uniprotkb/P15303/entry","name":"SEC23","description":"Protein transport protein SEC23","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11141","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16592","identifier":"P40482","identifierLink":"https://www.uniprot.org/uniprotkb/P40482/entry","name":"SEC24","description":"Protein transport protein SEC24","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13803","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20524","identifier":"P38968","identifierLink":"https://www.uniprot.org/uniprotkb/P38968/entry","name":"SEC31","description":"Protein transport protein SEC31","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13923","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-989053","identifier":"CHEBI:15996","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15996","name":"gtp","description":"guanosine triphosphate - GTP","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2524","complexName":"TLR2-TLR10 toll-like receptor complex","organismName":"Homo sapiens; 9606","description":"Type I membrane receptor that plays a crucial role in innate immunity by recognizing conserved patterns in diverse microbial molecules including lipoproteins, lipopeptides, lipopolysaccharide, flagellin, and nucleic acids","predictedComplex":false,"interactors":[{"ac":"EBI-16825459","identifier":"Q9BXR5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BXR5/entry","name":"TLR10","description":"Toll-like receptor 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24365","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-973722","identifier":"O60603","identifierLink":"https://www.uniprot.org/uniprotkb/O60603/entry","name":"TLR2","description":"Toll-like receptor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24365","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2525","complexName":"MLXIP-MLX transcription factor complex","organismName":"Homo sapiens; 9606","description":"Transcriptional activator which recognizes an E box hexanucleotide DNA consensus sequence 5'-CACGTG-3'  located within gene promoters. Regulates genes involved in glucose and glutamine metabolism. MondoA associates with the mitochondrial outer membrane, where it acts as a nutrient senor, binding glycolytic intermediates such as glucose 6-phosphate which trigger migration to the nucleus.","predictedComplex":false,"interactors":[{"ac":"EBI-2843709","identifier":"Q9HAP2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HAP2/entry","name":"MLXIP","description":"MLX-interacting protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15741","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-741109","identifier":"Q9UH92","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UH92/entry","name":"MLX","description":"Max-like protein X","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15741","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2526","complexName":"Replication fork protection complex","organismName":"Homo sapiens; 9606","description":"Required for chromosome segregation during meiosis and DNA damage repair. Acts at the intra-S-phase checkpoint pathway to stabilize stalled replication forks by maintaining the replisome at the arrested sites. Coordinates leading and lagging strand synthesis and moves with the replication fork, transfering cohesin from the front of the fork to the newly synthesized DNA. The complex is  involved in replication through difficult secondary structures such as G-quadruplexes by recruiting the DDX11 helicase (Q96FC9). It is recruited by PARP1 (P09874) to DNA damage to promote homologous recombination","predictedComplex":false,"interactors":[{"ac":"EBI-2212315","identifier":"Q9UNS1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UNS1/entry","name":"TIMELESS","description":"Protein timeless homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22940","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2515360","identifier":"Q9BVW5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BVW5/entry","name":"TIPIN","description":"TIMELESS-interacting protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2530","complexName":"MLXIPL-MLX transcription factor complex","organismName":"Homo sapiens; 9606","description":"Glucose-responsive transcriptional activator which recognizes an E box hexanucleotide DNA consensus sequence 5'-CACGTG-3'  located within gene promoters. Regulates transcription of genes encoding enzymes involved in de novo lipogenesis such as liver-type pyruvate kinase, acetyl-CoA carboxylase 1, and fatty acid synthase.","predictedComplex":false,"interactors":[{"ac":"EBI-3938757","identifier":"Q9NP71","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NP71/entry","name":"MLXIPL","description":"Carbohydrate-responsive element-binding protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15741","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-741109","identifier":"Q9UH92","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UH92/entry","name":"MLX","description":"Max-like protein X","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15741","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2531","complexName":"MKS transition zone complex","organismName":"Homo sapiens; 9606","description":"Part of  the transition zone, a barrier located at the base of cilia which separates the interior and exterior of cilia. The transition zone is characterized by Y-shaped structures that span from the axoneme to the ciliary membrane and comprises of the MKS and NPHP (CPX-2806) modules. The MKS1-B9D2-B9D1 sub-complex  functions as a diffusion barrier preventing exchange of transmembrane proteins between the cilia and plasma membranes","predictedComplex":false,"interactors":[{"ac":"EBI-10307654","identifier":"Q9H6L2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H6L2/entry","name":"TMEM231","description":"Transmembrane protein 231","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14605","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1049056","identifier":"Q8N157","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N157/entry","name":"AHI1","description":"Jouberin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44499","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11278332","identifier":"Q6NUS6","identifierLink":"https://www.uniprot.org/uniprotkb/Q6NUS6/entry","name":"TCTN3","description":"Tectonic-3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 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9606","xrefs":[{"identifier":"PTHR13531","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11349465","identifier":"Q96GX1","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GX1/entry","name":"TCTN2","description":"Tectonic-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14611","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11355646","identifier":"Q9P2K1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P2K1/entry","name":"CC2D2A","description":"Coiled-coil and C2 domain-containing protein 2A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20837","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12845616","identifier":"Q6UX40","identifierLink":"https://www.uniprot.org/uniprotkb/Q6UX40/entry","name":"TMEM107","description":"Transmembrane protein 107","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR34341","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2602465","identifier":"Q96Q45","identifierLink":"https://www.uniprot.org/uniprotkb/Q96Q45/entry","name":"TMEM237","description":"Transmembrane protein 237","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28388","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372535","identifier":"Q9UPM9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UPM9/entry","name":"B9D1","description":"B9 domain-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12968","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6958971","identifier":"Q9BPU9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BPU9/entry","name":"B9D2","description":"B9 domain-containing protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12968","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-719269","identifier":"Q9NXB0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NXB0/entry","name":"MKS1","description":"Tectonic-like complex member MKS1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12968","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-721260","identifier":"Q9P0N5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P0N5/entry","name":"TMEM216","description":"Transmembrane protein 216","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13531","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2532","complexName":"rpoe-rsea-rseb sigma-antisigma complex","organismName":"Escherichia coli (strain K12); 83333","description":"Regulates RpoE-mediated transcription activation by preventing the interaction between the primary sigma factor RpoE with DNA-directed RNA polymerase (RNAP).  rpoE-mediated envelope stress response is the major pathway to ensure homeostasis in the envelope compartment of the cell. In response to stress, outer membrane proteins accumulate in the periplasm and activate cleavage of rseA periplasmic domain by degS (P0AEE3), triggering a proteolytic cascade that frees rpoE to activate gene expression. rseB binding to RseA prevents activated degS from cleaving rseA.","predictedComplex":false,"interactors":[{"ac":"EBI-1117560","identifier":"P0AFX7","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFX7/entry","name":"rseA","description":"Anti-sigma-E factor RseA","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR38104","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1129580","identifier":"P0AGB6","identifierLink":"https://www.uniprot.org/uniprotkb/P0AGB6/entry","name":"rpoE","description":"ECF RNA polymerase sigma-E factor","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43133","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1135231","identifier":"P0AFX9","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFX9/entry","name":"rseB","description":"Sigma-E factor regulatory protein RseB","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR38782","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2533","complexName":"Kinetochore CCAN complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Interacts with duplex DNA and facilitates accurate chromosome segregation. Plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. It may be involved in incorporation of newly synthesized CENPA (P36012) into centromeres to form CENP-A nucleosomes (CPX-5705). Required for chromosome congression and efficient alignment of the chromosomes on a metaphase plate.","predictedComplex":false,"interactors":[{"ac":"EBI-10908","identifier":"P35201","identifierLink":"https://www.uniprot.org/uniprotkb/P35201/entry","name":"MIF2","description":"Inner kinetochore subunit MIF2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR16684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15968870","identifier":"Q3E829","identifierLink":"https://www.uniprot.org/uniprotkb/Q3E829/entry","name":"MHF2","description":"Inner kinetochore subunit MHF2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28680","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20972","identifier":"P38313","identifierLink":"https://www.uniprot.org/uniprotkb/P38313/entry","name":"AME1","description":"Inner kinetochore subunit AME1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 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559292","xrefs":[]},{"ac":"EBI-2881690","identifier":"Q3E835","identifierLink":"https://www.uniprot.org/uniprotkb/Q3E835/entry","name":"MHF1","description":"Inner kinetochore subunit MHF1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22980","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30457","identifier":"Q12748","identifierLink":"https://www.uniprot.org/uniprotkb/Q12748/entry","name":"CTF3","description":"Inner kinetochore subunit CTF3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-31487","identifier":"Q12262","identifierLink":"https://www.uniprot.org/uniprotkb/Q12262/entry","name":"MCM16","description":"Inner kinetochore subunit MCM16","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-32349","identifier":"Q06675","identifierLink":"https://www.uniprot.org/uniprotkb/Q06675/entry","name":"MCM21","description":"Inner kinetochore subunit MCM21","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-34256","identifier":"Q06162","identifierLink":"https://www.uniprot.org/uniprotkb/Q06162/entry","name":"NKP2","description":"Inner kinetochore subunit NKP2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28064","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-35840","identifier":"Q12493","identifierLink":"https://www.uniprot.org/uniprotkb/Q12493/entry","name":"NKP1","description":"Inner kinetochore subunit NKP1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-36999994","identifier":"Q2V2P8","identifierLink":"https://www.uniprot.org/uniprotkb/Q2V2P8/entry","name":"WIP1","description":"Inner kinetochore subunit WIP1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-4606","identifier":"P38907","identifierLink":"https://www.uniprot.org/uniprotkb/P38907/entry","name":"CHL4","description":"Inner kinetochore subunit CHL4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-5199","identifier":"Q02732","identifierLink":"https://www.uniprot.org/uniprotkb/Q02732/entry","name":"CTF19","description":"Inner kinetochore subunit CTF19","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-2535","complexName":"CCR4-NOT mRNA deadenylase complex, CNOT6L-CNOT8 variant","organismName":"Homo sapiens; 9606","description":"Major cellular mRNA deadenylase complex at least in part by  removing polyA tails that protect mRNA transcripts from degradation. Involved in the regulation of the cell cycle, chromatin modification, activation and inhibition of transcription initiation, control of transcription elongation, RNA export, nuclear RNA surveillance, and DNA damage repair in the nucleus. The CNOT4 ubiquitin ligase only weakly associates with the complex but is required for optimal deadenylation activity by the full CCR4-NOT complex.","predictedComplex":false,"interactors":[{"ac":"EBI-1046635","identifier":"Q96LI5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96LI5/entry","name":"CNOT6L","description":"CCR4-NOT transcription complex subunit 6-like","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12121","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1054261","identifier":"Q9H9A5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H9A5/entry","name":"CNOT10","description":"CCR4-NOT transcription complex subunit 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12979","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1222758","identifier":"A5YKK6","identifierLink":"https://www.uniprot.org/uniprotkb/A5YKK6/entry","name":"CNOT1","description":"CCR4-NOT transcription complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13162","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2104458","identifier":"Q9C0C2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9C0C2/entry","name":"TNKS1BP1","description":"182 kDa tankyrase-1-binding protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22042","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2129291","identifier":"O95628","identifierLink":"https://www.uniprot.org/uniprotkb/O95628/entry","name":"CNOT4","description":"CCR4-NOT transcription complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12603","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2562014","identifier":"Q9UKZ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UKZ1/entry","name":"CNOT11","description":"CCR4-NOT transcription complex subunit 11","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15975","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357079","identifier":"Q92600","identifierLink":"https://www.uniprot.org/uniprotkb/Q92600/entry","name":"CNOT9","description":"CCR4-NOT transcription complex subunit 9","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12262","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742299","identifier":"Q9UFF9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UFF9/entry","name":"CNOT8","description":"CCR4-NOT transcription complex subunit 8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10797","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743033","identifier":"Q9NZN8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZN8/entry","name":"CNOT2","description":"CCR4-NOT transcription complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23326","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743073","identifier":"O75175","identifierLink":"https://www.uniprot.org/uniprotkb/O75175/entry","name":"CNOT3","description":"CCR4-NOT transcription complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23326","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9097897","identifier":"CHEBI:60240","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60240","name":"divalent metal cation","description":"divalent metal cation","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2536","complexName":"CEP290-NPHP5 transition zone complex","organismName":"Homo sapiens; 9606","description":"Part of  the transition zone, a barrier located at the base of cilia which separates the interior and exterior of cilia. The transition zone is characterized by Y-shaped structures that span from the axoneme to the ciliary membrane and comprises of the MKS (CPX-2531) and NPHP (CPX-2806) modules. CEP290 binding blocks the calmodulin binding of NPHP5 and promotes the recruitment of NPHP5 to the transition zone, enabling ciliary gating, the selective import and export of molecules.","predictedComplex":false,"interactors":[{"ac":"EBI-1811944","identifier":"O15078","identifierLink":"https://www.uniprot.org/uniprotkb/O15078/entry","name":"CEP290","description":"Centrosomal protein of 290 kDa","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18879","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2805823","identifier":"Q15051","identifierLink":"https://www.uniprot.org/uniprotkb/Q15051/entry","name":"IQCB1","description":"IQ calmodulin-binding motif-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2537","complexName":"LINC complex, SUN1-KASH5 variant","organismName":"Homo sapiens; 9606","description":"Forms immediately below the outer nuclear membrane and traverses the nuclear envelope to mechanically couple cytoskeletal and nuclear components across the nuclear envelope, allowing the transmission of force. KASH5 binds to the dynein motor and through this with the microtubule network.","predictedComplex":false,"interactors":[{"ac":"EBI-2796904","identifier":"O94901","identifierLink":"https://www.uniprot.org/uniprotkb/O94901/entry","name":"SUN1","description":"SUN domain-containing protein 1","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12911","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749265","identifier":"Q8N6L0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N6L0/entry","name":"KASH5","description":"Protein KASH5","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47300","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2538","complexName":"SCF E3 ubiquitin ligase complex, KDM2A variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-765758","identifier":"Q9Y2K7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2K7/entry","name":"KDM2A","description":"Lysine-specific demethylase 2A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23123","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2539","complexName":"U2 small nuclear ribonucleoprotein complex","organismName":"Homo sapiens; 9606","description":"Non-coding RNA containing complex that is involved in mRNA splicing. U2 snRNP binds to the intron branch site of the commitment complex to form the pre-spliceosome in an ATP dependent step. Stably interacts with the pre-RNA intron branch site (BS), forming the spliceosomal A complex in which U2 snRNA base pairs with the BS, causing the branch site adenosine to bulge out from the U2/BS helix. The U2-BS interaction is reinforced by the U2AF65/35 heterodimer (CPX-1921), which binds the intron pyrimidine-rich region, and by the U2-associated, heteromeric protein complexes  SF3A (CPX-2565) and SF3B (CPX-2227)  that contact the intron 6 to 26 nucleotides upstream of the BS-A (anchoring site)  Prior to the first catalytic reaction,  SF3A and SF3B  dissociate from the spliceosome, presumably making the branch site accessible to lariat formation. The spliceosome is a highly dynamic structure, assembled by sequential binding and release of the small nuclear RNAs and protein factors which removes intronic sequence from pre-mRNA. During formation of the activated spliceosome, U2 will replace the dissociating U4 to form base pairs with U6.","predictedComplex":false,"interactors":[{"ac":"EBI-1046261","identifier":"Q9Y3B4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3B4/entry","name":"SF3B6","description":"Splicing factor 3B subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-1051880","identifier":"Q12874","identifierLink":"https://www.uniprot.org/uniprotkb/Q12874/entry","name":"SF3A3","description":"Splicing factor 3A subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12786","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1053651","identifier":"P08579","identifierLink":"https://www.uniprot.org/uniprotkb/P08579/entry","name":"SNRPB2","description":"U2 small nuclear ribonucleoprotein B''","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10501","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1054743","identifier":"Q15459","identifierLink":"https://www.uniprot.org/uniprotkb/Q15459/entry","name":"SF3A1","description":"Splicing factor 3A subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15316","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2462271","identifier":"Q15428","identifierLink":"https://www.uniprot.org/uniprotkb/Q15428/entry","name":"SF3A2","description":"Splicing factor 3A subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23205","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2555356","identifier":"Q7L014","identifierLink":"https://www.uniprot.org/uniprotkb/Q7L014/entry","name":"DDX46","description":"Probable ATP-dependent RNA helicase DDX46","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2555365","identifier":"Q7RTV0","identifierLink":"https://www.uniprot.org/uniprotkb/Q7RTV0/entry","name":"PHF5A","description":"PHD finger-like domain-containing protein 5A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13120","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2555428","identifier":"Q9BWJ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BWJ5/entry","name":"SF3B5","description":"Splicing factor 3B subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20978","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27124798","identifier":"URS00006A1489_9606","identifierLink":"http://rnacentral.org/rna/URS00006A1489_9606","name":"u2_human_snrna","description":"Human U2  spliceosomal RNA","stochiometry":null,"interactorType":"small nuclear rna","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-297993","identifier":"P62316","identifierLink":"https://www.uniprot.org/uniprotkb/P62316/entry","name":"SNRPD2","description":"Small nuclear ribonucleoprotein Sm D2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12777","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-346977","identifier":"Q15393","identifierLink":"https://www.uniprot.org/uniprotkb/Q15393/entry","name":"SF3B3","description":"Splicing factor 3B subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348082","identifier":"P62304","identifierLink":"https://www.uniprot.org/uniprotkb/P62304/entry","name":"SNRPE","description":"Small nuclear ribonucleoprotein E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11193","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348469","identifier":"Q15427","identifierLink":"https://www.uniprot.org/uniprotkb/Q15427/entry","name":"SF3B4","description":"Splicing factor 3B subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48030","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356900","identifier":"P62306","identifierLink":"https://www.uniprot.org/uniprotkb/P62306/entry","name":"SNRPF","description":"Small nuclear ribonucleoprotein F","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372177","identifier":"P62314","identifierLink":"https://www.uniprot.org/uniprotkb/P62314/entry","name":"SNRPD1","description":"Small nuclear ribonucleoprotein Sm D1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372458","identifier":"P14678","identifierLink":"https://www.uniprot.org/uniprotkb/P14678/entry","name":"SNRPB","description":"Small nuclear ribonucleoprotein-associated proteins B and B'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372789","identifier":"P62318","identifierLink":"https://www.uniprot.org/uniprotkb/P62318/entry","name":"SNRPD3","description":"Small nuclear ribonucleoprotein Sm D3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61277930","identifier":"CPX-26447","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-26447","name":"Retention and splicing complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-624585","identifier":"P62308","identifierLink":"https://www.uniprot.org/uniprotkb/P62308/entry","name":"SNRPG","description":"Small nuclear ribonucleoprotein G","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-720468","identifier":"O43719","identifierLink":"https://www.uniprot.org/uniprotkb/O43719/entry","name":"HTATSF1","description":"17S U2 SnRNP complex component HTATSF1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15608","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749111","identifier":"Q13435","identifierLink":"https://www.uniprot.org/uniprotkb/Q13435/entry","name":"SF3B2","description":"Splicing factor 3B subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12785","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-876439","identifier":"P09661","identifierLink":"https://www.uniprot.org/uniprotkb/P09661/entry","name":"SNRPA1","description":"U2 small nuclear ribonucleoprotein A'","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10552","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-876542","identifier":"O75533","identifierLink":"https://www.uniprot.org/uniprotkb/O75533/entry","name":"SF3B1","description":"Splicing factor 3B subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2540","complexName":"FERRY RAB5 effector complex","organismName":"Homo sapiens; 9606","description":"Recruited to the early endosome by binding of RAB5, the complex is involved in the localization and the distribution of specific mRNAs such as transcripts encoding mitochondrial proteins (e.g., mdh2 mRNA), most likely by mediating their endosomal transport. The complex recruits mRNAs and ribosomes to early endosomes through direct mRNA-interaction.","predictedComplex":false,"interactors":[{"ac":"EBI-11023114","identifier":"O95825","identifierLink":"https://www.uniprot.org/uniprotkb/O95825/entry","name":"CRYZL1","description":"Quinone oxidoreductase-like protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44461","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11090973","identifier":"Q9NQ89","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NQ89/entry","name":"FERRY3","description":"Ferry endosomal RAB5 effector complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16525","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11142401","identifier":"Q8TEA7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TEA7/entry","name":"TBCK","description":"TBC domain-containing protein kinase-like protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5235703","identifier":"Q6ZMI0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6ZMI0/entry","name":"PPP1R21","description":"Protein phosphatase 1 regulatory subunit 21","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21448","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-722742","identifier":"Q8NB37","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NB37/entry","name":"GATD1","description":"Glutamine amidotransferase-like class 1 domain-containing protein 1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48094","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2541","complexName":"MMS2-UBC13 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Ubiquitin ligase complex. Transfers the thioester-bound donor ubiquitin from Ubc13 onto the Mms2 catalytically inactive E2 variant. Functions in concert with RING E3 ubiquitin ligase RAD5 to catalyze the Lys-63-linked polyubiquitination of monoubiquitinated replication processivity factor PCNA (CPX-544). MMS2 positions the acceptor ubiquitin so that only Lys-63 approaches the active site cysteine of UBC13. This modification activates the recombination-like DNA damage-avoidance mechanism,  in which the replicating polymerase avoids synthesis opposite damaged DNA by transient switching of the template, from the damaged DNA strand to the intact newly synthesized strand of the sister chromatid.","predictedComplex":false,"interactors":[{"ac":"EBI-11035","identifier":"P53152","identifierLink":"https://www.uniprot.org/uniprotkb/P53152/entry","name":"MMS2","description":"Ubiquitin-conjugating enzyme variant MMS2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19777","identifier":"P52490","identifierLink":"https://www.uniprot.org/uniprotkb/P52490/entry","name":"UBC13","description":"Ubiquitin-conjugating enzyme E2 13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2542","complexName":"RAG guanosine triphosphatase complex, RAGA-RAGC variant","organismName":"Homo sapiens; 9606","description":"GTPase which is tethered to lysosomal membranes through its association with the Ragulator complex (CPX-4741). High amino acid levels drive GTP binding and the resulting active complex binds to RPTOR (Q8N122) thus recruiting the mTORC1 complex (CPX-503) to the lysosomal surface. Amino acid deprivation induces the conversion of the complex to its inactive GDP-bound state. GATOR1 (CPX-6226) functions as a GTPase activating protein (GAP) complex and stimulates RRAGA GTPase activity to turn it into its inactive GDP-bound form.","predictedComplex":false,"interactors":[{"ac":"EBI-25820308","identifier":"CHEBI:37565","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:37565","name":"gtp(4-)","description":"GTP(4-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-37001918","identifier":"CHEBI:58189","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58189","name":"gdp(3-)","description":"GDP(3-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-752376","identifier":"Q7L523","identifierLink":"https://www.uniprot.org/uniprotkb/Q7L523/entry","name":"RRAGA","description":"Ras-related GTP-binding protein A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11259","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752390","identifier":"Q9HB90","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HB90/entry","name":"RRAGC","description":"Ras-related GTP-binding protein C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11259","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2543","complexName":"Glutathione-regulated potassium-efflux system KefC-KefF complex","organismName":"Escherichia coli (strain K12); 83333","description":"Potassium efflux pore which protects the bacteria from the toxic effects of electrophilic compounds which react with nucleophiles found in the bases of DNA and the side chains of proteins, especially cysteine. Potassium efflux via KefC is accompanied by H+ and Na+ influx and hence causes acidification of the cytoplasm. KefC is activated by glutathione adducts and inactivated by glutathione which bind to the cytosolic regulatory K+ transport and nucleotide binding domain of KefC.","predictedComplex":false,"interactors":[{"ac":"EBI-547193","identifier":"P03819","identifierLink":"https://www.uniprot.org/uniprotkb/P03819/entry","name":"kefC","description":"Glutathione-regulated potassium-efflux system protein KefC","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR46157","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-562116","identifier":"P0A754","identifierLink":"https://www.uniprot.org/uniprotkb/P0A754/entry","name":"kefF","description":"Glutathione-regulated potassium-efflux system ancillary protein KefF","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR47307","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3090","complexName":"Glutathione-regulated potassium-efflux system KefB-KefG complex","organismName":"Escherichia coli (strain K12); 83333","description":"Potassium efflux pore which protects the bacteria from the toxic effects of electrophilic compounds which react with nucleophiles found in the bases of DNA and the side chains of proteins, especially cysteine. Potassium efflux via KefB is accompanied by H+ and Na+ influx and hence causes acidification of the cytoplasm. KefB is activated by glutathione adducts and inactivated by  glutathione which bind to the cytosolic regulatory K+ transport and nucleotide binding domain of KefB.","predictedComplex":false,"interactors":[{"ac":"EBI-1132491","identifier":"P0A756","identifierLink":"https://www.uniprot.org/uniprotkb/P0A756/entry","name":"kefG","description":"Glutathione-regulated potassium-efflux system ancillary protein KefG","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR47307","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9539623","identifier":"P45522","identifierLink":"https://www.uniprot.org/uniprotkb/P45522/entry","name":"kefB","description":"Glutathione-regulated potassium-efflux system protein KefB","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR46157","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2544","complexName":"TGF-beta-3-TGFR complex","organismName":"Homo sapiens; 9606","description":"Cytokine-receptor complex that plays an important role in embryogenesis, tissue development, cell proliferation, differentiation and maturation, immune regulation and carcinogenesis. Binding of TGFB3 (CPX-606) to its receptor subunits results in the phosphorylation of TGFBR1 on Thr-185 and Thr-186 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 (Q15796) which dissociates from the receptor and activates the canonical SMAD-dependent TGF-beta signaling cascade.","predictedComplex":false,"interactors":[{"ac":"EBI-1027557","identifier":"P36897","identifierLink":"https://www.uniprot.org/uniprotkb/P36897/entry","name":"TGFBR1","description":"TGF-beta receptor type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12502448","identifier":"P10600-PRO_0000033797","identifierLink":"https://www.uniprot.org/uniprotkb/P10600-PRO_0000033797/entry","name":"TGFB3","description":"Transforming growth factor beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-296151","identifier":"P37173","identifierLink":"https://www.uniprot.org/uniprotkb/P37173/entry","name":"TGFBR2","description":"TGF-beta receptor type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2545","complexName":"LY96-TLR4 toll-like receptor complex","organismName":"Homo sapiens; 9606","description":"Type I membrane receptor that plays a crucial role in innate immunity by recognizing conserved patterns in diverse microbial molecules including lipoproteins, lipopeptides, lipopolysaccharide, flagellin, and nucleic acids. In the early step of bacterial infection, serum lipopolysaccharide (LPS, CHEBI:16412) binds to the N-terminal of LBP (P18428), LPS is then presented to CD14 (P08571) and transferred to LY96 or the LY96-TLR4 toll-like receptor complex. This induces the dimerization of TLR4 TIR domains, initiating CD14-dependent TLR4 endocytosis, and TICAM1/TRIF(Q8IUC6)-dependent signal transduction to promote inflammation caused by LPS.","predictedComplex":false,"interactors":[{"ac":"EBI-1539247","identifier":"Q9Y6Y9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6Y9/entry","name":"LY96","description":"Lymphocyte antigen 96","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15218","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-528701","identifier":"O00206","identifierLink":"https://www.uniprot.org/uniprotkb/O00206/entry","name":"TLR4","description":"Toll-like receptor 4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24365","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2548","complexName":"MYCL-MAX transcriptional activator complex","organismName":"Homo sapiens; 9606","description":"Proto-oncogenic transcriptional activator recognizing E box hexanucleotides containing the DNA consensus sequence CACGTG within gene promoters. The MYCL-MAX heterodimer upregulates gene transcription by interaction with TATA binding protein (TBP, P20226), which in turn upregulates RNA polymerase transcription of the gene. Role in cellular proliferation and division.","predictedComplex":false,"interactors":[{"ac":"EBI-751711","identifier":"P61244","identifierLink":"https://www.uniprot.org/uniprotkb/P61244/entry","name":"MAX","description":"Protein max","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10328","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8833648","identifier":"P12524","identifierLink":"https://www.uniprot.org/uniprotkb/P12524/entry","name":"MYCL","description":"Protein L-Myc","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45851","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2549","complexName":"NXF5-NXT2 mRNA nuclear export factor complex","organismName":"Homo sapiens; 9606","description":"Mediates the export of bulk mRNA through direct interactions with both the mRNA cargo and nuclear pore proteins that contain characteristic phenylalanine-glycine repeating sequence motifs (FG-nucleoporins or FG-nups). Also facilitates the export of unspliced retroviral genomic RNA from simple type-D retro-viruses such as SRV-1 that contains a constitutive transport element (CTE), a cis-acting 2-fold symmetric RNA stem–loop motif.","predictedComplex":false,"interactors":[{"ac":"EBI-20868263","identifier":"Q9H1B4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H1B4/entry","name":"NXF5","description":"Nuclear RNA export factor 5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10662","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752122","identifier":"Q9NPJ8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPJ8/entry","name":"NXT2","description":"NTF2-related export protein 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12612","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2550","complexName":"Non-canonical polycomb repressive complex 1.6, RING1-YAF2 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin-protein ligase that acts as a transcriptional repressor by mediating the monoubiquitination of Lys-119 of histone H2A, compacting chromatin, stalling RNA polymerase II and transcriptionally silencing genes critical for development.","predictedComplex":false,"interactors":[{"ac":"EBI-1048026","identifier":"Q9BYE7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BYE7/entry","name":"PCGF6","description":"Polycomb group RING finger protein 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45893","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2842031","identifier":"Q8IY57","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IY57/entry","name":"YAF2","description":"YY1-associated factor 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12920","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-739909","identifier":"Q969R5","identifierLink":"https://www.uniprot.org/uniprotkb/Q969R5/entry","name":"L3MBTL2","description":"Lethal(3)malignant brain tumor-like protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12247","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752313","identifier":"Q06587","identifierLink":"https://www.uniprot.org/uniprotkb/Q06587/entry","name":"RING1","description":"E3 ubiquitin-protein ligase RING1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9019630","identifier":"CPX-2551","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-2551","name":"MGA-MAX transcriptional repressor complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-9019678","identifier":"CPX-2552","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-2552","name":"E2F6-DP1 transcriptional repressor complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-2551","complexName":"MGA-MAX transcriptional repressor complex","organismName":"Homo sapiens; 9606","description":"Transcriptional repressor which recognizes an E box hexanucleotide DNA consensus sequence 5'-CACGTG-3'  located within gene promoters. Antagonises transcriptional activation by MYC family members by competing for available MAX to form heterodimers, competiing with other heterodimers for E-box-binding sites, and also potentially directly repressing bound genes.","predictedComplex":false,"interactors":[{"ac":"EBI-2815196","identifier":"Q8IWI9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IWI9/entry","name":"MGA","description":"MAX gene-associated protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11267","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-751711","identifier":"P61244","identifierLink":"https://www.uniprot.org/uniprotkb/P61244/entry","name":"MAX","description":"Protein max","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10328","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2552","complexName":"E2F6-DP1 transcriptional repressor complex","organismName":"Homo sapiens; 9606","description":"Transcriptional repressor complex which binds DNA with a preference for the 5'-TTTCCCGC-3' E2F recognition site. E2F6 lacks the transcriptional activation and Retinoblastoma family pocket protein binding domains present in related E2F family members. During S-phase, the complex interacts with E2F target genes that are activated at G1/S, thus restricting their expression and promoting progression through the cell cycle","predictedComplex":false,"interactors":[{"ac":"EBI-749694","identifier":"O75461","identifierLink":"https://www.uniprot.org/uniprotkb/O75461/entry","name":"E2F6","description":"Transcription factor E2F6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12081","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749713","identifier":"Q14186","identifierLink":"https://www.uniprot.org/uniprotkb/Q14186/entry","name":"TFDP1","description":"Transcription factor Dp-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12548","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2553","complexName":"SCF E3 ubiquitin ligase complex, FBXL18 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. 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Activation of the canonical Wnt signaling pathway leads to beta-catenin/arm accumulation in the nucleus, incorporation into the enhanceosome and the stimulation of transcription. The Wnt response of this complex is conferred by Pygo, which facilitates loading of arm via an adaptor, lgs, thereby promoting transcriptional activation.  In the absence of arm, Wnt-responsive genes are silenced by the repressor gro (P16371) binding to the enhanceosome.","predictedComplex":false,"interactors":[{"ac":"EBI-152653","identifier":"Q9V9W8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V9W8/entry","name":"pygo","description":"Protein pygopus","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23194","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-216128","identifier":"P18824","identifierLink":"https://www.uniprot.org/uniprotkb/P18824/entry","name":"arm","description":"Armadillo segment polarity protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45976","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3406303","identifier":"Q8IMA8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IMA8/entry","name":"pan","description":"Protein pangolin, isoform J","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10373","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34618216","identifier":"Q7KVG9","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KVG9/entry","name":"Chi","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10378","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34618260","identifier":"A0A0B4KGW6","identifierLink":"https://www.uniprot.org/uniprotkb/A0A0B4KGW6/entry","name":"Ssdp","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12610","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-85519","identifier":"Q961D9","identifierLink":"https://www.uniprot.org/uniprotkb/Q961D9/entry","name":"lgs","description":"Protein BCL9 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23194","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2564","complexName":"Nucleosome, variant H3.1t-H2A.2-H2B.1","organismName":"Homo sapiens; 9606","description":"Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability.","predictedComplex":false,"interactors":[{"ac":"EBI-302023","identifier":"P62805","identifierLink":"https://www.uniprot.org/uniprotkb/P62805/entry","name":"H4C16","description":"Histone H4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10484","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358900","identifier":"Q16695","identifierLink":"https://www.uniprot.org/uniprotkb/Q16695/entry","name":"H3-4","description":"Histone H3.1t","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11426","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358971","identifier":"P04908","identifierLink":"https://www.uniprot.org/uniprotkb/P04908/entry","name":"H2AC4","description":"Histone H2A type 1-B/E","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23430","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6150252","identifier":"P06899","identifierLink":"https://www.uniprot.org/uniprotkb/P06899/entry","name":"H2BC11","description":"Histone H2B type 1-J","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23428","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9636457","identifier":"CHEBI:4705","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:4705","name":"double-stranded dna","description":"double-stranded DNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2565","complexName":"SF3A complex","organismName":"Homo sapiens; 9606","description":"Role in in pre-mRNA splicing. 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EZH1-containing PRC2 displays a high binding affinity towards nucleosomes and exhibits chromatin compaction activity.","predictedComplex":false,"interactors":[{"ac":"EBI-1264675","identifier":"Q15022","identifierLink":"https://www.uniprot.org/uniprotkb/Q15022/entry","name":"SUZ12","description":"Polycomb protein SUZ12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22597","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-530034","identifier":"O43189","identifierLink":"https://www.uniprot.org/uniprotkb/O43189/entry","name":"PHF1","description":"PHD finger protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-620823","identifier":"Q09028","identifierLink":"https://www.uniprot.org/uniprotkb/Q09028/entry","name":"RBBP4","description":"Histone-binding protein RBBP4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-746045","identifier":"Q96JN0","identifierLink":"https://www.uniprot.org/uniprotkb/Q96JN0/entry","name":"LCOR","description":"Ligand-dependent corepressor","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21545","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8830732","identifier":"Q92800","identifierLink":"https://www.uniprot.org/uniprotkb/Q92800/entry","name":"EZH1","description":"Histone-lysine N-methyltransferase EZH1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45747","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-923794","identifier":"O75530","identifierLink":"https://www.uniprot.org/uniprotkb/O75530/entry","name":"EED","description":"Polycomb protein EED","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10253","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2570","complexName":"Polycomb repressive complex 2.1, EZH1-RBBP7-PCL3-PALI1 variant","organismName":"Homo sapiens; 9606","description":"Histone-lysine N-methyltransferase which trimethylates Lys-10  (H3K9me3)  and Lys-28 on histone H3 (H3K27me3)  leading to transcriptional silencing of genes critical for development and stem cell differentiation. Also mediates mono and dimethylation of H3K27. PRC2 is preferably targeted to CpG islands in cells. EZH1-containing PRC2 displays a high binding affinity towards nucleosomes and exhibits chromatin compaction activity.","predictedComplex":false,"interactors":[{"ac":"EBI-1264675","identifier":"Q15022","identifierLink":"https://www.uniprot.org/uniprotkb/Q15022/entry","name":"SUZ12","description":"Polycomb protein SUZ12","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22597","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2339674","identifier":"Q5T6S3","identifierLink":"https://www.uniprot.org/uniprotkb/Q5T6S3/entry","name":"PHF19","description":"PHD finger protein 19","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352227","identifier":"Q16576","identifierLink":"https://www.uniprot.org/uniprotkb/Q16576/entry","name":"RBBP7","description":"Histone-binding protein RBBP7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-746045","identifier":"Q96JN0","identifierLink":"https://www.uniprot.org/uniprotkb/Q96JN0/entry","name":"LCOR","description":"Ligand-dependent corepressor","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21545","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8830732","identifier":"Q92800","identifierLink":"https://www.uniprot.org/uniprotkb/Q92800/entry","name":"EZH1","description":"Histone-lysine N-methyltransferase EZH1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45747","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-923794","identifier":"O75530","identifierLink":"https://www.uniprot.org/uniprotkb/O75530/entry","name":"EED","description":"Polycomb protein EED","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10253","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2244","complexName":"Translation initiation factor complex","organismName":"Escherichia coli (strain K12); 83333","description":"Required for initiation of protein synthesis, when the ribosome recruits an mRNA for translation and establishes the reading frame by binding initiator tRNA to the start codon in the P site of the small (30S) ribosomal subunit (CPX-3802). Assembles on the 30S subunit to form a transient 30S preinitiation complex (PIC). IF3 and IF2 are the first factors to arrive, forming an unstable 30S–IF2–IF3 complex. Subsequently, IF1 joins and locks the factors in a kinetically stable 30S PIC to which fMet-tRNAfMet is recruited. The complex dissociates on binding of the 50S ribosomal subunit.","predictedComplex":false,"interactors":[{"ac":"EBI-1120746","identifier":"P69222","identifierLink":"https://www.uniprot.org/uniprotkb/P69222/entry","name":"infA","description":"Translation initiation factor IF-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33370","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-542128","identifier":"P0A705","identifierLink":"https://www.uniprot.org/uniprotkb/P0A705/entry","name":"infB","description":"Translation initiation factor IF-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43381","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-546262","identifier":"P0A707","identifierLink":"https://www.uniprot.org/uniprotkb/P0A707/entry","name":"infC","description":"Translation initiation factor IF-3","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10938","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2245","complexName":"Trithorax acetylation complex 1","organismName":"Drosophila melanogaster; 7227","description":"Histone H3 Lys-4 methyltransferase and histone acetyltransferase complex which  activates transcription downstream of transcriptional initiation, potentially by promoting the elongation of noncoding RNAs that are responsible for transcriptional regulation of target genes. Maintains expression of homeotic genes throughout embryogenesis","predictedComplex":false,"interactors":[{"ac":"EBI-3404190","identifier":"Q9W321","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W321/entry","name":"nej","description":"histone acetyltransferase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-3413873","identifier":"Q9VGH9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VGH9/entry","name":"Sbf","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10807","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-591327","identifier":"P20659","identifierLink":"https://www.uniprot.org/uniprotkb/P20659/entry","name":"trx","description":"Histone-lysine N-methyltransferase trithorax","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45838","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2246","complexName":"KEOPS tRNA N6-adenosine threonylcarbamoyltransferase complex","organismName":"Drosophila melanogaster; 7227","description":"Catalyses the transfer of the threonylcarbamoyl-moiety of threonylcarbamoyladenylate (TCA) onto A37 of substrate tRNA in the cytoplasm. The N6-threonylcarbamoyladenosine (t6A) modification is present at position 37 of tRNAs that recognize ANN-codons, with N being any nucleotide, enhancing the codon-anti-codon interaction and is required for recognition of the AUG start codon. The modification is thus important for maintaining translational fidelity and also appears to play a role in transcription and telomere homeostasis. The unstable TCA intermediate is synthesised from ATP, threonine and bicarbonate by the Tcs1 (Q8SYJ9) enzyme. Appears to play a role in  larval size and transformation to pupa.","predictedComplex":false,"interactors":[{"ac":"EBI-15107177","identifier":"E1JIY8","identifierLink":"https://www.uniprot.org/uniprotkb/E1JIY8/entry","name":"Tcs6","description":"L antigen family member 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR31283","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-165278","identifier":"Q9VRJ6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VRJ6/entry","name":"Tcs5","description":"non-specific serine/threonine protein kinase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12209","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9097897","identifier":"CHEBI:60240","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60240","name":"divalent metal cation","description":"divalent metal cation","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-98375","identifier":"Q9VV41","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VV41/entry","name":"Tcs3","description":"Probable tRNA N6-adenosine threonylcarbamoyltransferase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11735","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2248","complexName":"General transcription factor complex TFIIA, TfIIA-S variant","organismName":"Drosophila melanogaster; 7227","description":"Transcription factor complex that regulates transcription initiation from RNA polymerase II promoters. Binding to the transcription factor complex TFIID-TBP enhances assembly of the transcriptional preinitiation complex PIC and its binding to the DNA at the TATA-box by displacing transcription inhibitors. Does not appear to be required for basal transcription but it stabilizes the TBP-DNA complex and stimulates constitutive transcription and activated transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-123680","identifier":"P52656","identifierLink":"https://www.uniprot.org/uniprotkb/P52656/entry","name":"TfIIA-S","description":"Transcription initiation factor IIA subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-132413","identifier":"P52654","identifierLink":"https://www.uniprot.org/uniprotkb/P52654/entry","name":"TfIIA-L","description":"Transcription initiation factor IIA subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12694","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2249","complexName":"Protein geranylgeranyltransferase type II complex","organismName":"Rattus norvegicus; 10116","description":"Catalyzes the transfer of a 20-hydrocarbon geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to a Rab protein having the C-terminal sequence -XXCC, -XCXC and -CCXX , where both cysteines may become modified. Requires both Zn2+ and Mg2+ for maximal activity. Associates with an accessory protein Rep (Rab escort protein).","predictedComplex":false,"interactors":[{"ac":"EBI-9010419","identifier":"Q08603","identifierLink":"https://www.uniprot.org/uniprotkb/Q08603/entry","name":"Rabggtb","description":"Geranylgeranyl transferase type-2 subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11774","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9010423","identifier":"Q08602","identifierLink":"https://www.uniprot.org/uniprotkb/Q08602/entry","name":"Rabggta","description":"Geranylgeranyl transferase type-2 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2250","complexName":"VHL-Elongin C-Elongin B E3 ubiquitin ligase complex","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase complex which targets the hypoxia-inducible factor-alpha (HIF-alpha) family of transcription factors, transcriptional regulators of the adaptive response to hypoxia, for ubiquitination and proteasomal degradation..","predictedComplex":false,"interactors":[{"ac":"EBI-301231","identifier":"Q15369","identifierLink":"https://www.uniprot.org/uniprotkb/Q15369/entry","name":"ELOC","description":"Elongin-C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301238","identifier":"Q15370","identifierLink":"https://www.uniprot.org/uniprotkb/Q15370/entry","name":"ELOB","description":"Elongin-B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13248","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301246","identifier":"P40337","identifierLink":"https://www.uniprot.org/uniprotkb/P40337/entry","name":"VHL","description":"von Hippel-Lindau disease tumor suppressor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15160","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456179","identifier":"Q13617","identifierLink":"https://www.uniprot.org/uniprotkb/Q13617/entry","name":"CUL2","description":"Cullin-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2919","complexName":"Protein geranylgeranyltransferase type II complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the transfer of a 20-hydrocarbon geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to a Rab protein having the C-terminal sequence -XXCC, -XCXC and -CCXX , where both cysteines may become modified. Requires both Zn2+ and Mg2+ for maximal activity. Associates with an accessory protein Rep (Rab escort protein).","predictedComplex":false,"interactors":[{"ac":"EBI-536715","identifier":"P53611","identifierLink":"https://www.uniprot.org/uniprotkb/P53611/entry","name":"RABGGTB","description":"Geranylgeranyl transferase type-2 subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11774","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9104196","identifier":"Q92696","identifierLink":"https://www.uniprot.org/uniprotkb/Q92696/entry","name":"RABGGTA","description":"Geranylgeranyl transferase type-2 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2920","complexName":"Protein geranylgeranyltransferase type II complex","organismName":"Mus musculus; 10090","description":"Catalyzes the transfer of a 20-hydrocarbon geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to a Rab protein having the C-terminal sequence -XXCC, -XCXC and -CCXX , where both cysteines may become modified. Requires both Zn2+ and Mg2+ for maximal activity. Associates with an accessory protein Rep (Rab escort protein).","predictedComplex":false,"interactors":[{"ac":"EBI-527539","identifier":"Q9JHK4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JHK4/entry","name":"Rabggta","description":"Geranylgeranyl transferase type-2 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9104297","identifier":"P53612","identifierLink":"https://www.uniprot.org/uniprotkb/P53612/entry","name":"Rabggtb","description":"Geranylgeranyl transferase type-2 subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11774","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2251","complexName":"General transcription factor complex TFIIA, TfIIA-S-2 variant","organismName":"Drosophila melanogaster; 7227","description":"Transcription factor complex that regulates transcription initiation from RNA polymerase II promoters. Binding to the transcription factor complex TFIID-TBP enhances assembly of the transcriptional preinitiation complex PIC and its binding to the DNA at the TATA-box by displacing transcription inhibitors. Does not appear to be required for basal transcription but it stabilizes the TBP-DNA complex and stimulates constitutive transcription and activated transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-132413","identifier":"P52654","identifierLink":"https://www.uniprot.org/uniprotkb/P52654/entry","name":"TfIIA-L","description":"Transcription initiation factor IIA subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12694","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-181168","identifier":"Q9W5B9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W5B9/entry","name":"TfIIA-S-2","description":"Transcription initiation factor IIA subunit 2-2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2252","complexName":"KEOPS tRNA N6-adenosine threonylcarbamoyltransferase complex","organismName":"Homo sapiens; 9606","description":"Catalyses the transfer of the threonylcarbamoyl-moiety of threonylcarbamoyladenylate (TCA) onto A37 of substrate tRNA in the cytoplasm. The N6-threonylcarbamoyladenosine (t6A) modification is present at position 37 of tRNAs that recognize ANN-codons, with N being any nucleotide, enhancing the codon-anti-codon interaction and is required for recognition of the AUG start codon. The modification is thus important for maintaining translational fidelity and also appears to play a role in transcription and telomere homeostasis.","predictedComplex":false,"interactors":[{"ac":"EBI-1052105","identifier":"Q14657","identifierLink":"https://www.uniprot.org/uniprotkb/Q14657/entry","name":"LAGE3","description":"EKC/KEOPS complex subunit LAGE3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31283","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1056510","identifier":"Q9NPF4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPF4/entry","name":"OSGEP","description":"tRNA N6-adenosine threonylcarbamoyltransferase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11735","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6256593","identifier":"Q9BXV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BXV9/entry","name":"GON7","description":"EKC/KEOPS complex subunit GON7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR37363","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-739588","identifier":"Q96S44","identifierLink":"https://www.uniprot.org/uniprotkb/Q96S44/entry","name":"TP53RK","description":"EKC/KEOPS complex subunit TP53RK","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12209","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-750123","identifier":"Q9Y3C4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3C4/entry","name":"TPRKB","description":"EKC/KEOPS complex subunit TPRKB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15840","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9097897","identifier":"CHEBI:60240","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60240","name":"divalent metal cation","description":"divalent metal cation","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2253","complexName":"General transcription factor TFIIE complex","organismName":"Drosophila melanogaster; 7227","description":"General transcription factor complex which recruits TFIIH  to complete the assembly of the preinitiation complex which forms on gene promoters during a transcription cycle and consists of Pol II (CPX-2625), general transcription factors (TFIID, TFIIA, TFIIB, TFIIF, TFIIE, and TFIIH) and the mediator complex (CPX-2308). Both subunits of the complex act to anchor the TFIIH kinase module (CAK) within the preinitiation complex. The TFIIE complex appears to directly influence the transition from initiation to elongation during transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-114089","identifier":"O96880","identifierLink":"https://www.uniprot.org/uniprotkb/O96880/entry","name":"TfIIEalpha","description":"General transcription factor IIE subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-176474","identifier":"O96881","identifierLink":"https://www.uniprot.org/uniprotkb/O96881/entry","name":"TfIIEbeta","description":"Transcription initiation factor IIE subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12716","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2254","complexName":"Cus cation efflux complex","organismName":"Escherichia coli (strain K12); 83333","description":"Transmembrane complex that mediates resistance to copper and silver by cation efflux directly from the cell using the proton-motive force. Spans the inner membrane, periplasm, and outer membrane. CusF delivers metal ions to the CusCBA tripartite efflux system in the periplasm, CusB then appears to deliver the bound metal ion from CusB  to the three-methionine cluster (Met-573, Met-623 and Met-672) inside the periplasmic cleft of CusA from where it is passed into the central funnel of CusA and eventually the CusC channel for final extrusion. Primarily activated under anaerobic conditions by CusR (P0ACZ8) and CusS (P77485) but also expressed under extreme copper stress, in aerobic growth. Member of the heavy-metal efflux resistance-nodulation-cell division (HME-RND) superfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1118835","identifier":"P77214","identifierLink":"https://www.uniprot.org/uniprotkb/P77214/entry","name":"cusF","description":"Cation efflux system protein CusF","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-1118842","identifier":"P77239","identifierLink":"https://www.uniprot.org/uniprotkb/P77239/entry","name":"cusB","description":"Cation efflux system protein CusB","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1126317","identifier":"P38054","identifierLink":"https://www.uniprot.org/uniprotkb/P38054/entry","name":"cusA","description":"Cation efflux system protein CusA","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32063","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9539649","identifier":"P77211","identifierLink":"https://www.uniprot.org/uniprotkb/P77211/entry","name":"cusC","description":"Cation efflux system protein CusC","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30203","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2255","complexName":"General transcription factor TFIIF complex","organismName":"Drosophila melanogaster; 7227","description":"TFIIF is a general transcription factor associated with RNA polymerase II (CPX-2625). It prevents the non-specific interaction of RNA Pol II with DNA and stabilizes the pre-initiation complex (PIC), in particular stabilizing TFIIB within the PIC, thus .promoting initiation and elongation. May also interact with paused Pol II causing a conformational change that facilitates the re-entry into elongation mode.","predictedComplex":false,"interactors":[{"ac":"EBI-174822","identifier":"Q05913","identifierLink":"https://www.uniprot.org/uniprotkb/Q05913/entry","name":"TfIIFalpha","description":"General transcription factor IIF subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13011","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2109663","identifier":"P41900","identifierLink":"https://www.uniprot.org/uniprotkb/P41900/entry","name":"TfIIFbeta","description":"General transcription factor IIF subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10445","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2256","complexName":"ASAP splicing-associated complex","organismName":"Homo sapiens; 9606","description":"Binds RNA in a sequence-independent manner and is recruited to the exon junction complex prior to or during the splicing process where it appears to regulate the excision of specific introns. The related complexes ASAP and PSAP (CPX-2257) confer distinct alternative splicing regulatory activities to exon-junction complexes. Also may play a role in aspects of RNA metabolism involved in transcription, translation and nonsense-mediated mRNA decay. Promotes apoptosis and is disassembled after induction of apoptosis.","predictedComplex":false,"interactors":[{"ac":"EBI-1044156","identifier":"O00422","identifierLink":"https://www.uniprot.org/uniprotkb/O00422/entry","name":"SAP18","description":"Histone deacetylase complex subunit SAP18","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395959","identifier":"Q15287","identifierLink":"https://www.uniprot.org/uniprotkb/Q15287/entry","name":"RNPS1","description":"RNA-binding protein with serine-rich domain 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15481","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-396258","identifier":"Q9UKV3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UKV3/entry","name":"ACIN1","description":"Apoptotic chromatin condensation inducer in the nucleus","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46589","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2257","complexName":"PSAP splicing-associated complex","organismName":"Homo sapiens; 9606","description":"Binds RNA in a sequence-independent manner and is recruited to the exon junction complex prior to or during the splicing process where it appears to regulate the excision of specific  introns. The related complexes ASAP (CPX-2256) and PSAP confer  distinct alternative splicing regulatory activities to exon-junction complexes.Also may play a role in aspects of RNA metabolism involved in transcription, translation and nonsense-mediated mRNA decay.","predictedComplex":false,"interactors":[{"ac":"EBI-1044156","identifier":"O00422","identifierLink":"https://www.uniprot.org/uniprotkb/O00422/entry","name":"SAP18","description":"Histone deacetylase complex subunit SAP18","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395959","identifier":"Q15287","identifierLink":"https://www.uniprot.org/uniprotkb/Q15287/entry","name":"RNPS1","description":"RNA-binding protein with serine-rich domain 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15481","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-681904","identifier":"Q9H307","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H307/entry","name":"PNN","description":"Pinin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12707","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2258","complexName":"General transcription factor TFIIH complex","organismName":"Drosophila melanogaster; 7227","description":"General transcription factor involved in transcriptional initiation, activation and elongation, the cell cycle and nucleotide excision repair. The ATPase/helicase activities of ERCC2/xpd and ERCC3/hay are required for promoter melting at transcription initiation sites and damaged DNA opening at nucleotide excision repair sites and the protein kinase activity of CDK7 is necessary for phosphorylation of the C-terminal domain of the largest subunit of RNA polymerase II, other transcription factors and nuclear receptors.","predictedComplex":false,"interactors":[{"ac":"EBI-104674","identifier":"Q960E8","identifierLink":"https://www.uniprot.org/uniprotkb/Q960E8/entry","name":"Tfb1","description":"General transcription factor IIH subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12856","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-105213","identifier":"Q7KPG8","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KPG8/entry","name":"Mat1","description":"CDK-activating kinase assembly factor MAT1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12683","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-132265","identifier":"O76513","identifierLink":"https://www.uniprot.org/uniprotkb/O76513/entry","name":"CycH","description":"Cyclin-H","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-132746","identifier":"Q9VUR1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VUR1/entry","name":"mrn","description":"General transcription factor IIH subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13152","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-139668","identifier":"Q24216","identifierLink":"https://www.uniprot.org/uniprotkb/Q24216/entry","name":"Cdk7","description":"Cyclin-dependent kinase 7","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-144861","identifier":"Q9VNP8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VNP8/entry","name":"Ssl1","description":"General transcription factor IIH subunit","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12695","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3424058","identifier":"Q7KVP9","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KVP9/entry","name":"Xpd","description":"General transcription and DNA repair factor IIH helicase subunit XPD","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11472","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34612364","identifier":"Q9VPX4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VPX4/entry","name":"Tfb4","description":"General transcription factor IIH subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12831","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34612406","identifier":"B7Z018","identifierLink":"https://www.uniprot.org/uniprotkb/B7Z018/entry","name":"Tfb5","description":"General transcription and DNA repair factor IIH subunit TFB5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR28580","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-74952","identifier":"Q02870","identifierLink":"https://www.uniprot.org/uniprotkb/Q02870/entry","name":"hay","description":"General transcription and DNA repair factor IIH helicase/translocase subunit XPB","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11274","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2259","complexName":"PAN2-PAN3 mRNA deadenylation complex","organismName":"Homo sapiens; 9606","description":"A poly(A)-specific 3' exoribonuclease required to regulate Poly(A) tails added to mRNA co-transcriptionally and  which are required for the export of mature mRNAs to the cytoplasm  The complex is responsible for the preliminary poly(A) trimming of the tail length to a transcript specific size which regulates translation repression and mRNA decay. The remaining trimming is performed by the CCR4-NOT complex (CPX-707/CPX-2522/CPX-2535/CPX-2849). This complex is non-essential, but its deletion results in increased poly(A)-tail length.","predictedComplex":false,"interactors":[{"ac":"EBI-1058976","identifier":"Q504Q3","identifierLink":"https://www.uniprot.org/uniprotkb/Q504Q3/entry","name":"PAN2","description":"PAN2-PAN3 deadenylation complex catalytic subunit PAN2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15728","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34614167","identifier":"Q58A45-2","identifierLink":"https://www.uniprot.org/uniprotkb/Q58A45-2/entry","name":"PAN3","description":"PAN2-PAN3 deadenylation complex subunit PAN3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-2260","complexName":"Non-canonical polycomb repressive complex 1.2, RING1-YAF2 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin-protein ligase that acts as a transcriptional repressor by mediating the monoubiquitination of Lys-119 of histone H2A, compacting chromatin, stalling RNA polymerase II and transcriptionally silencing genes critical for development.","predictedComplex":false,"interactors":[{"ac":"EBI-2129767","identifier":"P35227","identifierLink":"https://www.uniprot.org/uniprotkb/P35227/entry","name":"PCGF2","description":"Polycomb group RING finger protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10825","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2842031","identifier":"Q8IY57","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IY57/entry","name":"YAF2","description":"YY1-associated factor 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12920","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752313","identifier":"Q06587","identifierLink":"https://www.uniprot.org/uniprotkb/Q06587/entry","name":"RING1","description":"E3 ubiquitin-protein ligase RING1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2261","complexName":"TREX transcription-export complex","organismName":"Drosophila melanogaster; 7227","description":"Selectively binds maturing mRNA at the messenger ribonucleoprotein complex 5'-end, splice junctions, and 3'-end. Lcenses mRNA for nuclear export by loading the global mRNA-export factor NXF1-NXT. Essential for the biogenesis of piRNA, a distinct class of small noncoding RNAs that control expression of transposable elements (TEs) in the Drosophila germline.","predictedComplex":false,"interactors":[{"ac":"EBI-109769","identifier":"Q9V3E7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V3E7/entry","name":"Ref1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19965","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-150183","identifier":"Q8IRJ8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IRJ8/entry","name":"thoc7","description":"THO complex protein 7","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23405","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15143944","identifier":"Q9W1F4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W1F4/entry","name":"thoc5","description":"THO complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15789641","identifier":"Q9VNI8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VNI8/entry","name":"Hpr1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13265","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-176504","identifier":"Q27268","identifierLink":"https://www.uniprot.org/uniprotkb/Q27268/entry","name":"Hel25E","description":"ATP-dependent RNA helicase WM6","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR47958","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3410055","identifier":"Q9VHT2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VHT2/entry","name":"tex","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22839","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34612542","identifier":"E2QCS8","identifierLink":"https://www.uniprot.org/uniprotkb/E2QCS8/entry","name":"tho2","description":"THO complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21597","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34612573","identifier":"Q9VTV1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VTV1/entry","name":"thoc6","description":"THO complex subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR44411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2262","complexName":"26S proteasome complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Multi-enzyme complex that functions as the primary degradation machinery for the selective turnover of surplus or damaged proteins within the cell. Proteins targeted for degradation are covalently labeled with polyubiquitin chains which are recognized and removed by the proteasome. The core contains the protease active sites (chymotrypsin-like, trypsin-like and peptidylglutamyl-peptide hydrolyzing) that perform the proteolysis reactions in an internal chamber. The regulatory particles act as a discriminating gateway for potential substrates. The base drives the mechanical substrate unfolding and translocation of the unstructured polypeptides into the degradation chamber of the core peptidase. The lid contains the deubiquitinating enzyme (DUB) RPN11 that cleaves polyubiquitin chains from targeted substrates as an essential step in proteasomal substrate processing.","predictedComplex":false,"interactors":[{"ac":"EBI-11219","identifier":"P43588","identifierLink":"https://www.uniprot.org/uniprotkb/P43588/entry","name":"RPN11","description":"Ubiquitin carboxyl-terminal hydrolase RPN11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10410","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13901","identifier":"P40327","identifierLink":"https://www.uniprot.org/uniprotkb/P40327/entry","name":"RPT2","description":"26S proteasome regulatory subunit 4 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13905","identifier":"P33298","identifierLink":"https://www.uniprot.org/uniprotkb/P33298/entry","name":"RPT3","description":"26S proteasome regulatory subunit 6B homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13910","identifier":"P33299","identifierLink":"https://www.uniprot.org/uniprotkb/P33299/entry","name":"RPT1","description":"26S proteasome regulatory subunit 7 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13914","identifier":"Q01939","identifierLink":"https://www.uniprot.org/uniprotkb/Q01939/entry","name":"RPT6","description":"26S proteasome regulatory subunit 8 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13920","identifier":"P33297","identifierLink":"https://www.uniprot.org/uniprotkb/P33297/entry","name":"RPT5","description":"26S proteasome regulatory subunit 6A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13955","identifier":"P40302","identifierLink":"https://www.uniprot.org/uniprotkb/P40302/entry","name":"PRE5","description":"Proteasome subunit alpha type-6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13959","identifier":"P23639","identifierLink":"https://www.uniprot.org/uniprotkb/P23639/entry","name":"PRE8","description":"Proteasome subunit alpha type-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13963","identifier":"P21242","identifierLink":"https://www.uniprot.org/uniprotkb/P21242/entry","name":"PRE10","description":"Probable proteasome subunit alpha type-7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13967","identifier":"P23638","identifierLink":"https://www.uniprot.org/uniprotkb/P23638/entry","name":"PRE9","description":"Proteasome subunit alpha type-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13971","identifier":"P32379","identifierLink":"https://www.uniprot.org/uniprotkb/P32379/entry","name":"PUP2","description":"Proteasome subunit alpha type-5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13975","identifier":"P21243","identifierLink":"https://www.uniprot.org/uniprotkb/P21243/entry","name":"SCL1","description":"Proteasome subunit alpha type-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13980","identifier":"P40303","identifierLink":"https://www.uniprot.org/uniprotkb/P40303/entry","name":"PRE6","description":"Proteasome subunit alpha type-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13984","identifier":"P23724","identifierLink":"https://www.uniprot.org/uniprotkb/P23724/entry","name":"PRE7","description":"Proteasome subunit beta type-6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13988","identifier":"P22141","identifierLink":"https://www.uniprot.org/uniprotkb/P22141/entry","name":"PRE1","description":"Proteasome subunit beta type-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13993","identifier":"P25451","identifierLink":"https://www.uniprot.org/uniprotkb/P25451/entry","name":"PUP3","description":"Proteasome subunit beta type-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13997","identifier":"P30657","identifierLink":"https://www.uniprot.org/uniprotkb/P30657/entry","name":"PRE4","description":"Proteasome subunit beta type-7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14001","identifier":"P30656","identifierLink":"https://www.uniprot.org/uniprotkb/P30656/entry","name":"PRE2","description":"Proteasome subunit beta type-5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14005","identifier":"P38624","identifierLink":"https://www.uniprot.org/uniprotkb/P38624/entry","name":"PRE3","description":"Proteasome subunit beta type-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14009","identifier":"P25043","identifierLink":"https://www.uniprot.org/uniprotkb/P25043/entry","name":"PUP1","description":"Proteasome subunit beta type-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15913","identifier":"P38764","identifierLink":"https://www.uniprot.org/uniprotkb/P38764/entry","name":"RPN1","description":"26S proteasome regulatory subunit RPN1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10943","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15919","identifier":"P32565","identifierLink":"https://www.uniprot.org/uniprotkb/P32565/entry","name":"RPN2","description":"26S proteasome regulatory subunit RPN2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10943","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15927","identifier":"P40016","identifierLink":"https://www.uniprot.org/uniprotkb/P40016/entry","name":"RPN3","description":"26S proteasome regulatory subunit RPN3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10758","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15935","identifier":"Q12250","identifierLink":"https://www.uniprot.org/uniprotkb/Q12250/entry","name":"RPN5","description":"26S proteasome regulatory subunit RPN5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10855","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15940","identifier":"Q06103","identifierLink":"https://www.uniprot.org/uniprotkb/Q06103/entry","name":"RPN7","description":"26S proteasome regulatory subunit RPN7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14145","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15944","identifier":"Q04062","identifierLink":"https://www.uniprot.org/uniprotkb/Q04062/entry","name":"RPN9","description":"26S proteasome regulatory subunit RPN9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10539","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15949","identifier":"P38886","identifierLink":"https://www.uniprot.org/uniprotkb/P38886/entry","name":"RPN10","description":"26S proteasome regulatory subunit RPN10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10223","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15953","identifier":"P32496","identifierLink":"https://www.uniprot.org/uniprotkb/P32496/entry","name":"RPN12","description":"26S proteasome regulatory subunit RPN12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12387","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18520","identifier":"P53549","identifierLink":"https://www.uniprot.org/uniprotkb/P53549/entry","name":"RPT4","description":"26S proteasome subunit RPT4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-308","identifier":"Q12377","identifierLink":"https://www.uniprot.org/uniprotkb/Q12377/entry","name":"RPN6","description":"26S proteasome regulatory subunit RPN6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31337","identifier":"O94742","identifierLink":"https://www.uniprot.org/uniprotkb/O94742/entry","name":"SEM1","description":"26S proteasome complex subunit SEM1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR16771","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32948","identifier":"O13563","identifierLink":"https://www.uniprot.org/uniprotkb/O13563/entry","name":"RPN13","description":"26S proteasome regulatory subunit RPN13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-36176","identifier":"Q08723","identifierLink":"https://www.uniprot.org/uniprotkb/Q08723/entry","name":"RPN8","description":"26S proteasome regulatory subunit RPN8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10540","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2263","complexName":"TREX-2 transcription-export complex","organismName":"Drosophila melanogaster; 7227","description":"Couples SAGA (CPX-2644)-dependent gene expression and transcription elongation to mRNA export at the inner side of the nuclear pore complex (NPC). The TREX-2 complex is tethered to the inner side of the NPC and  facilitates the repositioning and association of actively transcribing genes with nuclear pores (gene gating). Provides a feedback mechanism for the control of transcription and the preservation of genetic integrity of transcribed DNA regions.","predictedComplex":false,"interactors":[{"ac":"EBI-101834","identifier":"Q9VM46","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VM46/entry","name":"Sem1","description":"Probable 26S proteasome complex subunit sem1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR16771","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-123918","identifier":"Q9VTL1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VTL1/entry","name":"PCID2","description":"PCI domain-containing protein 2 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12732","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2549759","identifier":"Q9VYX1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VYX1/entry","name":"e(y)2","description":"Enhancer of yellow 2 transcription factor","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12514","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2550689","identifier":"Q9U3V9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9U3V9/entry","name":"xmas","description":"Protein xmas","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12436","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2264","complexName":"NuA4 histone acetyltransferase complex","organismName":"Drosophila melanogaster; 7227","description":"Histone acetyl transferase (HAT) complex involved in transcriptional activation of selected genes. The major acetylation targets are lysines-5, 8, and 12 on nucleosomal H4, K5 and K15 on H2A, histone variants H2AZ and H2AX.","predictedComplex":false,"interactors":[{"ac":"EBI-102665","identifier":"Q9Y0I1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y0I1/entry","name":"MRG15","description":"NuA4 complex subunit EAF3 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10880","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-103202","identifier":"Q9VAM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VAM5/entry","name":"Brd8","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15398","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-105997","identifier":"Q7K3D8","identifierLink":"https://www.uniprot.org/uniprotkb/Q7K3D8/entry","name":"DMAP1","description":"DNA methyltransferase 1-associated protein 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 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7227","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-135521","identifier":"P10981","identifierLink":"https://www.uniprot.org/uniprotkb/P10981/entry","name":"Act87E","description":"Actin-87E","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-138158","identifier":"Q9VWS0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VWS0/entry","name":"Ing3","description":"Inhibitor of growth protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-140042","identifier":"Q9VRN3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VRN3/entry","name":"Eaf6","description":"Chromatin modification-related protein MEAF6","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-187741","identifier":"Q9VM63","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VM63/entry","name":"Gas41","description":"YEATS domain-containing protein 4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23195","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-192924","identifier":"Q9V3K3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V3K3/entry","name":"rept","description":"RuvB-like helicase 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-234957","identifier":"Q9VH07","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VH07/entry","name":"pont","description":"RuvB-like helicase 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2507795","identifier":"Q8I8U7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8I8U7/entry","name":"Nipped-A","description":"Transcription-associated protein 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34614390","identifier":"Q7K003","identifierLink":"https://www.uniprot.org/uniprotkb/Q7K003/entry","name":"MrgBP","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13581","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34614407","identifier":"A0A0B4KFP2","identifierLink":"https://www.uniprot.org/uniprotkb/A0A0B4KFP2/entry","name":"E(Pc)","description":"Enhancer of polycomb-like protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14898","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34614456","identifier":"Q9NDJ2-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NDJ2-1/entry","name":"dom","description":"Helicase domino","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]}]},{"complexAC":"CPX-2265","complexName":"TORC1 complex","organismName":"Drosophila melanogaster; 7227","description":"Serine/threonine protein kinase complex that regulates cellular metabolism, growth and survival in response to hormones, growth factors, nutrients, energy and stress signals. The complex can be inhibited by rapamycin.","predictedComplex":false,"interactors":[{"ac":"EBI-115381","identifier":"Q9W328","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W328/entry","name":"Lst8","description":"Protein LST8 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2507751","identifier":"Q9VK45","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VK45/entry","name":"mTor","description":"Serine/threonine-protein kinase mTor","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3404045","identifier":"Q9W437","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W437/entry","name":"raptor","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12848","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2267","complexName":"SOD1-CCS1 superoxide dismutase heterodimer","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Complex formation results in the activationof the antioxidant enzyme copper, zinc superoxide dismutase,SOD1 which protects cells against oxygen stress and reactive oxygen species by converting superoxide radicals into water and hydrogen peroxide. SOD1 (CPX-2896) activation involves  insertion of copper and oxidation of an intrasubunit disulfide bond. Insertion of copper is required for any enzymatic activity. Oxidation of the disulfide bond is required to increase the enzymatic activity from approximately 10 % in disulfide-reduced SOD1 to 100 % in disulfide-oxidized SOD1. The copper chaperone, CCS1 (CPX-2895), both delivers the copper and oxidises the disulfide bond.","predictedComplex":false,"interactors":[{"ac":"EBI-10287","identifier":"P40202","identifierLink":"https://www.uniprot.org/uniprotkb/P40202/entry","name":"CCS1","description":"Superoxide dismutase 1 copper chaperone","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10003","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17635","identifier":"P00445","identifierLink":"https://www.uniprot.org/uniprotkb/P00445/entry","name":"SOD1","description":"Superoxide dismutase [Cu-Zn]","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10003","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2008294","identifier":"CHEBI:29036","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29036","name":"copper(2+)","description":"Copper (Cu2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2268","complexName":"TIM9-TIM10 mitochondrial intermembrane space protein transporter complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Facilitates transport of hydrophobic precursors of a distinct subgroup of inner membrane proteins through the aqueous intermembrane space as they exit the TOM40 channel complex (CPX-474) in the outer membrane. Functions as a chaperone to maintain the hydrophobic membrane proteins in an import competent state and escort substrates to the TIM22 insertion complex (CPX-1629), which mediates protein insertion into the membrane.. Cross-links to the COOH-terminal domain of the essential import translocase protein TIM23 (P32897) and plays a key role in TIM23 import to the mitochondrial inner membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-9108","identifier":"O74700","identifierLink":"https://www.uniprot.org/uniprotkb/O74700/entry","name":"TIM9","description":"Mitochondrial import inner membrane translocase subunit TIM9","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13172","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9115","identifier":"P87108","identifierLink":"https://www.uniprot.org/uniprotkb/P87108/entry","name":"TIM10","description":"Mitochondrial import inner membrane translocase subunit TIM10","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11038","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2269","complexName":"TORC2 complex","organismName":"Drosophila melanogaster; 7227","description":"Serine/threonine protein kinase complex that regulates cellular processes including cell growth, survival and organization of the cytoskeleton in response to hormones and growth factors. Lst8 is a non-essential component of the TORC2 complex.","predictedComplex":false,"interactors":[{"ac":"EBI-115381","identifier":"Q9W328","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W328/entry","name":"Lst8","description":"Protein LST8 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2507751","identifier":"Q9VK45","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VK45/entry","name":"mTor","description":"Serine/threonine-protein kinase mTor","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2507904","identifier":"Q9V719","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V719/entry","name":"Sin1","description":"Stress-activated map kinase-interacting protein 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13335","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3410278","identifier":"Q9VWJ6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VWJ6/entry","name":"rictor","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13298","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2950","complexName":"TIM9-TIM10-TIM12 mitochondrial intermembrane space protein transporter complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Facilitates transport of hydrophobic precursors of a distinct subgroup of inner membrane proteins through the aqueous intermembrane space as they exit the TOM40 channel complex (CPX-474) in the outer membrane. 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Lacks ubiquitin ligase activity due to the inhibitory phosphorylation of RNF2 at serine 168 by casein kinase 2. The neuronal transcription factor AUTS2, recruits the EP300 transcriptional co-activator to promote gene activation.","predictedComplex":false,"interactors":[{"ac":"EBI-12625723","identifier":"CPX-914","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-914","name":"Casein kinase II complex, CSNK2A1 variant","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2339807","identifier":"Q3KNV8","identifierLink":"https://www.uniprot.org/uniprotkb/Q3KNV8/entry","name":"PCGF3","description":"Polycomb group RING finger protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45893","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2842031","identifier":"Q8IY57","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IY57/entry","name":"YAF2","description":"YY1-associated factor 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12920","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2875359","identifier":"Q8WXX7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WXX7/entry","name":"AUTS2","description":"Autism susceptibility gene 2 protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14429","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-722416","identifier":"Q99496","identifierLink":"https://www.uniprot.org/uniprotkb/Q99496/entry","name":"RNF2","description":"E3 ubiquitin-protein ligase RING2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2300","complexName":"CRL3 E3 ubiquitin ligase complex, SPOP variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SPOP is required to maintain normal cellular growth and development and its targets include the polycomb protein BMI1 (P35226), the apoptosis factor DAXX (Q9UER7), the pancreatic and duodenal homeobox protein PDX1 (P52945), and the Hedgehog signaling transcription factors GLI2 (P10070) and GLI3 (P10071). SPOP forms linear higher-order oligomers which enables it to present multiple MATH domains (IPR002083) for binding to multiple low-affinity motifs in a single substrate, resulting in an overall increased affinity through avidity effects. SPOP oligomerization is also involved in phase separation.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743549","identifier":"O43791","identifierLink":"https://www.uniprot.org/uniprotkb/O43791/entry","name":"SPOP","description":"Speckle-type POZ protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24413","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2301","complexName":"WRD-protein phosphatase 2A complex","organismName":"Drosophila melanogaster; 7227","description":"Serine/threonine phosphatase complex required for oocyte spindle assembly, maintenance of sister chromatid cohesion, establishment of end-on microtubule attachments, and metaphase arrest in oocytes.","predictedComplex":false,"interactors":[{"ac":"EBI-101960","identifier":"P23696","identifierLink":"https://www.uniprot.org/uniprotkb/P23696/entry","name":"mts","description":"Serine/threonine-protein phosphatase PP2A","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-139308","identifier":"P36179","identifierLink":"https://www.uniprot.org/uniprotkb/P36179/entry","name":"Pp2A-29B","description":"Serine/threonine-protein phosphatase PP2A 65 kDa regulatory subunit","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-58772129","identifier":"Q9VEC6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VEC6/entry","name":"wrd","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]}]},{"complexAC":"CPX-2302","complexName":"U2 small nuclear ribonucleoprotein auxiliary factor complex","organismName":"Drosophila melanogaster; 7227","description":"Ribonucleoprotein complex that recognizes an consensus AG-dinucleotide at the splice site junction and a preceding polypyrimidine tract and recruits the U2 small nuclear ribonucleoprotein particle (snRNP) of the spliceosome during the  removal of intervening sequences (introns) separating protein-coding regions within pre-mRNAs.  U2 snRNP defines the 3′ splice site.","predictedComplex":false,"interactors":[{"ac":"EBI-121011","identifier":"Q94535","identifierLink":"https://www.uniprot.org/uniprotkb/Q94535/entry","name":"U2af38","description":"Splicing factor U2af 38 kDa subunit","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12620","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-165226","identifier":"Q24562","identifierLink":"https://www.uniprot.org/uniprotkb/Q24562/entry","name":"U2af50","description":"Splicing factor U2AF 50 kDa subunit","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2304","complexName":"Heat-labile enterotoxin IIB complex","organismName":"Escherichia coli; 562","description":"Member of the AB class of bacterial toxins. Binds to the ganglioside receptors on epithelial host cells and forms a pore in the host cell membrane, leading to the endocytosis of the A subunit. The A1 chain then ADP-ribosylates the alpha-subunit of the host heterotrimeric G-protein Gs, inducing constitutive activation of the cell’s adenylate cyclase and dramatically increasing the intracellular concentration of the host cAMP (CHEBI:17489) cellular signaling molecule. This originally evolved as a strategy to capture energy from host biological systems but leads to degradation of the host intestinal epithelium, resulting in severe diarrhoea in humans, pigs and bovine species.","predictedComplex":false,"interactors":[{"ac":"EBI-9011989","identifier":"P43528","identifierLink":"https://www.uniprot.org/uniprotkb/P43528/entry","name":"e2ba","description":"Heat-labile enterotoxin IIB, A chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli; 562","xrefs":[]},{"ac":"EBI-9011997","identifier":"P43529","identifierLink":"https://www.uniprot.org/uniprotkb/P43529/entry","name":"e2bb","description":"Heat-labile enterotoxin IIB, B chain","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Escherichia coli; 562","xrefs":[]}]},{"complexAC":"CPX-2305","complexName":"Non-canonical polycomb repressive complex 1.6, RING1-RYBP variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin-protein ligase that acts as a transcriptional repressor by mediating the monoubiquitination of Lys-119 of histone H2A, compacting chromatin, stalling RNA polymerase II and transcriptionally silencing genes critical for development.","predictedComplex":false,"interactors":[{"ac":"EBI-1048026","identifier":"Q9BYE7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BYE7/entry","name":"PCGF6","description":"Polycomb group RING finger protein 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45893","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-739909","identifier":"Q969R5","identifierLink":"https://www.uniprot.org/uniprotkb/Q969R5/entry","name":"L3MBTL2","description":"Lethal(3)malignant brain tumor-like protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12247","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752313","identifier":"Q06587","identifierLink":"https://www.uniprot.org/uniprotkb/Q06587/entry","name":"RING1","description":"E3 ubiquitin-protein ligase RING1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752324","identifier":"Q8N488","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N488/entry","name":"RYBP","description":"RING1 and YY1-binding protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12920","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9019630","identifier":"CPX-2551","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-2551","name":"MGA-MAX transcriptional repressor complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-9019678","identifier":"CPX-2552","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-2552","name":"E2F6-DP1 transcriptional repressor complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-2307","complexName":"Polycomb repressive complex 2.1, EZH1-RBBP7-PCL1-PALI1 variant","organismName":"Homo sapiens; 9606","description":"Histone-lysine N-methyltransferase which trimethylates Lys-10  (H3K9me3)  and Lys-28 on histone H3 (H3K27me3)  leading to transcriptional silencing of genes critical for development and stem cell differentiation. Also mediates mono and dimethylation of H3K27. PRC2 is preferably targeted to CpG islands in cells. EZH1-containing PRC2 displays a high binding affinity towards nucleosomes and exhibits chromatin compaction activity.","predictedComplex":false,"interactors":[{"ac":"EBI-1264675","identifier":"Q15022","identifierLink":"https://www.uniprot.org/uniprotkb/Q15022/entry","name":"SUZ12","description":"Polycomb protein SUZ12","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22597","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352227","identifier":"Q16576","identifierLink":"https://www.uniprot.org/uniprotkb/Q16576/entry","name":"RBBP7","description":"Histone-binding protein RBBP7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-530034","identifier":"O43189","identifierLink":"https://www.uniprot.org/uniprotkb/O43189/entry","name":"PHF1","description":"PHD finger protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-746045","identifier":"Q96JN0","identifierLink":"https://www.uniprot.org/uniprotkb/Q96JN0/entry","name":"LCOR","description":"Ligand-dependent corepressor","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21545","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8830732","identifier":"Q92800","identifierLink":"https://www.uniprot.org/uniprotkb/Q92800/entry","name":"EZH1","description":"Histone-lysine N-methyltransferase EZH1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45747","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-923794","identifier":"O75530","identifierLink":"https://www.uniprot.org/uniprotkb/O75530/entry","name":"EED","description":"Polycomb protein EED","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10253","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2308","complexName":"Core mediator complex","organismName":"Drosophila melanogaster; 7227","description":"Plays an essential role in gene expression regulation by acting as a bridge between DNA-binding transcription factors and the RNA polymerase II (RNAPII) transcription machinery, serving as a central scaffold within the pre-initiation complex. The Mediator complex is also targeted by sequence-specific, DNA-binding transcription factors and appears to regulate RNAPII at both the initiation and elongation stages of transcription. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and unfolds to an extended conformation and partially surrounds RNAPII specifically interacting with the unphosphorylated form of its C-terminal domain. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.\r\n\r\nReversibly associates with the CKM complex (CPX-7701). Mediator lacking the CKM complex has a stimulatory effect on basal transcription. In contrast, Mediator containing the sub-complex represses basal transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-125442","identifier":"Q9VVL6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVL6/entry","name":"MED19","description":"Mediator of RNA polymerase II transcription subunit 19","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22536","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-135284","identifier":"Q9VEC1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VEC1/entry","name":"MED17","description":"Mediator of RNA polymerase II transcription subunit 17","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13114","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-138576","identifier":"Q9GYU7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9GYU7/entry","name":"MED10","description":"Mediator of RNA polymerase II transcription subunit 10","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 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7227","xrefs":[{"identifier":"PTHR13130","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-167203","identifier":"Q9W0P3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W0P3/entry","name":"MED30","description":"Mediator of RNA polymerase II transcription subunit 30","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR31705","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-174566","identifier":"Q9VBQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VBQ9/entry","name":"MED28","description":"Mediator of RNA polymerase II transcription subunit 28","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13512","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-175591","identifier":"P91641","identifierLink":"https://www.uniprot.org/uniprotkb/P91641/entry","name":"MED20","description":"Mediator of RNA polymerase II transcription subunit 20","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12465","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-187169","identifier":"Q9VS38","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VS38/entry","name":"MED4","description":"Mediator of RNA polymerase II transcription subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13208","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-188974","identifier":"Q9VVS4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVS4/entry","name":"MED11","description":"Mediator of RNA polymerase II transcription subunit 11","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-194372","identifier":"A1ZB42","identifierLink":"https://www.uniprot.org/uniprotkb/A1ZB42/entry","name":"MED9","description":"Mediator of RNA polymerase II transcription subunit 9","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR20844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-194467","identifier":"Q8MSX2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8MSX2/entry","name":"MED6","description":"Mediator of RNA polymerase II transcription subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13104","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-203492","identifier":"Q8IH24","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IH24/entry","name":"MED31","description":"Mediator of RNA polymerase II transcription subunit 31","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13186","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3406916","identifier":"Q9W278","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W278/entry","name":"MED16","description":"Mediator of RNA polymerase II transcription subunit 16","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13224","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3409937","identifier":"Q9VSF2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VSF2/entry","name":"MED24","description":"Mediator of RNA polymerase II transcription subunit 24","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12898","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3413235","identifier":"Q9W0P8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W0P8/entry","name":"MED14","description":"Mediator of RNA polymerase II transcription subunit 14","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12809","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3429527","identifier":"Q9VDR1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VDR1/entry","name":"MED25","description":"Mediator of RNA polymerase II transcription subunit 25","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12433","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34618526","identifier":"Q9W1X7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W1X7/entry","name":"MED23","description":"Mediator of RNA polymerase II transcription subunit 23","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-500435","identifier":"Q9W5P1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W5P1/entry","name":"MED21","description":"Mediator of RNA polymerase II transcription subunit 21","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13381","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-87701","identifier":"Q9V439","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V439/entry","name":"MED22","description":"Mediator of RNA polymerase II transcription subunit 22","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12434","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-90766","identifier":"A1ZBT5","identifierLink":"https://www.uniprot.org/uniprotkb/A1ZBT5/entry","name":"MED8","description":"Mediator of RNA polymerase II transcription subunit 8","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13074","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-91715","identifier":"Q9Y149","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y149/entry","name":"MED15","description":"Mediator of RNA polymerase II transcription subunit 15","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR31804","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-92171","identifier":"Q9VP05","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VP05/entry","name":"MED1","description":"Mediator of RNA polymerase II transcription subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12881","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-96589","identifier":"Q7KBL8","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KBL8/entry","name":"ix","description":"Mediator of RNA polymerase II transcription subunit 29","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR28314","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9697267","identifier":"Q9GYV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9GYV9/entry","name":"MED7","description":"Mediator of RNA polymerase II transcription subunit 7","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21428","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2309","complexName":"Polycomb repressive complex 2.1, EZH1-RBBP7-PCL2-PALI1 variant","organismName":"Homo sapiens; 9606","description":"Histone-lysine N-methyltransferase which trimethylates Lys-10  (H3K9me3)  and Lys-28 on histone H3 (H3K27me3)  leading to transcriptional silencing of genes critical for development and stem cell differentiation. Also mediates mono and dimethylation of H3K27. PRC2 is preferably targeted to CpG islands in cells. EZH1-containing PRC2 displays a high binding affinity towards nucleosomes and exhibits chromatin compaction activity. MTF2 regulates the transcriptional networks during embryonic stem cell self-renewal and differentiation","predictedComplex":false,"interactors":[{"ac":"EBI-1264675","identifier":"Q15022","identifierLink":"https://www.uniprot.org/uniprotkb/Q15022/entry","name":"SUZ12","description":"Polycomb protein SUZ12","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22597","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352227","identifier":"Q16576","identifierLink":"https://www.uniprot.org/uniprotkb/Q16576/entry","name":"RBBP7","description":"Histone-binding protein RBBP7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-725816","identifier":"Q9Y483","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y483/entry","name":"MTF2","description":"Metal-response element-binding transcription factor 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-746045","identifier":"Q96JN0","identifierLink":"https://www.uniprot.org/uniprotkb/Q96JN0/entry","name":"LCOR","description":"Ligand-dependent corepressor","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21545","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8830732","identifier":"Q92800","identifierLink":"https://www.uniprot.org/uniprotkb/Q92800/entry","name":"EZH1","description":"Histone-lysine N-methyltransferase EZH1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45747","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-923794","identifier":"O75530","identifierLink":"https://www.uniprot.org/uniprotkb/O75530/entry","name":"EED","description":"Polycomb protein EED","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10253","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2310","complexName":"Polycomb repressive complex 2.1, EZH1-RBBP4-PCL2-PALI1 variant","organismName":"Homo sapiens; 9606","description":"Histone-lysine N-methyltransferase which trimethylates Lys-10  (H3K9me3)  and Lys-28 on histone H3 (H3K27me3)  leading to transcriptional silencing of genes critical for development and stem cell differentiation. Also mediates mono and dimethylation of H3K27. PRC2 is preferably targeted to CpG islands in cells. EZH1-containing PRC2 displays a high binding affinity towards nucleosomes and exhibits chromatin compaction activity. MTF2 regulates the transcriptional networks during embryonic stem cell self-renewal and differentiation","predictedComplex":false,"interactors":[{"ac":"EBI-1264675","identifier":"Q15022","identifierLink":"https://www.uniprot.org/uniprotkb/Q15022/entry","name":"SUZ12","description":"Polycomb protein SUZ12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22597","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-620823","identifier":"Q09028","identifierLink":"https://www.uniprot.org/uniprotkb/Q09028/entry","name":"RBBP4","description":"Histone-binding protein RBBP4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-725816","identifier":"Q9Y483","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y483/entry","name":"MTF2","description":"Metal-response element-binding transcription factor 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-746045","identifier":"Q96JN0","identifierLink":"https://www.uniprot.org/uniprotkb/Q96JN0/entry","name":"LCOR","description":"Ligand-dependent corepressor","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21545","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8830732","identifier":"Q92800","identifierLink":"https://www.uniprot.org/uniprotkb/Q92800/entry","name":"EZH1","description":"Histone-lysine N-methyltransferase EZH1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45747","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-923794","identifier":"O75530","identifierLink":"https://www.uniprot.org/uniprotkb/O75530/entry","name":"EED","description":"Polycomb protein EED","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10253","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2311","complexName":"Polycomb repressive complex 2.1, EZH2-RBBP7-PCL1-PALI1 variant","organismName":"Homo sapiens; 9606","description":"Histone-lysine N-methyltransferase which trimethylates Lys-10  (H3K9me3)  and Lys-28 on histone H3 (H3K27me3)  leading to transcriptional silencing of genes critical for development and stem cell differentiation. 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PRC2.2 preferentially mediates de novo repression of active genes.","predictedComplex":false,"interactors":[{"ac":"EBI-1222720","identifier":"Q92833","identifierLink":"https://www.uniprot.org/uniprotkb/Q92833/entry","name":"JARID2","description":"Protein Jumonji","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10694","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1264675","identifier":"Q15022","identifierLink":"https://www.uniprot.org/uniprotkb/Q15022/entry","name":"SUZ12","description":"Polycomb protein SUZ12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22597","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-620823","identifier":"Q09028","identifierLink":"https://www.uniprot.org/uniprotkb/Q09028/entry","name":"RBBP4","description":"Histone-binding protein RBBP4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743256","identifier":"Q6ZN18","identifierLink":"https://www.uniprot.org/uniprotkb/Q6ZN18/entry","name":"AEBP2","description":"Zinc finger protein AEBP2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46541","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8830732","identifier":"Q92800","identifierLink":"https://www.uniprot.org/uniprotkb/Q92800/entry","name":"EZH1","description":"Histone-lysine N-methyltransferase EZH1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45747","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-923794","identifier":"O75530","identifierLink":"https://www.uniprot.org/uniprotkb/O75530/entry","name":"EED","description":"Polycomb protein EED","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10253","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2331","complexName":"MON1-CCZ1 guanyl-nucleotide exchange factor complex","organismName":"Drosophila melanogaster; 7227","description":"Guanyl-nucleotide exchange factor complex with a critical role in maintaining proper vacuole morphology in vacuole delivery pathways by regulating fusion of vesicles with the vacuole at the tethering/docking stage. The complex is activated by membrane-bound Rab5 (Q9V3I2) to facilitate nucleotide exchange of Rab7 (O76742) on membranes. Bulli appears to extend the ability of Mon1-Ccz1 to coordinate the Rab5 to Rab7 transition at endosomes potentially by may providing a docking platform for additional regulators of endosomal trafficking.","predictedComplex":false,"interactors":[{"ac":"EBI-32713579","identifier":"Q9VRX1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VRX1/entry","name":"Bulli","description":"Regulator of MON1-CCZ1 complex","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12897","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32713594","identifier":"Q9VZL5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VZL5/entry","name":"Ccz1","description":"Vacuolar fusion protein CCZ1 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3403501","identifier":"Q9VR38","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VR38/entry","name":"Mon1","description":"Vacuolar fusion protein MON1 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13027","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2332","complexName":"4EHP-GIGYF2 co-translational mRNA decay complex, ZNF598 variant","organismName":"Homo sapiens; 9606","description":"Triggers the co-translational decay of damaged or improperly processed mRNAs and induce decay of mRNAs with disturbed elongation. The E3 ubiquitin ligase ZNF598 acts to recruit 4EHP-GIGYF2 to bind the the mRNA molecules.","predictedComplex":false,"interactors":[{"ac":"EBI-398610","identifier":"O60573","identifierLink":"https://www.uniprot.org/uniprotkb/O60573/entry","name":"EIF4E2","description":"Eukaryotic translation initiation factor 4E type 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-719433","identifier":"Q86UK7","identifierLink":"https://www.uniprot.org/uniprotkb/Q86UK7/entry","name":"ZNF598","description":"E3 ubiquitin-protein ligase ZNF598","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22938","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-765394","identifier":"Q6Y7W6","identifierLink":"https://www.uniprot.org/uniprotkb/Q6Y7W6/entry","name":"GIGYF2","description":"GRB10-interacting GYF protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14445","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2333","complexName":"Mitochondrial calcium uniporter complex","organismName":"Drosophila melanogaster; 7227","description":"Highly selective, inward-rectifying Ca2+ channel located on the inner mitochondrial membrane. The uniporter is quiescent in resting cellular conditions and becomes activated only when local Ca2+ levels rise above approximately 1 microM with the MCU tetramer forming a calcium-conducting pore. Ca2+ uptake is driven by the large negative inner mitochondrial membrane potential generated by proton pumping into the intermembrane space by the electron transport chain.","predictedComplex":false,"interactors":[{"ac":"EBI-154727","identifier":"Q8IQ70","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IQ70/entry","name":"MCU","description":"Calcium uniporter protein, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32713866","identifier":"Q7JX57","identifierLink":"https://www.uniprot.org/uniprotkb/Q7JX57/entry","name":"EMRE","description":"Essential MCU regulator, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR33904","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32713884","identifier":"A2VEI2","identifierLink":"https://www.uniprot.org/uniprotkb/A2VEI2/entry","name":"MICU1","description":"Calcium uptake protein 1 homolog, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32713907","identifier":"A0A0B4KHF1","identifierLink":"https://www.uniprot.org/uniprotkb/A0A0B4KHF1/entry","name":"MICU3","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2334","complexName":"NatA N-alpha-acetyltransferase complex","organismName":"Drosophila melanogaster; 7227","description":"N(alpha)-acetyltransferases responsible for the covalent attachment of an acetyl group (CH3CO) to the free alpha-amino group (NH3+) at the N-terminal end of a polypeptide, one of the most common co-translational modifications. This changes the electrostatic properties of proteins and therefore protein function, stability and localization. NatA co-translationally acetylates N-termini that bear a small amino acid (Ala, Ser, Thr, Cys, and occasionally Val and Gly), which is exposed after methionine cleavage by methionine aminopeptidases.","predictedComplex":false,"interactors":[{"ac":"EBI-133584","identifier":"Q9VT75","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VT75/entry","name":"vnc","description":"N-terminal amino-acid N(alpha)-acetyltransferase NatA","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23091","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-149283","identifier":"Q9VWI2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VWI2/entry","name":"Naa15-16","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2335","complexName":"NatB N-alpha-acetyltransferase complex","organismName":"Drosophila melanogaster; 7227","description":"N(alpha)-acetyltransferases responsible for the covalent attachment of an acetyl group (CH3CO) to the free alpha-amino group (NH3+) at the N-terminal end of a polypeptide, one of the most common co-translational modifications. This changes the electrostatic properties of proteins and therefore protein function, stability and localization. NatB is responsible for the acetylation of methionine-acidic/hydrophilic N-termini (Met-Asp-, Met-Asn-, Met-Glu-, and Met-Gln-). Required for normal cell cycle progression.","predictedComplex":false,"interactors":[{"ac":"EBI-188148","identifier":"Q9VDQ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VDQ7/entry","name":"psidin","description":"Phagocyte signaling-impaired protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32715824","identifier":"M9PI14","identifierLink":"https://www.uniprot.org/uniprotkb/M9PI14/entry","name":"Naa20A","description":"N-alpha-acetyltransferase 20","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45910","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2336","complexName":"4EHP-GIGYF1 co-translational mRNA decay complex, ZNF598 variant","organismName":"Homo sapiens; 9606","description":"Triggers the co-translational decay of damaged or improperly processed mRNAs and induce decay of mRNAs with disturbed elongation. The E3 ubiquitin ligase ZNF598 acts to recruit 4EHP-GIGYF1 to bind the the mRNA molecules.","predictedComplex":false,"interactors":[{"ac":"EBI-398610","identifier":"O60573","identifierLink":"https://www.uniprot.org/uniprotkb/O60573/entry","name":"EIF4E2","description":"Eukaryotic translation initiation factor 4E type 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-719433","identifier":"Q86UK7","identifierLink":"https://www.uniprot.org/uniprotkb/Q86UK7/entry","name":"ZNF598","description":"E3 ubiquitin-protein ligase ZNF598","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22938","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-947774","identifier":"O75420","identifierLink":"https://www.uniprot.org/uniprotkb/O75420/entry","name":"GIGYF1","description":"GRB10-interacting GYF protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14445","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2337","complexName":"CSL-Notch-Mastermind transcriptional activation complex","organismName":"Drosophila melanogaster; 7227","description":"Transcriptional activation complex. Assembles in the nucleus following engagement of a Notch receptor ligand which results in the release of the intracellular portion of Notch (ICN, NICD or Notch-Intra) from the membrane allowing this to translocate to the nucleus. The complex binds to the promoter of genes containing a conserved pair of CSL binding sites in a psuedo-symmetrical head-to-head orientation that are separated by 15-19 base pairs - a Su(H)-paired site or sequence paired site (SPS).","predictedComplex":false,"interactors":[{"ac":"EBI-103438","identifier":"P07207","identifierLink":"https://www.uniprot.org/uniprotkb/P07207/entry","name":"N","description":"Neurogenic locus Notch protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22804","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-496767","identifier":"P21519","identifierLink":"https://www.uniprot.org/uniprotkb/P21519/entry","name":"mam","description":"Neurogenic protein mastermind","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR16431","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-92180","identifier":"P28159","identifierLink":"https://www.uniprot.org/uniprotkb/P28159/entry","name":"Su(H)","description":"Suppressor of hairless protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10665","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2338","complexName":"4EHP-GIGYF2 co-translational mRNA decay complex, DDX6 variant","organismName":"Homo sapiens; 9606","description":"Triggers the co-translational decay of damaged or improperly processed mRNAs and induce decay of mRNAs with disturbed elongation. The RNase helicase DDX6 acts to recruit 4EHP-GIGYF1 to bind the the mRNA molecules.","predictedComplex":false,"interactors":[{"ac":"EBI-351257","identifier":"P26196","identifierLink":"https://www.uniprot.org/uniprotkb/P26196/entry","name":"DDX6","description":"Probable ATP-dependent RNA helicase DDX6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398610","identifier":"O60573","identifierLink":"https://www.uniprot.org/uniprotkb/O60573/entry","name":"EIF4E2","description":"Eukaryotic translation initiation factor 4E type 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-765394","identifier":"Q6Y7W6","identifierLink":"https://www.uniprot.org/uniprotkb/Q6Y7W6/entry","name":"GIGYF2","description":"GRB10-interacting GYF protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14445","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2339","complexName":"MKS complex","organismName":"Drosophila melanogaster; 7227","description":"Plays a key role in establishing the ciliary transition zone (TZ), a structure found at the cilia base. Organises the TZ Y-shaped links which act as part of a selective barrier that prevents diffusion of proteins between the ciliary cytoplasm and cellular cytoplasm and between the ciliary membrane and plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-137534","identifier":"Q9VMH0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VMH0/entry","name":"tctn","description":"Tectonic","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14611","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-157974","identifier":"Q9VF59","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VF59/entry","name":"B9d1","description":"B9 domain-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12968","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32716317","identifier":"M9MRD5","identifierLink":"https://www.uniprot.org/uniprotkb/M9MRD5/entry","name":"B9d2","description":"B9 domain-containing protein 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12968","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32716332","identifier":"A1ZAV1","identifierLink":"https://www.uniprot.org/uniprotkb/A1ZAV1/entry","name":"Cc2d2a","description":"Coiled-coil and C2 domain-containing protein 2A","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR20837","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32716352","identifier":"Q9VYM3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VYM3/entry","name":"Mks1","description":"Tectonic-like complex member Mks1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12968","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2340","complexName":"Male specific lethal complex","organismName":"Drosophila melanogaster; 7227","description":"Site-specific histone acetylation complex required for dosage compensation, increasing the transcription of genes on the single X chromosome in Drosophila males to equal that of both X chromosomes in females. The complex acetylates histone 4 on lysine 16 which hyperactivates genes on the X chromosome.","predictedComplex":false,"interactors":[{"ac":"EBI-138539","identifier":"O02193","identifierLink":"https://www.uniprot.org/uniprotkb/O02193/entry","name":"mof","description":"Histone acetyltransferase MOF","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-155450","identifier":"P50535","identifierLink":"https://www.uniprot.org/uniprotkb/P50535/entry","name":"msl-1","description":"Protein male-specific lethal-1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-175115","identifier":"P24785","identifierLink":"https://www.uniprot.org/uniprotkb/P24785/entry","name":"mle","description":"Dosage compensation regulator mle","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR18934","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-175165","identifier":"P50534","identifierLink":"https://www.uniprot.org/uniprotkb/P50534/entry","name":"msl-2","description":"E3 ubiquitin-protein ligase msl-2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR16048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-273810","identifier":"P50536","identifierLink":"https://www.uniprot.org/uniprotkb/P50536/entry","name":"msl-3","description":"Protein male-specific lethal-3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10880","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32716390","identifier":"URS000007F891_7227","identifierLink":"http://rnacentral.org/rna/URS000007F891_7227","name":"x1_drome_lncrna","description":"Long non-coding RNA on the X 1","stochiometry":null,"interactorType":"long non-coding ribonucleic acid","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-32716831","identifier":"URS00003DAD4B_7227","identifierLink":"http://rnacentral.org/rna/URS00003DAD4B_7227","name":"x2_drome_lncrna","description":"long non-coding RNA on the X 2 (Dmel_CR32665)","stochiometry":null,"interactorType":"nucleic acid","organismName":"Drosophila melanogaster; 7227","xrefs":[]}]},{"complexAC":"CPX-2341","complexName":"NALCN channelosome complex","organismName":"Homo sapiens; 9606","description":"Voltage-gated ion channel responsible for the depolarizing sodium (Na+) leak currents that determine resting Na(+) permeability and control neuronal excitability. Plays a role in the regulation of neuronal excitability, motor function, pain sensitivity, and circadian rhythm.","predictedComplex":false,"interactors":[{"ac":"EBI-1221046","identifier":"Q9P2D8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P2D8/entry","name":"UNC79","description":"Protein unc-79 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21696","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2952637","identifier":"Q8N2C7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N2C7/entry","name":"UNC80","description":"Protein unc-80 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31781","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32716570","identifier":"B1AL88","identifierLink":"https://www.uniprot.org/uniprotkb/B1AL88/entry","name":"NALF1","description":"NALCN channel auxiliary factor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15819","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397435","identifier":"P62158","identifierLink":"https://www.uniprot.org/uniprotkb/P62158/entry","name":"calm_human","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-7085333","identifier":"Q8IZF0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IZF0/entry","name":"NALCN","description":"Sodium leak channel NALCN","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46141","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2342","complexName":"4EHP-GIGYF1 co-translational mRNA decay complex, DDX6 variant","organismName":"Homo sapiens; 9606","description":"Triggers the co-translational decay of damaged or improperly processed mRNAs and induce decay of mRNAs with disturbed elongation. The RNase helicase DDX6 acts to recruit 4EHP-GIGYF1 to bind the the mRNA molecules.","predictedComplex":false,"interactors":[{"ac":"EBI-351257","identifier":"P26196","identifierLink":"https://www.uniprot.org/uniprotkb/P26196/entry","name":"DDX6","description":"Probable ATP-dependent RNA helicase DDX6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398610","identifier":"O60573","identifierLink":"https://www.uniprot.org/uniprotkb/O60573/entry","name":"EIF4E2","description":"Eukaryotic translation initiation factor 4E type 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-947774","identifier":"O75420","identifierLink":"https://www.uniprot.org/uniprotkb/O75420/entry","name":"GIGYF1","description":"GRB10-interacting GYF protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14445","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2343","complexName":"SCF E3 ubiquitin ligase complex, FBXL16 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXL15 target proteins include the  transcriptional regulator of the adaptive response to hypoxia HIF1A (Q16665)","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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The toxin binds to the ganglioside GM1 of the intestinal epithelium leading to  endocytosis by the cell. ctxA1 catalyzes the ADP ribosylation of members of the signaling protein family guanine nucleotide-binding protein G(s) subunit alpha which results in activation of adenylate cyclase..This increases intracellular cAMP levels, which in turn causes an imbalance in electrolyte movement in the epithelial cell.","predictedComplex":false,"interactors":[{"ac":"EBI-1038383","identifier":"P01556","identifierLink":"https://www.uniprot.org/uniprotkb/P01556/entry","name":"ctxB","description":"Cholera enterotoxin subunit B","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961); 243277","xrefs":[]},{"ac":"EBI-32717390","identifier":"P01555-PRO_0000019342","identifierLink":"https://www.uniprot.org/uniprotkb/P01555-PRO_0000019342/entry","name":"ctxA","description":"Cholera enterotoxin subunit A1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961); 243277","xrefs":[]},{"ac":"EBI-32717397","identifier":"P01555-PRO_0000019343","identifierLink":"https://www.uniprot.org/uniprotkb/P01555-PRO_0000019343/entry","name":"ctxA","description":"Cholera enterotoxin subunit A2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961); 243277","xrefs":[]},{"ac":"EBI-32717409","identifier":"CHEBI:57540","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57540","name":"nad(1-)","description":"NAD(1-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2346","complexName":"Non-canonical BRAHMA-associated SWI/SNF ATP-dependent chromatin remodeling complex","organismName":"Drosophila melanogaster; 7227","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure.","predictedComplex":false,"interactors":[{"ac":"EBI-123863","identifier":"Q7K012","identifierLink":"https://www.uniprot.org/uniprotkb/Q7K012/entry","name":"Bap55","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-130188","identifier":"P10987","identifierLink":"https://www.uniprot.org/uniprotkb/P10987/entry","name":"Act5C","description":"Actin-5C","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-132623","identifier":"Q9VF03","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VF03/entry","name":"mor","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32717928","identifier":"A0A0B4KI51","identifierLink":"https://www.uniprot.org/uniprotkb/A0A0B4KI51/entry","name":"Bicra","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15572","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3417869","identifier":"Q9VLX2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VLX2/entry","name":"Brd7-9","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22881","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-75169","identifier":"Q9VYG2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VYG2/entry","name":"Bap60","description":"Brahma-associated protein of 60 kDa","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-868480","identifier":"P25439","identifierLink":"https://www.uniprot.org/uniprotkb/P25439/entry","name":"brm","description":"ATP-dependent helicase brm","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2347","complexName":"NoRC chromatin remodelling complex","organismName":"Drosophila melanogaster; 7227","description":"ATP-dependent nucleosome remodeling complex that represses ribosomal gene transcription. Cooperates with histone chaperones in the assembly and remodeling of chromatin.","predictedComplex":false,"interactors":[{"ac":"EBI-32717961","identifier":"A8DYA3","identifierLink":"https://www.uniprot.org/uniprotkb/A8DYA3/entry","name":"tou","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45915","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-367628","identifier":"Q24368","identifierLink":"https://www.uniprot.org/uniprotkb/Q24368/entry","name":"Iswi","description":"Chromatin-remodeling complex ATPase chain Iswi","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2348","complexName":"HUSH epigenetic repressor complex","organismName":"Homo sapiens; 9606","description":"Mediates epigenetic repression, responsible for position-effect variegation of integrated transgenes in human cells. Recruited to genomic loci rich in H3K9me3, where subsequent recruitment of the histone methyltransferase SETDB1 (Q15047) is required for further H3K9me3 deposition to maintain transcriptional silencing. Acts with MORC2 (Q9Y6X9) to repress LINE-1 class I transposable elements.","predictedComplex":false,"interactors":[{"ac":"EBI-2653928","identifier":"Q99549","identifierLink":"https://www.uniprot.org/uniprotkb/Q99549/entry","name":"MPHOSPH8","description":"M-phase phosphoprotein 8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24166","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-308354","identifier":"Q9UK61","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK61/entry","name":"TASOR","description":"Protein TASOR","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16207","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-474076","identifier":"Q8NEY8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NEY8/entry","name":"PPHLN1","description":"Periphilin-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15836","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2349","complexName":"eIF4E-CYFIP1-FMRP translational repressor complex","organismName":"Homo sapiens; 9606","description":"Represses the translation of specific classes of mRNAs by competing with the binding of eIF4G to m7GTP cap-bound eIF4E on the 5′UTR of mRNA. The complex  is present at synapses and synaptic activity releases CYFIP1 from eIF4E, as well as from bound RNAs, resulting in the alleviation of translation repression. Complex formation increases in presence of the brain cytoplasmic RNA BC1.","predictedComplex":false,"interactors":[{"ac":"EBI-1048143","identifier":"Q7L576","identifierLink":"https://www.uniprot.org/uniprotkb/Q7L576/entry","name":"CYFIP1","description":"Cytoplasmic FMR1-interacting protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12195","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366305","identifier":"Q06787","identifierLink":"https://www.uniprot.org/uniprotkb/Q06787/entry","name":"FMR1","description":"Fragile X messenger ribonucleoprotein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10603","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-73440","identifier":"P06730","identifierLink":"https://www.uniprot.org/uniprotkb/P06730/entry","name":"EIF4E","description":"Eukaryotic translation initiation factor 4E","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-663","complexName":"TP53-MDM4 transcription regulation complex","organismName":"Homo sapiens; 9606","description":"Transcriptional repressor complex, formation of which inhibits the ability of TP53/p53 to induce cell cycle arrest. The mechanism of action is primarily through the binding of MDM4 binds to the p53 transactivation domain.","predictedComplex":false,"interactors":[{"ac":"EBI-366083","identifier":"P04637","identifierLink":"https://www.uniprot.org/uniprotkb/P04637/entry","name":"TP53","description":"Cellular tumor antigen p53","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11447","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398437","identifier":"O15151","identifierLink":"https://www.uniprot.org/uniprotkb/O15151/entry","name":"MDM4","description":"Protein Mdm4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12183","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-664","complexName":"RXRalpha-RXRalpha retinoic acid receptor complex","organismName":"Homo sapiens; 9606","description":"Member of the nuclear receptor family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. Retinoid X nuclear receptors (RXRs) forms transcriptionally active homodimers although their physiological significance is not clear.","predictedComplex":false,"interactors":[{"ac":"EBI-78598","identifier":"P19793","identifierLink":"https://www.uniprot.org/uniprotkb/P19793/entry","name":"RXRA","description":"Retinoic acid receptor RXR-alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-665","complexName":"Follicle-stimulating hormone complex","organismName":"Homo sapiens; 9606","description":"Glycoprotein hormone synthesized and secreted by gonadotropes in the anterior pituitary gland. FSH enables ovarian folliculogenesis to the antral follicle stage and is essential for Sertoli cell proliferation and maintenance of sperm quality in the testis. It acts synergistically with the Luteinizing-stimulating hormone complex (CPX-6097). A member of the family of pituitary glycoprotein hormones that play key roles in human fertility.","predictedComplex":false,"interactors":[{"ac":"EBI-1030645","identifier":"P01225","identifierLink":"https://www.uniprot.org/uniprotkb/P01225/entry","name":"FSHB","description":"Follitropin subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11515","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-718913","identifier":"P01215","identifierLink":"https://www.uniprot.org/uniprotkb/P01215/entry","name":"CGA","description":"Glycoprotein hormones alpha chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11509","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-666","complexName":"RARalpha-NCOA2 activated retinoic acid receptor complex","organismName":"Homo sapiens; 9606","description":"Member of the nuclear receptor (NR) family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. The all-trans retinoic acid receptor (RARA) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including 9-cis retinoic acid receptors (retinoid X receptor, RXRs). Like other NRs, RARA contains DNA-binding and ligand-binding domains (DBD, LBD). In the absence of agonist, the complex recruits the corepressor proteins NCoR or SMRT and associated factors such as histone deacetylases or DNA-methyl transferases that may lead to an inactive condensed chromatin structure, preventing transcription. Upon ligand binding, RARs undergo a conformational change that results in the release of corepressors and transcriptional coactivators, such as NCOA2, are recruited to the LBD which activates transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-413374","identifier":"P10276","identifierLink":"https://www.uniprot.org/uniprotkb/P10276/entry","name":"RARA","description":"Retinoic acid receptor alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-81236","identifier":"Q15596","identifierLink":"https://www.uniprot.org/uniprotkb/Q15596/entry","name":"NCOA2","description":"Nuclear receptor coactivator 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-667","complexName":"RARalpha-NCOA1 activated retinoic acid receptor complex","organismName":"Mus musculus; 10090","description":"Member of the nuclear receptor (NR) family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. The all-trans retinoic acid receptor (Rara) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including 9-cis retinoic acid receptors (retinoid X receptor, RXRs). Like other NRs, Rara contains DNA-binding and ligand-binding domains (DBD, LBD). In the absence of agonist, the complex recruits the corepressor proteins NCoR or SMRT and associated factors such as histone deacetylases or DNA-methyl transferases that may lead to an inactive condensed chromatin structure, preventing transcription. Upon ligand binding, RARs undergo a conformational change that results in the release of corepressors and transcriptional coactivators, such as Ncoa1, are recruited to the LBD which activates transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-11171952","identifier":"P70365","identifierLink":"https://www.uniprot.org/uniprotkb/P70365/entry","name":"Ncoa1","description":"Nuclear receptor coactivator 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-346736","identifier":"P11416","identifierLink":"https://www.uniprot.org/uniprotkb/P11416/entry","name":"Rara","description":"Retinoic acid receptor alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-668","complexName":"RARalpha-NCOA2 activated retinoic acid receptor complex","organismName":"Mus musculus; 10090","description":"Member of the nuclear receptor (NR) family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. The all-trans retinoic acid receptor (Rara) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including 9-cis retinoic acid receptors (retinoid X receptor, RXRs). Like other NRs, Rara contains DNA-binding and ligand-binding domains (DBD, LBD). In the absence of agonist, the complex recruits the corepressor proteins NCoR or SMRT and associated factors such as histone deacetylases or DNA-methyl transferases that may lead to an inactive condensed chromatin structure, preventing transcription. Upon ligand binding, RARs undergo a conformational change that results in the release of corepressors and transcriptional coactivators, such as Ncoa2, are recruited to the LBD which activates transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-346736","identifier":"P11416","identifierLink":"https://www.uniprot.org/uniprotkb/P11416/entry","name":"Rara","description":"Retinoic acid receptor alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-688662","identifier":"Q61026","identifierLink":"https://www.uniprot.org/uniprotkb/Q61026/entry","name":"Ncoa2","description":"Nuclear receptor coactivator 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-670","complexName":"ERF1-ERF3 translation release factor complex, Gspt1 variant","organismName":"Mus musculus; 10090","description":"Required for the termination of protein synthesis which occurs when one of three stop codons (UAA, UAG or UGA) enters the ribosomal A site. Etf1 stimulates GTP binding to Gspt1, inducing the GTPase activity of Gspt1 that couples codon recognition and Etf1 peptidyl-tRNA hydrolysis to ensure rapid and efficient peptide release from the ribosome.","predictedComplex":false,"interactors":[{"ac":"EBI-25820308","identifier":"CHEBI:37565","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:37565","name":"gtp(4-)","description":"GTP(4-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-8322878","identifier":"Q8R050","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R050/entry","name":"Gspt1","description":"Eukaryotic peptide chain release factor GTP-binding subunit ERF3A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8737530","identifier":"Q8BWY3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BWY3/entry","name":"Etf1","description":"Eukaryotic peptide chain release factor subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10113","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-672","complexName":"RXRalpha-RXRalpha retinoic acid receptor complex","organismName":"Mus musculus; 10090","description":"Member of the nuclear receptor family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. Retinoid X nuclear receptors (RXRs) forms transcriptionally active homodimers although their physiological significance is not clear.","predictedComplex":false,"interactors":[{"ac":"EBI-346715","identifier":"P28700","identifierLink":"https://www.uniprot.org/uniprotkb/P28700/entry","name":"Rxra","description":"Retinoic acid receptor RXR-alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-673","complexName":"RXRalpha-VDR nuclear hormone receptor complex","organismName":"Mus musculus; 10090","description":"Member of the nuclear receptor family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. The Vitamin D receptor (Vdr)  mediates the transcriptional effects of Vitamin D and plays a central role in calcium homeostasis. The 9-cis retinoic acid receptor (retinoid X receptor, RXR) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including the all-trans retinoic acid receptor (RAR). Receptors bind to hormone response elements (HREs) via their DNA-binding domains (DBD) and contain a C-terminal ligand-binding domain (LBD) that binds the hormone. Unliganded Vdr can occupy its response elements as a homodimer. Rxra-Vdr is a non-permissive receptor that cannot be activated by an RXR agonist but only by an agonist of the dominant partner receptor, Vdr. Upon binding of ligand, Vdr forms a heterodimer with Rxra through their LBDs and binds to Vitamin D response elements. The ligand for Rxra, 9-cis retinoic acid, has the opposite effect of destabilizing the heterodimeric-DNA complex. \r\n\r\nLooking at RXRbeta-VDR now.","predictedComplex":false,"interactors":[{"ac":"EBI-346715","identifier":"P28700","identifierLink":"https://www.uniprot.org/uniprotkb/P28700/entry","name":"Rxra","description":"Retinoic acid receptor RXR-alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-346797","identifier":"P48281","identifierLink":"https://www.uniprot.org/uniprotkb/P48281/entry","name":"Vdr","description":"Vitamin D3 receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-674","complexName":"Calcineurin-Calmodulin-AKAP5 complex, alpha-R1 variant","organismName":"Homo sapiens; 9606","description":"Calcium-dependent, calmodulin-stimulated protein phosphatase calcineurin in complex with plasma-membrane anchor protein AKAP5. Calcineurin is important for cardiac development and pathophysiology, for nervous-system development and for some of the plastic changes in neurons that are believed to underlie learning and memory. AKAP5 recruits calcineurin to the vicinity of L-type Ca2+ channels for their activation by elevated Ca2+ entering the cell. AKAP5 balances the opposing effects of calcineurin and protein kinase A (PKA) (P17612) on neuronal voltage-gated L-type Ca2+ channels and coordinates the activities of calcineurin, PKA and PKC on a number of other channels and receptors. Despite its atypical PxIxIT calcineurin-recognition motif that confers stronger binding affinity by calcineurin than other substrates it allows for effective disengagement of calcineurin to couple channel activation with downstream signaling events. The calcineurin-AKAP5 complex has been shown to promote NFAT signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-352922","identifier":"Q08209","identifierLink":"https://www.uniprot.org/uniprotkb/Q08209/entry","name":"PPP3CA","description":"Protein phosphatase 3 catalytic subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397435","identifier":"P62158","identifierLink":"https://www.uniprot.org/uniprotkb/P62158/entry","name":"calm_human","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-703640","identifier":"P24588","identifierLink":"https://www.uniprot.org/uniprotkb/P24588/entry","name":"AKAP5","description":"A-kinase anchor protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15182","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-915984","identifier":"P63098","identifierLink":"https://www.uniprot.org/uniprotkb/P63098/entry","name":"PPP3R1","description":"Calcineurin subunit B type 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-676","complexName":"Nascent polypeptide-associated complex","organismName":"Homo sapiens; 9606","description":"Protein chaperone that reversibly binds to cytoplasmic ribosomes. Prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER) by binding to nascent polypeptide chains as they emerge from the ribosome and blocking their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER.","predictedComplex":false,"interactors":[{"ac":"EBI-1054687","identifier":"P20290","identifierLink":"https://www.uniprot.org/uniprotkb/P20290/entry","name":"BTF3","description":"Transcription factor BTF3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712216","identifier":"Q13765","identifierLink":"https://www.uniprot.org/uniprotkb/Q13765/entry","name":"NACA","description":"Nascent polypeptide-associated complex subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-677","complexName":"C5b6 complement complex","organismName":"Homo sapiens; 9606","description":"Involved in the complement system. The complement system is a part of the innate immune system that enhances (complements) the ability of antibodies and phagocytic cells to clear microbes and damaged cells from an organism. The complex is formed after C5 cleavage by C5 convertase into C5a and C5b. C5b has a transient binding site for C6. Without C6 binding, C5b will irreversibly decay to a state incapable of binding C6. The complex initiates pore formation via the sequential recruitment of homologous proteins: C7, C8, and 12-18 copies of C9, each of which comprises a central MAC-perforin domain flanked by auxiliary domains. Activation of the complement system results in formation of membrane attack complexes (MACs), pores that disrupt lipid bilayers and lyse bacteria and other pathogens.","predictedComplex":false,"interactors":[{"ac":"EBI-1753221","identifier":"P13671","identifierLink":"https://www.uniprot.org/uniprotkb/P13671/entry","name":"C6","description":"Complement component C6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25468097","identifier":"P01031-PRO_0000005985","identifierLink":"https://www.uniprot.org/uniprotkb/P01031-PRO_0000005985/entry","name":"C5","description":"Complement C5 beta chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25468103","identifier":"P01031-PRO_0000005989","identifierLink":"https://www.uniprot.org/uniprotkb/P01031-PRO_0000005989/entry","name":"C5","description":"Complement C5b","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-678","complexName":"RXRalpha-LXRbeta nuclear hormone receptor complex","organismName":"Homo sapiens; 9606","description":"Member of the nuclear receptor (NR) family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. Key modulator of macrophage cholesterol homeostasis and immune responses. Liver X receptors (LXR) function as lipid-activated transcription factors that mediate cholesterol, glucose and lipid metabolism and reverse cholesterol transport. The 9-cis retinoic acid receptor (retinoid X receptor, RXR) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including the all-trans retinoic acid receptor (RAR). The effects of ligands on LXR, RXR, and other NRs are mediated through the ligand-binding domain (LBD). RXRA-LXRB is a permissive receptor that can be activated by the ligands of either partner. Upon ligand binding, the LBD undergoes a conformational change that results in the release of corepressors, the recruitment of coactivators, and the activation of transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-745354","identifier":"P55055","identifierLink":"https://www.uniprot.org/uniprotkb/P55055/entry","name":"NR1H2","description":"Oxysterols receptor LXR-beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-78598","identifier":"P19793","identifierLink":"https://www.uniprot.org/uniprotkb/P19793/entry","name":"RXRA","description":"Retinoic acid receptor RXR-alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-679","complexName":"RXRalpha-LXRbeta nuclear hormone receptor complex","organismName":"Mus musculus; 10090","description":"Member of the nuclear receptor (NR) family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. Key modulator of macrophage cholesterol homeostasis and immune responses. Liver X receptors (LXR) function as lipid-activated transcription factors that mediate cholesterol, glucose and lipid metabolism and reverse cholesterol transport. The 9-cis retinoic acid receptor (retinoid X receptor, RXR) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including the all-trans retinoic acid receptor (RAR). The effects of ligands on LXR, RXR, and other NRs are mediated through the ligand-binding domain (LBD). RXRA-LXRB is a permissive receptor that can be activated by the ligands of either partner. Upon ligand binding, the LBD undergoes a conformational change that results in the release of corepressors, the recruitment of coactivators, and the activation of transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-346715","identifier":"P28700","identifierLink":"https://www.uniprot.org/uniprotkb/P28700/entry","name":"Rxra","description":"Retinoic acid receptor RXR-alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5276809","identifier":"Q60644","identifierLink":"https://www.uniprot.org/uniprotkb/Q60644/entry","name":"Nr1h2","description":"Oxysterols receptor LXR-beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-680","complexName":"Exon junction subcomplex MAGOHB-Y14","organismName":"Homo sapiens; 9606","description":"Component of the exon-junction complex (EJC, CPX-1941) that is formed in the nucleus and exported to the cytoplasm as part of the mature messenger ribonucleoprotein particle. Binding of the EJC key regulator PYM1 (Q9BRP8) to MAGOHB-Y14 in the cytoplasm triggers disassembly of the EJC. MAGOHB-Y14 complex remains bound in the same position on the spliced mRNA and requires translation of the mRNA for removal. When interacting with PYM1, associates with mRNA-degradation factors, including the mRNA-decapping complex and exoribonucleases and may play a role in preventing mRNA degradation during mRNA biogenesis. This complex itself does not bind RNA. Binding to IPO13 (O94829) leads to import back into the nucleus prior to reassembly of the EJC.","predictedComplex":false,"interactors":[{"ac":"EBI-447231","identifier":"Q9Y5S9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5S9/entry","name":"RBM8A","description":"RNA-binding protein 8A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-746778","identifier":"Q96A72","identifierLink":"https://www.uniprot.org/uniprotkb/Q96A72/entry","name":"MAGOHB","description":"Protein mago nashi homolog 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12638","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-681","complexName":"Exon junction subcomplex Magohb-Y14","organismName":"Mus musculus; 10090","description":"Component of the exon-junction complex (EJC, CPX-635) that is formed in the nucleus and exported to the cytoplasm as part of the mature messenger ribonucleoprotein particle. Binding of the EJC key regulator Pym1 (Q8CHP5) to Magohb-Y14 in the cytoplasm triggers disassembly of the EJC. Magohb-Y14 complex remains bound in the same position on the spliced mRNA and requires translation of the mRNA for removal. When interacting with Pym1, associates with mRNA-degradation factors, including the mRNA-decapping complex and exoribonucleases and may play a role in preventing mRNA degradation during mRNA biogenesis. This complex itself does not bind RNA. Binding to Ipo13 (Q8K0C1) leads to import back into the nucleus prior to reassembly of the EJC.","predictedComplex":false,"interactors":[{"ac":"EBI-12514027","identifier":"Q9CQL1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQL1/entry","name":"Magohb","description":"Protein mago nashi homolog 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12638","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1993805","identifier":"Q9CWZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CWZ3/entry","name":"Rbm8a","description":"RNA-binding protein 8A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-682","complexName":"Exon junction core complex, MAGOHB variant","organismName":"Homo sapiens; 9606","description":"Plays a role in translation, surveillance and localization of the maturing mRNA molecules. Deposited by spliceosomes at a conserved position of a pre-messenger RNA strand located upstream of exon junctions formed during RNA splicing. The EJC remains stably bound at this position as the mature messenger ribonucleoprotein particle is exported to the cytoplasm, potentially promoting export through its close association with the TREX complex. Binds RNA primarily through EIF4A3, a sequence-independent DEAD box protein that grasps RNA stably only when associated with its partners, RBM8A/Y14 and MAGOHB which inhibit the DEAD-box protein EIF4A3 ATPase activity, trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The EJC core serves as a binding platform for additional factors which together then interface with numerous machineries controlling mRNA export, translation, and decay. Discriminates between premature and normal translation termination events by providing architectural information regarding the position of (former) introns. When translation terminates on an mRNA upstream of at least one EJC, UPF3 (Q9H1J1/Q9BZI7) and its cofactors UPF1 (Q9H1J1) and UPF2 (Q9HAU5) orchestrate a series of events that destabilize the message by a process known as nonsense-mediated mRNA decay (NMD). Also enhances translation of newly synthesized mRNAs through interactions between POLDIP3 (Q9BY77) and activated S6-kinase.","predictedComplex":false,"interactors":[{"ac":"EBI-299104","identifier":"P38919","identifierLink":"https://www.uniprot.org/uniprotkb/P38919/entry","name":"EIF4A3","description":"Eukaryotic initiation factor 4A-III","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47958","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-299118","identifier":"O15234","identifierLink":"https://www.uniprot.org/uniprotkb/O15234/entry","name":"CASC3","description":"Protein CASC3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13434","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-447231","identifier":"Q9Y5S9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5S9/entry","name":"RBM8A","description":"RNA-binding protein 8A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-746778","identifier":"Q96A72","identifierLink":"https://www.uniprot.org/uniprotkb/Q96A72/entry","name":"MAGOHB","description":"Protein mago nashi homolog 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12638","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-683","complexName":"Exon junction core complex, Magohb variant","organismName":"Mus musculus; 10090","description":"Plays a role in translation, surveillance and localization of the maturing mRNA molecules. Deposited by spliceosomes at a conserved position of a pre-messenger RNA strand located upstream of exon junctions formed during RNA splicing. The EJC remains stably bound at this position as the mature messenger ribonucleoprotein particle is exported to the cytoplasm, potentially promoting export through its close association with the TREX complex. Binds RNA primarily through Eif4a3, a sequence-independent DEAD box protein  that grasps RNA stably only when associated with its partners, Rbm8a/Y14 and Magohb which inhibit the DEAD-box protein Eif4a3 ATPase activity, trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The EJC core serves as a binding platform for additional factors which together then interface with numerous machineries controlling mRNA export, translation, and decay. Discriminates between premature and normal translation termination events by providing architectural information regarding the position of (former) introns. When translation terminates on an mRNA upstream of at least one EJC, Upf3 (Q3ULJ3/Q3ULL6) and its cofactors Upf1 (Q9EPU0) and Upf2 (A2AT37) orchestrate a series of events that destabilize the message by a process known as nonsense-mediated mRNA decay (NMD). Also enhances translation of newly synthesized mRNAs through interactions between Poldip3 (Q8BG81)  and activated S6-kinase.","predictedComplex":false,"interactors":[{"ac":"EBI-12507190","identifier":"Q8K3W3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K3W3/entry","name":"Casc3","description":"Protein CASC3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13434","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12514027","identifier":"Q9CQL1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQL1/entry","name":"Magohb","description":"Protein mago nashi homolog 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12638","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1993805","identifier":"Q9CWZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CWZ3/entry","name":"Rbm8a","description":"RNA-binding protein 8A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2552399","identifier":"Q91VC3","identifierLink":"https://www.uniprot.org/uniprotkb/Q91VC3/entry","name":"Eif4a3","description":"Eukaryotic initiation factor 4A-III","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR47958","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-684","complexName":"Mating-type MATalpha2-MATa1 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Transcriptional repressor with a role in determining the three cell types of Saccharomyces cerevisiae: the a and alpha haploid cells and the a/alpha diploid cell type. Binds to a 21-base pair DNA sequence, the haploid-specific gene (hsg) operator, to repress transcription of haploid-specific genes and of MATALPHA1 (P0CY06).","predictedComplex":false,"interactors":[{"ac":"EBI-10443","identifier":"P0CY08","identifierLink":"https://www.uniprot.org/uniprotkb/P0CY08/entry","name":"MATALPHA2","description":"Mating-type protein ALPHA2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11530","identifier":"P0CY11","identifierLink":"https://www.uniprot.org/uniprotkb/P0CY11/entry","name":"HMRA1","description":"Silenced mating-type protein A1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-685","complexName":"c-Myb-C/EBPbeta complex","organismName":"Mus musculus; 10090","description":"A transcriptional regulatory complex. Interactions between c-Myb and the Cebpb homodimer enable or enhance their cooperative binding  and enables Cebpb bound to one site to interact with Myb at another site separated by 80 base pairs. The complex is mainly active in hematopoetic cells and is essential for myeloid differentiation.","predictedComplex":false,"interactors":[{"ac":"EBI-1029979","identifier":"P28033","identifierLink":"https://www.uniprot.org/uniprotkb/P28033/entry","name":"Cebpb","description":"CCAAT/enhancer-binding protein beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366934","identifier":"P06876","identifierLink":"https://www.uniprot.org/uniprotkb/P06876/entry","name":"Myb","description":"Transcriptional activator Myb","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45614","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-686","complexName":"Beta-hexosaminidase B complex","organismName":"Homo sapiens; 9606","description":"Hydrolyses the terminal non-reducing N-acetyl-D-hexosamine residues, such as N-acetylglucosamine and N-acetylgalactosamine, which are beta-linked to oligosaccharides, glycolipids, glycoproteins, and glycosaminoglycans (GAGs). Facilitates the degradation of GAGs in lysosomes of the central and peripheral nervous system. Member of the Family 20 glycoside hydrolases (glycosidase). Active predominantly on water-soluble neutral substrates. \r\n\r\nIntra-lysosomal accumulation of GM2 ganglioside leads to severely debilitating neurodegeneration associated with Sandoff disease.","predictedComplex":false,"interactors":[{"ac":"EBI-7133736","identifier":"P07686","identifierLink":"https://www.uniprot.org/uniprotkb/P07686/entry","name":"HEXB","description":"Beta-hexosaminidase subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22600","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-688","complexName":"NuRF chromatin remodeling complex","organismName":"Homo sapiens; 9606","description":"NuRF is an ATP-dependent chromatin-remodelling  complex with intrinsic nucleosome dependent ATPase activity. Appears to promote ATP-dependent nucleosome sliding and transcription from chromatin templates. The BPTF subunit binds H3K4me3. The complex binds to the promoters of the Engrailed genes, EN1 and EN2 and it may be involved in brain development.","predictedComplex":false,"interactors":[{"ac":"EBI-1560273","identifier":"Q12830","identifierLink":"https://www.uniprot.org/uniprotkb/Q12830/entry","name":"BPTF","description":"Nucleosome-remodeling factor subunit BPTF","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45975","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2822460","identifier":"P28370","identifierLink":"https://www.uniprot.org/uniprotkb/P28370/entry","name":"SMARCA1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352227","identifier":"Q16576","identifierLink":"https://www.uniprot.org/uniprotkb/Q16576/entry","name":"RBBP7","description":"Histone-binding protein RBBP7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-620823","identifier":"Q09028","identifierLink":"https://www.uniprot.org/uniprotkb/Q09028/entry","name":"RBBP4","description":"Histone-binding protein RBBP4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-687","complexName":"Beta-hexosaminidase S complex","organismName":"Homo sapiens; 9606","description":"Hydrolyses the terminal non-reducing N-acetyl-D-hexosamine residues, such as N-acetylglucosamine and N-acetylgalactosamine, which are beta-linked to oligosaccharides, glycolipids, glycoproteins, and glycosaminoglycans (GAGs). Facilitates the degradation of GAGs in lysosomes of the central and peripheral nervous system. Member of the Family 20 glycoside hydrolases (glycosidase). Active on water-soluble and amphiphilic glycoconjugates such as sulfated GAG fragments, and the sulfated glycosphingolipid SM2 (CHEBI:90163).  Works in association with the GM2A protein (P17900) and enhanced by the presence of anionic phospholipids, such as bis(monoacylglycero)phosphate.","predictedComplex":false,"interactors":[{"ac":"EBI-723519","identifier":"P06865","identifierLink":"https://www.uniprot.org/uniprotkb/P06865/entry","name":"HEXA","description":"Beta-hexosaminidase subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22600","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-689","complexName":"Beta-hexosaminidase A complex","organismName":"Mus musculus; 10090","description":"Hydrolyses the terminal non-reducing N-acetyl-D-hexosamine residues, such as N-acetylglucosamine and N-acetylgalactosamine, which are beta-linked to oligosaccharides, glycolipids, glycoproteins, and glycosaminoglycans (GAGs). Facilitates the degradation of GAGs in lysosomes of the central and peripheral nervous system. Member of the Family 20 glycoside hydrolases (glycosidase). Active on water-soluble and amphiphilic glycoconjugates such as sulfated GAG fragments, and the sulfated glycosphingolipid SM2 (CHEBI:90163). Only the heterodimeric complex HEXA is able to remove N-acetylgalactosamine from the ganglioside GM2 (CHEBI:60327), a molecule composed of a glycosphingolipid  with a single sialic acids linked on the sugar chain found in high concentrations in neuronal cell plasma membranes. Works in association with GM2A (Q60648) which extracts single GM2 molecules from membranes and presents them in soluble form to the enzyme.","predictedComplex":false,"interactors":[{"ac":"EBI-4282080","identifier":"P29416","identifierLink":"https://www.uniprot.org/uniprotkb/P29416/entry","name":"Hexa","description":"Beta-hexosaminidase subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22600","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8315763","identifier":"P20060","identifierLink":"https://www.uniprot.org/uniprotkb/P20060/entry","name":"Hexb","description":"Beta-hexosaminidase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22600","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-690","complexName":"Beta-hexosaminidase B complex","organismName":"Mus musculus; 10090","description":"Hydrolyses the terminal non-reducing N-acetyl-D-hexosamine residues, such as N-acetylglucosamine and N-acetylgalactosamine, which are beta-linked to oligosaccharides, glycolipids, glycoproteins, and glycosaminoglycans (GAGs). Facilitates the degradation of GAGs in lysosomes of the central and peripheral nervous system. Member of the Family 20 glycoside hydrolases (glycosidase). Active predominantly on water-soluble neutral substrates.","predictedComplex":false,"interactors":[{"ac":"EBI-8315763","identifier":"P20060","identifierLink":"https://www.uniprot.org/uniprotkb/P20060/entry","name":"Hexb","description":"Beta-hexosaminidase subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22600","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-691","complexName":"Beta-hexosaminidase S complex","organismName":"Mus musculus; 10090","description":"Hydrolyses the terminal non-reducing N-acetyl-D-hexosamine residues, such as N-acetylglucosamine and N-acetylgalactosamine, which are beta-linked to oligosaccharides, glycolipids, glycoproteins, and glycosaminoglycans (GAGs). Facilitates the degradation of GAGs in lysosomes of the central and peripheral nervous system. Member of the Family 20 glycoside hydrolases (glycosidase). Active on water-soluble and amphiphilic glycoconjugates such as sulfated GAG fragments, and the sulfated glycosphingolipid SM2 (CHEBI:90163).  Works in association with the GM2A protein (Q60648) and enhanced by the presence of anionic phospholipids, such as bis(monoacylglycero)phosphate.","predictedComplex":false,"interactors":[{"ac":"EBI-4282080","identifier":"P29416","identifierLink":"https://www.uniprot.org/uniprotkb/P29416/entry","name":"Hexa","description":"Beta-hexosaminidase subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22600","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-692","complexName":"Mating-type MATalpha2-MCM1 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Transcriptional repressor with a role in determining the three cell types of Saccharomyces cerevisiae: the a and alpha haploid cells and the a/alpha diploid cell type. Binds to a 30- or 31-base-pair (bp) a-specific operator DNA, which contains the pseudosymmetric MCM1 16-bp P-box-binding site flanked on either side by alpha2-binding sites, to repress transcription of a-specific genes.","predictedComplex":false,"interactors":[{"ac":"EBI-10443","identifier":"P0CY08","identifierLink":"https://www.uniprot.org/uniprotkb/P0CY08/entry","name":"MATALPHA2","description":"Mating-type protein ALPHA2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10528","identifier":"P11746","identifierLink":"https://www.uniprot.org/uniprotkb/P11746/entry","name":"MCM1","description":"Pheromone receptor transcription factor","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR48019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-693","complexName":"Mating-type MATalpha1-MCM1 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Transcriptional activator with a role in determining the three cell types of Saccharomyces cerevisiae: the a and alpha haploid cells and the a/alpha diploid cell type. Binds P-primeQ promoter elements to activate the expression of alpha-specific genes.","predictedComplex":false,"interactors":[{"ac":"EBI-10438","identifier":"P0CY06","identifierLink":"https://www.uniprot.org/uniprotkb/P0CY06/entry","name":"MATALPHA1","description":"Mating-type protein ALPHA1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-10528","identifier":"P11746","identifierLink":"https://www.uniprot.org/uniprotkb/P11746/entry","name":"MCM1","description":"Pheromone receptor transcription factor","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR48019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-694","complexName":"NuRF chromatin remodeling complex","organismName":"Mus musculus; 10090","description":"NuRF is an ATP-dependent chromatin-remodelling  complex with intrinsic nucleosome dependent ATPase activity. Appears to promote ATP-dependent nucleosome sliding and transcription from chromatin templates. The BPTF subunit binds H3K4me3. The complex binds to the promoters of the Engrailed genes, EN1 and EN2 and it may be involved in brain development.","predictedComplex":false,"interactors":[{"ac":"EBI-11786213","identifier":"Q6PGB8","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PGB8/entry","name":"Smarca1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302291","identifier":"Q60972","identifierLink":"https://www.uniprot.org/uniprotkb/Q60972/entry","name":"Rbbp4","description":"Histone-binding protein RBBP4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302297","identifier":"Q60973","identifierLink":"https://www.uniprot.org/uniprotkb/Q60973/entry","name":"Rbbp7","description":"Histone-binding protein RBBP7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5738095","identifier":"A2A654","identifierLink":"https://www.uniprot.org/uniprotkb/A2A654/entry","name":"Bptf","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45975","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-695","complexName":"Adenylyl cyclase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"An adenylate cyclase complex probably required for an enhanced response of adenylyl cyclase to activated RAS family members. Adenylyl cyclase catalyzes the synthesis of a second messenger, cAMP.","predictedComplex":false,"interactors":[{"ac":"EBI-4024","identifier":"P17555","identifierLink":"https://www.uniprot.org/uniprotkb/P17555/entry","name":"SRV2","description":"Adenylyl cyclase-associated protein","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10652","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5364","identifier":"P08678","identifierLink":"https://www.uniprot.org/uniprotkb/P08678/entry","name":"CYR1","description":"Adenylate cyclase","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR48051","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-696","complexName":"PRMT5 methylosome complex, CLNS1A variant","organismName":"Homo sapiens; 9606","description":"Type II arginine methyltransferase which dimethylates substrate proteins by catalyzing a 2-step transfer of 2 methyl groups from 2 S-adenosyl methionine (SAM) cofactor molecules to substrate arginine residues. CLNS1A recruits the complex to subunits of the spliceosome, SmB/B (P14678), SmD1 (P62314), and SmD2 (P62316), and ribosomal proteins, LSM4 (Q9Y4Z0), LSM10 (Q969L4) and LSM11 (P83369), for methylation thus regulating cellular splicing activity and the formation of RNA processing bodies. Binding to CHTOP (Q9Y3Y2) recruits the methylosome complex to selective sites on the chromosome, where it methylates Histone H4 Arg-3 and activates transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-1237307","identifier":"Q9BQA1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BQA1/entry","name":"WDR77","description":"Methylosome protein WDR77","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46853","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-351098","identifier":"O14744","identifierLink":"https://www.uniprot.org/uniprotkb/O14744/entry","name":"PRMT5","description":"Protein arginine N-methyltransferase 5","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10738","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724693","identifier":"P54105","identifierLink":"https://www.uniprot.org/uniprotkb/P54105/entry","name":"CLNS1A","description":"Methylosome subunit pICln","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21399","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-702","complexName":"PPARgamma-NCOA2 activated nuclear receptor complex","organismName":"Homo sapiens; 9606","description":"Member of the nuclear receptor family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. PPARgamma binds to fatty acids and their metabolites and serves as a key regulator of adipocyte differentation and glucose homeostasis. The effects of ligands on PPARgamma, RXR, and other nuclear receptors are mediated through the ligand-binding domain (LBD). Upon ligand binding, the LBD undergoes a conformational change that results in the release of corepressors, the recruitment of coactivators, such as NCOA2, and the activation of transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-781384","identifier":"P37231","identifierLink":"https://www.uniprot.org/uniprotkb/P37231/entry","name":"PPARG","description":"Peroxisome proliferator-activated receptor gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-81236","identifier":"Q15596","identifierLink":"https://www.uniprot.org/uniprotkb/Q15596/entry","name":"NCOA2","description":"Nuclear receptor coactivator 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-703","complexName":"PPARgamma-NCOA2 activated nuclear receptor complex","organismName":"Mus musculus; 10090","description":"Member of the nuclear receptor family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. PPARgamma binds to fatty acids and their metabolites and serves as a key regulator of adipocyte differentation and glucose homeostasis. The effects of ligands on PPARgamma, RXR, and other nuclear receptors are mediated through the ligand-binding domain (LBD). Upon ligand binding, the LBD undergoes a conformational change that results in the release of corepressors, the recruitment of coactivators (e.g. NCOA2), and the activation of transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-5260705","identifier":"P37238","identifierLink":"https://www.uniprot.org/uniprotkb/P37238/entry","name":"Pparg","description":"Peroxisome proliferator-activated receptor gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-688662","identifier":"Q61026","identifierLink":"https://www.uniprot.org/uniprotkb/Q61026/entry","name":"Ncoa2","description":"Nuclear receptor coactivator 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-704","complexName":"RXRalpha-TRalpha nuclear hormone receptor complex","organismName":"Gallus gallus; 9031","description":"Member of the nuclear receptor family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. Thyroid hormone receptors (TRs) regulate gene expression in response to thyroid hormone, predominantly triiodothyronine, T3. Thyroid hormones are essential for early development and also for metabolic balance. The 9-cis retinoic acid receptor (retinoid X receptor, RXR) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including the all-trans retinoic acid receptor (RAR). Receptors bind to T3 response elements (TREs) via their DNA-binding domains (DBD) and contain a C-terminal ligand-binding domain (LBD) that binds the hormone. Unliganded receptor generally represses basal transcription. RXRA-THRA is a non-permissive receptor that cannot be activated by an RXR agonist but only by an agonist of the dominant partner receptor, THRA. Upon ligand binding, the LBD undergoes a conformational change that results in the release of corepressors, the recruitment of coactivators, and the activation of transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-12683887","identifier":"A0A1D5P2B5","identifierLink":"https://www.uniprot.org/uniprotkb/A0A1D5P2B5/entry","name":"RXRA","description":"Retinoic acid receptor RXR","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-286261","identifier":"P04625","identifierLink":"https://www.uniprot.org/uniprotkb/P04625/entry","name":"THRA","description":"Thyroid hormone receptor alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-706","complexName":"RXRbeta-LXRbeta nuclear hormone receptor complex","organismName":"Mus musculus; 10090","description":"Member of the nuclear receptor (NR) family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. Liver X receptors (LXR) function as transcription factors that mediate cholesterol, glucose and lipid metabolism and reverse cholesterol transport. The 9-cis retinoic acid receptor (retinoid X receptor, RXR) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including the all-trans retinoic acid receptor (RAR). The effects of ligands on LXR, RXR, and other NRs are mediated through the ligand-binding domain (LBD). Upon ligand binding, the LBD undergoes a conformational change that results in the release of corepressors, the recruitment of coactivators, and the activation of transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-5276809","identifier":"Q60644","identifierLink":"https://www.uniprot.org/uniprotkb/Q60644/entry","name":"Nr1h2","description":"Oxysterols receptor LXR-beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6392036","identifier":"P28704","identifierLink":"https://www.uniprot.org/uniprotkb/P28704/entry","name":"Rxrb","description":"Retinoic acid receptor RXR-beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-707","complexName":"CCR4-NOT mRNA deadenylase complex, CNOT6-CNOT7 variant","organismName":"Homo sapiens; 9606","description":"Major cellular mRNA deadenylase complex at least in part by  removing polyA tails that protect mRNA transcripts from degradation. Involved in the regulation of the cell cycle, chromatin modification, activation and inhibition of transcription initiation, control of transcription elongation, RNA export, nuclear RNA surveillance, and DNA damage repair in the nucleus. The CNOT4 ubiquitin ligase only weakly associates with the complex but is required for optimal deadenylation activity by the full CCR4-NOT complex.","predictedComplex":false,"interactors":[{"ac":"EBI-1054261","identifier":"Q9H9A5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H9A5/entry","name":"CNOT10","description":"CCR4-NOT transcription complex subunit 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12979","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1222758","identifier":"A5YKK6","identifierLink":"https://www.uniprot.org/uniprotkb/A5YKK6/entry","name":"CNOT1","description":"CCR4-NOT transcription complex subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13162","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2104458","identifier":"Q9C0C2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9C0C2/entry","name":"TNKS1BP1","description":"182 kDa tankyrase-1-binding protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22042","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2104530","identifier":"Q9ULM6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ULM6/entry","name":"CNOT6","description":"CCR4-NOT transcription complex subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12121","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2105113","identifier":"Q9UIV1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UIV1/entry","name":"CNOT7","description":"CCR4-NOT transcription complex subunit 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10797","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2129291","identifier":"O95628","identifierLink":"https://www.uniprot.org/uniprotkb/O95628/entry","name":"CNOT4","description":"CCR4-NOT transcription complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12603","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2562014","identifier":"Q9UKZ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UKZ1/entry","name":"CNOT11","description":"CCR4-NOT transcription complex subunit 11","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15975","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357079","identifier":"Q92600","identifierLink":"https://www.uniprot.org/uniprotkb/Q92600/entry","name":"CNOT9","description":"CCR4-NOT transcription complex subunit 9","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12262","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743033","identifier":"Q9NZN8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZN8/entry","name":"CNOT2","description":"CCR4-NOT transcription complex subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23326","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743073","identifier":"O75175","identifierLink":"https://www.uniprot.org/uniprotkb/O75175/entry","name":"CNOT3","description":"CCR4-NOT transcription complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23326","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9097897","identifier":"CHEBI:60240","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60240","name":"divalent metal cation","description":"divalent metal cation","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-708","complexName":"RXRalpha-LXRalpha nuclear hormone receptor complex","organismName":"Mus musculus; 10090","description":"Member of the nuclear receptor (NR) family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. Key modulator of macrophage cholesterol homeostasis and immune responses. Liver X receptors (LXR) function as lipid-activated transcription factors that mediate cholesterol, glucose and lipid metabolism and reverse cholesterol transport. The 9-cis retinoic acid receptor (retinoid X receptor, RXR) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including the all-trans retinoic acid receptor (RAR). The effects of ligands on LXR, RXR, and other NRs are mediated through the ligand-binding domain (LBD). RXRA-LXRA is a permissive receptor that can be activated by the ligands of either partner. Upon ligand binding, the LBD undergoes a conformational change that results in the release of corepressors, the recruitment of coactivators, and the activation of transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-346715","identifier":"P28700","identifierLink":"https://www.uniprot.org/uniprotkb/P28700/entry","name":"Rxra","description":"Retinoic acid receptor RXR-alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5276764","identifier":"Q9Z0Y9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0Y9/entry","name":"Nr1h3","description":"Oxysterols receptor LXR-alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-709","complexName":"Piccolo NuA4 histone acetyltransferase complex","organismName":"Homo sapiens; 9606","description":"Histone acetyltransferase complex which is involved in transcriptional activation of selected genes, principally by acetylation of nucleosomal histone H4 and H2A. Also acts as the catalytic core of the NuA4 histone acetyltransferase complex.","predictedComplex":false,"interactors":[{"ac":"EBI-399080","identifier":"Q92993","identifierLink":"https://www.uniprot.org/uniprotkb/Q92993/entry","name":"KAT5","description":"Histone acetyltransferase KAT5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-769270","identifier":"Q9H2F5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H2F5/entry","name":"EPC1","description":"Enhancer of polycomb homolog 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14898","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-769503","identifier":"Q9NXR8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NXR8/entry","name":"ING3","description":"Inhibitor of growth protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-710","complexName":"RXRalpha-TRbeta nuclear hormone receptor complex","organismName":"Mus musculus; 10090","description":"Member of the nuclear receptor family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. Thyroid hormone receptors (TRs) regulate gene expression in response to thyroid hormone, predominantly triiodothyronine, T3. Thyroid hormones are essential for early development and also for metabolic balance. The 9-cis retinoic acid receptor (retinoid X receptor, RXR) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including the all-trans retinoic acid receptor (RAR). Receptors bind to T3 response elements (TREs) via their DNA-binding domains (DBD) and contain a C-terminal ligand-binding domain (LBD) that binds the hormone. Both Thrb isoforms contribute to T3 feedback on thyrotropin-releasing hormone (TRH), with Thrb1 having a more important role in the activation of TRH transcription. Unliganded receptor generally represses basal transcription. Rxra-Thrb is a non-permissive receptor that cannot be activated by an RXR agonist but only by an agonist of the dominant partner receptor, Thrb. Binding of Thrb induces a conformation changes which allosterically silences RXR. Upon ligand binding, the LBD undergoes a conformational change that results in the release of corepressors, the recruitment of coactivators, and the activation of transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-346715","identifier":"P28700","identifierLink":"https://www.uniprot.org/uniprotkb/P28700/entry","name":"Rxra","description":"Retinoic acid receptor RXR-alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6935043","identifier":"P37242","identifierLink":"https://www.uniprot.org/uniprotkb/P37242/entry","name":"Thrb","description":"Thyroid hormone receptor beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-711","complexName":"PPARgamma-NCOA1 activated nuclear receptor complex","organismName":"Homo sapiens; 9606","description":"Member of the nuclear receptor family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. PPARgamma binds to fatty acids and their metabolites and serves as a key regulator of adipocyte differentation and glucose homeostasis. The effects of ligands on PPARgamma, RXR, and other nuclear receptors are mediated through the ligand-binding domain (LBD). Upon ligand binding, the LBD undergoes a conformational change that results in the release of corepressors, the recruitment of coactivators such as NCOA1, and the activation of transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-455189","identifier":"Q15788","identifierLink":"https://www.uniprot.org/uniprotkb/Q15788/entry","name":"NCOA1","description":"Nuclear receptor coactivator 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-781384","identifier":"P37231","identifierLink":"https://www.uniprot.org/uniprotkb/P37231/entry","name":"PPARG","description":"Peroxisome proliferator-activated receptor gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-712","complexName":"Exocyst","organismName":"Caenorhabditis elegans; 6239","description":"Recruited to sites of active exocytosis and membrane expansion, where it mediates the tethering of secretory vesicles to the plasma membrane in preparation for soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein receptor (SNARE)-mediated membrane fusion. Functions with the small GTPase rab-10 to regulate the membrane trafficking of membranes and dendrite proteins from the Golgi and/or endosomal compartments to plasma membrane during dendrite morphogenesis in multi-dendritic PVD sensory neurons. \r\nActs downstream of the small GTPases ral-1 to regulate hypodermal cell migration. Furthermore, together with rab-10 regulates dendrite morphogenesis and anterior-posterior patterning of the PVD neurons dendritic arbor. The targeting of secretory vesicles to the plasma membrane involves direct interactions of the exocyst with PI(4,5)P2. In addition, a number of small GTP-binding proteins interact with components of the exocyst and regulate the assembly, localization, and function of this complex.\r\n\r\nIts involvement in membrane trafficking may be regulated by sur-6 a component of the PP2A-SUR-6 phosphatase complex (CPX-712).","predictedComplex":false,"interactors":[{"ac":"EBI-12518357","identifier":"Q22706","identifierLink":"https://www.uniprot.org/uniprotkb/Q22706/entry","name":"sec-5","description":"Exocyst complex component 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13043","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12518374","identifier":"Q19262","identifierLink":"https://www.uniprot.org/uniprotkb/Q19262/entry","name":"sec-6","description":"Exocyst complex component 3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR21292","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12518389","identifier":"Q95Q35","identifierLink":"https://www.uniprot.org/uniprotkb/Q95Q35/entry","name":"exoc-8","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR21426","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-317149","identifier":"P91149","identifierLink":"https://www.uniprot.org/uniprotkb/P91149/entry","name":"exoc-7","description":"Exocyst complex component 7","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12542","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-318051","identifier":"Q18286","identifierLink":"https://www.uniprot.org/uniprotkb/Q18286/entry","name":"sec-15","description":"Exocyst complex component 6","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12702","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-322886","identifier":"Q20678","identifierLink":"https://www.uniprot.org/uniprotkb/Q20678/entry","name":"sec-3","description":"Exocyst complex component 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR16092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-323526","identifier":"Q18406","identifierLink":"https://www.uniprot.org/uniprotkb/Q18406/entry","name":"sec-10","description":"Exocyst complex component 5","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12100","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-329897","identifier":"Q9XWS2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XWS2/entry","name":"sec-8","description":"Exocyst complex component 4","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR14146","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-713","complexName":"RXRalpha-TRalpha nuclear hormone receptor complex","organismName":"Mus musculus; 10090","description":"Member of the nuclear receptor family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. Thyroid hormone receptors (TRs) regulate gene expression in response to thyroid hormone, predominantly triiodothyronine, T3. Thyroid hormones are essential for early development and also for metabolic balance. The 9-cis retinoic acid receptor (retinoid X receptor, RXR) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including the all-trans retinoic acid receptor (RAR). Receptors bind to T3 response elements (TREs) via their DNA-binding domains (DBD) and contain a C-terminal ligand-binding domain (LBD) that binds the hormone. Unliganded receptor generally represses basal transcription. Rxra-Thra is a non-permissive receptor that cannot be activated by an RXR agonist but only by an agonist of the dominant partner receptor, Thra. Binding of Thra induces a conformation changes which allosterically silences RXR. Upon ligand binding, the LBD undergoes a conformational change that results in the release of corepressors, the recruitment of coactivators, and the activation of transcription. Several alternative splice product of Thra, for example variant alpha-2 (P63058-1), have alternative carboxyl-terminal domains, therefore are not capable of binding T3. Thra alpha-2 is not a functional TR but may act as an inhibitor of thyroid hormone action.","predictedComplex":false,"interactors":[{"ac":"EBI-12518675","identifier":"P63058-2","identifierLink":"https://www.uniprot.org/uniprotkb/P63058-2/entry","name":"Thra","description":"Thyroid hormone receptor alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-346715","identifier":"P28700","identifierLink":"https://www.uniprot.org/uniprotkb/P28700/entry","name":"Rxra","description":"Retinoic acid receptor RXR-alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-715","complexName":"BRCA1-BARD1 complex","organismName":"Homo sapiens; 9606","description":"A ligase complex that catalyses monoubiquitylation of heterologous substrates (especially core nucleosome histones) and Lys-6-linked polyubiquitylation of itself and coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Unusually, autopolyubiquitylation activates its ubiquitin ligase function >20-fold rather than marking the protein for degredation. Plays a central role in the control of the cell cycle in response to DNA damage. \r\n\r\nIs a subcomplex of at least three mutually exclusive complexes: BRCA1-A (CPX-4425), BRCA1-B (CPX-4426) and BRCA1-C (CPX-4441). \r\n\r\nIts E3 ligase activity is required for its tumor suppressor function.","predictedComplex":false,"interactors":[{"ac":"EBI-349905","identifier":"P38398","identifierLink":"https://www.uniprot.org/uniprotkb/P38398/entry","name":"BRCA1","description":"Breast cancer type 1 susceptibility protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13763","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-473181","identifier":"Q99728","identifierLink":"https://www.uniprot.org/uniprotkb/Q99728/entry","name":"BARD1","description":"BRCA1-associated RING domain protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24171","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-716","complexName":"RXRbeta-LXRalpha nuclear hormone receptor complex","organismName":"Homo sapiens; 9606","description":"Member of the nuclear receptor (NR) family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. Liver X receptors (LXR) function as transcription factors that mediate cholesterol, glucose and lipid metabolism and reverse cholesterol transport. The 9-cis retinoic acid receptor (retinoid X receptor, RXR) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including the all-trans retinoic acid receptor (RAR). The effects of ligands on LXR, RXR, and other NRs are mediated through the ligand-binding domain (LBD). Upon ligand binding, the LBD undergoes a conformational change that results in the release of corepressors, the recruitment of coactivators, and the activation of transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-748576","identifier":"P28702","identifierLink":"https://www.uniprot.org/uniprotkb/P28702/entry","name":"RXRB","description":"Retinoic acid receptor RXR-beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-781356","identifier":"Q13133","identifierLink":"https://www.uniprot.org/uniprotkb/Q13133/entry","name":"NR1H3","description":"Oxysterols receptor LXR-alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-717","complexName":"RXRbeta-LXRalpha nuclear hormone receptor complex","organismName":"Mus musculus; 10090","description":"Member of the nuclear receptor (NR) family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. Liver X receptors (LXR) function as transcription factors that mediate cholesterol, glucose and lipid metabolism and reverse cholesterol transport. The 9-cis retinoic acid receptor (retinoid X receptor, RXR) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including the all-trans retinoic acid receptor (RAR). The effects of ligands on LXR, RXR, and other NRs are mediated through the ligand-binding domain (LBD). Upon ligand binding, the LBD undergoes a conformational change that results in the release of corepressors, the recruitment of coactivators, and the activation of transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-5276764","identifier":"Q9Z0Y9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0Y9/entry","name":"Nr1h3","description":"Oxysterols receptor LXR-alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6392036","identifier":"P28704","identifierLink":"https://www.uniprot.org/uniprotkb/P28704/entry","name":"Rxrb","description":"Retinoic acid receptor RXR-beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-718","complexName":"HBO1-4.1 histone acetyltransferase complex","organismName":"Homo sapiens; 9606","description":"Regulates chromatin modification and structure via histone acetylation. The HBO1 complex  is a histone H4-specific acetyltransferase which targets H4K5/8/12 on chromatin and appears to be responsible for the bulk of histone H4 acetylation in vivo. It may also have a reduced activity toward histone H3. 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The complex also acts to direct pre-rRNA folding and rRNA processing through base pairing to the rRNA or flanking precursor sequences.","predictedComplex":false,"interactors":[{"ac":"EBI-12032","identifier":"P39990","identifierLink":"https://www.uniprot.org/uniprotkb/P39990/entry","name":"SNU13","description":"13 kDa ribonucleoprotein-associated protein","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12126","identifier":"Q12499","identifierLink":"https://www.uniprot.org/uniprotkb/Q12499/entry","name":"NOP58","description":"Nucleolar protein 58","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12520674","identifier":"CHEBI:67040","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:67040","name":"s-adenosyl-l-methioninate","description":"S-adenosyl-L-methioninate","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-12521462","identifier":"CHEBI:133335","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:133335","name":"c/d box small nucleolar rnas","description":"C/D box small nucleolar RNAs","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-17148","identifier":"Q12460","identifierLink":"https://www.uniprot.org/uniprotkb/Q12460/entry","name":"NOP56","description":"Nucleolar protein 56","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6838","identifier":"P15646","identifierLink":"https://www.uniprot.org/uniprotkb/P15646/entry","name":"NOP1","description":"rRNA 2'-O-methyltransferase fibrillarin","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10335","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-733","complexName":"MOZ2 histone acetyltransferase complex","organismName":"Homo sapiens; 9606","description":"Regulates chromatin modification and structure via histone acetylation. 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Discovered as a secreted cytokine synthesis inhibitory factor, produced by T helper (Th) 2 cell clones shown to inhibit cytokine production by Th1 cells.\r\n\r\nProduced by both innate and adaptive immune cells including activated Th cells, B cells, keratinocytes, macrophages and monocytes to function as effector and regulatory molecules of the immune system. A pleiotropic cytokine that inhibits cell-mediated immune responses while enhancing humoral immunity. Its primary role is to suppress immune function by blocking the synthesis of proinflammatory cytokines, including IFN-gamma, IL-1, IL-2, IL-3, IL-6, IL-8, IL-12, TNF and GM-CSF in T cells, monocytes, and macrophages, and by inhibiting the expression of cell surface molecules involved in antigen presentation and costimulation. \r\n\r\nPossessing both anti-inflammatory and immunostimulatory properties, it is a highly immunosuppressive cytokine and is frequently dysregulated in many human diseases including cancer, chronic inflammation and HIV. The genetic loss of either IL-10 or the IL-10 receptor results in severe inflammatory bowel disease (IBD).","predictedComplex":false,"interactors":[{"ac":"EBI-1031632","identifier":"P22301","identifierLink":"https://www.uniprot.org/uniprotkb/P22301/entry","name":"IL10","description":"Interleukin-10","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48482","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-736","complexName":"MOZ3 histone acetyltransferase complex","organismName":"Homo sapiens; 9606","description":"Regulates chromatin modification and structure via histone acetylation. The MOZ3 complex  is a histone H4-specific acetyltransferase which acetylates free histones H3, H4, H2A and H2B and has been shown to control expression of HOX genes. The complex  is a strong co-activator of the RUNX transcription factors, the master regulators of hematopoiesis and is required for the development and maintenance of hematopoietic stem cells.","predictedComplex":false,"interactors":[{"ac":"EBI-1753470","identifier":"Q9ULD4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ULD4/entry","name":"BRPF3","description":"Bromodomain and PHD finger-containing protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13793","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-399266","identifier":"Q9HAF1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HAF1/entry","name":"MEAF6","description":"Chromatin modification-related protein MEAF6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-488533","identifier":"Q8WYH8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WYH8/entry","name":"ING5","description":"Inhibitor of growth protein 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-948013","identifier":"Q92794","identifierLink":"https://www.uniprot.org/uniprotkb/Q92794/entry","name":"KAT6A","description":"Histone acetyltransferase KAT6A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-737","complexName":"Box H/ACA ribonucleoprotein complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Pseudouridine synthesis complex that converts uridine into pseudouridine at numerous specific sites within ribosomal RNAs (rRNAs) and spliceosomal small nuclear RNAs (snRNAs), isomerizing the uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine residues may serve to stabilize the conformation of rRNAs.","predictedComplex":false,"interactors":[{"ac":"EBI-12014","identifier":"P32495","identifierLink":"https://www.uniprot.org/uniprotkb/P32495/entry","name":"NHP2","description":"H/ACA ribonucleoprotein complex subunit NHP2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16413110","identifier":"CHEBI:133336","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:133336","name":"h/aca box small nucleolar rna","description":"H/ACA box small nucleolar RNA","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2052475","identifier":"Q6Q547","identifierLink":"https://www.uniprot.org/uniprotkb/Q6Q547/entry","name":"NOP10","description":"H/ACA ribonucleoprotein complex subunit NOP10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4105","identifier":"P33322","identifierLink":"https://www.uniprot.org/uniprotkb/P33322/entry","name":"CBF5","description":"H/ACA ribonucleoprotein complex subunit CBF5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23127","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7321","identifier":"P28007","identifierLink":"https://www.uniprot.org/uniprotkb/P28007/entry","name":"GAR1","description":"H/ACA ribonucleoprotein complex subunit GAR1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23237","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-738","complexName":"MORF1 histone acetyltransferase complex","organismName":"Homo sapiens; 9606","description":"Regulates chromatin modification and structure via histone acetylation. The MORF1 complex  is a histone H4-specific acetyltransferase which acetylates free histones H3, H4, H2A and H2B and has been shown to control expression of HOX genes. The complex  is a strong co-activator of the RUNX transcription factors, the master regulators of hematopoiesis and is required for the development and maintenance of hematopoietic stem cells.","predictedComplex":false,"interactors":[{"ac":"EBI-2837428","identifier":"P55201","identifierLink":"https://www.uniprot.org/uniprotkb/P55201/entry","name":"BRPF1","description":"Peregrin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13793","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-399266","identifier":"Q9HAF1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HAF1/entry","name":"MEAF6","description":"Chromatin modification-related protein MEAF6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-488533","identifier":"Q8WYH8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WYH8/entry","name":"ING5","description":"Inhibitor of growth protein 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-948029","identifier":"Q8WYB5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WYB5/entry","name":"KAT6B","description":"Histone acetyltransferase KAT6B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-739","complexName":"MORF2 histone acetyltransferase complex","organismName":"Homo sapiens; 9606","description":"Regulates chromatin modification and structure via histone acetylation. The MORF2 complex  is a histone H4-specific acetyltransferase which acetylates free histones H3, H4, H2A and H2B and has been shown to control expression of HOX genes. The complex  is a strong co-activator of the RUNX transcription factors, the master regulators of hematopoiesis and is required for the development and maintenance of hematopoietic stem cells.","predictedComplex":false,"interactors":[{"ac":"EBI-399266","identifier":"Q9HAF1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HAF1/entry","name":"MEAF6","description":"Chromatin modification-related protein MEAF6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-488533","identifier":"Q8WYH8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WYH8/entry","name":"ING5","description":"Inhibitor of growth protein 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714754","identifier":"O95696","identifierLink":"https://www.uniprot.org/uniprotkb/O95696/entry","name":"BRD1","description":"Bromodomain-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13793","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-948029","identifier":"Q8WYB5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WYB5/entry","name":"KAT6B","description":"Histone acetyltransferase KAT6B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-740","complexName":"MORF3 histone acetyltransferase complex","organismName":"Homo sapiens; 9606","description":"Regulates chromatin modification and structure via histone acetylation. The MORF3 complex  is a histone H4-specific acetyltransferase which acetylates free histones H3, H4, H2A and H2B and has been shown to control expression of HOX genes. The complex  is a strong co-activator of the RUNX transcription factors, the master regulators of hematopoiesis and is required for the development and maintenance of hematopoietic stem cells.","predictedComplex":false,"interactors":[{"ac":"EBI-1753470","identifier":"Q9ULD4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ULD4/entry","name":"BRPF3","description":"Bromodomain and PHD finger-containing protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13793","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-399266","identifier":"Q9HAF1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HAF1/entry","name":"MEAF6","description":"Chromatin modification-related protein MEAF6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-488533","identifier":"Q8WYH8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WYH8/entry","name":"ING5","description":"Inhibitor of growth protein 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-948029","identifier":"Q8WYB5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WYB5/entry","name":"KAT6B","description":"Histone acetyltransferase KAT6B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-743","complexName":"Transcription factor complex TFIIA","organismName":"Mus musculus; 10090","description":"Transcription factor complex that regulates transcription initiation from RNA polymerase II promoters. Binding to the transcription factor complex TFIID-TBP enhances assembly of the transcriptional preinitiation complex PIC and its binding to the DNA at the TATA-box by displacing transcription inhibitors, such as Drap1 (Q9D6N5) or Dr1 (Q91WV0), from TBP (P29037).","predictedComplex":false,"interactors":[{"ac":"EBI-12523782","identifier":"Q80ZM7","identifierLink":"https://www.uniprot.org/uniprotkb/Q80ZM7/entry","name":"Gtf2a2","description":"Transcription initiation factor IIA subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7640185","identifier":"Q99PM3","identifierLink":"https://www.uniprot.org/uniprotkb/Q99PM3/entry","name":"Gtf2a1","description":"Transcription initiation factor IIA subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12694","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-744","complexName":"c-MYC-BIN1 complex","organismName":"Mus musculus; 10090","description":"Transcriptional suppressor complex. Binding of BIN1 to c-MYC inhibits the transcription factor activity of c-MYC and the complex thus acts as a tumor suppressor.","predictedComplex":false,"interactors":[{"ac":"EBI-1183114","identifier":"P01108","identifierLink":"https://www.uniprot.org/uniprotkb/P01108/entry","name":"Myc","description":"Myc proto-oncogene protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45851","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-775152","identifier":"O08539","identifierLink":"https://www.uniprot.org/uniprotkb/O08539/entry","name":"Bin1","description":"Myc box-dependent-interacting protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46514","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-745","complexName":"RNase H2 complex","organismName":"Homo sapiens; 9606","description":"Specifically degrades the RNA species of RNA:DNA duplexes and removal of ribonucleotides misincorporated in genomic DNA, thus, preventing genomic instability and the accumulation of aberrant nucleic acid. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication.","predictedComplex":false,"interactors":[{"ac":"EBI-9027329","identifier":"Q5TBB1","identifierLink":"https://www.uniprot.org/uniprotkb/Q5TBB1/entry","name":"RNASEH2B","description":"Ribonuclease H2 subunit B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13383","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9027335","identifier":"Q8TDP1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TDP1/entry","name":"RNASEH2C","description":"Ribonuclease H2 subunit C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47063","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9027352","identifier":"O75792","identifierLink":"https://www.uniprot.org/uniprotkb/O75792/entry","name":"RNASEH2A","description":"Ribonuclease H2 subunit A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10954","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-747","complexName":"Piccolo NuA4 histone acetyltransferase complex","organismName":"Mus musculus; 10090","description":"Histone acetyltransferase complex which is involved in transcriptional activation of selected genes, principally by acetylation of nucleosomal histone H4 and H2A. Also acts as the catalytic core of the NuA4 histone acetyltransferase complex.","predictedComplex":false,"interactors":[{"ac":"EBI-1169948","identifier":"Q8CHK4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CHK4/entry","name":"Kat5","description":"Histone acetyltransferase KAT5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942636","identifier":"Q8C9X6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C9X6/entry","name":"Epc1","description":"Enhancer of polycomb homolog 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14898","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942903","identifier":"Q8VEK6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VEK6/entry","name":"Ing3","description":"Inhibitor of growth protein 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-748","complexName":"Chorionic gonadotropin hormone complex","organismName":"Homo sapiens; 9606","description":"Glycoprotein hormone secreted by the placenta during the early weeks of pregnancy. It stimulates the ovarian corpus luteum to produce progesterone until the placenta itself acquires the ability to produce this pregnancy sustaining steroid. A member of the family of pituitary glycoprotein hormones that play key roles in human fertility.","predictedComplex":false,"interactors":[{"ac":"EBI-718913","identifier":"P01215","identifierLink":"https://www.uniprot.org/uniprotkb/P01215/entry","name":"CGA","description":"Glycoprotein hormones alpha chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11509","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8626304","identifier":"P0DN86","identifierLink":"https://www.uniprot.org/uniprotkb/P0DN86/entry","name":"CGB5","description":"Choriogonadotropin subunit beta 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11515","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-757","complexName":"WICH chromatin remodelling complex","organismName":"Homo sapiens; 9606","description":"Chromatin remodeling complex required for maintaining chromatin structure by regulating the spacing of nuclesomes during replication. It is recruited to the replication foci through a direct interaction between the BAZ1B subunit and the DNA clamp PCNA. It opens up chromatin after nucleosome assembly upstream of the replication fork and prevents aberrant heterochromatin formation shortly after DNA replication. The BAZ1B subunit phosphorylates H2A.X Tyr-142 regulating the H2A.X DNA damage response. \r\n\r\nParticularly important during embryonic and neonatal development, especially for craniofacial features.","predictedComplex":false,"interactors":[{"ac":"EBI-352588","identifier":"O60264","identifierLink":"https://www.uniprot.org/uniprotkb/O60264/entry","name":"SMARCA5","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-927482","identifier":"Q9UIG0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UIG0/entry","name":"BAZ1B","description":"Tyrosine-protein kinase BAZ1B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-759","complexName":"TP53-MDM2 transcription regulation complex","organismName":"Homo sapiens; 9606","description":"Transcriptional repressor complex, formation of which inhibits the ability of TP53/p53 to induce cell cycle arrest. The mechanism of action is primarily through the ubiquitinylation of p53, a critical step in mediating its degradation by nuclear and cytoplasmic proteasomes, and by directly inhibiting p53 transactivation capacity and by promoting the nuclear export of p53.","predictedComplex":false,"interactors":[{"ac":"EBI-366083","identifier":"P04637","identifierLink":"https://www.uniprot.org/uniprotkb/P04637/entry","name":"TP53","description":"Cellular tumor antigen p53","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11447","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-389668","identifier":"Q00987","identifierLink":"https://www.uniprot.org/uniprotkb/Q00987/entry","name":"MDM2","description":"E3 ubiquitin-protein ligase Mdm2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46858","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-768","complexName":"Nuclear origin recognition complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Protein complex that binds to origin DNA in an ATP-dependent manner and recruits other essential proteins, such as the initiation factors CDC6 (P09119), Cdt1 (P47112), and the presumptive DNA helicase complex MCM (CPX-2944), to the autonomously replicating sequence (ARS) to form a pre-replicative complex before the initiation of DNA replication that occurs in S phase.","predictedComplex":false,"interactors":[{"ac":"EBI-12568","identifier":"P54784","identifierLink":"https://www.uniprot.org/uniprotkb/P54784/entry","name":"ORC1","description":"Origin recognition complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10763","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12572","identifier":"P32833","identifierLink":"https://www.uniprot.org/uniprotkb/P32833/entry","name":"ORC2","description":"Origin recognition complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14052","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12576","identifier":"P54790","identifierLink":"https://www.uniprot.org/uniprotkb/P54790/entry","name":"ORC3","description":"Origin recognition complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12748","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12580","identifier":"P54791","identifierLink":"https://www.uniprot.org/uniprotkb/P54791/entry","name":"ORC4","description":"Origin recognition complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12087","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12584","identifier":"P50874","identifierLink":"https://www.uniprot.org/uniprotkb/P50874/entry","name":"ORC5","description":"Origin recognition complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12705","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12588","identifier":"P38826","identifierLink":"https://www.uniprot.org/uniprotkb/P38826/entry","name":"ORC6","description":"Origin recognition complex subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-785","complexName":"CHRAC chromatin remodeling complex","organismName":"Homo sapiens; 9606","description":"ATP-dependent chromatin remodeling complex required for efficient DNA replication through highly condensed chromatin. It facilitates this process by mediating the sliding of nucleosomes from an end position to the center of a 248 base pair rDNA without causing major trans displacement of histones.","predictedComplex":false,"interactors":[{"ac":"EBI-2795492","identifier":"Q9NRG0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NRG0/entry","name":"CHRAC1","description":"Chromatin accessibility complex protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10252","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352588","identifier":"O60264","identifierLink":"https://www.uniprot.org/uniprotkb/O60264/entry","name":"SMARCA5","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744901","identifier":"Q9NRF9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NRF9/entry","name":"POLE3","description":"DNA polymerase epsilon subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46172","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-927511","identifier":"Q9NRL2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NRL2/entry","name":"BAZ1A","description":"Bromodomain adjacent to zinc finger domain protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46510","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-787","complexName":"GINS complex","organismName":"Homo sapiens; 9606","description":"Required for the initiation of replication and for replication fork progression, mediating interactions with replication factors. Binds to and enhances the enzymatic function of the MCM helicase (CPX-2940) during the initiation and elongation stages of replication. Core component of the replicative helicase CMG (CPX-4526) complex that serves as the replicative helicase unwinding duplex DNA ahead of moving replication fork during chromosome duplication. Also appears to interact with and stimulate the polymerase activities of DNA polymerase epsilon  complex (CPX-2108) and the DNA polymerase alpha:primase complex (CPX-2087).","predictedComplex":false,"interactors":[{"ac":"EBI-2857315","identifier":"Q9BRX5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BRX5/entry","name":"GINS3","description":"DNA replication complex GINS protein PSF3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22768","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-747491","identifier":"Q9Y248","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y248/entry","name":"GINS2","description":"DNA replication complex GINS protein PSF2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12772","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-747500","identifier":"Q9BRT9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BRT9/entry","name":"GINS4","description":"DNA replication complex GINS protein SLD5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21206","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9019496","identifier":"Q14691","identifierLink":"https://www.uniprot.org/uniprotkb/Q14691/entry","name":"GINS1","description":"DNA replication complex GINS protein PSF1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12914","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-791","complexName":"Talin-1-Vinculin focal adhesion activation complex","organismName":"Homo sapiens; 9606","description":"Plays a crucial role in the assembly and growth of focal adhesions which anchor the cell to the extracellular matrix through transmembrane adhesion receptor integrins and play a central role in cell migration. The assembly of focal adhesions requires the recruitment and activation of vinculin which is is present in the cytoplasm in an autoinhibited conformation with its tail is held in a pincer by its head domains, further stabilized by two high-affinity head-tail interfaces. Vinculin isactivated by talin, modulated by tensile force generated by transient associations with F-actin which leads to release of its head-tail associations.  The complex helps to link integrins to the actomyosin contractile machinery. \r\nBinding of the talin head to integrins regulates their affinity for the extracellular matrix,  maintains integrins in an active conformation and stabilizes the entire focal adhesion structure which contains multiple signalling components.","predictedComplex":false,"interactors":[{"ac":"EBI-2462036","identifier":"Q9Y490","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y490/entry","name":"TLN1","description":"Talin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19981","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-716775","identifier":"P18206","identifierLink":"https://www.uniprot.org/uniprotkb/P18206/entry","name":"VCL","description":"Vinculin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46180","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-793","complexName":"XRCC1 DNA repair complex","organismName":"Homo sapiens; 9606","description":"DNA repair scaffold that supports base excision repair, single strand break repair, and other repair pathways.  sensing of single strand breaks relies primarily on poly(ADP-ribose)polymerase 1 (PARP1)-dependent auto PARylation. The ADP-ribose of PAR polymers mediate recruitment of XRCC1 via binding at its BRCT I domain. DNA end processing; Poly(ADP-ribosylation) results in the recruitment of the XRCC1 complex which converts different types of damaged termini to 3'-hydroxyl and 5'-phosphate termini. POLB removes 5'-deoxyribose phosphate termini during break excision repair, PNKP removes 3'-phosphate and 5'-hydroxyl termini.  APTX removes 5'-AMP during abortive DNA ligation events, and TDP1 can remove a variety of covalent adducts from DNA through hydrolysis of a 3'-phosphodiester bond, giving rise to DNA with a free 3' phosphate. Gap filling. POLB replaces the single missing nucleotide at the SSBs during short-patch repair. The remaining nick is ligated by the LIG3. APLF supports non-homologous end joining and requires binding to XRCC1 for transport into the nucleus.","predictedComplex":false,"interactors":[{"ac":"EBI-1045072","identifier":"Q96T60","identifierLink":"https://www.uniprot.org/uniprotkb/Q96T60/entry","name":"PNKP","description":"Bifunctional polynucleotide phosphatase/kinase","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1256044","identifier":"Q8IW19","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IW19/entry","name":"APLF","description":"Aprataxin and PNK-like factor","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21315","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1753381","identifier":"P49916","identifierLink":"https://www.uniprot.org/uniprotkb/P49916/entry","name":"LIG3","description":"DNA ligase 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45674","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2902553","identifier":"Q9NUW8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NUW8/entry","name":"TDP1","description":"Tyrosyl-DNA phosphodiesterase 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12415","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-713836","identifier":"P06746","identifierLink":"https://www.uniprot.org/uniprotkb/P06746/entry","name":"POLB","description":"DNA polymerase beta","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11276","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-847814","identifier":"Q7Z2E3","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z2E3/entry","name":"APTX","description":"Aprataxin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12486","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-947466","identifier":"P18887","identifierLink":"https://www.uniprot.org/uniprotkb/P18887/entry","name":"XRCC1","description":"DNA repair protein XRCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11370","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-794","complexName":"HBO1-4.1 histone acetyltransferase complex","organismName":"Mus musculus; 10090","description":"Regulates chromatin modification and structure via histone acetylation. The HBO1 complex  is a histone H4-specific acetyltransferase which targets H4K5/8/12 on chromatin and appears to be responsible for the bulk of histone H4 acetylation in vivo. It may also have a reduced activity toward histone H3. The p53 pathway appears to be a main target of the complex, at least in part through direct transcription regulation at the initiation site of p21/CDKN1A.","predictedComplex":false,"interactors":[{"ac":"EBI-3043928","identifier":"Q5SVQ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q5SVQ0/entry","name":"Kat7","description":"Histone acetyltransferase KAT7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3043943","identifier":"Q6ZPI0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6ZPI0/entry","name":"Jade1","description":"Protein Jade-1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13793","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-645598","identifier":"Q8C0D7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C0D7/entry","name":"Ing4","description":"Inhibitor of growth protein 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8338571","identifier":"Q2VPQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q2VPQ9/entry","name":"Meaf6","description":"Chromatin modification-related protein MEAF6","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-795","complexName":"HBO1-4.2 histone acetyltransferase complex","organismName":"Mus musculus; 10090","description":"Regulates chromatin modification and structure via histone acetylation. The HBO1 complex  is a histone H4-specific acetyltransferase which targets H4K5/8/12 on chromatin and appears to be responsible for the bulk of histone H4 acetylation in vivo. It may also have a reduced activity toward histone H3. The p53 pathway appears to be a main target of the complex, at least in part through direct transcription regulation at the initiation site of p21/CDKN1A.","predictedComplex":false,"interactors":[{"ac":"EBI-12553300","identifier":"Q6ZQF7","identifierLink":"https://www.uniprot.org/uniprotkb/Q6ZQF7/entry","name":"Jade2","description":"E3 ubiquitin-protein ligase Jade-2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13793","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3043928","identifier":"Q5SVQ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q5SVQ0/entry","name":"Kat7","description":"Histone acetyltransferase KAT7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-645598","identifier":"Q8C0D7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C0D7/entry","name":"Ing4","description":"Inhibitor of growth protein 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8338571","identifier":"Q2VPQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q2VPQ9/entry","name":"Meaf6","description":"Chromatin modification-related protein MEAF6","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-796","complexName":"HBO1-4.3 histone acetyltransferase complex","organismName":"Mus musculus; 10090","description":"Regulates chromatin modification and structure via histone acetylation. The HBO1 complex  is a histone H4-specific acetyltransferase which targets H4K5/8/12 on chromatin and appears to be responsible for the bulk of histone H4 acetylation in vivo. It may also have a reduced activity toward histone H3. The p53 pathway appears to be a main target of the complex, at least in part through direct transcription regulation at the initiation site of p21/CDKN1A.","predictedComplex":false,"interactors":[{"ac":"EBI-12553408","identifier":"Q6IE82","identifierLink":"https://www.uniprot.org/uniprotkb/Q6IE82/entry","name":"Jade3","description":"Protein Jade-3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13793","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3043928","identifier":"Q5SVQ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q5SVQ0/entry","name":"Kat7","description":"Histone acetyltransferase KAT7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-645598","identifier":"Q8C0D7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C0D7/entry","name":"Ing4","description":"Inhibitor of growth protein 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8338571","identifier":"Q2VPQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q2VPQ9/entry","name":"Meaf6","description":"Chromatin modification-related protein MEAF6","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-797","complexName":"HBO1-5.1 histone acetyltransferase complex","organismName":"Mus musculus; 10090","description":"Regulates chromatin modification and structure via histone acetylation. The HBO1 complex  is a histone H4-specific acetyltransferase which targets H4K5/8/12 on chromatin and appears to be responsible for the bulk of histone H4 acetylation in vivo. It may also have a reduced activity toward histone H3. The p53 pathway appears to be a main target of the complex, at least in part through direct transcription regulation at the initiation site of p21/CDKN1A. HBO1 complexes containing the ING5 subunit play an essential role in DNA replication.","predictedComplex":false,"interactors":[{"ac":"EBI-12553510","identifier":"Q9D8Y8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D8Y8/entry","name":"Ing5","description":"Inhibitor of growth protein 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3043928","identifier":"Q5SVQ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q5SVQ0/entry","name":"Kat7","description":"Histone acetyltransferase KAT7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3043943","identifier":"Q6ZPI0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6ZPI0/entry","name":"Jade1","description":"Protein Jade-1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13793","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8338571","identifier":"Q2VPQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q2VPQ9/entry","name":"Meaf6","description":"Chromatin modification-related protein MEAF6","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-798","complexName":"HBO1-5.2 histone acetyltransferase complex","organismName":"Mus musculus; 10090","description":"Regulates chromatin modification and structure via histone acetylation. The HBO1 complex  is a histone H4-specific acetyltransferase which targets H4K5/8/12 on chromatin and appears to be responsible for the bulk of histone H4 acetylation in vivo. It may also have a reduced activity toward histone H3. The p53 pathway appears to be a main target of the complex, at least in part through direct transcription regulation at the initiation site of p21/CDKN1A. HBO1 complexes containing the Ing5 subunit play an essential role in DNA replication.","predictedComplex":false,"interactors":[{"ac":"EBI-12553300","identifier":"Q6ZQF7","identifierLink":"https://www.uniprot.org/uniprotkb/Q6ZQF7/entry","name":"Jade2","description":"E3 ubiquitin-protein ligase Jade-2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13793","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12553510","identifier":"Q9D8Y8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D8Y8/entry","name":"Ing5","description":"Inhibitor of growth protein 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3043928","identifier":"Q5SVQ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q5SVQ0/entry","name":"Kat7","description":"Histone acetyltransferase KAT7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8338571","identifier":"Q2VPQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q2VPQ9/entry","name":"Meaf6","description":"Chromatin modification-related protein MEAF6","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-799","complexName":"HBO1-5.3 histone acetyltransferase complex","organismName":"Mus musculus; 10090","description":"Regulates chromatin modification and structure via histone acetylation. The HBO1 complex  is a histone H4-specific acetyltransferase which targets H4K5/8/12 on chromatin and appears to be responsible for the bulk of histone H4 acetylation in vivo. It may also have a reduced activity toward histone H3. The p53 pathway appears to be a main target of the complex, at least in part through direct transcription regulation at the initiation site of p21/CDKN1A. HBO1 complexes containing the Ing5 subunit play an essential role in DNA replication.","predictedComplex":false,"interactors":[{"ac":"EBI-12553408","identifier":"Q6IE82","identifierLink":"https://www.uniprot.org/uniprotkb/Q6IE82/entry","name":"Jade3","description":"Protein Jade-3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13793","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12553510","identifier":"Q9D8Y8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D8Y8/entry","name":"Ing5","description":"Inhibitor of growth protein 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3043928","identifier":"Q5SVQ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q5SVQ0/entry","name":"Kat7","description":"Histone acetyltransferase KAT7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8338571","identifier":"Q2VPQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q2VPQ9/entry","name":"Meaf6","description":"Chromatin modification-related protein MEAF6","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-800","complexName":"MOZ1 histone acetyltransferase complex","organismName":"Mus musculus; 10090","description":"Regulates chromatin modification and structure via histone acetylation. The MOZ1 complex  is a histone H4-specific acetyltransferase which acetylates free histones H3, H4, H2A and H2B and has been shown to control expression of HOX genes. The complex  is a strong co-activator of the RUNX transcription factors, the master regulators of hematopoiesis and is required for the development and maintenance of hematopoietic stem cells.","predictedComplex":false,"interactors":[{"ac":"EBI-12553510","identifier":"Q9D8Y8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D8Y8/entry","name":"Ing5","description":"Inhibitor of growth protein 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12553811","identifier":"A0A0N4SUT9","identifierLink":"https://www.uniprot.org/uniprotkb/A0A0N4SUT9/entry","name":"Brpf1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-8338571","identifier":"Q2VPQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q2VPQ9/entry","name":"Meaf6","description":"Chromatin modification-related protein MEAF6","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9662202","identifier":"Q8BZ21","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BZ21/entry","name":"Kat6a","description":"Histone acetyltransferase KAT6A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-801","complexName":"MOZ2 histone acetyltransferase complex","organismName":"Mus musculus; 10090","description":"Regulates chromatin modification and structure via histone acetylation. The MOZ2 complex  is a histone H4-specific acetyltransferase which acetylates free histones H3, H4, H2A and H2B and has been shown to control expression of HOX genes. The complex  is a strong co-activator of the RUNX transcription factors, the master regulators of hematopoiesis and is required for the development and maintenance of hematopoietic stem cells.","predictedComplex":false,"interactors":[{"ac":"EBI-12553510","identifier":"Q9D8Y8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D8Y8/entry","name":"Ing5","description":"Inhibitor of growth protein 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12555449","identifier":"G5E8P1","identifierLink":"https://www.uniprot.org/uniprotkb/G5E8P1/entry","name":"Brd1","description":"Bromodomain-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13793","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8338571","identifier":"Q2VPQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q2VPQ9/entry","name":"Meaf6","description":"Chromatin modification-related protein MEAF6","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9662202","identifier":"Q8BZ21","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BZ21/entry","name":"Kat6a","description":"Histone acetyltransferase KAT6A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-802","complexName":"MOZ3 histone acetyltransferase complex","organismName":"Mus musculus; 10090","description":"Regulates chromatin modification and structure via histone acetylation. The MOZ3 complex  is a histone H4-specific acetyltransferase which acetylates free histones H3, H4, H2A and H2B and has been shown to control expression of HOX genes. The complex  is a strong co-activator of the RUNX transcription factors, the master regulators of hematopoiesis and is required for the development and maintenance of hematopoietic stem cells.","predictedComplex":false,"interactors":[{"ac":"EBI-12553510","identifier":"Q9D8Y8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D8Y8/entry","name":"Ing5","description":"Inhibitor of growth protein 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12553979","identifier":"B2KF05","identifierLink":"https://www.uniprot.org/uniprotkb/B2KF05/entry","name":"Brpf3","description":"Bromodomain and PHD finger-containing protein 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13793","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8338571","identifier":"Q2VPQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q2VPQ9/entry","name":"Meaf6","description":"Chromatin modification-related protein MEAF6","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9662202","identifier":"Q8BZ21","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BZ21/entry","name":"Kat6a","description":"Histone acetyltransferase KAT6A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-803","complexName":"MORF1 histone acetyltransferase complex","organismName":"Mus musculus; 10090","description":"Regulates chromatin modification and structure via histone acetylation. The MORF1 complex  is a histone H4-specific acetyltransferase which acetylates free histones H3, H4, H2A and H2B and has been shown to control expression of HOX genes. The complex  is a strong co-activator of the RUNX transcription factors, the master regulators of hematopoiesis and is required for the development and maintenance of hematopoietic stem cells.","predictedComplex":false,"interactors":[{"ac":"EBI-12553510","identifier":"Q9D8Y8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D8Y8/entry","name":"Ing5","description":"Inhibitor of growth protein 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12553811","identifier":"A0A0N4SUT9","identifierLink":"https://www.uniprot.org/uniprotkb/A0A0N4SUT9/entry","name":"Brpf1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-12555312","identifier":"Q8BRB7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BRB7/entry","name":"Kat6b","description":"Histone acetyltransferase KAT6B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8338571","identifier":"Q2VPQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q2VPQ9/entry","name":"Meaf6","description":"Chromatin modification-related protein MEAF6","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-804","complexName":"MORF3 histone acetyltransferase complex","organismName":"Mus musculus; 10090","description":"Regulates chromatin modification and structure via histone acetylation. The MORF3 complex  is a histone H4-specific acetyltransferase which acetylates free histones H3, H4, H2A and H2B and has been shown to control expression of HOX genes. The complex  is a strong co-activator of the RUNX transcription factors, the master regulators of hematopoiesis and is required for the development and maintenance of hematopoietic stem cells.","predictedComplex":false,"interactors":[{"ac":"EBI-12553510","identifier":"Q9D8Y8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D8Y8/entry","name":"Ing5","description":"Inhibitor of growth protein 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12553979","identifier":"B2KF05","identifierLink":"https://www.uniprot.org/uniprotkb/B2KF05/entry","name":"Brpf3","description":"Bromodomain and PHD finger-containing protein 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13793","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12555312","identifier":"Q8BRB7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BRB7/entry","name":"Kat6b","description":"Histone acetyltransferase KAT6B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8338571","identifier":"Q2VPQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q2VPQ9/entry","name":"Meaf6","description":"Chromatin modification-related protein MEAF6","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-805","complexName":"MORF2 histone acetyltransferase complex","organismName":"Mus musculus; 10090","description":"Regulates chromatin modification and structure via histone acetylation. The MORF2 complex  is a histone H4-specific acetyltransferase which acetylates free histones H3, H4, H2A and H2B and has been shown to control expression of HOX genes. The complex  is a strong co-activator of the RUNX transcription factors, the master regulators of hematopoiesis and is required for the development and maintenance of hematopoietic stem cells.","predictedComplex":false,"interactors":[{"ac":"EBI-12553510","identifier":"Q9D8Y8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D8Y8/entry","name":"Ing5","description":"Inhibitor of growth protein 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12555312","identifier":"Q8BRB7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BRB7/entry","name":"Kat6b","description":"Histone acetyltransferase KAT6B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12555449","identifier":"G5E8P1","identifierLink":"https://www.uniprot.org/uniprotkb/G5E8P1/entry","name":"Brd1","description":"Bromodomain-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13793","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8338571","identifier":"Q2VPQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q2VPQ9/entry","name":"Meaf6","description":"Chromatin modification-related protein MEAF6","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-806","complexName":"Ndc80 complex","organismName":"Caenorhabditis elegans; 6239","description":"Crucial for the stable kinetochore-microtubule attachments that are needed to sustain the centromere tensions involved in achieving proper chromosome alignment in eukaryotic cells. Plays a role in chromosome alignment and microtubule-dependent control of Mad-1/Mad-2 (CPX-402) and dynein complexes at kinetochores, and also chromosome segregation in mitosis and meiosis and spindle checkpoint activity.\r\n\r\nThe complex is recruited to microtubules by kinetochore protein knl-1, which in turn is recruited by knl-3, a component of the MIND complex (CPX-807). Incorrect microtubule binding is controlled by phosphorylation of the ndc-80 subunit by ipl-1/Aurora kinase B. Phosphorylation of ndc-80 reduces the microtubule binding affinity of the complex. Erroneous microtubule-kinetochore attachments are also controlled by the Rzz complex (CPX-810), which interacts with the Ndc80 complex to inhibit irregular microtubule binding. This inhibition is relieved by recruitment of dynein to kinetochores by the coiled-coil protein Spindly/spdl-1.\r\n\r\nSynergistically enhances the affinity of the Ska-1 complex (CPX-811) for microtubules, which may furthermore allow the Ndc80 complex to track depolymerizing microtubules.","predictedComplex":false,"interactors":[{"ac":"EBI-1175834","identifier":"O45406","identifierLink":"https://www.uniprot.org/uniprotkb/O45406/entry","name":"kbp-3","description":"Kinetochore-binding protein 3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-1175844","identifier":"Q9N2X3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9N2X3/entry","name":"kbp-4","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-314429","identifier":"Q17635","identifierLink":"https://www.uniprot.org/uniprotkb/Q17635/entry","name":"ndc-80","description":"Kinetochore protein ndc-80","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10643","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-326288","identifier":"Q21952","identifierLink":"https://www.uniprot.org/uniprotkb/Q21952/entry","name":"him-10","description":"Kinetochore protein Nuf2 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR21650","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-807","complexName":"Kinetochore Mis12 complex","organismName":"Caenorhabditis elegans; 6239","description":"Required for normal chromosome alignment and segregation, kinetochore formation during mitosis, proper kinetochore microtubule attachments and for the spindle assembly checkpoint. The complex plays a role in establishing a bipolar spindle-kinetochore interaction by joining kinetochore subunits contacting DNA to those contacting microtubules. Mis12/MIND is part of a tridentate linker layer, which also contains the Ndc80 complex.\r\n\r\nAlone, the Mis12/MIND complex does not bind to microtubules, but interaction with kinetochore protein knl-1 (P34278) increases the microtubule binding affinity. knl-3 recruits knl-1 to the complex which in turn recruits the Ndc80 complex to microtubules.","predictedComplex":false,"interactors":[{"ac":"EBI-1175918","identifier":"O76406","identifierLink":"https://www.uniprot.org/uniprotkb/O76406/entry","name":"knl-3","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-1175923","identifier":"Q9N3R7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9N3R7/entry","name":"mis-12","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-1175928","identifier":"Q95QB8","identifierLink":"https://www.uniprot.org/uniprotkb/Q95QB8/entry","name":"kbp-1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-1175933","identifier":"Q8MNT1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8MNT1/entry","name":"kbp-2","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]}]},{"complexAC":"CPX-808","complexName":"Knl-1/Mis12/MIND complex","organismName":"Caenorhabditis elegans; 6239","description":"Required for the stable kinetochore-microtubule attachments that are needed to sustain the centromere tensions involved in achieving proper chromosome alignment in eukaryotic cells.\r\n\r\nKinetochore protein knl-1 is essential for the kinetochore-microtubule interactions and increases the microtubule binding affinity of the Mis12 complex to aid in chromosome segregation during meiotic and mitotic cell division. knl-3 recruits knl-1 to the Mis12 complex which in turn recruits the Ndc80 complex to microtubules.","predictedComplex":false,"interactors":[{"ac":"EBI-1175918","identifier":"O76406","identifierLink":"https://www.uniprot.org/uniprotkb/O76406/entry","name":"knl-3","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-1175923","identifier":"Q9N3R7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9N3R7/entry","name":"mis-12","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-1175928","identifier":"Q95QB8","identifierLink":"https://www.uniprot.org/uniprotkb/Q95QB8/entry","name":"kbp-1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-1175933","identifier":"Q8MNT1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8MNT1/entry","name":"kbp-2","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-313751","identifier":"P34278","identifierLink":"https://www.uniprot.org/uniprotkb/P34278/entry","name":"knl-1","description":"Outer kinetochore KNL1 complex subunit knl-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]}]},{"complexAC":"CPX-809","complexName":"NSL histone acetyltransferase complex","organismName":"Homo sapiens; 9606","description":"A histone acetyltransferase complex that catalyzes the acetylation of  histone H4 on lysines 5, 8, and 16 but not on lysine 12. The complex is recruited by phosphorylated  c-Jun to the promoter of its target genes where it then catalyzes  H4K16  acetylation  to  promote  gene transcription and causes the  release of the repressive NuRD complex from c-Jun target genes.  Coordination between the NSL complex and MLL/SET complexes promotes histone H3K4 dimethylation via an acetylation-dependent mechanism, further contributing to gene regulation. The NSL complex also plays an important role in the maintenance of pluripotency factors which indirectly ensure the proper expression of the X chromosome in embryonic stem cells.","predictedComplex":false,"interactors":[{"ac":"EBI-2560802","identifier":"Q9BVI0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BVI0/entry","name":"PHF20","description":"PHD finger protein 20","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15856","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2560840","identifier":"Q9H9L4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H9L4/entry","name":"KANSL2","description":"KAT8 regulatory NSL complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13453","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348259","identifier":"Q96EZ8","identifierLink":"https://www.uniprot.org/uniprotkb/Q96EZ8/entry","name":"MCRS1","description":"Microspherule protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13233","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395317","identifier":"Q9P2N6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P2N6/entry","name":"KANSL3","description":"KAT8 regulatory NSL complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13136","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-396176","identifier":"P51610","identifierLink":"https://www.uniprot.org/uniprotkb/P51610/entry","name":"HCFC1","description":"Host cell factor 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46003","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-539828","identifier":"O15294","identifierLink":"https://www.uniprot.org/uniprotkb/O15294/entry","name":"OGT","description":"UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44366","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-540834","identifier":"P61964","identifierLink":"https://www.uniprot.org/uniprotkb/P61964/entry","name":"WDR5","description":"WD repeat-containing protein 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-740244","identifier":"Q7Z3B3","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z3B3/entry","name":"KANSL1","description":"KAT8 regulatory NSL complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22443","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-896414","identifier":"Q9H7Z6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H7Z6/entry","name":"KAT8","description":"Histone acetyltransferase KAT8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-810","complexName":"RZZ complex","organismName":"Caenorhabditis elegans; 6239","description":"An essential component of the kinetochore required for both meiotic and mitotic spindle assembly checkpoints.  Plays a required role in spindle assembly checkpoint, blocking the metaphase-to-anaphase transition until all chromosomes are properly aligned in a metaphase plate. Targets mdf-2 of the mad-1/mad-2 complex (CPX-402) and also dynein/dynactin to kinetochores via the coiled-coil protein Spindly/spdl-1. This allows for the formation of stable spindle microtubule to kinetochore attachments, which in turn are required for activation of the spindle checkpoint and chromosome segregation. In order to prevent erroneous kinetochore attachments, the Rzz complex also interacts with the Ndc-80 complex (CPX-806) to inhibit the binding of the Ndc80 complex to microtubules. The recruitment of dynein to kinetochores by Spindly/spdl-1 relieves this inhibition.","predictedComplex":false,"interactors":[{"ac":"EBI-12556035","identifier":"Q20849","identifierLink":"https://www.uniprot.org/uniprotkb/Q20849/entry","name":"rod-1","description":"Kinetochore-associated protein rod-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR15688","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12556047","identifier":"Q19642","identifierLink":"https://www.uniprot.org/uniprotkb/Q19642/entry","name":"czw-1","description":"Centromere/kinetochore protein zw10 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12205","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12556063","identifier":"Q95XP9","identifierLink":"https://www.uniprot.org/uniprotkb/Q95XP9/entry","name":"zwl-1","description":"Protein zwilch homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR15995","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-811","complexName":"Ska1 complex","organismName":"Caenorhabditis elegans; 6239","description":"A microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation. The Ska1 complex is a direct component of the kinetochore-microtubule interface and directly associates with microtubules as oligomeric assemblies. The complex tracks with depolymerizing microtubule ends and associates with the microtubule lattice and curved protofilaments, and thus facilitates the processive movement of microspheres along a microtubule in a depolymerization-coupled manner. Synergistically enhances the affinity of the Ndc80 complex (CPX-806) for microtubules, which may furthermore allow the Ndc80 complex to track depolymerizing microtubules.","predictedComplex":false,"interactors":[{"ac":"EBI-329888","identifier":"Q9XWS0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XWS0/entry","name":"ska-1","description":"SKA complex subunit 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR28573","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-329893","identifier":"Q9BI86","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BI86/entry","name":"ska-3","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]}]},{"complexAC":"CPX-812","complexName":"Knl1-Zwint1 complex","organismName":"Caenorhabditis elegans; 6239","description":"Recruits the Rzz (CPX-810) and mad-1/mad-2  (CPX-402) complexes to the outer kinetochore to allow for the formation of stable microtubule and kinetochore attachments during chromosome segregation.","predictedComplex":false,"interactors":[{"ac":"EBI-313751","identifier":"P34278","identifierLink":"https://www.uniprot.org/uniprotkb/P34278/entry","name":"knl-1","description":"Outer kinetochore KNL1 complex subunit knl-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-325730","identifier":"O44956","identifierLink":"https://www.uniprot.org/uniprotkb/O44956/entry","name":"kbp-5","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]}]},{"complexAC":"CPX-813","complexName":"Palmitoyltransferase ERF2-SHR5 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Palmitoyltransferase complex that catalyzes the palmitoylation of proteins through a two step reaction - the autopalmitoylation of the enzyme to create a palmitoyl-ERF2 intermediate followed by the transfer of the palmitoyl moiety to the RAS substrate. Palmitoyl-CoA serves as the palmitate donor.","predictedComplex":false,"interactors":[{"ac":"EBI-2087870","identifier":"P41912","identifierLink":"https://www.uniprot.org/uniprotkb/P41912/entry","name":"SHR5","description":"Ras modification protein ERF4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13254","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-37230","identifier":"Q06551","identifierLink":"https://www.uniprot.org/uniprotkb/Q06551/entry","name":"ERF2","description":"Palmitoyltransferase ERF2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22883","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-815","complexName":"MSL histone acetyltransferase complex","organismName":"Homo sapiens; 9606","description":"Responsible for genome-wide H4K16 acetylation. Important for ATM-dependent cell cycle checkpoint control as well astranscriptional activation of Hox genes in coordination with the H3K4 methyltransferase, MLL. May achieve dosage compensation, equalizing the expression levels of X-chromosomal genes between males and females, by stochastic inactivation of one of the female X chromosomes.","predictedComplex":false,"interactors":[{"ac":"EBI-2560775","identifier":"Q9HCI7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HCI7/entry","name":"MSL2","description":"E3 ubiquitin-protein ligase MSL2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2560796","identifier":"Q8N5Y2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N5Y2/entry","name":"MSL3","description":"MSL complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10880","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2560816","identifier":"Q68DK7","identifierLink":"https://www.uniprot.org/uniprotkb/Q68DK7/entry","name":"MSL1","description":"Male-specific lethal 1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-896414","identifier":"Q9H7Z6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H7Z6/entry","name":"KAT8","description":"Histone acetyltransferase KAT8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-816","complexName":"RXRalpha-RARalpha-NCOA2 retinoic acid receptor complex","organismName":"Homo sapiens; 9606","description":"Member of the nuclear receptor family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. The 9-cis retinoic acid receptor (retinoid X receptor, RXR) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including the all-trans retinoic acid receptor (RAR). RAR and RXR transduce the retinoid signal into a variety of genetic responses, and their functions underlie the essential role played by retinoids in the development and homeostasis of vertebrates. A general model of RAR-RXR-mediated transcription proposes that unliganded RAR-RXR heterodimers are bound to regulatory elements of their target genes and interact with transcriptional repressor complexes such as NCOR/SMRT/SIN3 to recruit histone deacetylases that lead to repression of target gene transcription. Binding of agonist ligand to the nuclear receptor, triggers a conformational change in the ligand binding domain (LBD) with the repositioning of the C-terminal helix H12 creating a binding surface that allow coactivator to bind. Antagonist ligands that prevent the C-terminal helix H12 from adopting its active conformation facilitate the interactions with corepressors.","predictedComplex":false,"interactors":[{"ac":"EBI-413374","identifier":"P10276","identifierLink":"https://www.uniprot.org/uniprotkb/P10276/entry","name":"RARA","description":"Retinoic acid receptor alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-78598","identifier":"P19793","identifierLink":"https://www.uniprot.org/uniprotkb/P19793/entry","name":"RXRA","description":"Retinoic acid receptor RXR-alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-81236","identifier":"Q15596","identifierLink":"https://www.uniprot.org/uniprotkb/Q15596/entry","name":"NCOA2","description":"Nuclear receptor coactivator 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-818","complexName":"RXRalpha-RARalpha-NCOA2 retinoic acid receptor complex","organismName":"Mus musculus; 10090","description":"Member of the nuclear receptor family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. The 9-cis retinoic acid receptor (retinoid X receptor, RXR) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including the all-trans retinoic acid receptor (RAR). RAR and RXR transduce the retinoid signal into a variety of genetic responses, and their functions underlie the essential role played by retinoids in the development and homeostasis of vertebrates. A general model of RAR-RXR-mediated transcription proposes that unliganded RAR-RXR heterodimers are bound to regulatory elements of their target genes and interact with transcriptional repressor complexes such as NCOR/SMRT/SIN3 to recruit histone deacetylases that lead to repression of target gene transcription. Binding of agonist ligand to the nuclear receptor, triggers a conformational change in the ligand binding domain (LBD) with the repositioning of the C-terminal helix H12 creating a binding surface that allow coactivator to bind. Antagonist ligands that prevent the C-terminal helix H12 from adopting its active conformation facilitate the interactions with corepressors.","predictedComplex":false,"interactors":[{"ac":"EBI-346715","identifier":"P28700","identifierLink":"https://www.uniprot.org/uniprotkb/P28700/entry","name":"Rxra","description":"Retinoic acid receptor RXR-alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-346736","identifier":"P11416","identifierLink":"https://www.uniprot.org/uniprotkb/P11416/entry","name":"Rara","description":"Retinoic acid receptor alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-688662","identifier":"Q61026","identifierLink":"https://www.uniprot.org/uniprotkb/Q61026/entry","name":"Ncoa2","description":"Nuclear receptor coactivator 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-821","complexName":"TGF-beta-1 complex","organismName":"Mus musculus; 10090","description":"Cytokine complex that plays an important role in embryogenesis, tissue development, cell proliferation, differentiation and maturation, immune regulation and carcinogenesis. Binding to form its receptor complex CPX-823) results in the phosphorylation of Tgfbr1 on Thr-185 and Thr-186 by the constitutively active Tgfbr2. Activated Tgfbr1 phosphorylates Smad2 (Q62432) which dissociates from the receptor and activates the canonical SMAD-dependent TGF-beta signaling cascade. Plays an important role in bone remodeling as it is a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts.","predictedComplex":false,"interactors":[{"ac":"EBI-12558133","identifier":"P04202-PRO_0000033767","identifierLink":"https://www.uniprot.org/uniprotkb/P04202-PRO_0000033767/entry","name":"Tgfb1","description":"Transforming growth factor beta-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-823","complexName":"TGF-beta-1-TGFR complex","organismName":"Mus musculus; 10090","description":"Cytokine-receptor complex that plays an important role in embryogenesis, tissue development, cell proliferation, differentiation and maturation, immune regulation and carcinogenesis. Binding of Tgfb1 (CPX-821) to its receptor subunits results in the phosphorylation of Tgfbr1 on Thr-185 and Thr-186 by the constitutively active Tgfbr2. Activated Tgfbr1 phosphorylates Smad2 (Q62432) which dissociates from the receptor and activates the canonical SMAD-dependent TGF-beta signaling cascade.","predictedComplex":false,"interactors":[{"ac":"EBI-12558133","identifier":"P04202-PRO_0000033767","identifierLink":"https://www.uniprot.org/uniprotkb/P04202-PRO_0000033767/entry","name":"Tgfb1","description":"Transforming growth factor beta-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-2899332","identifier":"Q62312","identifierLink":"https://www.uniprot.org/uniprotkb/Q62312/entry","name":"Tgfbr2","description":"TGF-beta receptor type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2899393","identifier":"Q64729","identifierLink":"https://www.uniprot.org/uniprotkb/Q64729/entry","name":"Tgfbr1","description":"TGF-beta receptor type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-825","complexName":"TGF-beta-3 complex","organismName":"Mus musculus; 10090","description":"Cytokine complex that plays an important role in embryogenesis, tissue development, cell proliferation, differentiation and maturation, immune regulation and carcinogenesis. Binding to form its receptor complex (CPX-826) results in the phosphorylation of Tgfbr1 on Thr-185 and Thr-186 by the constitutively active Tgfbr2. Activated Tgfbr1 phosphorylates Smad2 (Q62432) which dissociates from the receptor and activates the canonical SMAD-dependent TGF-beta signaling cascade.","predictedComplex":false,"interactors":[{"ac":"EBI-12558414","identifier":"P17125-PRO_0000033799","identifierLink":"https://www.uniprot.org/uniprotkb/P17125-PRO_0000033799/entry","name":"Tgfb3","description":"Transforming growth factor beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-826","complexName":"TGF-beta-3-TGFR complex","organismName":"Mus musculus; 10090","description":"Cytokine-receptor complex that plays an important role in embryogenesis, tissue development, cell proliferation, differentiation and maturation, immune regulation and carcinogenesis. Binding of Tgfb3 (CPX-825) to its receptor subunits results in the phosphorylation of Tgfbr1 on Thr-185 and Thr-186 by the constitutively active Tgfbr2. Activated Tgfbr1 phosphorylates Smad2 (Q62432) which dissociates from the receptor and activates the canonical SMAD-dependent TGF-beta signaling cascade.","predictedComplex":false,"interactors":[{"ac":"EBI-12558414","identifier":"P17125-PRO_0000033799","identifierLink":"https://www.uniprot.org/uniprotkb/P17125-PRO_0000033799/entry","name":"Tgfb3","description":"Transforming growth factor beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-2899332","identifier":"Q62312","identifierLink":"https://www.uniprot.org/uniprotkb/Q62312/entry","name":"Tgfbr2","description":"TGF-beta receptor type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2899393","identifier":"Q64729","identifierLink":"https://www.uniprot.org/uniprotkb/Q64729/entry","name":"Tgfbr1","description":"TGF-beta receptor type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-487","complexName":"uPA-uPAR complex","organismName":"Homo sapiens; 9606","description":"Regulates the activity of the plasminogen activation system, an extracellular proteolytic cascade. uPAR (PLAUR) localizes uPA (PLAU) and its zymogen form, pro-uPA, to the cell surface. Activated uPA cleaves the zymogen plasminogen (P00747), generating the protease plasmin. Plasmin cleaves a range of extra-cellular matrix components, is essential for fibrinolysis, the degradation and clearance of fibrin blood clots, and activates matrix metalloproteases, affecting a number of physiological and disease processes including tumor growth and metastasis, angiogenesis and inflammation. May also mediate the proteolysis-independent signal transduction activation effects of uPA. uPAR is subject to negative-feedback regulation by uPA which cleaves it into an inactive form.","predictedComplex":false,"interactors":[{"ac":"EBI-3905042","identifier":"P00749","identifierLink":"https://www.uniprot.org/uniprotkb/P00749/entry","name":"PLAU","description":"Urokinase-type plasminogen activator","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-716505","identifier":"Q03405","identifierLink":"https://www.uniprot.org/uniprotkb/Q03405/entry","name":"PLAUR","description":"Urokinase plasminogen activator surface receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10624","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-489","complexName":"VAPA-OSBP complex","organismName":"Homo sapiens; 9606","description":"Essential for stimulation of sphingomyelin synthesis by 25-hydroxycholesterol. The complex is formed on the endoplasmic reticulum membrane and acts to tether the membrane to Golgi PI(4)P phosphoinositide molecules or the GTP-binding protein ARF1 (P84077), to promote the specific exchange of lipids from the ER to the Golgi apparatus.","predictedComplex":false,"interactors":[{"ac":"EBI-1059156","identifier":"Q9P0L0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P0L0/entry","name":"VAPA","description":"Vesicle-associated membrane protein-associated protein A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10809","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2681902","identifier":"P22059","identifierLink":"https://www.uniprot.org/uniprotkb/P22059/entry","name":"OSBP","description":"Oxysterol-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10972","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-490","complexName":"bZIP transcription factor complex, JUN-JUN","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The JUN dimer acts as co-activator for a range of transcription factors, e.g. PU.1 (P17947), CEBPB (P17676) and bZIP domain-containing proteins (e.g. complex CPX-486), but is probably not functional on its own.","predictedComplex":false,"interactors":[{"ac":"EBI-852823","identifier":"P05412","identifierLink":"https://www.uniprot.org/uniprotkb/P05412/entry","name":"JUN","description":"Transcription factor Jun","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-491","complexName":"Ercc1-Xpf endonuclease complex","organismName":"Mus musculus; 10090","description":"Structure-specific DNA endonuclease with a role in multiple DNA repair pathways. Participates in nucleotide excision repair mechanism by incising a DNA strand on the 5-prime side of the lesion. The complex is also involved in homologous recombination that assists in removing interstrand cross-links.","predictedComplex":false,"interactors":[{"ac":"EBI-11891313","identifier":"Q9QZD4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9QZD4/entry","name":"Ercc4","description":"DNA repair endonuclease XPF","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10150","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11891361","identifier":"P07903","identifierLink":"https://www.uniprot.org/uniprotkb/P07903/entry","name":"Ercc1","description":"DNA excision repair protein ERCC-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12749","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-492","complexName":"Vitronectin-PAI-1 complex","organismName":"Mus musculus; 10090","description":"Regulates the activity of the plasminogen activation system, an extracellular proteolytic cascade. Vitronectin binding extends the lifetime of active Pai-1, by slowing its transition to an inactive latent form, thus directly influencing angiogenesis and affecting cell adhesion and motility. Inhibits fibrinolysis, the breakdown of the fibrin clot which is the product of coagulation, transition to the inactive latent form.","predictedComplex":false,"interactors":[{"ac":"EBI-490898","identifier":"P22777","identifierLink":"https://www.uniprot.org/uniprotkb/P22777/entry","name":"Serpine1","description":"Plasminogen activator inhibitor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11461","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8354207","identifier":"P29788","identifierLink":"https://www.uniprot.org/uniprotkb/P29788/entry","name":"Vtn","description":"Vitronectin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22917","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-494","complexName":"tPA-PAI-1 complex","organismName":"Homo sapiens; 9606","description":"Regulates the activity of the plasminogen activation system, an extracellular proteolytic cascade. Inhibited form of tissue plasminogen activator tPA (PLAT), an enzyme responsible for the cleavage of plasminogen (P00747) to form plasmin, which then degrades fibrin. PAI-1 (SERPINE1) inhibits tPA rapidly and irreversibly and is the primary negative regulator of the fibrinolytic system. High levels of PAI-1 therefore prevent formation of plasmin, resulting in fibrin accumulation and thrombosis.","predictedComplex":false,"interactors":[{"ac":"EBI-5605520","identifier":"P00750","identifierLink":"https://www.uniprot.org/uniprotkb/P00750/entry","name":"PLAT","description":"Tissue-type plasminogen activator","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-953978","identifier":"P05121","identifierLink":"https://www.uniprot.org/uniprotkb/P05121/entry","name":"SERPINE1","description":"Plasminogen activator inhibitor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11461","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-495","complexName":"uPA-PAI-1 complex","organismName":"Mus musculus; 10090","description":"Regulates the activity of the plasminogen activation system, an extracellular proteolytic cascade. Inhibited form of urokinase plasminogen activator uPA (Plau), an enzyme responsible for the cleavage of plasminogen (P20918) to form plasmin. Formation of the complex plays a crucial role in fibrinolysis, cell adhesion and migration and tissue remodeling including tumor progression and metastasis.","predictedComplex":false,"interactors":[{"ac":"EBI-490898","identifier":"P22777","identifierLink":"https://www.uniprot.org/uniprotkb/P22777/entry","name":"Serpine1","description":"Plasminogen activator inhibitor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11461","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8365661","identifier":"P06869","identifierLink":"https://www.uniprot.org/uniprotkb/P06869/entry","name":"Plau","description":"Urokinase-type plasminogen activator","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-496","complexName":"RXRalpha-PXR nuclear receptor complex","organismName":"Homo sapiens; 9606","description":"Member of the nuclear receptor (NR) family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in metabolism. The pregnane X receptor (NR1I2/PXR) is a central xenobiotic sensor that detects potentially toxic chemicals and regulates the expression of genes central to their breakdown and removal. NR1I2 binds as a heterodimer with the 9-cis retinoic acid receptor (RXRA) to xenobiotic response elements in cytochrome P450 3A (CYP3A) gene promoters and is activated by the spectrum of chemicals that are known to induce CYP3A gene expression. Like other NRs, RXRA and NR1I2 contain DNA-binding and ligand-binding domain (DBD, LBD). Upon ligand binding, corepressors dissociate from RXRA and transcriptional coactivators, such as NCOA1 (Q15788), are recruited leading to transcriptional activation.","predictedComplex":false,"interactors":[{"ac":"EBI-3905991","identifier":"O75469","identifierLink":"https://www.uniprot.org/uniprotkb/O75469/entry","name":"NR1I2","description":"Nuclear receptor subfamily 1 group I member 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-78598","identifier":"P19793","identifierLink":"https://www.uniprot.org/uniprotkb/P19793/entry","name":"RXRA","description":"Retinoic acid receptor RXR-alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-497","complexName":"Menin-JUND transcription inhibition complex","organismName":"Homo sapiens; 9606","description":"Transcription inhibitor complex. Menin binds the Jun family transcription factor JUND and blocks JNK kinase-mediated JUND phosphorylation, thereby inhibiting transcriptional activation.","predictedComplex":false,"interactors":[{"ac":"EBI-2682803","identifier":"P17535","identifierLink":"https://www.uniprot.org/uniprotkb/P17535/entry","name":"JUND","description":"Transcription factor JunD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-592789","identifier":"O00255","identifierLink":"https://www.uniprot.org/uniprotkb/O00255/entry","name":"MEN1","description":"Menin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12693","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-499","complexName":"Catenin-Cadherin complex","organismName":"Caenorhabditis elegans; 6239","description":"Adherens junction component that regulates cell-cell adhesion during development and specifically during tissue organization. Important for gastrulation, ventral enclosure and embryonic elongation.","predictedComplex":false,"interactors":[{"ac":"EBI-11891915","identifier":"P90947","identifierLink":"https://www.uniprot.org/uniprotkb/P90947/entry","name":"hmp-1","description":"Alpha-catenin-like protein hmp-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR18914","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2528888","identifier":"Q967F4","identifierLink":"https://www.uniprot.org/uniprotkb/Q967F4/entry","name":"hmr-1","description":"Cadherin-related hmr-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-317320","identifier":"O44326","identifierLink":"https://www.uniprot.org/uniprotkb/O44326/entry","name":"hmp-2","description":"Beta-catenin-like protein hmp-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45976","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-498","complexName":"Slx4-Terf2 complex","organismName":"Mus musculus; 10090","description":"Role in maintaining an average equilibrium telomere length thus preventing telomere overlengthening. Trf2 binds to telomeric DNA and functions as a measuring device to assess telomere length. Longer telomeres are bound by larger amount of Trf2, which subsequently recruits more Slx4 to telomeres. The double-layered Slx4-Trf2 platform then assembles a nuclease toolkit at telomeres for homologous-recombination-mediated telomere recombination, including telomere sister chromatid exchange and resolution of the t-loop formed by the 3-prime single-stranded overhang, base-pairing with the C-strand of the duplex region of telomeric DNAs.","predictedComplex":false,"interactors":[{"ac":"EBI-11891941","identifier":"Q6P1D7","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P1D7/entry","name":"Slx4","description":"Structure-specific endonuclease subunit SLX4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21541","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6919263","identifier":"O35144","identifierLink":"https://www.uniprot.org/uniprotkb/O35144/entry","name":"Terf2","description":"Telomeric repeat-binding factor 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46833","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-500","complexName":"Interleukin-5 complex","organismName":"Homo sapiens; 9606","description":"Powerful pro-inflammatory cytokine produced by T-helper type 2 (Th2) cells, Mast cells, Eosinophils and Natural killer (NK, NKT) cells. Essential for the maturation of eosinophils in the bone marrow and their release into the blood. Also acts on activated and resting B-cells to induce immunoglobulin production, growth, and differentiation.\r\n\r\nExerts a pathogenic role in the differentiation, recruitment, survival, and degranulation of eosinophils. Overactive IL-5 is implicated in the pathogenesis of allergic inflammatory diseases, such as asthma, and various hypereosinophilic diseases.","predictedComplex":false,"interactors":[{"ac":"EBI-2435811","identifier":"P05113","identifierLink":"https://www.uniprot.org/uniprotkb/P05113/entry","name":"IL5","description":"Interleukin-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48491","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-501","complexName":"uPA-uPAR-vitronectin complex","organismName":"Homo sapiens; 9606","description":"Links proteolytic degradation of the extracellular matrix to integrin-mediated adhesion. The formation of this complex results in altered cell adhesion, migration, survival and proliferation. Components of the plasminogen activation system including urokinase plasminogen activator uPA (PLAU) and its cell surface receptor uPAR (PLAUR) have been implicated in a wide variety of biological processes related to tissue homoeostasis. The high affinity binding of uPA regulates the binding of uPAR to matrix-embedded vitronectin. Activated uPA cleaves the zymogen plasminogen, generating the protease plasmin. uPA and plasmin induces a potent negative feedback on cell adhesion through specific cleavage of the RGD motif in vitronectin. Cleavage of vitronectin by uPA requires concomitant binding of both uPA and vitronectin to uPAR.","predictedComplex":false,"interactors":[{"ac":"EBI-1036653","identifier":"P04004","identifierLink":"https://www.uniprot.org/uniprotkb/P04004/entry","name":"VTN","description":"Vitronectin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22917","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3905042","identifier":"P00749","identifierLink":"https://www.uniprot.org/uniprotkb/P00749/entry","name":"PLAU","description":"Urokinase-type plasminogen activator","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-716505","identifier":"Q03405","identifierLink":"https://www.uniprot.org/uniprotkb/Q03405/entry","name":"PLAUR","description":"Urokinase plasminogen activator surface receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10624","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-502","complexName":"Beta-hexosaminidase A complex","organismName":"Homo sapiens; 9606","description":"Hydrolyses the terminal non-reducing N-acetyl-D-hexosamine residues, such as N-acetylglucosamine and N-acetylgalactosamine, which are beta-linked to oligosaccharides, glycolipids, glycoproteins, and glycosaminoglycans (GAGs). Facilitates the degradation of GAGs in lysosomes of the central and peripheral nervous system. Member of the Family 20 glycoside hydrolases (glycosidase). Active on water-soluble and amphiphilic glycoconjugates such as sulfated GAG fragments, and the sulfated glycosphingolipid SM2 (CHEBI:90163). Only the heterodimeric complex HEX A is able to remove N-acetylgalactosamine from the ganglioside GM2 (CHEBI:60327), a molecule composed of a glycosphingolipid  with a single sialic acids linked on the sugar chain found in high concentrations in neuronal cell plasma membranes. Works in association with the GM2A (P17900) which extracts single GM2 molecules from membranes and presents them in soluble form to the enzyme or hydrolyses sulphated, membrane-bound substrates. \r\n\r\nIntra-lysosomal accumulation of GM2 ganglioside leads to severely debilitating neurodegeneration associated with Tay-Sachs disease, Sandoff disease and AB variant.","predictedComplex":false,"interactors":[{"ac":"EBI-7133736","identifier":"P07686","identifierLink":"https://www.uniprot.org/uniprotkb/P07686/entry","name":"HEXB","description":"Beta-hexosaminidase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22600","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-723519","identifier":"P06865","identifierLink":"https://www.uniprot.org/uniprotkb/P06865/entry","name":"HEXA","description":"Beta-hexosaminidase subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22600","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-503","complexName":"mTORC1 complex","organismName":"Homo sapiens; 9606","description":"Serine/threonine protein kinase complex that regulates cellular metabolism, growth and survival in response to hormones, growth factors, nutrients, energy and stress signals by way of, directly or indirectly, affecting the phosphorylation of at least 800 proteins. Key pathways regulated by mTORC1 include: protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis; pyrimidine biosynthesis pathway; ribosome synthesis by activating RNA polymerase III-dependent transcription; lipid synthesis; mitochondrial biogenesis to maintain energy homeostasis; negative regulation of autophagy; feedback control on upstream growth factor signaling; regulation of microtubules. Inactivated by Rapamycin, stress and starvation, which, consequently, induces autophagy and ensures that cells grow only during favourable conditions. mTORC1 plays a role in cancer and obesity. Subcellular localization varies and may ensure precise spatial and temporal control of cell growth.","predictedComplex":false,"interactors":[{"ac":"EBI-1387471","identifier":"Q9BVC4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BVC4/entry","name":"MLST8","description":"Target of rapamycin complex subunit LST8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1567928","identifier":"Q8N122","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N122/entry","name":"RPTOR","description":"Regulatory-associated protein of mTOR","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12848","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359260","identifier":"P42345","identifierLink":"https://www.uniprot.org/uniprotkb/P42345/entry","name":"MTOR","description":"Serine/threonine-protein kinase mTOR","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-504","complexName":"c-Myb-C/EBPbeta complex","organismName":"Homo sapiens; 9606","description":"A transcriptional regulatory complex. Interactions between c-Myb and the Cebpb homodimer enable or enhance their cooperative binding  and enables CEBPB bound to one site to interact with MYB at another site separated by 80 base pairs. The complex is mainly active in hematopoetic cells and is essential for myeloid differentiation.","predictedComplex":false,"interactors":[{"ac":"EBI-298355","identifier":"P10242","identifierLink":"https://www.uniprot.org/uniprotkb/P10242/entry","name":"MYB","description":"Transcriptional activator Myb","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45614","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-969696","identifier":"P17676","identifierLink":"https://www.uniprot.org/uniprotkb/P17676/entry","name":"CEBPB","description":"CCAAT/enhancer-binding protein beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-505","complexName":"RXRalpha-PXR nuclear receptor complex","organismName":"Mus musculus; 10090","description":"Member of the nuclear receptor (NR) family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in metabolism. The pregnane X receptor (Nr1i2/Pxr) is a central xenobiotic sensor that detects potentially toxic chemicals and regulates the expression of genes central to their breakdown and removal. Nr1i2 binds as a heterodimer with the 9-cis retinoic acid receptor (Rxra) to xenobiotic response elements in cytochrome P450 3A (CYP3A) gene promoters and is activated by the spectrum of chemicals that are known to induce CYP3A gene expression. Like other NRs, Rxra and Nr1i2 contain DNA-binding and ligand-binding domain (DBD, LBD). Upon ligand binding, corepressors dissociate from Rxra and transcriptional coactivators, such as Ncoa1 (P70365), are recruited leading to transcriptional activation.","predictedComplex":false,"interactors":[{"ac":"EBI-11892436","identifier":"O54915","identifierLink":"https://www.uniprot.org/uniprotkb/O54915/entry","name":"Nr1i2","description":"Nuclear receptor subfamily 1 group I member 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-346715","identifier":"P28700","identifierLink":"https://www.uniprot.org/uniprotkb/P28700/entry","name":"Rxra","description":"Retinoic acid receptor RXR-alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-506","complexName":"Interleukin-5 receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Transmembrane complex formed on the binding of a dimeric, extracellular interleukin (IL-5) to its receptor, IL-5R, a Class I hematopoietin receptor.  Ligand binding results in the assembly of the complete complex, inducing the transphosphorylation of JAK1/2 molecules as well as phosphorylation of the cytoplasmic tails of the receptors. STAT1/5 monomers bind to the phosphorylated site of the receptor and are phosphorylated by JAK1/2. Phosphorylated STAT1/5 dissociate from the receptors, dimerize, and translocate into the nucleus where they induce the transcription of target genes.\r\n\r\n\r\nIL-5 is a powerful pro-inflammatory cytokine produced by T-helper type 2 cells, mast cells, eosinophils, and natural killer T-cells. Essential for the maturation of eosinophils in the bone marrow and their release into the blood. Also acts on activated and resting B-cells to induce immunoglobulin production, growth, and differentiation. Overactive IL-5 is implicated in the pathogenesis of allergic inflammatory diseases, such as asthma, and various hypereosinophilic diseases.","predictedComplex":false,"interactors":[{"ac":"EBI-1383438","identifier":"P23458","identifierLink":"https://www.uniprot.org/uniprotkb/P23458/entry","name":"JAK1","description":"Tyrosine-protein kinase JAK1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45807","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1383454","identifier":"P29597","identifierLink":"https://www.uniprot.org/uniprotkb/P29597/entry","name":"TYK2","description":"Non-receptor tyrosine-protein kinase TYK2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45807","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1759442","identifier":"Q01344","identifierLink":"https://www.uniprot.org/uniprotkb/Q01344/entry","name":"IL5RA","description":"Interleukin-5 receptor subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1809771","identifier":"P32927","identifierLink":"https://www.uniprot.org/uniprotkb/P32927/entry","name":"CSF2RB","description":"Cytokine receptor common subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23037","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2435811","identifier":"P05113","identifierLink":"https://www.uniprot.org/uniprotkb/P05113/entry","name":"IL5","description":"Interleukin-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48491","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-518647","identifier":"O60674","identifierLink":"https://www.uniprot.org/uniprotkb/O60674/entry","name":"JAK2","description":"Tyrosine-protein kinase JAK2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45807","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-507","complexName":"Vapa-Osbp complex","organismName":"Mus musculus; 10090","description":"Essential for stimulation of sphingomyelin synthesis by 25-hydroxycholesterol. The complex is formed on the endoplasmic reticulum membrane and acts to tether the membrane to Golgi PI(4)P phosphoinositide molecules or the GTP-binding protein Arf1 (P84078), to promote the specific exchange of lipids from the ER to the Golgi apparatus.","predictedComplex":false,"interactors":[{"ac":"EBI-11892761","identifier":"Q3B7Z2","identifierLink":"https://www.uniprot.org/uniprotkb/Q3B7Z2/entry","name":"Osbp","description":"Oxysterol-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10972","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-645974","identifier":"Q9WV55","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WV55/entry","name":"Vapa","description":"Vesicle-associated membrane protein-associated protein A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10809","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-508","complexName":"RXRalpha-RARalpha retinoic acid receptor complex","organismName":"Homo sapiens; 9606","description":"Member of the nuclear receptor family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. The 9-cis retinoic acid receptor (retinoid X receptor, RXR) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including the all-trans retinoic acid receptor (RAR). RAR and RXR transduce the retinoid signal into a variety of genetic responses, and their functions underlie the essential role played by retinoids in the development and homeostasis of vertebrates. In the absence of RAR agonist, the RXR-RAR heterodimer recruits the corepressor proteins NCoR or SMRT and associated factors such as histone deacetylases or DNA-methyl transferases that may lead to an inactive condensed chromatin structure, preventing transcription. RXRA-RARA is a non-permissive receptor that cannot be activated by an RXR agonist but only by an agonist of the dominant partner receptor, RARA.  Upon RAR agonist binding, corepressors are released, and coactivator complexes such as histone acetyltransferases or histone arginine methyltransferases are recruited to activate transcription. The RXR-RAR heterodimer binds more efficiently to retinoic acid response elements (RAREs), composed typically of two direct repeats of a core hexameric motif, PuG [G/T] TCA, than do either of the homodimeric forms of RXR or RAR.","predictedComplex":false,"interactors":[{"ac":"EBI-413374","identifier":"P10276","identifierLink":"https://www.uniprot.org/uniprotkb/P10276/entry","name":"RARA","description":"Retinoic acid receptor alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-78598","identifier":"P19793","identifierLink":"https://www.uniprot.org/uniprotkb/P19793/entry","name":"RXRA","description":"Retinoic acid receptor RXR-alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-509","complexName":"bZIP transcription factor complex, CEBPA-CEBPB","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-1172054","identifier":"P49715","identifierLink":"https://www.uniprot.org/uniprotkb/P49715/entry","name":"CEBPA","description":"CCAAT/enhancer-binding protein alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-969696","identifier":"P17676","identifierLink":"https://www.uniprot.org/uniprotkb/P17676/entry","name":"CEBPB","description":"CCAAT/enhancer-binding protein beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-510","complexName":"uPA-uPAR complex","organismName":"Mus musculus; 10090","description":"Regulates the activity of the plasminogen activation system, an extracellular proteolytic cascade. uPAR (Plaur) localizes uPA (Plau) and its zymogen form, pro-uPA, to the cell surface. Activated uPA cleaves the zymogen plasminogen (P20918), generating the protease plasmin. Plasmin cleaves a range of extra-cellular matrix components, is essential for fibrinolysis, the degradation and clearance of fibrin blood clots, and activates matrix metalloproteases, affecting a number of physiological and disease processes including tumor growth and metastasis, angiogenesis and inflammation. May also mediates the proteolysis-independent signal transduction activation effects of uPA. uPAR is subject to negative-feedback regulation by uPA which cleaves it into an inactive form.","predictedComplex":false,"interactors":[{"ac":"EBI-5606940","identifier":"P35456","identifierLink":"https://www.uniprot.org/uniprotkb/P35456/entry","name":"Plaur","description":"Urokinase plasminogen activator surface receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10624","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8365661","identifier":"P06869","identifierLink":"https://www.uniprot.org/uniprotkb/P06869/entry","name":"Plau","description":"Urokinase-type plasminogen activator","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-511","complexName":"MUS81-EME1 structure-specific endonuclease complex","organismName":"Homo sapiens; 9606","description":"Structure-specific endonuclease that plays an important role in rescuing stalled replication forks and resolving the mitotic recombination intermediates. The complex recognizes the branched DNA intermediates and typically cleaves 3-6 base pairs of the 5-prime regions of the junction crossover point. Preferentially cleaves four-way DNA junctions, such as nicked Holliday Junctions (nHJs), D-loops, 3-prime flap DNA substrates that contain an exposed 5-prime DNA strand end at or close to the junction crossover point and replication forks, via the “nick and counternick” mechanism. DNA binding induces conformational changes in the linkers connecting the nuclease and HhH2 domains of MUS81 and EME1, which transforms the complex from a compact to an open state. These changes unmask the hydrophobic wedge that separates pre‐ and post‐nick duplex and create the 5-prime end binding pocket facilitating the DNA substrate bending by the complex, ultimately placing the incision strand at the active site of MUS81.","predictedComplex":false,"interactors":[{"ac":"EBI-2370806","identifier":"Q96NY9","identifierLink":"https://www.uniprot.org/uniprotkb/Q96NY9/entry","name":"MUS81","description":"Structure-specific endonuclease subunit MUS81","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13451","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2370825","identifier":"Q96AY2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96AY2/entry","name":"EME1","description":"Structure-specific endonuclease subunit EME1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-512","complexName":"Granulocyte-macrophage colony-stimulating factor-receptor complex","organismName":"Homo sapiens; 9606","description":"Cytokine receptor complex that activates the JAK/STAT signaling cascade. Stimulates the growth and development of progenitors of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes and the production and maturation of dendritic cells and T cells. Enhances the activity of neutrophils and macrophages. \r\n\r\nBinding of CSF2 stimulates tyrosine phosphorylation of the receptor subunits and associated JAK2.","predictedComplex":false,"interactors":[{"ac":"EBI-1763264","identifier":"P15509","identifierLink":"https://www.uniprot.org/uniprotkb/P15509/entry","name":"CSF2RA","description":"Granulocyte-macrophage colony-stimulating factor receptor subunit alpha","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1809771","identifier":"P32927","identifierLink":"https://www.uniprot.org/uniprotkb/P32927/entry","name":"CSF2RB","description":"Cytokine receptor common subunit beta","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23037","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1809826","identifier":"P04141","identifierLink":"https://www.uniprot.org/uniprotkb/P04141/entry","name":"CSF2","description":"Granulocyte-macrophage colony-stimulating factor","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10059","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-518647","identifier":"O60674","identifierLink":"https://www.uniprot.org/uniprotkb/O60674/entry","name":"JAK2","description":"Tyrosine-protein kinase JAK2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45807","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-513","complexName":"RXRalpha-NCOA2 activated retinoic acid receptor complex","organismName":"Homo sapiens; 9606","description":"Member of the nuclear receptor (NR) family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. The 9-cis retinoic acid receptor (retinoid X receptor, RXRA) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including the all-trans retinoic acid receptors (RARs). Like other NRs, RXRA contains DNA-binding and ligand-binding domain (DBD, LBD). In the absence of agonist, the complex recruits the corepressor proteins NCoR or SMRT and associated factors such as histone deacetylases or DNA-methyl transferases that may lead to an inactive condensed chromatin structure, preventing transcription. Upon ligand binding, RXRs undergo a conformational change that results in the release of corepressors and transcriptional coactivators, such as NCOA2, are recruited to the LBD which activates transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-78598","identifier":"P19793","identifierLink":"https://www.uniprot.org/uniprotkb/P19793/entry","name":"RXRA","description":"Retinoic acid receptor RXR-alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-81236","identifier":"Q15596","identifierLink":"https://www.uniprot.org/uniprotkb/Q15596/entry","name":"NCOA2","description":"Nuclear receptor coactivator 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-514","complexName":"c-MYC-BIN1 complex","organismName":"Homo sapiens; 9606","description":"Transcriptional suppressor complex. Binding of BIN1 to c-MYC inhibits the transcription factor activity of c-MYC and the complex thus acts as a tumor suppressor.","predictedComplex":false,"interactors":[{"ac":"EBI-447544","identifier":"P01106","identifierLink":"https://www.uniprot.org/uniprotkb/P01106/entry","name":"MYC","description":"Myc proto-oncogene protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45851","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-719094","identifier":"O00499","identifierLink":"https://www.uniprot.org/uniprotkb/O00499/entry","name":"BIN1","description":"Myc box-dependent-interacting protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46514","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-516","complexName":"bZIP transcription factor complex, CEBPG-CEBPG","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-740209","identifier":"P53567","identifierLink":"https://www.uniprot.org/uniprotkb/P53567/entry","name":"CEBPG","description":"CCAAT/enhancer-binding protein gamma","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-517","complexName":"PXR-NCOA1 activated nuclear receptor complex","organismName":"Homo sapiens; 9606","description":"Member of the nuclear receptor (NR) family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in metabolism. The pregnane X receptor (NR1I2/PXR) is a central xenobiotic sensor that detects potentially toxic chemicals and regulates the expression of genes central to their breakdown and removal. Like other members of the orphan class of the NR superfamily, NR1I2 contains DNA-binding and ligand-binding domain (DBD, LBD). Upon ligand binding, transcriptional coactivators, such as NCOA1 (Q15788), are recruited leading to transcriptional activation. \r\n\r\nNR1I2 also binds as a heterotetramer with the 9-cis retinoic acid receptor (RXRA, P19793, CPX-496) to xenobiotic response elements in cytochrome P450 3A (CYP3A) gene promoters and is activated by the spectrum of chemicals that are known to induce CYP3A gene expression.","predictedComplex":false,"interactors":[{"ac":"EBI-3905991","identifier":"O75469","identifierLink":"https://www.uniprot.org/uniprotkb/O75469/entry","name":"NR1I2","description":"Nuclear receptor subfamily 1 group I member 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455189","identifier":"Q15788","identifierLink":"https://www.uniprot.org/uniprotkb/Q15788/entry","name":"NCOA1","description":"Nuclear receptor coactivator 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-518","complexName":"tPA-PAI-1 complex","organismName":"Mus musculus; 10090","description":"Regulates the activity of the plasminogen activation system, an extracellular proteolytic cascade. Inhibited form of tissue plasminogen activator tPA (Plat), an enzyme responsible for the cleavage of plasminogen (P20918) to form plasmin, which then degrades fibrin. PAI-1 (Serpine1) inhibits tPA rapidly and irreversibly and is the primary negative regulator of the fibrinolytic system. High levels of PAI-1 therefore prevent formation of plasmin, resulting in fibrin accumulation and thrombosis.","predictedComplex":false,"interactors":[{"ac":"EBI-2794225","identifier":"P11214","identifierLink":"https://www.uniprot.org/uniprotkb/P11214/entry","name":"Plat","description":"Tissue-type plasminogen activator","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-490898","identifier":"P22777","identifierLink":"https://www.uniprot.org/uniprotkb/P22777/entry","name":"Serpine1","description":"Plasminogen activator inhibitor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11461","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-519","complexName":"General transcription factor complex TFIIA","organismName":"Homo sapiens; 9606","description":"Transcription factor complex that regulates transcription initiation from RNA polymerase II promoters. Binding to the transcription factor complex TFIID-TBP enhances assembly of the transcriptional preinitiation complex PIC and its binding to the DNA at the TATA-box by displacing transcription inhibitors, such as DRAP1 (Q14919) or DR1 (Q01658), from TBP (P20226).","predictedComplex":false,"interactors":[{"ac":"EBI-1045262","identifier":"P52657","identifierLink":"https://www.uniprot.org/uniprotkb/P52657/entry","name":"GTF2A2","description":"Transcription initiation factor IIA subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-389518","identifier":"P52655","identifierLink":"https://www.uniprot.org/uniprotkb/P52655/entry","name":"GTF2A1","description":"Transcription initiation factor IIA subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12694","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-522","complexName":"Interleukin-1 beta ligand-decoy receptor type 2 complex","organismName":"Homo sapiens; 9606","description":"A decoy receptor complex which acts by competitively binding both IL1B and  IL1RAP with high affinity, preventing their binding to IL1R1 thus inhibiting IL1 induced inflammation  \r\nNon-signaling IL1R2 is the predominant IL1 binding receptor expressed by monocytes, neutrophils and B cells. Regulatory T-cells also express membrane-bound and soluble IL1R2 (sIL1R2) but pro-inflammatory molecules are thought to inhibit IL1R2 expression. \r\n\r\nPlasma of healthy individuals are thought to contain high levels of sIL1R2, while defective or increased expression sIL1R2 in tissue or bodily fluids are ascribed to a range of pathological conditions, including critical autoimmune diseases, tumours and neuroinflammatory diseases.","predictedComplex":false,"interactors":[{"ac":"EBI-2831568","identifier":"P27930","identifierLink":"https://www.uniprot.org/uniprotkb/P27930/entry","name":"IL1R2","description":"Interleukin-1 receptor type 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52378185","identifier":"P01584-PRO_0000015302","identifierLink":"https://www.uniprot.org/uniprotkb/P01584-PRO_0000015302/entry","name":"IL1B","description":"Interleukin-1 beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-525939","identifier":"Q9NPH3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPH3/entry","name":"IL1RAP","description":"Interleukin-1 receptor accessory protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-525","complexName":"RARalpha-NCOA1 activated retinoic acid receptor complex","organismName":"Homo sapiens; 9606","description":"Member of the nuclear receptor (NR) family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. The all-trans retinoic acid receptor (RARA) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including 9-cis retinoic acid receptors (retinoid X receptor, RXRs). Like other NRs, RARA contains DNA-binding and ligand-binding domains (DBD, LBD). In the absence of agonist, the complex recruits the corepressor proteins NCoR or SMRT and associated factors such as histone deacetylases or DNA-methyl transferases that may lead to an inactive condensed chromatin structure, preventing transcription. Upon ligand binding, RARs undergo a conformational change that results in the release of corepressors and transcriptional coactivators, such as NCOA1, are recruited to the LBD which activates transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-413374","identifier":"P10276","identifierLink":"https://www.uniprot.org/uniprotkb/P10276/entry","name":"RARA","description":"Retinoic acid receptor alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455189","identifier":"Q15788","identifierLink":"https://www.uniprot.org/uniprotkb/Q15788/entry","name":"NCOA1","description":"Nuclear receptor coactivator 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-526","complexName":"uPA-uPAR-vitronectin complex","organismName":"Mus musculus; 10090","description":"Links proteolytic degradation of the extracellular matrix to integrin-mediated adhesion. The formation of this complex results in altered cell adhesion, migration, survival and proliferation. Components of the plasminogen activation system including urokinase urokinase plasminogen uPA (PLAU) and its cell surface receptor uPAR (PLAUR) have been implicated in a wide variety of biological processes related to tissue homoeostasis. The high affinity binding of uPA regulates the binding of uPAR to matrix-embedded vitronectin. Activated uPA cleaves the zymogen plasminogen, generating the protease plasmin. uPA and plasmin induces a potent negative feedback on cell adhesion through specific cleavage of the RGD motif in vitronectin. Cleavage of vitronectin by uPA requires concomitant binding of both uPA and vitronectin to uPAR.","predictedComplex":false,"interactors":[{"ac":"EBI-5606940","identifier":"P35456","identifierLink":"https://www.uniprot.org/uniprotkb/P35456/entry","name":"Plaur","description":"Urokinase plasminogen activator surface receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10624","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8354207","identifier":"P29788","identifierLink":"https://www.uniprot.org/uniprotkb/P29788/entry","name":"Vtn","description":"Vitronectin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22917","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8365661","identifier":"P06869","identifierLink":"https://www.uniprot.org/uniprotkb/P06869/entry","name":"Plau","description":"Urokinase-type plasminogen activator","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-527","complexName":"Interleukin-1 beta ligand-membrane bound receptor type 1 complex","organismName":"Homo sapiens; 9606","description":"Complex formed on the binding of a pre-bound extracellular interleukin-1 beta (IL1B) and a membrane-bound form of its receptor, interleukin-1R1 (IL1R1) to its coreceptor, interleukin-1 receptor accessory protein (IL1RAP). Recruitment of IL1RAP completes complex assembly and initiates activation of the NFKB signalling pathway. IL1R1 signalling is regulated by the interleukin-1 receptor antagonist (IL1RA, P18510) which competes with IL1B for IL1R1 binding (CPX-9126).\r\n\r\nA member of the IL1 family of cytokines, IL1B is closely related to interleukin-1 alpha (IL1A, P01583) carrying out similar biological functions by binding to their shared receptor complex. Although both IL1A and IL1B function via the same IL1R1 to drive an inflammatory response, IL1A is thought to act as an alarmin which regulates local inflammation while IL1B acts as a master regulator of systemic inflammation.  IL1B is an inducible cytokine produced mainly by blood myeloid cells, pathogenic lymphocytes and the central nervous system's (CNS) microglia and astroyctes during autoimmune, metabolic and neurodegenerative disorders.\r\n\r\nIL1B activity is regulated by two forms of the IL1R1: a membrane-bound form (mIL1R1, this complex) and a soluble form (sIL1R1, CPX-9128) created through proteolytic release of the ectodomain (ECD) of mIL1R1 via matrix metalloproteases. The ECD in both forms is vital for ligand recognition and binding. Both forms of IL1R1 are biologically active, mediating an inflammatory response through agonistic and antagonistic regulation of cytokine activity.","predictedComplex":false,"interactors":[{"ac":"EBI-52378176","identifier":"P14778-PRO_0000015435","identifierLink":"https://www.uniprot.org/uniprotkb/P14778-PRO_0000015435/entry","name":"IL1R1","description":"Interleukin-1 receptor type 1, membrane form","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-52378185","identifier":"P01584-PRO_0000015302","identifierLink":"https://www.uniprot.org/uniprotkb/P01584-PRO_0000015302/entry","name":"IL1B","description":"Interleukin-1 beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-525939","identifier":"Q9NPH3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPH3/entry","name":"IL1RAP","description":"Interleukin-1 receptor accessory protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-529","complexName":"TGF-beta-1-TGFR complex","organismName":"Homo sapiens; 9606","description":"Cytokine-receptor complex that plays an important role in embryogenesis, tissue development, cell proliferation, differentiation and maturation, immune regulation and carcinogenesis. Binding of TGFB1 (CPX-602) to its receptor subunits results in the phosphorylation of TGFBR1 on Thr185 & Thr186 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 (Q15796) which dissociates from the receptor and activates the canonical SMAD-dependent TGF-beta signaling cascade.","predictedComplex":false,"interactors":[{"ac":"EBI-1027557","identifier":"P36897","identifierLink":"https://www.uniprot.org/uniprotkb/P36897/entry","name":"TGFBR1","description":"TGF-beta receptor type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12502180","identifier":"P01137-PRO_0000033763","identifierLink":"https://www.uniprot.org/uniprotkb/P01137-PRO_0000033763/entry","name":"TGFB1","description":"Transforming growth factor beta-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-296151","identifier":"P37173","identifierLink":"https://www.uniprot.org/uniprotkb/P37173/entry","name":"TGFBR2","description":"TGF-beta receptor type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-530","complexName":"UBC13-MMS2 ubiquitin-conjugating enzyme E2 complex","organismName":"Homo sapiens; 9606","description":"Implicated in the non-proteolytic regulation of signaling pathways by contributing to the addition of lysine 63-linked ubiquitin chains to proteins. Transfers the thioester-bound donor ubiquitin from UBE2N onto the UBE2V2 catalytically inactive E2 variant. The heterodimer, together with the RING ubiquitin ligase TRAF6, then catalyzes the formation of diubiquitin chains linked by isopeptide bonds between Lys-63 and the C-terminus of the next monomer in the chain. This type of ubiquitination does not lead to protein degradation by the proteasome but instead mediates error-free DNA repair and contributes to the survival of cells after DNA damage.","predictedComplex":false,"interactors":[{"ac":"EBI-1052908","identifier":"P61088","identifierLink":"https://www.uniprot.org/uniprotkb/P61088/entry","name":"UBE2N","description":"Ubiquitin-conjugating enzyme E2 N","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714329","identifier":"Q15819","identifierLink":"https://www.uniprot.org/uniprotkb/Q15819/entry","name":"UBE2V2","description":"Ubiquitin-conjugating enzyme E2 variant 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-531","complexName":"Tapasin-ERp57 complex","organismName":"Mus musculus; 10090","description":"Role in the assembly of the heavy-chain-beta2-microglobulin dimers of the MHC class I molecules that fold with eight to ten residue peptides in the endoplasmic reticulum. Final assembly and peptide binding take place within the peptide-loading complex (PLC), where the heterodimers undergo peptide editing. The complex seems to be required for the inhibition of the reduction of the disulfide bonds of the heavy chains and the assembly and stabilization of the PLC, suggesting Pdia3/ERp57 may play a structural role rather than a catalytic one.","predictedComplex":false,"interactors":[{"ac":"EBI-1183750","identifier":"P27773","identifierLink":"https://www.uniprot.org/uniprotkb/P27773/entry","name":"Pdia3","description":"Protein disulfide-isomerase A3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18929","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8381478","identifier":"Q9R233","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R233/entry","name":"Tapbp","description":"Tapasin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-532","complexName":"Adaptor complex AP-1","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Plays a central role in clathrin-coated vesicle formation by coupling coat assembly and cargo collection. Binds short linear motifs on cargo proteins and incorporates them into the clathrin coat of forming vesicles. Mediates the bi-directional transfer of membrane proteins between the trans-Golgi network and the early endosome. Related complexes AP-1 and AP-1R (CPX-533) differ only in the mu chain and sort different cargoes: for example, only AP-1 binds and transports chitin synthase 3 (CHS3, P29465) and the salt stress-induced hydrophobic SNA2 protein (P56508).","predictedComplex":false,"interactors":[{"ac":"EBI-2206","identifier":"P36000","identifierLink":"https://www.uniprot.org/uniprotkb/P36000/entry","name":"APL2","description":"AP-1 complex subunit beta-1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2612","identifier":"P35181","identifierLink":"https://www.uniprot.org/uniprotkb/P35181/entry","name":"APS1","description":"AP-1 complex subunit sigma-1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2624","identifier":"Q00776","identifierLink":"https://www.uniprot.org/uniprotkb/Q00776/entry","name":"APM1","description":"AP-1 complex subunit mu-1-I","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-33025","identifier":"Q12028","identifierLink":"https://www.uniprot.org/uniprotkb/Q12028/entry","name":"APL4","description":"AP-1 complex subunit gamma-1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-533","complexName":"Adaptor complex AP-1R","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Plays a central role in clathrin-coated vesicle formation by coupling coat assembly and cargo collection. Binds short linear motifs on cargo proteins and incorporates them into the clathrin coat of forming vesicles. Mediates the bi-directional transfer of membrane proteins between the trans-Golgi network and the early endosome. Related complexes AP-1 (CPX-532) and AP-1R differ only in the mu chain and sort different cargoes: for example, only AP-1R binds Yfl034w (P43564), a predicted serine hydrolase that is required for APM2-dependent sorting processes and has a role in recruiting APM2 to membranes.","predictedComplex":false,"interactors":[{"ac":"EBI-2206","identifier":"P36000","identifierLink":"https://www.uniprot.org/uniprotkb/P36000/entry","name":"APL2","description":"AP-1 complex subunit beta-1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2612","identifier":"P35181","identifierLink":"https://www.uniprot.org/uniprotkb/P35181/entry","name":"APS1","description":"AP-1 complex subunit sigma-1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2705","identifier":"P38700","identifierLink":"https://www.uniprot.org/uniprotkb/P38700/entry","name":"APM2","description":"Adaptin medium chain homolog APM2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-33025","identifier":"Q12028","identifierLink":"https://www.uniprot.org/uniprotkb/Q12028/entry","name":"APL4","description":"AP-1 complex subunit gamma-1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-534","complexName":"Adapter complex AP-2","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Probably acts in a clathrin-independent protein sorting pathway. Found at the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-2181","identifier":"P38065","identifierLink":"https://www.uniprot.org/uniprotkb/P38065/entry","name":"APL3","description":"AP-2 complex subunit alpha","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2202","identifier":"P27351","identifierLink":"https://www.uniprot.org/uniprotkb/P27351/entry","name":"APL1","description":"AP-2 complex subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2608","identifier":"Q00381","identifierLink":"https://www.uniprot.org/uniprotkb/Q00381/entry","name":"APS2","description":"AP-2 complex subunit sigma","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2715","identifier":"Q99186","identifierLink":"https://www.uniprot.org/uniprotkb/Q99186/entry","name":"APM4","description":"AP-2 complex subunit mu","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-535","complexName":"Adapter complex AP-3","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Probably acts in clathrin-independent traffic of membrane proteins from the Golgi apparatus to vacuoles.","predictedComplex":false,"interactors":[{"ac":"EBI-2213","identifier":"P46682","identifierLink":"https://www.uniprot.org/uniprotkb/P46682/entry","name":"APL6","description":"AP-3 complex subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2619","identifier":"P47064","identifierLink":"https://www.uniprot.org/uniprotkb/P47064/entry","name":"APS3","description":"AP-3 complex subunit sigma","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2710","identifier":"P38153","identifierLink":"https://www.uniprot.org/uniprotkb/P38153/entry","name":"APM3","description":"AP-3 complex subunit mu","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29702","identifier":"Q08951","identifierLink":"https://www.uniprot.org/uniprotkb/Q08951/entry","name":"APL5","description":"AP-3 complex subunit delta","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22781","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-536","complexName":"cAMP-dependent protein kinase complex variant 1","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Inactive form of the cAMP-dependent protein kinase which assembles when cAMP concentrations are low. Exists as a tetramer composed of two catalytic subunits and two regulatory subunits. When cAMP concentrations are high, the nucleotide binds to the inhibitory BCY1 subunits, causing dissociation from, and activation of, the catalytic subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-9458","identifier":"P06244","identifierLink":"https://www.uniprot.org/uniprotkb/P06244/entry","name":"TPK1","description":"cAMP-dependent protein kinase type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9475","identifier":"P07278","identifierLink":"https://www.uniprot.org/uniprotkb/P07278/entry","name":"BCY1","description":"cAMP-dependent protein kinase regulatory subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11635","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-537","complexName":"cAMP-dependent protein kinase complex variant 2","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Inactive form of the cAMP-dependent protein kinase which assembles when cAMP concentrations are low. Exists as a tetramer composed of two catalytic subunits and two regulatory subunits. When cAMP concentrations are high, the nucleotide binds to the inhibitory BCY1 subunits, causing dissociation from and activation of the catalytic subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-9465","identifier":"P06245","identifierLink":"https://www.uniprot.org/uniprotkb/P06245/entry","name":"TPK2","description":"cAMP-dependent protein kinase type 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9475","identifier":"P07278","identifierLink":"https://www.uniprot.org/uniprotkb/P07278/entry","name":"BCY1","description":"cAMP-dependent protein kinase regulatory subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11635","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-571","complexName":"cAMP-dependent protein kinase complex variant 3","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Inactive form of the cAMP-dependent protein kinase which assembles when cAMP concentrations are low. Exists as a tetramer composed of two catalytic subunits and two regulatory subunits. When cAMP concentrations are high, the nucleotide binds to the inhibitory BCY1 subunits, causing dissociation from and activation of the catalytic subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-9470","identifier":"P05986","identifierLink":"https://www.uniprot.org/uniprotkb/P05986/entry","name":"TPK3","description":"cAMP-dependent protein kinase type 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9475","identifier":"P07278","identifierLink":"https://www.uniprot.org/uniprotkb/P07278/entry","name":"BCY1","description":"cAMP-dependent protein kinase regulatory subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11635","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-572","complexName":"cAMP-dependent protein kinase complex variant 4","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Inactive form of the cAMP-dependent protein kinase which assembles when cAMP concentrations are low. Exists as a tetramer composed of two catalytic subunits and two regulatory subunits. When cAMP concentrations are high, the nucleotide binds to the inhibitory BCY1 subunits, causing dissociation from and activation of the catalytic subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-9458","identifier":"P06244","identifierLink":"https://www.uniprot.org/uniprotkb/P06244/entry","name":"TPK1","description":"cAMP-dependent protein kinase type 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9465","identifier":"P06245","identifierLink":"https://www.uniprot.org/uniprotkb/P06245/entry","name":"TPK2","description":"cAMP-dependent protein kinase type 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9475","identifier":"P07278","identifierLink":"https://www.uniprot.org/uniprotkb/P07278/entry","name":"BCY1","description":"cAMP-dependent protein kinase regulatory subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11635","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-573","complexName":"cAMP-dependent protein kinase complex variant 5","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Inactive form of the cAMP-dependent protein kinase which assembles when cAMP concentrations are low. Exists as a tetramer composed of two catalytic subunits and two regulatory subunits. When cAMP concentrations are high, the nucleotide binds to the inhibitory BCY1 subunits, causing dissociation from and activation of the catalytic subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-9458","identifier":"P06244","identifierLink":"https://www.uniprot.org/uniprotkb/P06244/entry","name":"TPK1","description":"cAMP-dependent protein kinase type 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9470","identifier":"P05986","identifierLink":"https://www.uniprot.org/uniprotkb/P05986/entry","name":"TPK3","description":"cAMP-dependent protein kinase type 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9475","identifier":"P07278","identifierLink":"https://www.uniprot.org/uniprotkb/P07278/entry","name":"BCY1","description":"cAMP-dependent protein kinase regulatory subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11635","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-574","complexName":"cAMP-dependent protein kinase complex variant 6","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Inactive form of the cAMP-dependent protein kinase which assembles when cAMP concentrations are low. Exists as a tetramer composed of two catalytic subunits and two regulatory subunits. When cAMP concentrations are high, the nucleotide binds to the inhibitory BCY1 subunits, causing dissociation from and activation of the catalytic subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-9465","identifier":"P06245","identifierLink":"https://www.uniprot.org/uniprotkb/P06245/entry","name":"TPK2","description":"cAMP-dependent protein kinase type 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9470","identifier":"P05986","identifierLink":"https://www.uniprot.org/uniprotkb/P05986/entry","name":"TPK3","description":"cAMP-dependent protein kinase type 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9475","identifier":"P07278","identifierLink":"https://www.uniprot.org/uniprotkb/P07278/entry","name":"BCY1","description":"cAMP-dependent protein kinase regulatory subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11635","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-575","complexName":"Ste12/Dig1/Dig2 transcription regulation complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Translational repressor complex which binds to the pheromone response elements (PREs; TGAAACR) in mating gene promoters. Upon pheromone stimulation, Fus3 MAPK (P16892) phosphorylates members of the Ste12 complex leading to dissociation and/or conformational change of the complex and to relief of Ste12 repression.","predictedComplex":false,"interactors":[{"ac":"EBI-18264","identifier":"P13574","identifierLink":"https://www.uniprot.org/uniprotkb/P13574/entry","name":"STE12","description":"Protein STE12","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47427","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29752","identifier":"Q03063","identifierLink":"https://www.uniprot.org/uniprotkb/Q03063/entry","name":"DIG1","description":"Down-regulator of invasive growth 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-34019","identifier":"Q03373","identifierLink":"https://www.uniprot.org/uniprotkb/Q03373/entry","name":"DIG2","description":"Down-regulator of invasive growth 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-576","complexName":"Tec1/Ste12/Dig1 transcription regulation complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Translational repressor complex which binds to the filamentation response elements (FREs) on filamentous growth-specific target genes and, at much lower levels, at the pheremone response elements (PREs) of mating genes. Upon pheromone stimulation, Fus3 MAPK (P16892) phosphorylates members of the Ste12 complex leading to dissociation and/or conformational change of the complex and to relief of Ste12 repression.","predictedComplex":false,"interactors":[{"ac":"EBI-18264","identifier":"P13574","identifierLink":"https://www.uniprot.org/uniprotkb/P13574/entry","name":"STE12","description":"Protein STE12","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47427","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19091","identifier":"P18412","identifierLink":"https://www.uniprot.org/uniprotkb/P18412/entry","name":"TEC1","description":"Ty transcription activator TEC1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11834","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29752","identifier":"Q03063","identifierLink":"https://www.uniprot.org/uniprotkb/Q03063/entry","name":"DIG1","description":"Down-regulator of invasive growth 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-584","complexName":"RXRalpha-RARalpha retinoic acid receptor complex","organismName":"Mus musculus; 10090","description":"Member of the nuclear receptor family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. The 9-cis retinoic acid receptor (retinoid X receptor, RXR) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including the all-trans retinoic acid receptor (RAR). RAR and RXR transduce the retinoid signal into a variety of genetic responses, and their functions underlie the essential role played by retinoids in the development and homeostasis of vertebrates. In the absence of RAR agonist, the RXR-RAR heterodimer recruits the corepressor proteins NCoR or SMRT and associated factors such as histone deacetylases or DNA-methyl transferases that may lead to an inactive condensed chromatin structure, preventing transcription. Rxra-Rara is a non-permissive receptor that cannot be activated by an RXR agonist but only by an agonist of the dominant partner receptor, Rara. Upon RAR agonist binding, corepressors are released, and coactivator complexes such as histone acetyltransferases or histone arginine methyltransferases are recruited to activate transcription. The RXR-RAR heterodimer binds more efficiently to retinoic acid response elements (RAREs), composed typically of two direct repeats of a core hexameric motif, PuG [G/T] TCA, than do either of the homodimeric forms of RXR or RAR.","predictedComplex":false,"interactors":[{"ac":"EBI-346715","identifier":"P28700","identifierLink":"https://www.uniprot.org/uniprotkb/P28700/entry","name":"Rxra","description":"Retinoic acid receptor RXR-alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-346736","identifier":"P11416","identifierLink":"https://www.uniprot.org/uniprotkb/P11416/entry","name":"Rara","description":"Retinoic acid receptor alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-585","complexName":"MUS81-EME1 structure-specific endonuclease complex","organismName":"Mus musculus; 10090","description":"Structure-specific endonuclease that plays an important role in rescuing stalled replication forks and resolving the mitotic recombination intermediates. The complex recognizes the branched DNA intermediates and typically cleaves 3-6 base pairs of the 5-prime regions of the junction crossover point. Preferentially cleaves four-way DNA junctions, such as nicked Holliday Junctions (nHJs), D-loops, 3-prime flap DNA substrates that contain an exposed 5-prime DNA strand end at or close to the junction crossover point and replication forks, via the “nick and counternick” mechanism. DNA binding induces conformational changes in the linkers connecting the nuclease and HhH2 domains of Mus81 and Eme1, which transforms the complex from a compact to an open state. These changes unmask the hydrophobic wedge that separates pre‐ and post‐nick duplex and create the 5-prime end binding pocket facilitating the DNA substrate bending by the complex, ultimately placing the incision strand at the active site of Mus81.","predictedComplex":false,"interactors":[{"ac":"EBI-11131709","identifier":"Q91ZJ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q91ZJ0/entry","name":"Mus81","description":"Structure-specific endonuclease subunit MUS81","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13451","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12498569","identifier":"Q8BJW7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BJW7/entry","name":"Eme1","description":"Structure-specific endonuclease subunit EME1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-586","complexName":"MUS81-EME2 structure-specific endonuclease complex","organismName":"Homo sapiens; 9606","description":"Structure-specific endonuclease that plays an important role in rescuing stalled replication forks and resolving the mitotic recombination intermediates. The complex recognizes the branched DNA intermediates and typically cleaves 3-6 base pairs of the 5-prime regions of the junction crossover point. Preferentially cleaves four-way DNA junctions, such as nicked Holliday Junctions (nHJs), D-loops, 3-prime flap DNA substrates and splayed-arm DNA (not found in MUS81-EME complex) that contain an exposed 5-prime DNA strand end at or close to the junction crossover point and replication forks, via the “nick and counternick” mechanism. DNA binding induces conformational changes in the linkers connecting the nuclease and HhH2 domains of MUS81 and EME2, which transforms the complex from a compact to an open state. These changes unmask the hydrophobic wedge that separates pre‐ and post‐nick duplex and create the 5-prime end binding pocket facilitating the DNA substrate bending by the complex, ultimately placing the incision strand at the active site of MUS81.","predictedComplex":false,"interactors":[{"ac":"EBI-2370806","identifier":"Q96NY9","identifierLink":"https://www.uniprot.org/uniprotkb/Q96NY9/entry","name":"MUS81","description":"Structure-specific endonuclease subunit MUS81","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13451","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7838486","identifier":"A4GXA9","identifierLink":"https://www.uniprot.org/uniprotkb/A4GXA9/entry","name":"EME2","description":"Structure-specific endonuclease subunit EME2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-587","complexName":"MUS81-EME2 structure-specific endonuclease complex","organismName":"Mus musculus; 10090","description":"Structure-specific endonuclease that plays an important role in rescuing stalled replication forks and resolving the mitotic recombination intermediates. The complex recognizes the branched DNA intermediates and typically cleaves 3-6 base pairs of the 5-prime regions of the junction crossover point. Preferentially cleaves four-way DNA junctions, such as nicked Holliday Junctions (nHJs), D-loops, 3-prime flap DNA substrates and splayed-arm DNA (not found in Mus81-Eme1 complex, CPX-585) that contain an exposed 5-prime DNA strand end at or close to the junction crossover point and replication forks, via the “nick and counternick” mechanism. DNA binding induces conformational changes in the linkers connecting the nuclease and HhH2 domains of Mus81 and Eme2, which transforms the complex from a compact to an open state. These changes unmask the hydrophobic wedge that separates pre‐ and post‐nick duplex and create the 5-prime end binding pocket facilitating the DNA substrate bending by the complex, ultimately placing the incision strand at the active site of Mus81.","predictedComplex":false,"interactors":[{"ac":"EBI-11131709","identifier":"Q91ZJ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q91ZJ0/entry","name":"Mus81","description":"Structure-specific endonuclease subunit MUS81","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13451","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12498685","identifier":"Q56A04","identifierLink":"https://www.uniprot.org/uniprotkb/Q56A04/entry","name":"Eme2","description":"Structure-specific endonuclease subunit EME2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-591","complexName":"Nucleolar exosome complex, EXOSC10 variant","organismName":"Homo sapiens; 9606","description":"3'-5' exoribonuclease complex that is involved in RNA maturation and degradation which include the removal of unstable and aberrant transcripts and may also regulate the levels of specific transcripts in response to environmental factors. Restricted to processing linear and circular single-stranded RNAs only. RNAs with complex secondary structures, particularly at the 3' end of the molecule, may have to be unwound or pre-processed by co-factors prior to entering the complex. Although some RNAs may be targeted directly to the catalytic subunit, the majority of substrates enter the barrel-like structure of the exosome through a pore at the centre of the cap and are threaded through the central channel in a 3-prime to 5-prime orientation. The exoribonuclease activity of the catalytic subunit facilitates the degradation process. \r\n\r\nA number of different exosome variants exist in the cell that are distinguished by the inclusion of their respective catalytic subunit(s): the main cytoplasmic exosome with DIS3L (CPX-592) or DIS3L and EXOSC10 (CPX-600),  the main nuclear exosome with DIS3 and EXOSC10 (CPX-476), the nucleolar exosome with EXOSC10 (this complex) and a rare variant found in both, the nucleus and cytosol, (CPX-593). \r\n\r\nThe precise function of the nucleolar RNA exosome has not been determined but as it shares the EXOSC10 subunit with the nuclear exosome it is thought its functions are related.","predictedComplex":false,"interactors":[{"ac":"EBI-2841747","identifier":"Q5RKV6","identifierLink":"https://www.uniprot.org/uniprotkb/Q5RKV6/entry","name":"EXOSC6","description":"Exosome complex component MTR3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301735","identifier":"Q13868","identifierLink":"https://www.uniprot.org/uniprotkb/Q13868/entry","name":"EXOSC2","description":"Exosome complex component RRP4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347966","identifier":"Q06265","identifierLink":"https://www.uniprot.org/uniprotkb/Q06265/entry","name":"EXOSC9","description":"Exosome complex component RRP45","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358236","identifier":"Q01780","identifierLink":"https://www.uniprot.org/uniprotkb/Q01780/entry","name":"EXOSC10","description":"Exosome complex component 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12124","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371823","identifier":"Q9NPD3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPD3/entry","name":"EXOSC4","description":"Exosome complex component RRP41","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371841","identifier":"Q15024","identifierLink":"https://www.uniprot.org/uniprotkb/Q15024/entry","name":"EXOSC7","description":"Exosome complex component RRP42","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371866","identifier":"Q9NQT5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NQT5/entry","name":"EXOSC3","description":"Exosome complex component RRP40","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371876","identifier":"Q9NQT4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NQT4/entry","name":"EXOSC5","description":"Exosome complex component RRP46","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371892","identifier":"Q9Y3B2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3B2/entry","name":"EXOSC1","description":"Exosome complex component CSL4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12686","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371922","identifier":"Q96B26","identifierLink":"https://www.uniprot.org/uniprotkb/Q96B26/entry","name":"EXOSC8","description":"Exosome complex component RRP43","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-592","complexName":"Cytoplasmic exosome complex, DIS3L variant","organismName":"Homo sapiens; 9606","description":"3' to 5' exoribonuclease complex that is involved in RNA maturation and degradation which include the removal of unstable and aberrant transcripts and may also regulate the levels of specific transcripts in response to environmental factors. Restricted to processing linear and circular single-stranded RNAs only. RNAs with complex secondary structures, particularly at the 3' end of the molecule, may have to be unwound or pre-processed by co-factors prior to entering the complex. Although some RNAs may be targeted directly to the catalytic subunit, the majority of substrates enter the barrel-like structure of the exosome through a pore at the centre of the cap and are threaded through the central channel in a 3' to 5' orientation. The exoribonuclease activity of the catalytic subunit facilitates the degradation process. \r\n\r\nA number of different exosome variants exist in the cell that are distinguished by the inclusion of their respective catalytic subunit(s): the main cytoplasmic exosome with DIS3L (this complex) or DIS3L and EXOSC10 (CPX-600),  the main nuclear exosome with DIS3 and EXOSC10 (CPX-476), the nucleolar exosome with EXOSC10 (CPX-591) and a rare variant found in both, the nucleus and cytosol, (CPX-593). \r\n\r\nThe cytoplasmic RNA exosome is involved in general mRNA turnover (esp of Polymerase III transcripts) and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3-prime untranslated regions and cytoplasmic rRNAs that have undergone polyadenylation. Degrades mRNAs subject to RNA interference and is involved in the following mRNA decay pathways: mRNAs with premature termination codons (PTCs; the nonsense mediated decay (NMD) pathway), ones lacking termination codons altogether (the non-stop decay (NSD) pathway) and ones where ribosomes stall (the no-go decay (NGD) pathway). Seems to be involved in degradation of histone mRNA.","predictedComplex":false,"interactors":[{"ac":"EBI-2841747","identifier":"Q5RKV6","identifierLink":"https://www.uniprot.org/uniprotkb/Q5RKV6/entry","name":"EXOSC6","description":"Exosome complex component MTR3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301735","identifier":"Q13868","identifierLink":"https://www.uniprot.org/uniprotkb/Q13868/entry","name":"EXOSC2","description":"Exosome complex component RRP4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347966","identifier":"Q06265","identifierLink":"https://www.uniprot.org/uniprotkb/Q06265/entry","name":"EXOSC9","description":"Exosome complex component RRP45","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3672244","identifier":"Q8TF46","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TF46/entry","name":"DIS3L","description":"DIS3-like exonuclease 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23355","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371823","identifier":"Q9NPD3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPD3/entry","name":"EXOSC4","description":"Exosome complex component RRP41","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371841","identifier":"Q15024","identifierLink":"https://www.uniprot.org/uniprotkb/Q15024/entry","name":"EXOSC7","description":"Exosome complex component RRP42","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371866","identifier":"Q9NQT5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NQT5/entry","name":"EXOSC3","description":"Exosome complex component RRP40","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371876","identifier":"Q9NQT4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NQT4/entry","name":"EXOSC5","description":"Exosome complex component RRP46","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371892","identifier":"Q9Y3B2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3B2/entry","name":"EXOSC1","description":"Exosome complex component CSL4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12686","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371922","identifier":"Q96B26","identifierLink":"https://www.uniprot.org/uniprotkb/Q96B26/entry","name":"EXOSC8","description":"Exosome complex component RRP43","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-593","complexName":"Exosome complex, DIS3 variant","organismName":"Homo sapiens; 9606","description":"3-prime to 5-prime exo- and endoribonuclease complex that is involved in RNA maturation and degradation which include the removal of unstable and aberrant transcripts and may also regulate the levels of specific transcripts in response to environmental factors. Restricted to processing linear and circular single-stranded RNAs only. RNAs with complex secondary structures, particularly at the 3-prime end of the molecule, may have to be unwound or pre-processed by co-factors prior to entering the complex. Although some RNAs may be targeted directly to the catalytic subunit, the majority of substrates enter the barrel-like structure of the exosome through a pore at the centre of the cap and are threaded through the central channel in a 3-prime to 5-prime orientation. The ribonuclease activity of the catalytic subunit facilitates the degradation process. \r\n\r\nA number of different exosome variants exist in the cell that are distinguished by the inclusion of their respective catalytic subunit(s): the main cytoplasmic exosome with DIS3L (CPX-592) or DIS3L and EXOSC10 (CPX-600),  the main nuclear exosome with DIS3 and EXOSC10 (CPX-476), the nucleolar exosome with EXOSC10 (CPX-591) and a rare variant found in both, the nucleus and cytosol, (this complex).","predictedComplex":false,"interactors":[{"ac":"EBI-2841747","identifier":"Q5RKV6","identifierLink":"https://www.uniprot.org/uniprotkb/Q5RKV6/entry","name":"EXOSC6","description":"Exosome complex component MTR3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301735","identifier":"Q13868","identifierLink":"https://www.uniprot.org/uniprotkb/Q13868/entry","name":"EXOSC2","description":"Exosome complex component RRP4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347966","identifier":"Q06265","identifierLink":"https://www.uniprot.org/uniprotkb/Q06265/entry","name":"EXOSC9","description":"Exosome complex component RRP45","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371823","identifier":"Q9NPD3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPD3/entry","name":"EXOSC4","description":"Exosome complex component RRP41","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371841","identifier":"Q15024","identifierLink":"https://www.uniprot.org/uniprotkb/Q15024/entry","name":"EXOSC7","description":"Exosome complex component RRP42","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371866","identifier":"Q9NQT5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NQT5/entry","name":"EXOSC3","description":"Exosome complex component RRP40","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371876","identifier":"Q9NQT4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NQT4/entry","name":"EXOSC5","description":"Exosome complex component RRP46","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371892","identifier":"Q9Y3B2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3B2/entry","name":"EXOSC1","description":"Exosome complex component CSL4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12686","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371922","identifier":"Q96B26","identifierLink":"https://www.uniprot.org/uniprotkb/Q96B26/entry","name":"EXOSC8","description":"Exosome complex component RRP43","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373539","identifier":"Q9Y2L1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2L1/entry","name":"DIS3","description":"Exosome complex exonuclease RRP44","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23355","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-594","complexName":"Nuclear exosome complex, Dis3-Exosc10 variant","organismName":"Mus musculus; 10090","description":"3-prime to 5-prime exo- and endoribonuclease complex that is involved in RNA maturation and degradation which include the removal of unstable and aberrant transcripts and may also regulate the levels of specific transcripts in response to environmental factors. Restricted to processing linear and circular single-stranded RNAs only. RNAs with complex secondary structures, particularly at the 3-prime end of the molecule, may have to be unwound or pre-processed by co-factors prior to entering the complex. Although some RNAs may be targeted directly to the catalytic subunits, the majority of substrates enter the barrel-like structure of the exosome through a pore at the centre of the cap and are threaded through the central channel in a 3-prime to 5-prime orientation. The ribonuclease activity of the catalytic subunits facilitate the degradation process. \r\n\r\nA number of different exosome variants exist in the cell that are distinguished by the inclusion of their respective catalytic subunit(s): the main cytoplasmic exosome with DIS3L (CPX-596) or DIS3L and EXOSC10 (CPX-601),  the main nuclear exosome with DIS3 and EXOSC10 (this complex), the nucleolar exosome with EXOSC10 (CPX-595) and a rare variant found in both, the nucleus and cytosol, (CPX-598). \r\n\r\nThe nuclear RNA exosome is involved in a) proper maturation of most RNA species such as intron-removal from pre-mRNAs and tRNA precursors and rRNA, snRNA, snoRNA, lncRNA and enhancer RNA processing, especially the removal of their 3-prime ends, b) the elimination of RNA processing by-products and non-coding, cryptic transcripts, such as upstream antisense RNA species (uaRNA), enhancer RNAs (eRNAs), heterochromatin-forming repetitive elements (ribosomal DNA repeats and centromeres) and long non-coding RNAs, c) the elimination of mRNAs with processing defects and mRNAs that fail to undergo proper splicing or 3-prime end formation and d) gene expression either by mRNA processing or coordination of intron retention leading to regulation of decay of otherwise intact mRNAs. Nuclear exosome activity therefore limits or excludes export of target RNAs to the cytoplasm. Possibly involved in the degradation of mRNAs with defects in their co-transcriptional packaging into ribonucleoprotein particles (mRNPs), retention of aberrant transcripts on the chromatin, immunoglobulin (Ig) class switch recombination (CSR), Ig variable region somatic hypermutation (SHM) transcription termination or DNA damage repair processes. \r\n\r\nA small amount of this complex has also been found in the cytoplasm.","predictedComplex":false,"interactors":[{"ac":"EBI-11149613","identifier":"Q9DAA6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DAA6/entry","name":"Exosc1","description":"Exosome complex component CSL4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12686","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11518619","identifier":"Q8VBV3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VBV3/entry","name":"Exosc2","description":"Exosome complex component RRP4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12500436","identifier":"Q9D0M0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D0M0/entry","name":"Exosc7","description":"Exosome complex exonuclease RRP42","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3835562","identifier":"Q8BTW3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BTW3/entry","name":"Exosc6","description":"Exosome complex component MTR3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3835564","identifier":"Q7TQK4","identifierLink":"https://www.uniprot.org/uniprotkb/Q7TQK4/entry","name":"Exosc3","description":"Exosome complex component RRP40","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-644704","identifier":"Q9CRA8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CRA8/entry","name":"Exosc5","description":"Exosome complex component RRP46","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8316161","identifier":"P56960","identifierLink":"https://www.uniprot.org/uniprotkb/P56960/entry","name":"Exosc10","description":"Exosome complex component 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12124","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8357473","identifier":"Q921I9","identifierLink":"https://www.uniprot.org/uniprotkb/Q921I9/entry","name":"Exosc4","description":"Exosome complex component RRP41","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8387079","identifier":"Q9D753","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D753/entry","name":"Exosc8","description":"Exosome complex component RRP43","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8586419","identifier":"Q9CSH3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CSH3/entry","name":"Dis3","description":"Exosome complex exonuclease RRP44","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23355","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9988220","identifier":"Q9JHI7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JHI7/entry","name":"Exosc9","description":"Exosome complex component RRP45","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-595","complexName":"Nucleolar exosome complex, Exosc10 variant","organismName":"Mus musculus; 10090","description":"3'-5' exoribonuclease complex that is involved in RNA maturation and degradation which include the removal of unstable and aberrant transcripts and may also regulate the levels of specific transcripts in response to environmental factors. Restricted to processing linear and circular single-stranded RNAs only. RNAs with complex secondary structures, particularly at the 3' end of the molecule, may have to be unwound or pre-processed by co-factors prior to entering the complex. Although some RNAs may be targeted directly to the catalytic subunit, the majority of substrates enter the barrel-like structure of the exosome through a pore at the centre of the cap and are threaded through the central channel in a 3' to 5' orientation. The exoribonuclease activity of the catalytic subunit facilitates the degradation process. \r\n\r\nA number of different exosome variants exist in the cell that are distinguished by the inclusion of their respective catalytic subunit(s): the main cytoplasmic exosome with DIS3L (CPX-596) or DIS3L and EXOSC10 (CPX-601),  the main nuclear exosome with DIS3 and EXOSC10 (CPX-594), the nucleolar exosome with EXOSC10 (this complex) and a rare variant found in both, the nucleus and cytosol, (CPX-598). \r\n\r\nThe precise function of the nucleolar RNA exosome has not been determined but as it shares Exosc10 with the nuclear exosome it is thought its functions are related.","predictedComplex":false,"interactors":[{"ac":"EBI-11149613","identifier":"Q9DAA6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DAA6/entry","name":"Exosc1","description":"Exosome complex component CSL4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12686","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11518619","identifier":"Q8VBV3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VBV3/entry","name":"Exosc2","description":"Exosome complex component RRP4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12500436","identifier":"Q9D0M0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D0M0/entry","name":"Exosc7","description":"Exosome complex exonuclease RRP42","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3835562","identifier":"Q8BTW3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BTW3/entry","name":"Exosc6","description":"Exosome complex component MTR3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3835564","identifier":"Q7TQK4","identifierLink":"https://www.uniprot.org/uniprotkb/Q7TQK4/entry","name":"Exosc3","description":"Exosome complex component RRP40","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-644704","identifier":"Q9CRA8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CRA8/entry","name":"Exosc5","description":"Exosome complex component RRP46","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8316161","identifier":"P56960","identifierLink":"https://www.uniprot.org/uniprotkb/P56960/entry","name":"Exosc10","description":"Exosome complex component 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12124","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8357473","identifier":"Q921I9","identifierLink":"https://www.uniprot.org/uniprotkb/Q921I9/entry","name":"Exosc4","description":"Exosome complex component RRP41","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8387079","identifier":"Q9D753","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D753/entry","name":"Exosc8","description":"Exosome complex component RRP43","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9988220","identifier":"Q9JHI7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JHI7/entry","name":"Exosc9","description":"Exosome complex component RRP45","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-596","complexName":"Cytoplasmic exosome complex, Dis3l variant","organismName":"Mus musculus; 10090","description":"3'-5' exoribonuclease complex that is involved in RNA maturation and degradation which include the removal of unstable and aberrant transcripts and may also regulate the levels of specific transcripts in response to environmental factors. Restricted to processing linear and circular single-stranded RNAs only. RNAs with complex secondary structures, particularly at the 3' end of the molecule, may have to be unwound or pre-processed by co-factors prior to entering the complex. Although some RNAs may be targeted directly to the catalytic subunit, the majority of substrates enter the barrel-like structure of the exosome through a pore at the centre of the cap and are threaded through the central channel in a 3' to 5' orientation. The exoribonuclease activity of the catalytic subunit facilitates the degradation process. \r\n\r\nA number of different exosome variants exist in the cell that are distinguished by the inclusion of their respective catalytic subunit(s): the main cytoplasmic exosome with DIS3L (this complex) or DIS3L and EXOSC10 (CPX-601),  the main nuclear exosome with DIS3 and EXOSC10 (CPX-594), the nucleolar exosome with EXOSC10 (CPX-595) and a rare variant found in both, the nucleus and cytosol, (CPX-598). \r\n\r\nThe cytoplasmic RNA exosome is involved in general mRNA turnover (esp of Polymerase III transcripts) and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3-prime untranslated regions and cytoplasmic rRNAs that have undergone polyadenylation. Degrades mRNAs subject to RNA interference and is involved in the following mRNA decay pathways: mRNAs with premature termination codons (PTCs; the nonsense mediated decay (NMD) pathway), ones lacking termination codons altogether (the non-stop decay (NSD) pathway) and ones where ribosomes stall (the no-go decay (NGD) pathway). Seems to be involved in degradation of histone mRNA.","predictedComplex":false,"interactors":[{"ac":"EBI-11149613","identifier":"Q9DAA6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DAA6/entry","name":"Exosc1","description":"Exosome complex component CSL4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12686","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11518619","identifier":"Q8VBV3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VBV3/entry","name":"Exosc2","description":"Exosome complex component RRP4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12500436","identifier":"Q9D0M0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D0M0/entry","name":"Exosc7","description":"Exosome complex exonuclease RRP42","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12500927","identifier":"Q8C0S1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C0S1/entry","name":"Dis3l","description":"DIS3-like exonuclease 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23355","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3835562","identifier":"Q8BTW3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BTW3/entry","name":"Exosc6","description":"Exosome complex component MTR3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3835564","identifier":"Q7TQK4","identifierLink":"https://www.uniprot.org/uniprotkb/Q7TQK4/entry","name":"Exosc3","description":"Exosome complex component RRP40","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-644704","identifier":"Q9CRA8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CRA8/entry","name":"Exosc5","description":"Exosome complex component RRP46","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8357473","identifier":"Q921I9","identifierLink":"https://www.uniprot.org/uniprotkb/Q921I9/entry","name":"Exosc4","description":"Exosome complex component RRP41","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8387079","identifier":"Q9D753","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D753/entry","name":"Exosc8","description":"Exosome complex component RRP43","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9988220","identifier":"Q9JHI7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JHI7/entry","name":"Exosc9","description":"Exosome complex component RRP45","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-598","complexName":"Exosome complex, Dis3 variant","organismName":"Mus musculus; 10090","description":"3-prime to 5-prime exo- and endoribonuclease complex that is involved in RNA maturation and degradation which include the removal of unstable and aberrant transcripts and may also regulate the levels of specific transcripts in response to environmental factors. Restricted to processing linear and circular single-stranded RNAs only. RNAs with complex secondary structures, particularly at the 3-prime end of the molecule, may have to be unwound or pre-processed by co-factors prior to entering the complex. Although some RNAs may be targeted directly to the catalytic subunit, the majority of substrates enter the barrel-like structure of the exosome through a pore at the centre of the cap and are threaded through the central channel in a 3-prime to 5-prime orientation. The ribonuclease activity of the catalytic subunit facilitates the degradation process. \r\n\r\nA number of different exosome variants exist in the cell that are distinguished by the inclusion of their respective catalytic subunit(s): the main cytoplasmic exosome with DIS3L (CPX-596) or DIS3L and EXOSC10 (CPX-601),  the main nuclear exosome with DIS3 and EXOSC10 (CPX-594), the nucleolar exosome with EXOSC10 (CPX-595) and a rare variant found in both, the nucleus and cytosol, (this complex).","predictedComplex":false,"interactors":[{"ac":"EBI-11149613","identifier":"Q9DAA6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DAA6/entry","name":"Exosc1","description":"Exosome complex component CSL4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12686","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11518619","identifier":"Q8VBV3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VBV3/entry","name":"Exosc2","description":"Exosome complex component RRP4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12500436","identifier":"Q9D0M0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D0M0/entry","name":"Exosc7","description":"Exosome complex exonuclease RRP42","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3835562","identifier":"Q8BTW3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BTW3/entry","name":"Exosc6","description":"Exosome complex component MTR3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3835564","identifier":"Q7TQK4","identifierLink":"https://www.uniprot.org/uniprotkb/Q7TQK4/entry","name":"Exosc3","description":"Exosome complex component RRP40","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-644704","identifier":"Q9CRA8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CRA8/entry","name":"Exosc5","description":"Exosome complex component RRP46","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8357473","identifier":"Q921I9","identifierLink":"https://www.uniprot.org/uniprotkb/Q921I9/entry","name":"Exosc4","description":"Exosome complex component RRP41","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8387079","identifier":"Q9D753","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D753/entry","name":"Exosc8","description":"Exosome complex component RRP43","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8586419","identifier":"Q9CSH3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CSH3/entry","name":"Dis3","description":"Exosome complex exonuclease RRP44","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23355","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9988220","identifier":"Q9JHI7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JHI7/entry","name":"Exosc9","description":"Exosome complex component RRP45","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-599","complexName":"Nuclear/nucleolar exosome complex, DIS3-RRP6 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"3' to 5' exo- and endoribonuclease complex that is involved in RNA maturation and degradation which include the removal of unstable and aberrant transcripts and may also regulate the levels of specific transcripts in response to environmental factors. Restricted to processing linear and circular single-stranded RNAs only. RNAs with complex secondary structures, particularly at the 3' end of the molecule, may have to be unwound or pre-processed by co-factors prior to entering the complex. Although some RNAs may be targeted directly to the catalytic subunits, the majority of substrates enter the barrel-like structure of the exosome through a pore at the centre of the cap and are threaded through the central channel in a 3' to 5' orientation. The ribonuclease activity of the catalytic subunits facilitates the degradation process. \r\n\r\nTwo different exosomes exist in yeast, one found in the nucleus and nucleolus (this complex), the other form is lacking the RRP6 subunit and is found in the cytosol (CPX-603).\r\n\r\nThe nuclear/nucleolar RNA exosome is involved in a) proper maturation of most RNA species such as intron-removal from pre-mRNAs and tRNA precursors and rRNA, snRNA, snoRNA, lncRNA and enhancer RNA processing, especially the removal of their 3-prime ends, b) the elimination of RNA processing by-products and non-coding, cryptic transcripts, such as upstream antisense RNA species (uaRNA), enhancer RNAs (eRNAs), heterochromatin-forming repetitive elements (ribosomal DNA repeats and centromeres) and long non-coding RNAs, c) the elimination of mRNAs with processing defects and mRNAs that fail to undergo proper splicing or 3′ end formation and d) gene expression either by mRNA processing or coordination of intron retention leading to regulation of decay of otherwise intact mRNAs. Nuclear exosome activity therefore limits or excludes export of target RNAs to the cytoplasm. Possibly also involved in the degradation of mRNAs with defects in their co-transcriptional packaging into ribonucleoprotein particles (mRNPs), retention of aberrant transcripts on the chromatin and transcription termination or DNA damage repair processes.","predictedComplex":false,"interactors":[{"ac":"EBI-1731","identifier":"P53859","identifierLink":"https://www.uniprot.org/uniprotkb/P53859/entry","name":"CSL4","description":"Exosome complex component CSL4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12686","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1740","identifier":"Q08162","identifierLink":"https://www.uniprot.org/uniprotkb/Q08162/entry","name":"DIS3","description":"Exosome complex exonuclease DIS3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23355","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1749","identifier":"P48240","identifierLink":"https://www.uniprot.org/uniprotkb/P48240/entry","name":"MTR3","description":"Exosome complex component MTR3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1757","identifier":"P38792","identifierLink":"https://www.uniprot.org/uniprotkb/P38792/entry","name":"RRP4","description":"Exosome complex component RRP4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1765","identifier":"Q12277","identifierLink":"https://www.uniprot.org/uniprotkb/Q12277/entry","name":"RRP42","description":"Exosome complex component RRP42","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1773","identifier":"P25359","identifierLink":"https://www.uniprot.org/uniprotkb/P25359/entry","name":"RRP43","description":"Exosome complex component RRP43","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1782","identifier":"Q12149","identifierLink":"https://www.uniprot.org/uniprotkb/Q12149/entry","name":"RRP6","description":"Exosome complex exonuclease RRP6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12124","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1788","identifier":"P46948","identifierLink":"https://www.uniprot.org/uniprotkb/P46948/entry","name":"SKI6","description":"Exosome complex component SKI6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1810","identifier":"Q05636","identifierLink":"https://www.uniprot.org/uniprotkb/Q05636/entry","name":"RRP45","description":"Exosome complex component RRP45","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1831","identifier":"Q08285","identifierLink":"https://www.uniprot.org/uniprotkb/Q08285/entry","name":"RRP40","description":"Exosome complex component RRP40","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1842","identifier":"P53256","identifierLink":"https://www.uniprot.org/uniprotkb/P53256/entry","name":"RRP46","description":"Exosome complex component RRP46","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-600","complexName":"Cytoplasmic exosome complex, DIS3L-EXOSC10 variant","organismName":"Homo sapiens; 9606","description":"3' to 5' exoribonuclease complex that is involved in RNA maturation and degradation which include the removal of unstable and aberrant transcripts and may also regulate the levels of specific transcripts in response to environmental factors. Restricted to processing linear and circular single-stranded RNAs only. RNAs with complex secondary structures, particularly at the 3' end of the molecule, may have to be unwound or pre-processed by co-factors prior to entering the complex. Although some RNAs may be targeted directly to the catalytic subunits, the majority of substrates enter the barrel-like structure of the exosome through a pore at the centre of the cap and are threaded through the central channel in a 3' to 5' orientation. The exoribonuclease activity of the catalytic subunits facilitates the degradation process. \r\n\r\nA number of different exosome variants exist in the cell that are distinguished by the inclusion of their respective catalytic subunit(s): the main cytoplasmic exosome with DIS3L (CPX-592) or DIS3L and EXOSC10 (this complex),  the main nuclear exosome with DIS3 and EXOSC10 (CPX-476), the nucleolar exosome with EXOSC10 (CPX-591) and a rare variant found in both, the nucleus and cytosol, (CPX-593). \r\n\r\nThe cytoplasmic RNA exosome is involved in general mRNA turnover (esp of Polymerase III transcripts) and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions and cytoplasmic rRNAs that have undergone polyadenylation. Degrades mRNAs subject to RNA interference and is involved in the following mRNA decay pathways: mRNAs with prem-primature termination codons (PTCs; the nonsense mediated decay (NMD) pathway), ones lacking termination codons altogether (the non-stop decay (NSD) pathway) and ones where ribosomes stall (the no-go decay (NGD) pathway). Seems to be involved in degradation of histone mRNA. \r\n\r\nThis cytoplasmic exosome variant is rare compared to the variant lacking the Exosc10 catalytic subunit (CPX-592).","predictedComplex":false,"interactors":[{"ac":"EBI-2841747","identifier":"Q5RKV6","identifierLink":"https://www.uniprot.org/uniprotkb/Q5RKV6/entry","name":"EXOSC6","description":"Exosome complex component MTR3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301735","identifier":"Q13868","identifierLink":"https://www.uniprot.org/uniprotkb/Q13868/entry","name":"EXOSC2","description":"Exosome complex component RRP4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347966","identifier":"Q06265","identifierLink":"https://www.uniprot.org/uniprotkb/Q06265/entry","name":"EXOSC9","description":"Exosome complex component RRP45","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358236","identifier":"Q01780","identifierLink":"https://www.uniprot.org/uniprotkb/Q01780/entry","name":"EXOSC10","description":"Exosome complex component 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12124","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3672244","identifier":"Q8TF46","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TF46/entry","name":"DIS3L","description":"DIS3-like exonuclease 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23355","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371823","identifier":"Q9NPD3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPD3/entry","name":"EXOSC4","description":"Exosome complex component RRP41","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371841","identifier":"Q15024","identifierLink":"https://www.uniprot.org/uniprotkb/Q15024/entry","name":"EXOSC7","description":"Exosome complex component RRP42","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371866","identifier":"Q9NQT5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NQT5/entry","name":"EXOSC3","description":"Exosome complex component RRP40","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371876","identifier":"Q9NQT4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NQT4/entry","name":"EXOSC5","description":"Exosome complex component RRP46","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371892","identifier":"Q9Y3B2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3B2/entry","name":"EXOSC1","description":"Exosome complex component CSL4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12686","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371922","identifier":"Q96B26","identifierLink":"https://www.uniprot.org/uniprotkb/Q96B26/entry","name":"EXOSC8","description":"Exosome complex component RRP43","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-601","complexName":"Cytoplasmic exosome complex, Dis3l-Exosc10 variant","organismName":"Mus musculus; 10090","description":"3-prime to 5-prime exoribonuclease complex that is involved in RNA maturation and degradation which include the removal of unstable and aberrant transcripts and may also regulate the levels of specific transcripts in response to environmental factors. Restricted to processing linear and circular single-stranded RNAs only. RNAs with complex secondary structures, particularly at the 3-prime end of the molecule, may have to be unwound or pre-processed by co-factors prior to entering the complex. Although some RNAs may be targeted directly to the catalytic subunits, the majority of substrates enter the barrel-like structure of the exosome through a pore at the centre of the cap and are threaded through the central channel in a 3-prime to 5-prime orientation. The exoribonuclease activity of the catalytic subunits facilitates the degradation process. \r\n\r\nA number of different exosome variants exist in the cell that are distinguished by the inclusion of their respective catalytic subunit(s): the main cytoplasmic exosome with DIS3L (CPX-596) or DIS3L and EXOSC10 (this complex),  the main nuclear exosome with DIS3 and EXOSC10 (CPX-594), the nucleolar exosome with EXOSC10 (CPX-595) and a rare variant found in both, the nucleus and cytosol, (CPX-598). \r\n\r\nThe cytoplasmic RNA exosome is involved in general mRNA turnover (esp of Polymerase III transcripts) and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3-prime untranslated regions and cytoplasmic rRNAs that have undergone polyadenylation. Degrades mRNAs subject to RNA interference and is involved in the following mRNA decay pathways: mRNAs with premature termination codons (PTCs; the nonsense mediated decay (NMD) pathway), ones lacking termination codons altogether (the non-stop decay (NSD) pathway) and ones where ribosomes stall (the no-go decay (NGD) pathway). Seems to be involved in degradation of histone mRNA. \r\n\r\nThis cytoplasmic exosome variant is rare compared to the variant lacking the Exosc10 catalytic subunit (CPX-596).","predictedComplex":false,"interactors":[{"ac":"EBI-11149613","identifier":"Q9DAA6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DAA6/entry","name":"Exosc1","description":"Exosome complex component CSL4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12686","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11518619","identifier":"Q8VBV3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VBV3/entry","name":"Exosc2","description":"Exosome complex component RRP4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12500436","identifier":"Q9D0M0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D0M0/entry","name":"Exosc7","description":"Exosome complex exonuclease RRP42","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12500927","identifier":"Q8C0S1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C0S1/entry","name":"Dis3l","description":"DIS3-like exonuclease 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23355","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3835562","identifier":"Q8BTW3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BTW3/entry","name":"Exosc6","description":"Exosome complex component MTR3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3835564","identifier":"Q7TQK4","identifierLink":"https://www.uniprot.org/uniprotkb/Q7TQK4/entry","name":"Exosc3","description":"Exosome complex component RRP40","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-644704","identifier":"Q9CRA8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CRA8/entry","name":"Exosc5","description":"Exosome complex component RRP46","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8316161","identifier":"P56960","identifierLink":"https://www.uniprot.org/uniprotkb/P56960/entry","name":"Exosc10","description":"Exosome complex component 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12124","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8357473","identifier":"Q921I9","identifierLink":"https://www.uniprot.org/uniprotkb/Q921I9/entry","name":"Exosc4","description":"Exosome complex component RRP41","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8387079","identifier":"Q9D753","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D753/entry","name":"Exosc8","description":"Exosome complex component RRP43","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9988220","identifier":"Q9JHI7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JHI7/entry","name":"Exosc9","description":"Exosome complex component RRP45","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-602","complexName":"TGF-beta-1 complex","organismName":"Homo sapiens; 9606","description":"Cytokine complex that plays an important role in embryogenesis, tissue development, cell proliferation, differentiation and maturation, immune regulation and carcinogenesis. Binding to form its receptor complex (CPX-529) results in the phosphorylation of TGFBR1 on Thr-185 and Thr-186 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 (Q15796) which dissociates from the receptor and activates the canonical SMAD-dependent TGF-beta signaling cascade. Plays an important role in bone remodeling as it is a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts.","predictedComplex":false,"interactors":[{"ac":"EBI-12502180","identifier":"P01137-PRO_0000033763","identifierLink":"https://www.uniprot.org/uniprotkb/P01137-PRO_0000033763/entry","name":"TGFB1","description":"Transforming growth factor beta-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-603","complexName":"Cytoplasmic exosome complex, DIS3 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"3-prime to 5-prime exo- and endoribonuclease complex that is involved in RNA maturation and degradation which include the removal of unstable and aberrant transcripts and may also regulate the levels of specific transcripts in response to environmental factors. Restricted to processing linear and circular single-stranded RNAs only. RNAs with complex secondary structures, particularly at the 3-prime end of the molecule, may have to be unwound or pre-processed by co-factors prior to entering the complex. Although some RNAs may be targeted directly to the catalytic subunit, the majority of substrates enter the barrel-like structure of the exosome through a pore at the centre of the cap and are threaded through the central channel in a 3-prime to 5-prime orientation. The ribonuclease activity of the catalytic subunit facilitates the degradation process. \r\n\r\nTwo different exosomes exist in yeast, one found in the nucleus and nucleolus (CPX-599), the other form is lacking the RRP6 (Q12149) subunit and is found in the cytosol (this complex).\r\n\r\nThe cytoplasmic RNA exosome is involved in general mRNA turnover (esp of Polymerase III transcripts) and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3-prime untranslated regions and cytoplasmic rRNAs that have undergone polyadenylation. Degrades mRNAs subject to RNA interference and is involved in the following mRNA decay pathways: mRNAs with premature termination codons (PTCs; the nonsense mediated decay (NMD) pathway), ones lacking termination codons altogether (the non-stop decay (NSD) pathway) and ones where ribosomes stall (the no-go decay (NGD) pathway). May be involved in degradation of histone mRNA.","predictedComplex":false,"interactors":[{"ac":"EBI-1731","identifier":"P53859","identifierLink":"https://www.uniprot.org/uniprotkb/P53859/entry","name":"CSL4","description":"Exosome complex component CSL4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12686","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1740","identifier":"Q08162","identifierLink":"https://www.uniprot.org/uniprotkb/Q08162/entry","name":"DIS3","description":"Exosome complex exonuclease DIS3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23355","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1749","identifier":"P48240","identifierLink":"https://www.uniprot.org/uniprotkb/P48240/entry","name":"MTR3","description":"Exosome complex component MTR3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1757","identifier":"P38792","identifierLink":"https://www.uniprot.org/uniprotkb/P38792/entry","name":"RRP4","description":"Exosome complex component RRP4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1765","identifier":"Q12277","identifierLink":"https://www.uniprot.org/uniprotkb/Q12277/entry","name":"RRP42","description":"Exosome complex component RRP42","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1773","identifier":"P25359","identifierLink":"https://www.uniprot.org/uniprotkb/P25359/entry","name":"RRP43","description":"Exosome complex component RRP43","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1788","identifier":"P46948","identifierLink":"https://www.uniprot.org/uniprotkb/P46948/entry","name":"SKI6","description":"Exosome complex component SKI6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1810","identifier":"Q05636","identifierLink":"https://www.uniprot.org/uniprotkb/Q05636/entry","name":"RRP45","description":"Exosome complex component RRP45","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1831","identifier":"Q08285","identifierLink":"https://www.uniprot.org/uniprotkb/Q08285/entry","name":"RRP40","description":"Exosome complex component RRP40","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1842","identifier":"P53256","identifierLink":"https://www.uniprot.org/uniprotkb/P53256/entry","name":"RRP46","description":"Exosome complex component RRP46","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-604","complexName":"UBC13-MMS2 ubiquitin-conjugating enzyme E2 complex","organismName":"Mus musculus; 10090","description":"Implicated in the non-proteolytic regulation of signaling pathways by contributing to the addition of lysine 63-linked ubiquitin chains to proteins. Transfers the thioester-bound donor ubiquitin from Ube2n onto the Ube2v2 catalytically inactive E2 variant. The heterodimer, together with the RING ubiquitin ligase Traf6, then catalyzes the formation of diubiquitin chains linked by isopeptide bonds between Lys-63 and the C-terminus of the next monomer in the chain. This type of ubiquitination does not lead to protein degradation by the proteasome but instead mediates error-free DNA repair and contributes to the survival of cells after DNA damage.","predictedComplex":false,"interactors":[{"ac":"EBI-494560","identifier":"P61089","identifierLink":"https://www.uniprot.org/uniprotkb/P61089/entry","name":"Ube2n","description":"Ubiquitin-conjugating enzyme E2 N","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-911251","identifier":"Q9D2M8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D2M8/entry","name":"Ube2v2","description":"Ubiquitin-conjugating enzyme E2 variant 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-605","complexName":"TGF-beta-2 complex","organismName":"Homo sapiens; 9606","description":"Cytokine complex that plays an important role in embryogenesis, tissue development, cell proliferation, differentiation and maturation, immune regulation and carcinogenesis. Binding to form its receptor complex (CPX-834) results in the phosphorylation of TGFBR1 on Thr-185 and Thr-186 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 (Q15796) which dissociates from the receptor and activates the canonical SMAD-dependent TGF-beta signaling cascade. Involved in wound healing, bone formation and modulation of immune functions. Has suppressive effects on interleukin-2 dependent T-cell growth.","predictedComplex":false,"interactors":[{"ac":"EBI-12502259","identifier":"P61812-PRO_0000033785","identifierLink":"https://www.uniprot.org/uniprotkb/P61812-PRO_0000033785/entry","name":"TGFB2","description":"Transforming growth factor beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-606","complexName":"TGF-beta-3 complex","organismName":"Homo sapiens; 9606","description":"Cytokine complex that plays an important role in embryogenesis, tissue development, cell proliferation, differentiation and maturation, immune regulation and carcinogenesis. Binding to form its receptor complex (CPX-2544) results in the phosphorylation of TGFBR1 on Thr-185 and Thr-186 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 (Q15796) which dissociates from the receptor and activates the canonical SMAD-dependent TGF-beta signaling cascade.","predictedComplex":false,"interactors":[{"ac":"EBI-12502448","identifier":"P10600-PRO_0000033797","identifierLink":"https://www.uniprot.org/uniprotkb/P10600-PRO_0000033797/entry","name":"TGFB3","description":"Transforming growth factor beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-610","complexName":"AP-1 transcription factor complex FOS-JUN-NFATC2","organismName":"Mus musculus; 10090","description":"Member of the AP-1 transcription factor family which assemble through the homo- or hetrodimerization of proteins containing a characteristic bZIP domain (basic region leucine zipper). Regulates DNA transcription and gene expression of many immuno-response genes.","predictedComplex":false,"interactors":[{"ac":"EBI-4288185","identifier":"P01101","identifierLink":"https://www.uniprot.org/uniprotkb/P01101/entry","name":"Fos","description":"Protein c-Fos","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-643104","identifier":"Q60591","identifierLink":"https://www.uniprot.org/uniprotkb/Q60591/entry","name":"Nfatc2","description":"Nuclear factor of activated T-cells, cytoplasmic 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12533","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-764369","identifier":"P05627","identifierLink":"https://www.uniprot.org/uniprotkb/P05627/entry","name":"Jun","description":"Transcription factor Jun","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-611","complexName":"bZIP transcription factor complex, Fos-Jun","organismName":"Mus musculus; 10090","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site. Fos-Jun is capable of binding DNA on its own or as part of larger, ternary complexes with more specific transcription factor activity.","predictedComplex":false,"interactors":[{"ac":"EBI-4288185","identifier":"P01101","identifierLink":"https://www.uniprot.org/uniprotkb/P01101/entry","name":"Fos","description":"Protein c-Fos","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-764369","identifier":"P05627","identifierLink":"https://www.uniprot.org/uniprotkb/P05627/entry","name":"Jun","description":"Transcription factor Jun","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-612","complexName":"bZIP transcription factor complex, Jun-Jun","organismName":"Mus musculus; 10090","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site.   The Jun dimer acts as co-activator for a range of transcription factors, e.g. PU.1 (P17433), Cebpb (P28033) and bZIP domain-containing proteins (e.g. complex CPX-611), but probably not functional on its own.","predictedComplex":false,"interactors":[{"ac":"EBI-764369","identifier":"P05627","identifierLink":"https://www.uniprot.org/uniprotkb/P05627/entry","name":"Jun","description":"Transcription factor Jun","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-613","complexName":"SOSS1 complex","organismName":"Mus musculus; 10090","description":"A double-stranded DNA break repair complex that senses single-stranded DNA (ssDNA) and promotes repair of DNA double-strand breaks (DSBs). The binding affinity for ssDNA becomes more significant the longer the ssDNA fragment is. Influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation (G2/M), homologous recombination-dependent repair of DSBs, ATM-dependent signaling pathways and maintenance of genomic stability. The SOSSA (Int3) subunit promotes nuclear localization of the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-6910093","identifier":"Q7TPD0","identifierLink":"https://www.uniprot.org/uniprotkb/Q7TPD0/entry","name":"Ints3","description":"Integrator complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13587","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8412131","identifier":"Q8R2Y9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R2Y9/entry","name":"Nabp2","description":"SOSS complex subunit B1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13356","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8412386","identifier":"Q3TXT3","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TXT3/entry","name":"Inip","description":"SOSS complex subunit C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR31526","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-614","complexName":"SOSS2 complex","organismName":"Homo sapiens; 9606","description":"A double-stranded DNA break repair complex that senses single-stranded DNA (ssDNA) and promotes repair of DNA double-strand breaks (DSBs). The binding affinity for ssDNA becomes more significant the longer the ssDNA fragment is. Influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation (G2/M), homologous recombination-dependent repair of DSBs, ATM-dependent signaling pathways and maintenance of genomic stability. The SOSSA (INT3) subunit promotes nuclear localization of the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-2680854","identifier":"Q68E01","identifierLink":"https://www.uniprot.org/uniprotkb/Q68E01/entry","name":"INTS3","description":"Integrator complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13587","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2881520","identifier":"Q9NRY2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NRY2/entry","name":"INIP","description":"SOSS complex subunit C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31526","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2889252","identifier":"Q96AH0","identifierLink":"https://www.uniprot.org/uniprotkb/Q96AH0/entry","name":"NABP1","description":"SOSS complex subunit B2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13356","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-615","complexName":"SOSS2 complex","organismName":"Mus musculus; 10090","description":"A double-stranded DNA break repair complex that senses single-stranded DNA (ssDNA) and promotes repair of DNA double-strand breaks (DSBs). The binding affinity for ssDNA becomes more significant the longer the ssDNA fragment is. Influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation (G2/M), homologous recombination-dependent repair of DSBs, ATM-dependent signaling pathways and maintenance of genomic stability. The SOSSA (Int3) subunit promotes nuclear localization of the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-12505271","identifier":"Q8BGW5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BGW5/entry","name":"Nabp1","description":"SOSS complex subunit B2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13356","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6910093","identifier":"Q7TPD0","identifierLink":"https://www.uniprot.org/uniprotkb/Q7TPD0/entry","name":"Ints3","description":"Integrator complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13587","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8412386","identifier":"Q3TXT3","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TXT3/entry","name":"Inip","description":"SOSS complex subunit C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR31526","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-616","complexName":"UBC13-UEV1A ubiquitin-conjugating enzyme E2 complex","organismName":"Mus musculus; 10090","description":"Implicated in the non-proteolytic regulation of signaling pathways by contributing to the addition of lysine 63-linked ubiquitin chains to proteins. Transfers the thioester-bound donor ubiquitin from Ube2n onto the Ube2v1 catalytically inactive E2 variant. The heterodimer, together with the RING ubiquitin ligase Traf6, then catalyzes the formation of multiubiquitin chains linked by isopeptide bonds between Lys-63 and the C-terminus of the next monomer in the chain. This type of polyubiquitination does not lead to protein degradation by the proteasome but instead mediates activation of target genes by activating intracellular signaling cascades, in particular TRAF-dependent NF-kappa-B signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-2310567","identifier":"Q9CZY3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CZY3/entry","name":"Ube2v1","description":"Ubiquitin-conjugating enzyme E2 variant 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-494560","identifier":"P61089","identifierLink":"https://www.uniprot.org/uniprotkb/P61089/entry","name":"Ube2n","description":"Ubiquitin-conjugating enzyme E2 N","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-617","complexName":"bZIP transcription factor complex, CEBPD-CEBPD","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription","predictedComplex":false,"interactors":[{"ac":"EBI-7962058","identifier":"P49716","identifierLink":"https://www.uniprot.org/uniprotkb/P49716/entry","name":"CEBPD","description":"CCAAT/enhancer-binding protein delta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-618","complexName":"DNA ligase IV complex","organismName":"Homo sapiens; 9606","description":"DNA ligase which catalyses the final ligation step in the non-homologous end-joining DNA repair pathway. Ligates DNA strands to restore the continuity of the chromosome in non-homologous end joining DNA double-strand break repair. Deficiency in any of NHEJ complex subunits gives rise to radiosensitive severe combined immunodeficiency syndromes in human patients.","predictedComplex":false,"interactors":[{"ac":"EBI-717592","identifier":"Q13426","identifierLink":"https://www.uniprot.org/uniprotkb/Q13426/entry","name":"XRCC4","description":"DNA repair protein XRCC4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28559","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-847896","identifier":"P49917","identifierLink":"https://www.uniprot.org/uniprotkb/P49917/entry","name":"LIG4","description":"DNA ligase 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45997","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-628","complexName":"Menin-JUND transcription inhibition complex","organismName":"Mus musculus; 10090","description":"Transcription inhibitor complex. Menin binds the Jun family transcription factor Jund and blocks JNK kinase-mediated Jund phosphorylation, thereby inhibiting transcriptional activation.","predictedComplex":false,"interactors":[{"ac":"EBI-3990176","identifier":"O88559","identifierLink":"https://www.uniprot.org/uniprotkb/O88559/entry","name":"Men1","description":"Menin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12693","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5347821","identifier":"P15066","identifierLink":"https://www.uniprot.org/uniprotkb/P15066/entry","name":"Jund","description":"Transcription factor JunD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-629","complexName":"MCL-1-BIM complex","organismName":"Mus musculus; 10090","description":"An apoptotic regulatory complex where pro-apoptotic, BH3 domain-containing Bcl2l11 can inhibit anti-apoptotic Mcl1 and vice versa.","predictedComplex":false,"interactors":[{"ac":"EBI-526067","identifier":"O54918","identifierLink":"https://www.uniprot.org/uniprotkb/O54918/entry","name":"Bcl2l11","description":"Bcl-2-like protein 11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-707292","identifier":"P97287","identifierLink":"https://www.uniprot.org/uniprotkb/P97287/entry","name":"Mcl1","description":"Induced myeloid leukemia cell differentiation protein Mcl-1 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11256","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-630","complexName":"Signal recognition particle receptor complex","organismName":"Homo sapiens; 9606","description":"Mediates the co-translational targeting of membrane and secretory proteins. The signal recognition particle (SRP) binds to 9-12 large hydrophobic residues that constitute the signal sequences of nascent proteins as they emerge from the exit tunnel of the ribosome. The resulting targeting complex, composed of the SRP and the ribosome-nascent chain complex, then docks with the Signal recognition particle receptor.  This interaction catalyzes the GTP-dependent transfer of the nascent chain from SRP to the protein translocation apparatus in the ER membrane. Following GTP hydrolysis, the complex dissociates.","predictedComplex":false,"interactors":[{"ac":"EBI-355393","identifier":"Q9Y5M8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5M8/entry","name":"SRPRB","description":"Signal recognition particle receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11485","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-726981","identifier":"P08240","identifierLink":"https://www.uniprot.org/uniprotkb/P08240/entry","name":"SRPRA","description":"Signal recognition particle receptor subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-989053","identifier":"CHEBI:15996","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15996","name":"gtp","description":"guanosine triphosphate - GTP","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-631","complexName":"RXRalpha-VDR nuclear hormone receptor complex","organismName":"Homo sapiens; 9606","description":"Member of the nuclear receptor family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. The Vitamin D receptor (VDR)  mediates the transcriptional effects of Vitamin D and plays a central role in calcium homeostasis. The 9-cis retinoic acid receptor (retinoid X receptor, RXR) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including the all-trans retinoic acid receptor (RAR). Receptors bind to hormone response elements (HREs) via their DNA-binding domains (DBD) and contain a C-terminal ligand-binding domain (LBD) that binds the hormone. Unliganded VDR can occupy its response elements as a homodimer. RXRA-VDR is a non-permissive receptor that cannot be activated by an RXR agonist but only by an agonist of the dominant partner receptor, VDR. Upon binding of ligand, VDR forms a heterodimer with RXRA through their LBDs and binds to Vitamin D response elements. The ligand for RXRA, 9-cis retinoic acid, has the opposite effect of destabilizing the heterodimeric-DNA complex.","predictedComplex":false,"interactors":[{"ac":"EBI-286357","identifier":"P11473","identifierLink":"https://www.uniprot.org/uniprotkb/P11473/entry","name":"VDR","description":"Vitamin D3 receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-78598","identifier":"P19793","identifierLink":"https://www.uniprot.org/uniprotkb/P19793/entry","name":"RXRA","description":"Retinoic acid receptor RXR-alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-632","complexName":"RXRalpha-LXRalpha nuclear hormone receptor complex","organismName":"Homo sapiens; 9606","description":"Member of the nuclear receptor (NR) family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. Key modulator of macrophage cholesterol homeostasis and immune responses. Liver X receptors (LXR) function as lipid-activated transcription factors that mediate cholesterol, glucose and lipid metabolism and reverse cholesterol transport. The 9-cis retinoic acid receptor (retinoid X receptor, RXR) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including the all-trans retinoic acid receptor (RAR). The effects of ligands on LXR, RXR, and other NRs are mediated through the ligand-binding domain (LBD). RXRA-LXRA is a permissive receptor that can be activated by the ligands of either partner. Upon ligand binding, the LBD undergoes a conformational change that results in the release of corepressors, the recruitment of coactivators, and the activation of transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-781356","identifier":"Q13133","identifierLink":"https://www.uniprot.org/uniprotkb/Q13133/entry","name":"NR1H3","description":"Oxysterols receptor LXR-alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-78598","identifier":"P19793","identifierLink":"https://www.uniprot.org/uniprotkb/P19793/entry","name":"RXRA","description":"Retinoic acid receptor RXR-alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-634","complexName":"Ccr4-Not complex","organismName":"Caenorhabditis elegans; 6239","description":"Major cellular mRNA deadenylase complex, removing polyA tails that protect transcripts from degradation and promotes translation in the cytoplasm. The complex is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation, and general transcription regulation, potentially by promoting the resumption of elongation of arrested RNAPII when it encounters transcriptional blocks in vivo.\r\n\r\n\r\nThe complex is required for germ cell development in adult hermaphrodites.","predictedComplex":false,"interactors":[{"ac":"EBI-12507045","identifier":"Q9U1P4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9U1P4/entry","name":"ccr-4","description":"poly(A)-specific ribonuclease","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-12507059","identifier":"Q20937","identifierLink":"https://www.uniprot.org/uniprotkb/Q20937/entry","name":"let-711","description":"CCR4-NOT transcription complex subunit let-711","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13162","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12509760","identifier":"Q18224","identifierLink":"https://www.uniprot.org/uniprotkb/Q18224/entry","name":"ntl-9","description":"CCR4-NOT transcription complex subunit 9","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12262","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12509774","identifier":"W6RTE4","identifierLink":"https://www.uniprot.org/uniprotkb/W6RTE4/entry","name":"ntl-4","description":"CCR4-NOT transcription complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12603","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12509811","identifier":"Q9NA34","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NA34/entry","name":"ntl-11","description":"CCR4-NOT transcription complex subunit 11","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR15975","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2006376","identifier":"G5EFX8","identifierLink":"https://www.uniprot.org/uniprotkb/G5EFX8/entry","name":"ntl-3","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR23326","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-313231","identifier":"Q10923","identifierLink":"https://www.uniprot.org/uniprotkb/Q10923/entry","name":"ntl-2","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR23326","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-331358","identifier":"Q17345","identifierLink":"https://www.uniprot.org/uniprotkb/Q17345/entry","name":"ccf-1","description":"CCR4-NOT transcription complex subunit 7","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10797","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-635","complexName":"Exon junction core complex, Magoh variant","organismName":"Mus musculus; 10090","description":"Plays a role in translation, surveillance and localization of the maturing mRNA molecules. Deposited by spliceosomes at a conserved position of a pre-messenger RNA strand located upstream of exon junctions formed during RNA splicing. The EJC remains stably bound at this position as the mature messenger ribonucleoprotein particle is exported to the cytoplasm, potentially promoting export through its close association with the TREX complex. Binds RNA primarily through Eif4a3, a sequence-independent DEAD box protein  that grasps RNA stably only when associated with its partners, Rbm8a/Y14 and Magoh which inhibit the DEAD-box protein Eif4a3 ATPase activity, trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The EJC core serves as a binding platform for additional factors which together then interface with numerous machineries controlling mRNA export, translation, and decay. Discriminates between premature and normal translation termination events by providing architectural information regarding the position of (former) introns. When translation terminates on an mRNA upstream of at least one EJC, Upf3 (Q3ULJ3/Q3ULL6) and its cofactors Upf1 (Q9EPU0) and Upf2 (A2AT37) orchestrate a series of events that destabilize the message by a process known as nonsense-mediated mRNA decay (NMD). Also enhances translation of newly synthesized mRNAs through interactions between Poldip3 (Q8BG81)  and activated S6-kinase.","predictedComplex":false,"interactors":[{"ac":"EBI-12507190","identifier":"Q8K3W3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K3W3/entry","name":"Casc3","description":"Protein CASC3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13434","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1993805","identifier":"Q9CWZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CWZ3/entry","name":"Rbm8a","description":"RNA-binding protein 8A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2552399","identifier":"Q91VC3","identifierLink":"https://www.uniprot.org/uniprotkb/Q91VC3/entry","name":"Eif4a3","description":"Eukaryotic initiation factor 4A-III","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR47958","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8317341","identifier":"P61327","identifierLink":"https://www.uniprot.org/uniprotkb/P61327/entry","name":"Magoh","description":"Protein mago nashi homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12638","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-638","complexName":"Exon junction subcomplex magoh-y14","organismName":"Mus musculus; 10090","description":"Component of the exon-junction complex (EJC, CPX-635) that is formed in the nucleus and exported to the cytoplasm as part of the mature messenger ribonucleoprotein particle. Binding of the EJC key regulator Pym1 (Q8CHP5) to Magoh-Y14 in the cytoplasm triggers disassembly of the EJC. Magoh-Y14 complex remains bound in the same position on the spliced mRNA and requires translation of the mRNA for removal. When interacting with Pym1, associates with mRNA-degradation factors, including the mRNA-decapping complex and exoribonucleases and may play a role in preventing mRNA degradation during mRNA biogenesis. This complex itself does not bind RNA. Binding to Ipo13 (Q8K0C1) leads to import back into the nucleus prior to reassembly of the EJC.","predictedComplex":false,"interactors":[{"ac":"EBI-1993805","identifier":"Q9CWZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CWZ3/entry","name":"Rbm8a","description":"RNA-binding protein 8A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8317341","identifier":"P61327","identifierLink":"https://www.uniprot.org/uniprotkb/P61327/entry","name":"Magoh","description":"Protein mago nashi homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12638","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-642","complexName":"Negative cofactor 2 transcriptional regulator complex","organismName":"Homo sapiens; 9606","description":"Represses RNA polymerase II transcription through binding to TBP (P20226) and thereby inhibiting the assembly of the transcription preinitiation complex..","predictedComplex":false,"interactors":[{"ac":"EBI-712941","identifier":"Q14919","identifierLink":"https://www.uniprot.org/uniprotkb/Q14919/entry","name":"DRAP1","description":"Dr1-associated corepressor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10252","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-750300","identifier":"Q01658","identifierLink":"https://www.uniprot.org/uniprotkb/Q01658/entry","name":"DR1","description":"Protein Dr1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46138","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-643","complexName":"RXRalpha-NCOA2 activated retinoic acid receptor complex","organismName":"Mus musculus; 10090","description":"Member of the nuclear receptor (NR) family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. The 9-cis retinoic acid receptor (retinoid X receptor, Rxra) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including the all-trans retinoic acid receptors (RARs). Like other NRs, Rxra contains DNA-binding and ligand-binding domain (DBD, LBD). In the absence of agonist, the complex recruits the corepressor proteins NCoR or SMRT and associated factors such as histone deacetylases or DNA-methyl transferases that may lead to an inactive condensed chromatin structure, preventing transcription. Upon ligand binding, RXRs undergo a conformational change that results in the release of corepressors and transcriptional coactivators, such as Ncoa2, are recruited to the LBD which activates transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-346715","identifier":"P28700","identifierLink":"https://www.uniprot.org/uniprotkb/P28700/entry","name":"Rxra","description":"Retinoic acid receptor RXR-alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-688662","identifier":"Q61026","identifierLink":"https://www.uniprot.org/uniprotkb/Q61026/entry","name":"Ncoa2","description":"Nuclear receptor coactivator 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-644","complexName":"PXR-NCOA1 activated nuclear receptor complex","organismName":"Mus musculus; 10090","description":"Member of the nuclear receptor (NR) family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in metabolism. The pregnane X receptor (Nr1i2/Pxr) is a central xenobiotic sensor that detects potentially toxic chemicals and regulates the expression of genes central to their breakdown and removal. Like other members of the orphan class of the NR superfamily, NR1I2 contains DNA-binding and ligand-binding domain (DBD, LBD). Upon ligand binding, transcriptional coactivators, such as Ncoa1 (P70365), are recruited leading to transcriptional activation. \r\n\r\nNr1i2 also binds as a heterotetramer with the 9-cis retinoic acid receptor (Rxra, P28700, CPX-505) to xenobiotic response elements in cytochrome P450 3A (CYP3A) gene promoters and is activated by the spectrum of chemicals that are known to induce CYP3A gene expression.","predictedComplex":false,"interactors":[{"ac":"EBI-11171952","identifier":"P70365","identifierLink":"https://www.uniprot.org/uniprotkb/P70365/entry","name":"Ncoa1","description":"Nuclear receptor coactivator 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11892436","identifier":"O54915","identifierLink":"https://www.uniprot.org/uniprotkb/O54915/entry","name":"Nr1i2","description":"Nuclear receptor subfamily 1 group I member 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-647","complexName":"CD1B-B2M complex","organismName":"Homo sapiens; 9606","description":"An antigen-presenting complex that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells. The antigen binding specificity of CD1B is very broad in terms of length of the acyl chains. CD1B also presents endogenous gangliosides, such as GM1, to specific T cells, suggesting their involvement in autoimmune diseases such as multiple sclerosis.","predictedComplex":false,"interactors":[{"ac":"EBI-1033762","identifier":"P29016","identifierLink":"https://www.uniprot.org/uniprotkb/P29016/entry","name":"CD1B","description":"T-cell surface glycoprotein CD1b","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16675","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714718","identifier":"P61769","identifierLink":"https://www.uniprot.org/uniprotkb/P61769/entry","name":"B2M","description":"Beta-2-microglobulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19944","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-648","complexName":"CRL4-DDB2 E3 ubiquitin ligase complex, CUL4B variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor DDB2. The complex recognises UV-induced cyclobutane pyrimidine dimers in chromatin and facilitates nucleotide excision repair. Ubiquitinates XPC (Q01831), histones and other chromatin-associated proteins located within approximately 100A around the DNA lesion. Ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair. Mutations in DDB2 can cause Xeroderma pigmentosum and other solar photosensitivity related diseases. Mutations in CUL4B are related to the Cabezas type of X-linked intellectual disabilities. Inactivated by the binding of the COP9 signalosome (CPX-1870 & CPX-1871) which is overcome by substrate binding to the DDB2 subunit.","predictedComplex":false,"interactors":[{"ac":"EBI-1176171","identifier":"Q92466","identifierLink":"https://www.uniprot.org/uniprotkb/Q92466/entry","name":"DDB2","description":"DNA damage-binding protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15169","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456067","identifier":"Q13620","identifierLink":"https://www.uniprot.org/uniprotkb/Q13620/entry","name":"CUL4B","description":"Cullin-4B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-650","complexName":"CRL4-DDB2 E3 ubiquitin ligase complex, CUL4A variant","organismName":"Mus musculus; 10090","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor Ddb2. The complex recognises UV-induced cyclobutane pyrimidine dimers in chromatin and facilitates nucleotide excision repair. Ubiquitinates XPC (P51612), histones and other chromatin-associated proteins located within approximately 100 A around the DNA lesion. Ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair. Involved in Xeroderma pigmentosum and other solar photosensitivity related diseases.  Inactivated by the binding of the COP9 signalosome which is overcome by substrate binding to the DDB2 subunit.","predictedComplex":false,"interactors":[{"ac":"EBI-12510080","identifier":"Q99J79","identifierLink":"https://www.uniprot.org/uniprotkb/Q99J79/entry","name":"Ddb2","description":"DNA damage-binding protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15169","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2507414","identifier":"P62878","identifierLink":"https://www.uniprot.org/uniprotkb/P62878/entry","name":"Rbx1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2552275","identifier":"Q3U1J4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3U1J4/entry","name":"Ddb1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8320699","identifier":"Q3TCH7","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TCH7/entry","name":"Cul4a","description":"Cullin-4A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-651","complexName":"CRL4-DDB2 E3 ubiquitin ligase complex, CUL4B variant","organismName":"Mus musculus; 10090","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor Ddb2. The complex recognises UV-induced cyclobutane pyrimidine dimers in chromatin and facilitates nucleotide excision repair. Ubiquitinates XPC (P51612), histones and other chromatin-associated proteins located within approximately 100 A around the DNA lesion. Ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair. Involved in Xeroderma pigmentosum and other solar photosensitivity related diseases. Inactivated by the binding of the COP9 signalosome which is overcome by substrate binding to the DDB2 subunit.","predictedComplex":false,"interactors":[{"ac":"EBI-12510080","identifier":"Q99J79","identifierLink":"https://www.uniprot.org/uniprotkb/Q99J79/entry","name":"Ddb2","description":"DNA damage-binding protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15169","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2507414","identifier":"P62878","identifierLink":"https://www.uniprot.org/uniprotkb/P62878/entry","name":"Rbx1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2552275","identifier":"Q3U1J4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3U1J4/entry","name":"Ddb1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3043864","identifier":"A2A432","identifierLink":"https://www.uniprot.org/uniprotkb/A2A432/entry","name":"Cul4b","description":"Cullin-4B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-652","complexName":"RXRbeta-LXRbeta nuclear hormone receptor complex","organismName":"Homo sapiens; 9606","description":"Member of the nuclear receptor (NR) family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. Liver X receptors (LXR) function as transcription factors that mediate cholesterol, glucose and lipid metabolism and reverse cholesterol transport. The 9-cis retinoic acid receptor (retinoid X receptor, RXR) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including the all-trans retinoic acid receptor (RAR). The effects of ligands on LXR, RXR, and other NRs are mediated through the ligand-binding domain (LBD). Upon ligand binding, the LBD undergoes a conformational change that results in the release of corepressors, the recruitment of coactivators, and the activation of transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-745354","identifier":"P55055","identifierLink":"https://www.uniprot.org/uniprotkb/P55055/entry","name":"NR1H2","description":"Oxysterols receptor LXR-beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-748576","identifier":"P28702","identifierLink":"https://www.uniprot.org/uniprotkb/P28702/entry","name":"RXRB","description":"Retinoic acid receptor RXR-beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-653","complexName":"PAN2-PAN3 mRNA deadenylation complex","organismName":"Caenorhabditis elegans; 6239","description":"A poly(A)-specific 3' exoribonuclease required to regulate Poly(A) tails added to mRNA co-transcriptionally and  which are required for the export of mature mRNAs to the cytoplasm  The complex is responsible for the poly(A) trimming of the tail length to a transcript specific size which regulates  translation repression and mRNA decay. The complex is non-essential, but its deletion results in increased polyA-tail length.","predictedComplex":false,"interactors":[{"ac":"EBI-12510166","identifier":"P53015","identifierLink":"https://www.uniprot.org/uniprotkb/P53015/entry","name":"panl-2","description":"PolyA-specific ribonuclease subunit panl-2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR15728","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-330772","identifier":"P34653","identifierLink":"https://www.uniprot.org/uniprotkb/P34653/entry","name":"panl-3","description":"PAN2-PAN3 deadenylation complex subunit PAN3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12272","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-654","complexName":"RXRalpha-TRbeta nuclear hormone receptor complex","organismName":"Homo sapiens; 9606","description":"Member of the nuclear receptor family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. Thyroid hormone receptors (TRs) regulate gene expression in response to thyroid hormone, predominantly triiodothyronine, T3. Thyroid hormones are essential for early development and also for metabolic balance. The 9-cis retinoic acid receptor (retinoid X receptor, RXR) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including the all-trans retinoic acid receptor (RAR). Receptors bind to T3 response elements (TREs) via their DNA-binding domains (DBD) and contain a C-terminal ligand-binding domain (LBD) that binds the hormone. Both THRB isoforms contribute to T3 feedback on thyrotropin-releasing hormone (TRH), with THRB1 having a more important role in the activation of TRH transcription. Unliganded receptor generally represses basal transcription. Unliganded receptor generally represses basal transcription. RXRA-THRB is a non-permissive receptor that cannot be activated by an RXR agonist but only by an agonist of the dominant partner receptor, THRB. Binding of THRB induces a conformation changes which allosterically silences RXR. Upon ligand binding, the LBD undergoes a conformational change that results in the release of corepressors, the recruitment of coactivators, and the activation of transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-78558","identifier":"P10828","identifierLink":"https://www.uniprot.org/uniprotkb/P10828/entry","name":"THRB","description":"Thyroid hormone receptor beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-78598","identifier":"P19793","identifierLink":"https://www.uniprot.org/uniprotkb/P19793/entry","name":"RXRA","description":"Retinoic acid receptor RXR-alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-658","complexName":"Actin junctional complex","organismName":"Homo sapiens; 9606","description":"Binds actin-spectrin meshwork structures to form erythrocyte membrane skeletons, which support the erythrocyte membrane and provide stability, especially under blood flow","predictedComplex":false,"interactors":[{"ac":"EBI-1050906","identifier":"P11171","identifierLink":"https://www.uniprot.org/uniprotkb/P11171/entry","name":"EPB41","description":"Protein 4.1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23280","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-711788","identifier":"Q00013","identifierLink":"https://www.uniprot.org/uniprotkb/Q00013/entry","name":"MPP1","description":"55 kDa erythrocyte membrane protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23122","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7797098","identifier":"P04921","identifierLink":"https://www.uniprot.org/uniprotkb/P04921/entry","name":"GYPC","description":"Glycophorin-C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47614","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-659","complexName":"CDT1-Geminin complex","organismName":"Homo sapiens; 9606","description":"Regulates DNA replication during the S and G2 phases of the cell cycle. Complex formation inhibits the DNA replication licensing factor CDT1 from initiating a further round of DNA replication, preventing the MCM complex (CPX-2940) from being reloaded to chromatin until the end of mitosis.This maintains genomic stability, ensuring once-per-cell-cycle genome replication.","predictedComplex":false,"interactors":[{"ac":"EBI-371669","identifier":"O75496","identifierLink":"https://www.uniprot.org/uniprotkb/O75496/entry","name":"GMNN","description":"Geminin","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13372","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456953","identifier":"Q9H211","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H211/entry","name":"CDT1","description":"DNA replication factor Cdt1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28637","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-660","complexName":"HOXC9-Geminin transcriptional repressor complex","organismName":"Homo sapiens; 9606","description":"Plays a role in preventing the HOXC9  transcription factor from binding to DNA, thus inhibiting Hox-dependent transcriptional activation of downstream target genes.May also play a role in cell cycle progression, inhibiting the formation of the Cdt1-Geminin complex (CPX-659), thus inhibiting the function of Geminin in DNA replication licensing regulation.","predictedComplex":false,"interactors":[{"ac":"EBI-1779423","identifier":"P31274","identifierLink":"https://www.uniprot.org/uniprotkb/P31274/entry","name":"HOXC9","description":"Homeobox protein Hox-C9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45970","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371669","identifier":"O75496","identifierLink":"https://www.uniprot.org/uniprotkb/O75496/entry","name":"GMNN","description":"Geminin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13372","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-661","complexName":"IDAS-Geminin complex","organismName":"Homo sapiens; 9606","description":"Required for cell cycle progression, inhibiting the formation of the Cdt1-Geminin complex (CPX-659), thus inhibiting the function of Geminin in DNA replication licensing regulation.","predictedComplex":false,"interactors":[{"ac":"EBI-371669","identifier":"O75496","identifierLink":"https://www.uniprot.org/uniprotkb/O75496/entry","name":"GMNN","description":"Geminin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13372","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3954372","identifier":"D6RGH6","identifierLink":"https://www.uniprot.org/uniprotkb/D6RGH6/entry","name":"MCIDAS","description":"Multicilin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13372","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-662","complexName":"RXRalpha-TRalpha nuclear hormone receptor complex","organismName":"Homo sapiens; 9606","description":"Member of the nuclear receptor family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. Thyroid hormone receptors (TRs) regulate gene expression in response to thyroid hormone, predominantly triiodothyronine, T3. Thyroid hormones are essential for early development and also for metabolic balance. The 9-cis retinoic acid receptor (retinoid X receptor, RXR) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including the all-trans retinoic acid receptor (RAR). Receptors bind to T3 response elements (TREs) via their DNA-binding domains (DBD) and contain a C-terminal ligand-binding domain (LBD) that binds the hormone. Unliganded receptor generally represses basal transcription. RXRA-THRA is a non-permissive receptor that cannot be activated by an RXR agonist but only by an agonist of the dominant partner receptor, THRA. Binding of THRA induces a conformation changes which allosterically silences RXR. Upon ligand binding, the LBD undergoes a conformational change that results in the release of corepressors, the recruitment of coactivators, and the activation of transcription. Several alternative splice product of THRA, for example variant alpha-2 (P10827-1), have alternative carboxyl-terminal domains, therefore are not capable of binding T3. THRA alpha-2 is not a functional TR but may act as an inhibitor of thyroid hormone action.","predictedComplex":false,"interactors":[{"ac":"EBI-12518328","identifier":"P10827-2","identifierLink":"https://www.uniprot.org/uniprotkb/P10827-2/entry","name":"THRA","description":"Thyroid hormone receptor alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-78598","identifier":"P19793","identifierLink":"https://www.uniprot.org/uniprotkb/P19793/entry","name":"RXRA","description":"Retinoic acid receptor RXR-alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2351","complexName":"ToRC chromatin remodelling complex","organismName":"Drosophila melanogaster; 7227","description":"ATP-dependent nucleosome remodeling complex that represses ribosomal gene transcription. 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KDM2B contributes to generic genomic localization of this complex variant around promoters and other loci enriched for unmethylated CpG islands.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3955564","identifier":"Q8NHM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NHM5/entry","name":"KDM2B","description":"Lysine-specific demethylase 2B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23123","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749901","identifier":"Q9BSM1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BSM1/entry","name":"PCGF1","description":"Polycomb group RING finger protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10825","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752313","identifier":"Q06587","identifierLink":"https://www.uniprot.org/uniprotkb/Q06587/entry","name":"RING1","description":"E3 ubiquitin-protein ligase RING1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752324","identifier":"Q8N488","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N488/entry","name":"RYBP","description":"RING1 and YY1-binding protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12920","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-950027","identifier":"Q6W2J9","identifierLink":"https://www.uniprot.org/uniprotkb/Q6W2J9/entry","name":"BCOR","description":"BCL-6 corepressor","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2355","complexName":"Mi2/NuRD nucleosome remodeling and deacetylase complex","organismName":"Drosophila melanogaster; 7227","description":"Corepressor complex that couples histone deacetylase and ATP-dependent chromatin remodeling activities. 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Gene duplications have led to expansions of most COPII proteins in vertebrates suggesting multiple complex variants exist.","predictedComplex":false,"interactors":[{"ac":"EBI-1046596","identifier":"P55735","identifierLink":"https://www.uniprot.org/uniprotkb/P55735/entry","name":"SEC13","description":"Protein SEC13 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11024","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1767898","identifier":"O94979","identifierLink":"https://www.uniprot.org/uniprotkb/O94979/entry","name":"SEC31A","description":"Protein transport protein Sec31A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13923","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3893064","identifier":"Q9NQW1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NQW1/entry","name":"SEC31B","description":"Protein transport protein Sec31B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13923","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3920694","identifier":"Q9NR31","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NR31/entry","name":"SAR1A","description":"Small COPII coat GTPase SAR1A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4290665","identifier":"Q9Y6B6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6B6/entry","name":"SAR1B","description":"Small COPII coat GTPase SAR1B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-748817","identifier":"O94855","identifierLink":"https://www.uniprot.org/uniprotkb/O94855/entry","name":"SEC24D","description":"Protein transport protein Sec24D","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13803","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749911","identifier":"O95486","identifierLink":"https://www.uniprot.org/uniprotkb/O95486/entry","name":"SEC24A","description":"Protein transport protein Sec24A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13803","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-81101","identifier":"O95487","identifierLink":"https://www.uniprot.org/uniprotkb/O95487/entry","name":"SEC24B","description":"Protein transport protein Sec24B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13803","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-81134","identifier":"P53992","identifierLink":"https://www.uniprot.org/uniprotkb/P53992/entry","name":"SEC24C","description":"Protein transport protein Sec24C","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13803","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2362","complexName":"NuRF nucleosome remodelling factor","organismName":"Drosophila melanogaster; 7227","description":"ATP-dependent chromatin-remodelling complex with intrinsic nucleosome dependent ATPase activity. Appears to promote ATP-dependent nucleosome sliding and transcription from chromatin templates. NURF binds the nucleosome near the\r\nDNA entry sites in an asymmetrical fashion and nucleosome sliding occurs in increments of 10 base pairs.","predictedComplex":false,"interactors":[{"ac":"EBI-132817","identifier":"Q9W0T1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W0T1/entry","name":"E(bx)","description":"Nucleosome-remodeling factor subunit NURF301","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45975","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-367628","identifier":"Q24368","identifierLink":"https://www.uniprot.org/uniprotkb/Q24368/entry","name":"Iswi","description":"Chromatin-remodeling complex ATPase chain Iswi","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-75924","identifier":"Q24572","identifierLink":"https://www.uniprot.org/uniprotkb/Q24572/entry","name":"Caf1-55","description":"Chromatin assembly factor 1 p55 subunit","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-96355","identifier":"O77460","identifierLink":"https://www.uniprot.org/uniprotkb/O77460/entry","name":"Nurf-38","description":"Inorganic pyrophosphatase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10286","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2363","complexName":"BCDX2 complex","organismName":"Homo sapiens; 9606","description":"Functions during fork protection by restraining fork progression, \r\ndriving reversed replication fork formation, presumably by assisting the central recombinase RAD51 (Q06609). It may also assist DNA translocases and RAD51 in driving parental strand reannealing. BCDX2 stimulates the nucleation and extension of RAD51 filaments,, essential for recombinational DNA repair in reactions that depend on the coupled ATPase activities of RAD51B and RAD51C. The complex binds to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks and appears to be active downstream of BRCA2 recruitment and upstream of RAD51 recruitment.","predictedComplex":false,"interactors":[{"ac":"EBI-1055693","identifier":"O75771","identifierLink":"https://www.uniprot.org/uniprotkb/O75771/entry","name":"RAD51D","description":"DNA repair protein RAD51 homolog 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46457","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2267048","identifier":"O43502","identifierLink":"https://www.uniprot.org/uniprotkb/O43502/entry","name":"RAD51C","description":"DNA repair protein RAD51 homolog 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2824089","identifier":"O15315","identifierLink":"https://www.uniprot.org/uniprotkb/O15315/entry","name":"RAD51B","description":"DNA repair protein RAD51 homolog 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46456","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3918457","identifier":"O43543","identifierLink":"https://www.uniprot.org/uniprotkb/O43543/entry","name":"XRCC2","description":"DNA repair protein XRCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2365","complexName":"SCF E3 ubiquitin ligase complex, BTRC variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-BTRC target proteins include PDCD4 (Q53EL6), proteasomal destruction of which prevents inhibition of the eukaryotic translation initiation factor eIF4A (P6084/Q14240) by PDCD4, enabling efficient protein translation and cell growth, and CDC25A (P30304) thus regulating CDK1 (P06493) activity.during S-phase. By late G2 SCF-BTRC no longer targets CDC25A but instead ubiquitinates the WEE1 (P06493) G2 checkpoint kinase. Ubiquitinates phosphorylated CTNNB1 (P35222) thus participating in the regulation of Wnt signaling, and phosphorylated NFKBIA (P25963), degradation of which frees the associated NFKB1 (P19838) to translocate into the nucleus and to activate transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-307461","identifier":"Q9Y297","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y297/entry","name":"BTRC","description":"F-box/WD repeat-containing protein 1A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14604","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2366","complexName":"Myb-MuvB transcriptional activation complex","organismName":"Homo sapiens; 9606","description":"Transcriptional activation complex which forms in the S phase and transactivates cell-cycle genes related to the S/G2/M phase. Genes activated by Myb-MuvB  contain a cell-cycle homology region (CHR) DNA element in their promoters which is bound by LIN54","predictedComplex":false,"interactors":[{"ac":"EBI-1389411","identifier":"Q6MZP7","identifierLink":"https://www.uniprot.org/uniprotkb/Q6MZP7/entry","name":"LIN54","description":"Protein lin-54 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12446","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1389424","identifier":"Q5TKA1","identifierLink":"https://www.uniprot.org/uniprotkb/Q5TKA1/entry","name":"LIN9","description":"Protein lin-9 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21689","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1389456","identifier":"Q52LA3","identifierLink":"https://www.uniprot.org/uniprotkb/Q52LA3/entry","name":"LIN52","description":"Protein lin-52 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31489","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1389468","identifier":"P10244","identifierLink":"https://www.uniprot.org/uniprotkb/P10244/entry","name":"MYBL2","description":"Myb-related protein B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45614","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-620823","identifier":"Q09028","identifierLink":"https://www.uniprot.org/uniprotkb/Q09028/entry","name":"RBBP4","description":"Histone-binding protein RBBP4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-748884","identifier":"Q96GY3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GY3/entry","name":"LIN37","description":"Protein lin-37 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31336","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2368","complexName":"DREAM transcriptional repressor complex, RBL1 variant","organismName":"Homo sapiens; 9606","description":"Mediates gene repression during the G0 phase and coordinates periodic gene expression with peaks during the G1/S and G2/M phases. In early G1, the complex binds to E2F, CHR, CDE (cell cycle-dependent element), and CLE (CHR-like element) promoter sites and represses more than 800 cell cycle-dependent genes in quiescent cells, mediating TP53 activity. In the late stage of G1, DREAM-specific protein separates from the MuvB core (LIN9, LIN37, LIN52, LIN53, and LIN54) and then binds to MYBB (P10244) in the S phase to form the MMB complex (CPX-2366) which transactivates cell-cycle genes related to the S/G2/M phase.","predictedComplex":false,"interactors":[{"ac":"EBI-1389411","identifier":"Q6MZP7","identifierLink":"https://www.uniprot.org/uniprotkb/Q6MZP7/entry","name":"LIN54","description":"Protein lin-54 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12446","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1389424","identifier":"Q5TKA1","identifierLink":"https://www.uniprot.org/uniprotkb/Q5TKA1/entry","name":"LIN9","description":"Protein lin-9 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21689","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1389456","identifier":"Q52LA3","identifierLink":"https://www.uniprot.org/uniprotkb/Q52LA3/entry","name":"LIN52","description":"Protein lin-52 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31489","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1389773","identifier":"Q15329","identifierLink":"https://www.uniprot.org/uniprotkb/Q15329/entry","name":"E2F5","description":"Transcription factor E2F5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12081","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-448943","identifier":"Q16254","identifierLink":"https://www.uniprot.org/uniprotkb/Q16254/entry","name":"E2F4","description":"Transcription factor E2F4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12081","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-620823","identifier":"Q09028","identifierLink":"https://www.uniprot.org/uniprotkb/Q09028/entry","name":"RBBP4","description":"Histone-binding protein RBBP4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-748884","identifier":"Q96GY3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GY3/entry","name":"LIN37","description":"Protein lin-37 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31336","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749713","identifier":"Q14186","identifierLink":"https://www.uniprot.org/uniprotkb/Q14186/entry","name":"TFDP1","description":"Transcription factor Dp-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12548","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752268","identifier":"Q14188","identifierLink":"https://www.uniprot.org/uniprotkb/Q14188/entry","name":"TFDP2","description":"Transcription factor Dp-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12548","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-971402","identifier":"P28749","identifierLink":"https://www.uniprot.org/uniprotkb/P28749/entry","name":"RBL1","description":"Retinoblastoma-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2369","complexName":"Nuclear origin recognition complex","organismName":"Drosophila melanogaster; 7227","description":"Binds and encircles origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not yet been identified. ORC recruits cdc6 (Q9VSM9) and dup/cdt1 (Q7JVY2) to promote the loading of the MCM2-7 mini-chromosome maintenance complex (CPX-2942) onto chromatin to form the pre-replication complex necessary to initiate DNA replication. ORC is dynamically assembled and disassembled during the cell cycle. The complex is formed in an ATP-dependent manner at the exit from anaphase of mitosis and the complex binds to chromatin in an ORC1-dependent manner. ORC is disassembled in S phase, either by degradation of ORC1 or by a process involving ATP hydrolysis in the complex. ORC1 is thought to be regenerated and to cooperate with ORC4 to initiate a new cycle of pre-RC formation.","predictedComplex":false,"interactors":[{"ac":"EBI-113296","identifier":"Q9Y1B2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y1B2/entry","name":"Orc6","description":"Origin recognition complex subunit 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13394","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-137663","identifier":"Q24169","identifierLink":"https://www.uniprot.org/uniprotkb/Q24169/entry","name":"Orc5","description":"Origin recognition complex subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12705","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-156676","identifier":"Q9W102","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W102/entry","name":"Orc4","description":"Origin recognition complex subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12087","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-179453","identifier":"Q24168","identifierLink":"https://www.uniprot.org/uniprotkb/Q24168/entry","name":"Orc2","description":"Origin recognition complex subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14052","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-182021","identifier":"Q7K2L1","identifierLink":"https://www.uniprot.org/uniprotkb/Q7K2L1/entry","name":"Orc3","description":"Origin recognition complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12748","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-90907","identifier":"O16810","identifierLink":"https://www.uniprot.org/uniprotkb/O16810/entry","name":"Orc1","description":"Origin recognition complex subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10763","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2370","complexName":"PAF1 complex","organismName":"Drosophila melanogaster; 7227","description":"A multifunctional complex involved in many aspects of RNA polymerase II (Pol II, CPX-2625) transcriptional regulation, including transcriptional elongation, 3'-terminal end processing, and histone modification. Role in 3'-end formation of mRNAs, required for the recruitment of cleavage and polyadenylation factors CFT1 and PCF11 to RNA polymerase II.","predictedComplex":false,"interactors":[{"ac":"EBI-111745","identifier":"Q9W261","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W261/entry","name":"Rtf1","description":"RNA polymerase-associated protein Rtf1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-133299","identifier":"Q94546","identifierLink":"https://www.uniprot.org/uniprotkb/Q94546/entry","name":"Atu","description":"Another transcription unit protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23146","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-144765","identifier":"Q7K0X3","identifierLink":"https://www.uniprot.org/uniprotkb/Q7K0X3/entry","name":"Ctr9","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14027","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-186961","identifier":"Q9VHI1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VHI1/entry","name":"hyx","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12466","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6102707","identifier":"Q9VN55","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VN55/entry","name":"atms","description":"RNA polymerase II-associated factor 1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23188","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2371","complexName":"TIM8-TIM13 mitochondrial intermembrane space protein transporter complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Facilitates transport of hydrophobic precursors of a distinct subgroup of inner membrane proteins through the aqueous intermembrane space as they exit the TOM40 channel complex (CPX-474) in the outer membrane. Plays a role in the import of a distinct subgroup of inner membrane proteins, functioning as a chaperone to maintain the hydrophobic membrane proteins in an import competent state and escort substrates to the TIM22 insertion complex (CPX-1629), which mediates protein insertion into the membrane. Cross-links to the COOH-terminal domain of the essential import translocase protein TIM23 (P32897) and plays a key role in TIM23 import to the mitochondrial inner membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-9013892","identifier":"P57744","identifierLink":"https://www.uniprot.org/uniprotkb/P57744/entry","name":"TIM8","description":"Mitochondrial import inner membrane translocase subunit TIM8","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9121","identifier":"P53299","identifierLink":"https://www.uniprot.org/uniprotkb/P53299/entry","name":"TIM13","description":"Mitochondrial import inner membrane translocase subunit TIM13","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2372","complexName":"POMT1-POMT2 O-mannosyltransferase complex","organismName":"Drosophila melanogaster; 7227","description":"Catalyzes the addition of an O-linked mannose to the hydroxyl group of serines or threonines of proteins such as  the transmembrane protein dystroglycan (A0A0C4DHF6). Drosophila O-mannose exists on proteins as a monosaccharide. 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Mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. 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Appear to mediate the targeted action of an enhancer, mediating transcription  in a pattern that is generated by enhancers close to the insertion site in multiple loci throughout the genome.","predictedComplex":false,"interactors":[{"ac":"EBI-110368","identifier":"P02572","identifierLink":"https://www.uniprot.org/uniprotkb/P02572/entry","name":"Act42A","description":"Actin-42A","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-123863","identifier":"Q7K012","identifierLink":"https://www.uniprot.org/uniprotkb/Q7K012/entry","name":"Bap55","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-126851","identifier":"A1Z6M0","identifierLink":"https://www.uniprot.org/uniprotkb/A1Z6M0/entry","name":"Bap170","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22970","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-130188","identifier":"P10987","identifierLink":"https://www.uniprot.org/uniprotkb/P10987/entry","name":"Act5C","description":"Actin-5C","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-131186","identifier":"Q9VWF2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VWF2/entry","name":"e(y)3","description":"Supporter of activation of yellow protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23202","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-132623","identifier":"Q9VF03","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VF03/entry","name":"mor","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-151570","identifier":"Q24090","identifierLink":"https://www.uniprot.org/uniprotkb/Q24090/entry","name":"Snr1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-163765","identifier":"Q9W384","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W384/entry","name":"Bap111","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-184086","identifier":"Q9VC36","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VC36/entry","name":"polybromo","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR16062","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3417869","identifier":"Q9VLX2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VLX2/entry","name":"Brd7-9","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22881","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-75169","identifier":"Q9VYG2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VYG2/entry","name":"Bap60","description":"Brahma-associated protein of 60 kDa","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-868480","identifier":"P25439","identifierLink":"https://www.uniprot.org/uniprotkb/P25439/entry","name":"brm","description":"ATP-dependent helicase brm","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2384","complexName":"Phosphatidylinositol 3-kinase complex class IA, p110alpha/p85alpha","organismName":"Homo sapiens; 9606","description":"Uses 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate/PI(4,5)P2 (CHEBI:18348) as a substrate to generate the product 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate/PI(3,4,5)P3 (CHEBI:16618) which initiates major signaling pathways downstream. Performs a central role in cellular signaling, mediating responses to growth factors and extracellular stimuli. This variant is found to be ubiquitously expressed in human cells.","predictedComplex":false,"interactors":[{"ac":"EBI-2116585","identifier":"P42336","identifierLink":"https://www.uniprot.org/uniprotkb/P42336/entry","name":"PIK3CA","description":"Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-79464","identifier":"P27986","identifierLink":"https://www.uniprot.org/uniprotkb/P27986/entry","name":"PIK3R1","description":"Phosphatidylinositol 3-kinase regulatory subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10155","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2385","complexName":"Hypoxia-inducible transcription factor complex, HIF2","organismName":"Homo sapiens; 9606","description":"A basic helix-loop-helix-PER-ARNT-SIM (bHLH-PAS) family transcription factor complex composed of a constitutively expressed HIF-beta subunit and an oxygen-regulated HIF-alpha subunit which mediates hypoxia-dependent transcription.  Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element  of target gene promoters. HIF-dependent transcription is activated by insulin and mediated by the PI3K-AKT and TOR pathways and  regulates the transcription of genes involved in a multitude of processes including angiogenesis, erythropoiesis, cell proliferation/survival, glucose metabolism, and iron metabolism.","predictedComplex":false,"interactors":[{"ac":"EBI-447470","identifier":"Q99814","identifierLink":"https://www.uniprot.org/uniprotkb/Q99814/entry","name":"EPAS1","description":"Endothelial PAS domain-containing protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23043","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-80809","identifier":"P27540","identifierLink":"https://www.uniprot.org/uniprotkb/P27540/entry","name":"ARNT","description":"Aryl hydrocarbon receptor nuclear translocator","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23042","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2386","complexName":"DNA-directed RNA polymerase I complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the transcription of ribosomal RNA from a DNA template by acting as a nucleotidyl transferase that polymerizes ribonucleotides at the 3' end of an RNA transcript synthesizing precursors of rRNAs.","predictedComplex":false,"interactors":[{"ac":"EBI-1055079","identifier":"O15160","identifierLink":"https://www.uniprot.org/uniprotkb/O15160/entry","name":"POLR1C","description":"DNA-directed RNA polymerases I and III subunit RPAC1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1642554","identifier":"Q3B726","identifierLink":"https://www.uniprot.org/uniprotkb/Q3B726/entry","name":"POLR1F","description":"DNA-directed RNA polymerase I subunit RPA43","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12709","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355434","identifier":"Q9P1U0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P1U0/entry","name":"POLR1H","description":"DNA-directed RNA polymerase I subunit RPA12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355441","identifier":"Q9H9Y6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H9Y6/entry","name":"POLR1B","description":"DNA-directed RNA polymerase I subunit RPA2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20856","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359424","identifier":"O15446","identifierLink":"https://www.uniprot.org/uniprotkb/O15446/entry","name":"POLR1G","description":"DNA-directed RNA polymerase I subunit RPA34","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15484","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359458","identifier":"Q9GZS1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9GZS1/entry","name":"POLR1E","description":"DNA-directed RNA polymerase I subunit RPA49","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14440","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359472","identifier":"O95602","identifierLink":"https://www.uniprot.org/uniprotkb/O95602/entry","name":"POLR1A","description":"DNA-directed RNA polymerase I subunit RPA1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19376","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359498","identifier":"P0DPB6","identifierLink":"https://www.uniprot.org/uniprotkb/P0DPB6/entry","name":"POLR1D","description":"DNA-directed RNA polymerases I and III subunit RPAC2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13946","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359505","identifier":"P52434","identifierLink":"https://www.uniprot.org/uniprotkb/P52434/entry","name":"POLR2H","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10917","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359527","identifier":"P62875","identifierLink":"https://www.uniprot.org/uniprotkb/P62875/entry","name":"POLR2L","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23431","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395180","identifier":"P61218","identifierLink":"https://www.uniprot.org/uniprotkb/P61218/entry","name":"POLR2F","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47227","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395189","identifier":"P19388","identifierLink":"https://www.uniprot.org/uniprotkb/P19388/entry","name":"POLR2E","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10535","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395357","identifier":"P53803","identifierLink":"https://www.uniprot.org/uniprotkb/P53803/entry","name":"POLR2K","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2387","complexName":"DNA-directed RNA polymerase II complex, Pol II(G) variant","organismName":"Homo sapiens; 9606","description":"Catalyzes the transcription of RNA from a DNA template by acting as a nucleotidyl transferase that polymerizes ribonucleotides at the 3' end of an RNA transcript. Synthesizes precursors of mRNAs, and most snRNA and microRNAs. In the absence of Mediator, Pol II(G), unlike Pol II, inhibits transcription.\r\n\r\nDuring a transcription cycle, Pol II, general transcription factors and the mediator complex (CPX-3227) assemble as the preinitiation complex (PIC) at the promoter. 11-15 base pairs of DNA surrounding the transcription start site are melted and the single-stranded DNA template strand of the promoter is positioned deeply within the central active site cleft of Pol II to form the open complex. After synthesis of about 30 bases of RNA, Pol II releases its contacts with the core promoter and the rest of the transcription machinery (promoter clearance) and enters the stage of transcription elongation in which it moves on the template as the transcript elongates. Pol II appears to oscillate between inactive and active conformations at each step of nucleotide addition. The formation of PolII(G) by the binding of POLR2M represses RNA polymerase II  function by preventing TFIIF (CPX-79) and TFIIB (CPX-2398) from binding to Pol II, which contributes to the maintenance of Pol II an inactive state in the absence of Mediator. POLR2M and TFIIF associate with Pol II in a mutually exclusive manner, thus the formation of Pol II(G) prevents TFIIF from binding and leads to inhibition of PIC assembly.","predictedComplex":false,"interactors":[{"ac":"EBI-295301","identifier":"P24928","identifierLink":"https://www.uniprot.org/uniprotkb/P24928/entry","name":"POLR2A","description":"DNA-directed RNA polymerase II subunit RPB1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19376","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347928","identifier":"P62487","identifierLink":"https://www.uniprot.org/uniprotkb/P62487/entry","name":"POLR2G","description":"DNA-directed RNA polymerase II subunit RPB7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12709","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359505","identifier":"P52434","identifierLink":"https://www.uniprot.org/uniprotkb/P52434/entry","name":"POLR2H","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10917","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359527","identifier":"P62875","identifierLink":"https://www.uniprot.org/uniprotkb/P62875/entry","name":"POLR2L","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23431","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394712","identifier":"P30876","identifierLink":"https://www.uniprot.org/uniprotkb/P30876/entry","name":"POLR2B","description":"DNA-directed RNA polymerase II subunit RPB2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20856","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394729","identifier":"P19387","identifierLink":"https://www.uniprot.org/uniprotkb/P19387/entry","name":"POLR2C","description":"DNA-directed RNA polymerase II subunit RPB3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394737","identifier":"O15514","identifierLink":"https://www.uniprot.org/uniprotkb/O15514/entry","name":"POLR2D","description":"DNA-directed RNA polymerase II subunit RPB4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21297","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394753","identifier":"P52435","identifierLink":"https://www.uniprot.org/uniprotkb/P52435/entry","name":"POLR2J","description":"DNA-directed RNA polymerase II subunit RPB11-a","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13946","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395180","identifier":"P61218","identifierLink":"https://www.uniprot.org/uniprotkb/P61218/entry","name":"POLR2F","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47227","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395189","identifier":"P19388","identifierLink":"https://www.uniprot.org/uniprotkb/P19388/entry","name":"POLR2E","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10535","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395202","identifier":"P36954","identifierLink":"https://www.uniprot.org/uniprotkb/P36954/entry","name":"POLR2I","description":"DNA-directed RNA polymerase II subunit RPB9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395357","identifier":"P53803","identifierLink":"https://www.uniprot.org/uniprotkb/P53803/entry","name":"POLR2K","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9657655","identifier":"P0CAP2","identifierLink":"https://www.uniprot.org/uniprotkb/P0CAP2/entry","name":"POLR2M","description":"DNA-directed RNA polymerase II subunit GRINL1A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23171","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2389","complexName":"Prefoldin co-chaperone complex","organismName":"Drosophila melanogaster; 7227","description":"Co-chaperone that works together with HSP90 in the activation and assembly of several macromolecular complexes. It binds specifically to cytosolic CCT complex (CPX-2772) and transfers target proteins to it. Synergistically regulates the asymmetric division of neuroblasts and intermediate neural progenitor cells with infertile partners (Pins, Q9VB22) by stabilizing tubulin, and hence inhibits neuroblast overgrowth in the brain of Drosophila larvae","predictedComplex":false,"interactors":[{"ac":"EBI-100237","identifier":"Q9VRL3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VRL3/entry","name":"Pfdn4","description":"Probable prefoldin subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21100","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-100243","identifier":"Q9VCZ8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VCZ8/entry","name":"Pfdn5","description":"Probable prefoldin subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12674","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-108827","identifier":"Q9VMH8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VMH8/entry","name":"Pfdn1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR20903","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-112583","identifier":"Q9VTE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VTE5/entry","name":"Pfdn2","description":"Probable prefoldin subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13303","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-162978","identifier":"Q9VW56","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VW56/entry","name":"Pfdn6","description":"Probable prefoldin subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21431","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-186707","identifier":"Q9VGP6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VGP6/entry","name":"mgr","description":"Prefoldin subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12409","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2390","complexName":"Class IA phosphatidylinositol 3-kinase complex","organismName":"Drosophila melanogaster; 7227","description":"Uses 1-phosphatidyl-1D-myo-inositol (CHEBI:16749),  1-phosphatidyl-1D-myo-inositol 4-phosphate (CHEBI:17526)  1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate/PI(4,5)P2 (CHEBI:18348) as substrates to generate the products 1-phosphatidyl-1D-myo-inositol 3-phosphate (CHEBI:17283), 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate (CHEBI:16152) and 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate/PI(3,4,5)P3 (CHEBI:16618) respectively, thus initiating major signaling pathways downstream. Performs a central role in cellular signaling, mediating responses to growth factors and extracellular stimuli.","predictedComplex":false,"interactors":[{"ac":"EBI-173369","identifier":"P91634","identifierLink":"https://www.uniprot.org/uniprotkb/P91634/entry","name":"Pi3K92E","description":"phosphatidylinositol 3-kinase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34592500","identifier":"Q7KTZ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KTZ2/entry","name":"Pi3K21B","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10155","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2392","complexName":"U1 small nuclear ribonucleoprotein complex","organismName":"Homo sapiens; 9606","description":"Recognizes the 5' splice site within precursor messenger RNAs and initiates the assembly of the spliceosome. U1 snRNP interacts with the pre-mRNA, via base-pairing between the 5' end of U1 snRNA and the 5' splice site in pre-mRNA. The spliceosome is a highly dynamic structure, assembled by sequential binding and release of the small nuclear RNAs and protein factors which removes intronic sequence from pre-mRNA.","predictedComplex":false,"interactors":[{"ac":"EBI-1049228","identifier":"P08621","identifierLink":"https://www.uniprot.org/uniprotkb/P08621/entry","name":"SNRNP70","description":"U1 small nuclear ribonucleoprotein 70 kDa","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13952","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2107782","identifier":"URS0001BC29EB_9606","identifierLink":"http://rnacentral.org/rna/URS0001BC29EB_9606","name":"u1_human_snrna","description":"Human U1 spliceosomal RNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small nuclear rna","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-297993","identifier":"P62316","identifierLink":"https://www.uniprot.org/uniprotkb/P62316/entry","name":"SNRPD2","description":"Small nuclear ribonucleoprotein Sm D2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12777","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348082","identifier":"P62304","identifierLink":"https://www.uniprot.org/uniprotkb/P62304/entry","name":"SNRPE","description":"Small nuclear ribonucleoprotein E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11193","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356900","identifier":"P62306","identifierLink":"https://www.uniprot.org/uniprotkb/P62306/entry","name":"SNRPF","description":"Small nuclear ribonucleoprotein F","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372177","identifier":"P62314","identifierLink":"https://www.uniprot.org/uniprotkb/P62314/entry","name":"SNRPD1","description":"Small nuclear ribonucleoprotein Sm D1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372458","identifier":"P14678","identifierLink":"https://www.uniprot.org/uniprotkb/P14678/entry","name":"SNRPB","description":"Small nuclear ribonucleoprotein-associated proteins B and B'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372789","identifier":"P62318","identifierLink":"https://www.uniprot.org/uniprotkb/P62318/entry","name":"SNRPD3","description":"Small nuclear ribonucleoprotein Sm D3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-607085","identifier":"P09012","identifierLink":"https://www.uniprot.org/uniprotkb/P09012/entry","name":"SNRPA","description":"U1 small nuclear ribonucleoprotein A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10501","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-624585","identifier":"P62308","identifierLink":"https://www.uniprot.org/uniprotkb/P62308/entry","name":"SNRPG","description":"Small nuclear ribonucleoprotein G","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-766589","identifier":"P09234","identifierLink":"https://www.uniprot.org/uniprotkb/P09234/entry","name":"SNRPC","description":"U1 small nuclear ribonucleoprotein C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31148","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2393","complexName":"DNA-directed RNA polymerase III complex, POLR3G variant","organismName":"Homo sapiens; 9606","description":"Catalyzes the transcription of RNA from an DNA template by acting as a nucleotidyl transferase that polymerizes ribonucleotides at the 3' end of an RNA transcript. Responsible for the transcription of genes encoding short non-coding RNAs, such as tRNA, 5S rRNA and U6 snRNA transcripts. \r\n\r\nPol III machinery recognizes conserved promoter elements located within the transcribed region, generally the box A and box B sequences, which contribute to the  D- and T-loops in the tRNA structure. POLR3F, POLR3G and POLR3C play a role in transcription initiation whereas the POLR3D-POLR3E heterodimer is crucial for the correct recognition of the termination signals of class III genes. POLR3K is required for RNA cleavage. Pol III initiation does not require ATP hydrolysis to open a transcription bubble to isolate and secure the template strand in the catalytic site and Pol III is capable of reinitiating transcription more rapidly on the same gene after the first transcription cycle without being released (facilitated reinitiation), resulting in a higher initiation efficiency; this appears to require an POLR3K-dependent conformational change of Pol III.","predictedComplex":false,"interactors":[{"ac":"EBI-1055079","identifier":"O15160","identifierLink":"https://www.uniprot.org/uniprotkb/O15160/entry","name":"POLR1C","description":"DNA-directed RNA polymerases I and III subunit RPAC1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11023785","identifier":"Q9Y2Y1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2Y1/entry","name":"POLR3K","description":"DNA-directed RNA polymerase III subunit RPC10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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Both subunits of the complex act to anchor the TFIIH kinase module (CAK) within the preinitiation complex. The TFIIE complex appears to directly influence the transition from initiation to elongation during transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-2853321","identifier":"P29084","identifierLink":"https://www.uniprot.org/uniprotkb/P29084/entry","name":"GTF2E2","description":"Transcription initiation factor IIE subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12716","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5462215","identifier":"P29083","identifierLink":"https://www.uniprot.org/uniprotkb/P29083/entry","name":"GTF2E1","description":"General transcription factor IIE subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2395","complexName":"General transcription factor TFIIH complex","organismName":"Homo sapiens; 9606","description":"General transcription factor involved in transcriptional initiation, activation and elongation, the cell cycle and nucleotide excision repair. The ATPase/helicase activities of ERCC2 and ERCC3 are required for promoter melting at transcription initiation sites and damaged DNA opening at nucleotide excision repair sites and the protein kinase activity of CDK7 is necessary for phosphorylation of the C-terminal domain of the largest subunit of RNA polymerase II, other transcription factors and nuclear receptors.","predictedComplex":false,"interactors":[{"ac":"EBI-1183307","identifier":"P19447","identifierLink":"https://www.uniprot.org/uniprotkb/P19447/entry","name":"ERCC3","description":"General transcription and DNA repair factor IIH helicase/translocase subunit XPB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11274","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1245958","identifier":"P50613","identifierLink":"https://www.uniprot.org/uniprotkb/P50613/entry","name":"CDK7","description":"Cyclin-dependent kinase 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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TF3IIIB also plays a role in the opening of the transcription bubble.","predictedComplex":false,"interactors":[{"ac":"EBI-1055224","identifier":"Q9HAW0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HAW0/entry","name":"BRF2","description":"Transcription factor IIIB 50 kDa subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11618","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2825167","identifier":"A6H8Y1","identifierLink":"https://www.uniprot.org/uniprotkb/A6H8Y1/entry","name":"BDP1","description":"Transcription factor TFIIIB component B'' homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22929","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355371","identifier":"P20226","identifierLink":"https://www.uniprot.org/uniprotkb/P20226/entry","name":"TBP","description":"TATA-box-binding protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10126","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2398","complexName":"General transcription factor TFIIB-TBP complex","organismName":"Homo sapiens; 9606","description":"Plays an essential role in transcription initiation from RNA polymerase II promoters. Binding of this factor to the DNA is an  early stage in pre-initiation complex (PIC) formation.","predictedComplex":false,"interactors":[{"ac":"EBI-355371","identifier":"P20226","identifierLink":"https://www.uniprot.org/uniprotkb/P20226/entry","name":"TBP","description":"TATA-box-binding protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10126","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-389564","identifier":"Q00403","identifierLink":"https://www.uniprot.org/uniprotkb/Q00403/entry","name":"GTF2B","description":"Transcription initiation factor IIB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11618","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2399","complexName":"CRL4-DCAF13 E3 ubiquitin ligase complex, CUL4A variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor DCAF13. The complex is active in preimplantation embryonic development by ubiqitinating and targeting for destruction SUV39H1/2 (O43463/Q9H5I1) thereby triggering histone H3 lysine‐9 demethylation and zygotic genome reprogramming.","predictedComplex":false,"interactors":[{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456106","identifier":"Q13619","identifierLink":"https://www.uniprot.org/uniprotkb/Q13619/entry","name":"CUL4A","description":"Cullin-4A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7402939","identifier":"Q9NV06","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NV06/entry","name":"DCAF13","description":"DDB1- and CUL4-associated factor 13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22851","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2400","complexName":"COPII vesicle coat complex","organismName":"Drosophila melanogaster; 7227","description":"Mediates formation of the membrane vesicles that export newly synthesised proteins from the endoplasmic reticulum.","predictedComplex":false,"interactors":[{"ac":"EBI-165474","identifier":"Q9VD29","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VD29/entry","name":"Sar1","description":"small monomeric GTPase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-169056","identifier":"Q9V3J4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V3J4/entry","name":"Sec13","description":"Protein SEC13 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11024","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-183080","identifier":"A1Z813","identifierLink":"https://www.uniprot.org/uniprotkb/A1Z813/entry","name":"Sec24AB","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13803","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26774045","identifier":"M9PC99","identifierLink":"https://www.uniprot.org/uniprotkb/M9PC99/entry","name":"Sec24CD","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13803","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30873030","identifier":"A0A0B4K5Z8","identifierLink":"https://www.uniprot.org/uniprotkb/A0A0B4K5Z8/entry","name":"Sec23","description":"Protein transport protein SEC23","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11141","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30873091","identifier":"A0A0B4LEZ1","identifierLink":"https://www.uniprot.org/uniprotkb/A0A0B4LEZ1/entry","name":"Sec31","description":"Protein transport protein Sec31A","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13923","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2401","complexName":"NXF2-NXT2 mRNA nuclear export factor complex","organismName":"Homo sapiens; 9606","description":"Mediates the export of bulk mRNA through direct interactions with both the mRNA cargo and nuclear pore proteins that contain characteristic phenylalanine-glycine repeating sequence motifs (FG-nucleoporins or FG-nups).","predictedComplex":false,"interactors":[{"ac":"EBI-444173","identifier":"Q9GZY0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9GZY0/entry","name":"NXF2B","description":"Nuclear RNA export factor 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10662","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752122","identifier":"Q9NPJ8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPJ8/entry","name":"NXT2","description":"NTF2-related export protein 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12612","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2402","complexName":"Calcium release-activated calcium channel","organismName":"Drosophila melanogaster; 7227","description":"Ca[2+] release-activated Ca[2+] channel which functions in store-operated Ca[2+] entry, a mechanism for Ca[2+] entry across the plasma membrane modulated by intracellular (mainly endoplasmic reticulum) Ca[2+] stores.","predictedComplex":false,"interactors":[{"ac":"EBI-109721","identifier":"P83094","identifierLink":"https://www.uniprot.org/uniprotkb/P83094/entry","name":"Stim","description":"Stromal interaction molecule homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15136","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-118501","identifier":"Q9U6B8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9U6B8/entry","name":"Orai","description":"Calcium release-activated calcium channel protein 1","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR31501","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2403","complexName":"CRL4-DCAF11 E3 ubiquitin ligase complex, CUL4A variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor DCAF11. The complex is active in the regulation of stress response in the cell by ubiquitinating and targetting for destruction the NFE2L2 (Q16236) transcription factor. Also plays a role in a mitotic surveillance pathway preventing the nucleosomal protein CENPA (P49450) from targeting to the non-centromeric regions. During early mitotic phase, newly synthesized CENPA is phosphorylated at Ser-68 by Cyclin B1-CDK1 complex (CPX-2007, CPX-2008). This is recognized by the ubiquitin ligase resulting in polyubiquitination and proteasome-mediated degradation of CENPA.","predictedComplex":false,"interactors":[{"ac":"EBI-2213388","identifier":"Q8TEB1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TEB1/entry","name":"DCAF11","description":"DDB1- and CUL4-associated factor 11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456106","identifier":"Q13619","identifierLink":"https://www.uniprot.org/uniprotkb/Q13619/entry","name":"CUL4A","description":"Cullin-4A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2404","complexName":"CRL4-DCAF11 E3 ubiquitin ligase complex, CUL4B variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor DCAF11. The complex is active in the regulation of stress response in the cell by ubiquitinating and targetting for destruction the NFE2L2 (Q16236) transcription factor. Also plays a role in a mitotic surveillance pathway preventing the nucleosomal protein CENPA (P49450) from targeting to the non-centromeric regions. During early mitotic phase, newly synthesized CENPA is phosphorylated at Ser-68 by Cyclin B1-CDK1 complex (CPX-2007, CPX-2008). This is recognized by the ubiquitin ligase resulting in polyubiquitination and proteasome-mediated degradation of CENPA.","predictedComplex":false,"interactors":[{"ac":"EBI-2213388","identifier":"Q8TEB1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TEB1/entry","name":"DCAF11","description":"DDB1- and CUL4-associated factor 11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456067","identifier":"Q13620","identifierLink":"https://www.uniprot.org/uniprotkb/Q13620/entry","name":"CUL4B","description":"Cullin-4B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2405","complexName":"CRL4-DCAF12 E3 ubiquitin ligase complex, CUL4A variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor DCAF12. The complex is active in the regulation of autophagy by ubiquitinating and targeting for destruction MAGEA3 (P43357) and MAGEA6 (P43360) activators of RING-type zinc finger-containing E3 ubiquitin-protein ligases that acts as repressors of autophagy. Regulates HIPPO pathway-mediated cellular proliferation and apoptosis by targeting YP1 (P46937) for ubiquitination. Regulates spermatogenesis and T-cell activation by ubiquitinating the MOV10 (Q9HCE1) helicase, thus effecting miRNA gene silencing.\r\nRecognizes a specific motif, a degron, which is less then 10 amino acids long and contains a diglutamate (Glu-Glu) and is present in the C-terminus of substrate proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-2559113","identifier":"Q5T6F0","identifierLink":"https://www.uniprot.org/uniprotkb/Q5T6F0/entry","name":"DCAF12","description":"DDB1- and CUL4-associated factor 12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19860","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456106","identifier":"Q13619","identifierLink":"https://www.uniprot.org/uniprotkb/Q13619/entry","name":"CUL4A","description":"Cullin-4A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2406","complexName":"CRL4-DCAF12 E3 ubiquitin ligase complex, CUL4B variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor DCAF12. The complex is active in the regulation of autophagy by ubiquitinating and targeting for destruction MAGEA3 (P43357) and MAGEA6 (P43360) activators of RING-type zinc finger-containing E3 ubiquitin-protein ligases that acts as repressors of autophagy. Regulates HIPPO pathway-mediated cellular proliferation and apoptosis by targeting YP1 (P46937) for ubiquitination. Regulates spermatogenesis and T-cell activation by ubiquitinating the MOV10 (Q9HCE1) helicase, thus effecting miRNA gene silencing.\r\nRecognizes a specific motif, a degron, which is less then 10 amino acids long and contains a diglutamate (Glu-Glu) and is present in the C-terminus of substrate proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-2559113","identifier":"Q5T6F0","identifierLink":"https://www.uniprot.org/uniprotkb/Q5T6F0/entry","name":"DCAF12","description":"DDB1- and CUL4-associated factor 12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19860","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456067","identifier":"Q13620","identifierLink":"https://www.uniprot.org/uniprotkb/Q13620/entry","name":"CUL4B","description":"Cullin-4B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2407","complexName":"CRL4-DCAF13 E3 ubiquitin ligase complex, CUL4B variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor DCAF13. The complex is active in preimplantation embryonic development by ubiqitinating and targeting for destruction SUV39H1/2 (O43463/Q9H5I1) thereby triggering histone H3 lysine‐9 demethylation and zygotic genome reprogramming.","predictedComplex":false,"interactors":[{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456067","identifier":"Q13620","identifierLink":"https://www.uniprot.org/uniprotkb/Q13620/entry","name":"CUL4B","description":"Cullin-4B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7402939","identifier":"Q9NV06","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NV06/entry","name":"DCAF13","description":"DDB1- and CUL4-associated factor 13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22851","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2408","complexName":"CRUMBS-PALS1-PATJ cell polarity complex","organismName":"Drosophila melanogaster; 7227","description":"Evolutionarily conserved complex that acts as a key regulator of cell polarity and cell shape. It localizes at the subapical region (SAR) above the adherens junction of epithelial cells where it plays a major role in establishment, regulation, and maintenance of apical polarity and acts as an apical component of tight junctions. In addition to the core components (which are always found together), other proteins can associate with the complex, depending on the type and developmental stage of the cell, thus providing it with functional diversity and flexibility. Mutations in its components are associated with a variety of retinal degenerations.","predictedComplex":false,"interactors":[{"ac":"EBI-30873541","identifier":"E2QD98","identifierLink":"https://www.uniprot.org/uniprotkb/E2QD98/entry","name":"sdt","description":"Protein PALS1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23122","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-442573","identifier":"Q9NB04","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NB04/entry","name":"Patj","description":"Patj homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-672928","identifier":"P10040","identifierLink":"https://www.uniprot.org/uniprotkb/P10040/entry","name":"crb","description":"Protein crumbs","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR24044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2409","complexName":"PAR cell polarity complex","organismName":"Drosophila melanogaster; 7227","description":"Conserved serine/threonine kinase complex that localises at tight junctions where it is required for the establishment of a cell polarity axis during the cell division cycle of epithelial cells.","predictedComplex":false,"interactors":[{"ac":"EBI-160861","identifier":"A1Z9X0","identifierLink":"https://www.uniprot.org/uniprotkb/A1Z9X0/entry","name":"aPKC","description":"Atypical protein kinase C","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR24356","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-186645","identifier":"O97111","identifierLink":"https://www.uniprot.org/uniprotkb/O97111/entry","name":"par-6","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30873633","identifier":"Q0KHR3","identifierLink":"https://www.uniprot.org/uniprotkb/Q0KHR3/entry","name":"baz","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR16484","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2410","complexName":"Scribble cell polarity complex","organismName":"Drosophila melanogaster; 7227","description":"Evolutionarily conserved complex that acts as a key regulator of cell polarity and cell shape. It plays a major role in establishment, regulation, and maintenance of apicobasal polarity in epithelial cells. It localizes to the basolateral membrane in epithelial cells and is required for proper localization of the other PDZ protein complexes involved in apicobasal polarity and asymmetric cleavage: CRUMBS (CPX-2408) and PAR (CPX-2409).","predictedComplex":false,"interactors":[{"ac":"EBI-389374","identifier":"P31007","identifierLink":"https://www.uniprot.org/uniprotkb/P31007/entry","name":"dlg1","description":"Disks large 1 tumor suppressor protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-419788","identifier":"Q7KRY7","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KRY7/entry","name":"scrib","description":"Protein lap4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-497569","identifier":"P08111","identifierLink":"https://www.uniprot.org/uniprotkb/P08111/entry","name":"l(2)gl","description":"Lethal(2) giant larvae protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10241","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2411","complexName":"CRL4-DCAF14 E3 ubiquitin ligase complex, CUL4A variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor PHIP/DCAF14. The complex is active in stabilizing stalled replication forks,  protecting nascent DNA from nuclease-mediated digestion. This activity is RAD51-dependent. PHIP binds replication origins and recruits the complex to chromatin prior to DNA replication.","predictedComplex":false,"interactors":[{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456106","identifier":"Q13619","identifierLink":"https://www.uniprot.org/uniprotkb/Q13619/entry","name":"CUL4A","description":"Cullin-4A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-722984","identifier":"Q8WWQ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WWQ0/entry","name":"PHIP","description":"PH-interacting protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2412","complexName":"CRL4-DCAF14 E3 ubiquitin ligase complex, CUL4B variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor PHIP/DCAF14. The complex is active in stabilizing stalled replication forks,  protecting nascent DNA from nuclease-mediated digestion. This activity is RAD51-dependent. PHIP binds replication origins and recruits the complex to chromatin prior to DNA replication.","predictedComplex":false,"interactors":[{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456067","identifier":"Q13620","identifierLink":"https://www.uniprot.org/uniprotkb/Q13620/entry","name":"CUL4B","description":"Cullin-4B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-722984","identifier":"Q8WWQ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WWQ0/entry","name":"PHIP","description":"PH-interacting protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2413","complexName":"CRL4-DCAF16 E3 ubiquitin ligase complex, CUL4A variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor DCAF16. The complex is active in regulating serine biosynthesis, 1-carbon metabolism, and epigenetics by mono-ubiqitinating PHGDH (O43175). This increases PHGDH activity by facilitating tetramer formation, and thus increases the downstream levels of methyl donor S-adenosylmethionine (CHEBI:15414), thereby upregulating cell adhesion gene expression via SETD1A (O15047)-mediated  histone methylation. Also mediates ubiquitination and proteasome-dependent degradation of nuclear proteins such a SPIN4 (Q56A73) which interacts with the trimethylated lysine-3 of histone H3 (H3K4me3).","predictedComplex":false,"interactors":[{"ac":"EBI-2559096","identifier":"Q9NXF7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NXF7/entry","name":"DCAF16","description":"DDB1- and CUL4-associated factor 16","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16194","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456106","identifier":"Q13619","identifierLink":"https://www.uniprot.org/uniprotkb/Q13619/entry","name":"CUL4A","description":"Cullin-4A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2414","complexName":"CRL4-DCAF16 E3 ubiquitin ligase complex, CUL4B variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor DCAF16. The complex is active in regulating serine biosynthesis, 1-carbon metabolism, and epigenetics by mono-ubiqitinating PHGDH (O43175). This increases PHGDH activity by facilitating tetramer formation, and thus increases the downstream levels of methyl donor S-adenosylmethionine (CHEBI:15414), thereby upregulating cell adhesion gene expression via SETD1A (O15047) -mediated  histone methylation. Also mediates ubiquitination and proteasome-dependent degradation of nuclear proteins such a SPIN4 (Q56A73) which interacts with the trimethylated lysine-3 of histone H3 (H3K4me3).","predictedComplex":false,"interactors":[{"ac":"EBI-2559096","identifier":"Q9NXF7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NXF7/entry","name":"DCAF16","description":"DDB1- and CUL4-associated factor 16","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16194","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456067","identifier":"Q13620","identifierLink":"https://www.uniprot.org/uniprotkb/Q13620/entry","name":"CUL4B","description":"Cullin-4B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2415","complexName":"CRL4-DCAF17 E3 ubiquitin ligase complex, CUL4A variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor DCAF17. The complex is potentially active in regulating spermatogenesis.","predictedComplex":false,"interactors":[{"ac":"EBI-3253152","identifier":"Q5H9S7","identifierLink":"https://www.uniprot.org/uniprotkb/Q5H9S7/entry","name":"DCAF17","description":"DDB1- and CUL4-associated factor 17","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14815","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456106","identifier":"Q13619","identifierLink":"https://www.uniprot.org/uniprotkb/Q13619/entry","name":"CUL4A","description":"Cullin-4A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2416","complexName":"CRL4-DCAF17 E3 ubiquitin ligase complex, CUL4B variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor DCAF17. The complex is potentially active in regulating spermatogenesis.","predictedComplex":false,"interactors":[{"ac":"EBI-3253152","identifier":"Q5H9S7","identifierLink":"https://www.uniprot.org/uniprotkb/Q5H9S7/entry","name":"DCAF17","description":"DDB1- and CUL4-associated factor 17","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14815","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456067","identifier":"Q13620","identifierLink":"https://www.uniprot.org/uniprotkb/Q13620/entry","name":"CUL4B","description":"Cullin-4B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2417","complexName":"Beta-catenin destruction complex, Apc2 variant","organismName":"Drosophila melanogaster; 7227","description":"Phosphorylates cytoplasmic beta-catenin (arm, P18824) in the absence of WNT-signalling, thus positively controlling its continuous proteasome-mediated degradation. This constitutively suppresses the canonical Wnt signaling pathway by preventing the accumulation of cytoplasmic beta-catenin.","predictedComplex":false,"interactors":[{"ac":"EBI-114593","identifier":"Q9Y1T2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y1T2/entry","name":"Apc2","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-129996","identifier":"P54367","identifierLink":"https://www.uniprot.org/uniprotkb/P54367/entry","name":"CkIalpha","description":"Casein kinase I isoform alpha","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11909","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-196300","identifier":"Q9V407","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V407/entry","name":"Axn","description":"Axin","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-242141","identifier":"P18431","identifierLink":"https://www.uniprot.org/uniprotkb/P18431/entry","name":"sgg","description":"Protein kinase shaggy","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR24057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2418","complexName":"Beta-catenin destruction complex, Apc variant","organismName":"Drosophila melanogaster; 7227","description":"Phosphorylates cytoplasmic beta-catenin (arm, P18824) in the absence of WNT-signalling, thus positively controlling its continuous proteasome-mediated degradation. This constitutively suppresses the canonical Wnt signaling pathway by preventing the accumulation of cytoplasmic beta-catenin.","predictedComplex":false,"interactors":[{"ac":"EBI-129996","identifier":"P54367","identifierLink":"https://www.uniprot.org/uniprotkb/P54367/entry","name":"CkIalpha","description":"Casein kinase I isoform alpha","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11909","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-158553","identifier":"Q9VAS9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VAS9/entry","name":"Apc","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-196300","identifier":"Q9V407","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V407/entry","name":"Axn","description":"Axin","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-242141","identifier":"P18431","identifierLink":"https://www.uniprot.org/uniprotkb/P18431/entry","name":"sgg","description":"Protein kinase shaggy","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR24057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2419","complexName":"Hemoglobin HbA2 complex","organismName":"Homo sapiens; 9606","description":"Adult hemoglobin A2 (HbA2) is expressed in erythrocytes in the bone marrow. Binds oxygen in the lungs and transports it to the various peripheral tissues. Transports CO2 back from the cells to the lungs. It is a minor form and makes up about 2-3% of adult hemoglobins, first appearing in late pregnancy.","predictedComplex":false,"interactors":[{"ac":"EBI-6152722","identifier":"P02042","identifierLink":"https://www.uniprot.org/uniprotkb/P02042/entry","name":"HBD","description":"Hemoglobin subunit delta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-714680","identifier":"P69905","identifierLink":"https://www.uniprot.org/uniprotkb/P69905/entry","name":"HBA1","description":"Hemoglobin subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2927","complexName":"Hemoglobin E complex","organismName":"Homo sapiens; 9606","description":"Embryonic hemoglobin E (HbE) complex is the main embryonic hemoglobin type, expressed predominantly in fetal liver and embryonic erythrocytes. Binds and transports oxygen and carbon dioxide to/from the peripheral tissues.  It replaces embryonic Gower-1 hemoglobin (CPX-2928) and is itself replaced by fetal hemoglobin (CPX-2932, CPX-2933) after about 8 weeks gestation.","predictedComplex":false,"interactors":[{"ac":"EBI-6190240","identifier":"P02100","identifierLink":"https://www.uniprot.org/uniprotkb/P02100/entry","name":"HBE1","description":"Hemoglobin subunit epsilon","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-714680","identifier":"P69905","identifierLink":"https://www.uniprot.org/uniprotkb/P69905/entry","name":"HBA1","description":"Hemoglobin subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2928","complexName":"Embryonic hemoglobin Gower-1 complex","organismName":"Homo sapiens; 9606","description":"Embryonic hemoglobin Gower-1 complex is the early embryonic hemoglobin type and expressed predominantly in the yolk sac. Binds and transports oxygen and carbon dioxide to/from the peripheral tissues. It is replaced by embryonic hemoglobin HbE (Gower-2) (CPX-2927).","predictedComplex":false,"interactors":[{"ac":"EBI-6190240","identifier":"P02100","identifierLink":"https://www.uniprot.org/uniprotkb/P02100/entry","name":"HBE1","description":"Hemoglobin subunit epsilon","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-719843","identifier":"P02008","identifierLink":"https://www.uniprot.org/uniprotkb/P02008/entry","name":"HBZ","description":"Hemoglobin subunit zeta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2929","complexName":"Hemoglobin Portland-2 complex","organismName":"Homo sapiens; 9606","description":"Embryonic hemoglobin Portland-2 complex is found during early embryonic development, predominantly in the yolk sac. It is linked to severe alpha-thalassemia. Has reduced oxygen binding and transport capacity.","predictedComplex":false,"interactors":[{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-715554","identifier":"P68871","identifierLink":"https://www.uniprot.org/uniprotkb/P68871/entry","name":"HBB","description":"Hemoglobin subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-719843","identifier":"P02008","identifierLink":"https://www.uniprot.org/uniprotkb/P02008/entry","name":"HBZ","description":"Hemoglobin subunit zeta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2930","complexName":"Hemoglobin Portland-1 Variant 1 complex","organismName":"Homo sapiens; 9606","description":"Embryonic hemoglobin Portland-1 complex is found during early embryonic development, predominantly in the yolk sac. It is linked to severe alpha-thalassemia. Has reduced oxygen binding and transport capacity.","predictedComplex":false,"interactors":[{"ac":"EBI-1056789","identifier":"P69891","identifierLink":"https://www.uniprot.org/uniprotkb/P69891/entry","name":"HBG1","description":"Hemoglobin subunit gamma-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-719843","identifier":"P02008","identifierLink":"https://www.uniprot.org/uniprotkb/P02008/entry","name":"HBZ","description":"Hemoglobin subunit zeta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2931","complexName":"Hemoglobin Portland-1 Variant 2 complex","organismName":"Homo sapiens; 9606","description":"Embryonic hemoglobin Portland-1 complex is found during early embryonic development, predominantly in the yolk sac. It is linked to severe alpha-thalassemia. Has reduced oxygen binding and transport capacity.","predictedComplex":false,"interactors":[{"ac":"EBI-3910089","identifier":"P69892","identifierLink":"https://www.uniprot.org/uniprotkb/P69892/entry","name":"HBG2","description":"Hemoglobin subunit gamma-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-719843","identifier":"P02008","identifierLink":"https://www.uniprot.org/uniprotkb/P02008/entry","name":"HBZ","description":"Hemoglobin subunit zeta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2932","complexName":"Hemoglobin HbF Variant 1 complex","organismName":"Homo sapiens; 9606","description":"Fetal hemoglobin (HbF) complex is expressed in the fetal liver from around 9 weeks gestation until 4-5 week after birth. It can be detected for up to 6 months after birth. Binds and transports oxygen and carbon dioxide to/from the peripheral tissues. It replaces embryonic hemoglobins Gower-1 (CPX-2928) and hemoglobin HbE (Gower-2) (CPX-2927).","predictedComplex":false,"interactors":[{"ac":"EBI-1056789","identifier":"P69891","identifierLink":"https://www.uniprot.org/uniprotkb/P69891/entry","name":"HBG1","description":"Hemoglobin subunit gamma-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-714680","identifier":"P69905","identifierLink":"https://www.uniprot.org/uniprotkb/P69905/entry","name":"HBA1","description":"Hemoglobin subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2933","complexName":"Hemoglobin HbF Variant 2 complex","organismName":"Homo sapiens; 9606","description":"Fetal hemoglobin (HbF) complex is expressed in the fetal liver from around 9 weeks gestation until 4-5 week after birth. It can be detected for up to 6 months after birth. Binds and transports oxygen and carbon dioxide to/from the peripheral tissues. It replaces embryonic hemoglobins Gower-1 (CPX-2928) and hemoglobin HbE (Gower-2) (CPX-2927).","predictedComplex":false,"interactors":[{"ac":"EBI-3910089","identifier":"P69892","identifierLink":"https://www.uniprot.org/uniprotkb/P69892/entry","name":"HBG2","description":"Hemoglobin subunit gamma-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-714680","identifier":"P69905","identifierLink":"https://www.uniprot.org/uniprotkb/P69905/entry","name":"HBA1","description":"Hemoglobin subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2934","complexName":"Hemoglobin Bart's complex","organismName":"Homo sapiens; 9606","description":"Fetal hemoglobin Bart's complex consisting of only four beta-type, gamma chains. It is non-functional, exhibiting neither Bohr effect nor heme-heme cooperativity and is a poor transporter of oxygen. Its formation is usually lethal in utero.","predictedComplex":false,"interactors":[{"ac":"EBI-1056789","identifier":"P69891","identifierLink":"https://www.uniprot.org/uniprotkb/P69891/entry","name":"HBG1","description":"Hemoglobin subunit gamma-1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2938","complexName":"Early embryonic hemoglobin complex","organismName":"Mus musculus; 10090","description":"Embryonic hemoglobin zeta-beta complex is the early embryonic hemoglobin type and expressed predominantly in the yolk sac. Binds and transports oxygen and carbon dioxide to/from the peripheral tissues. It is replaced by embryonic hemoglobin zeta-epsilon (CPX-2939).","predictedComplex":false,"interactors":[{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-8347246","identifier":"P06467","identifierLink":"https://www.uniprot.org/uniprotkb/P06467/entry","name":"Hbz","description":"Hemoglobin subunit zeta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9120401","identifier":"P04444","identifierLink":"https://www.uniprot.org/uniprotkb/P04444/entry","name":"Hbb-bh1","description":"Hemoglobin subunit beta-H1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2939","complexName":"Embryonic hemoglobin complex","organismName":"Mus musculus; 10090","description":"Embryonic hemoglobin zeta-epsilon complex is the embryonic hemoglobin type and expressed predominantly in embryonic erythrocytes. Binds and transports oxygen and carbon dioxide to/from the peripheral tissues. It replaces the early embryonic hemoglobin zeta-beta (CPX-2938) and is replaced by the adult hemoglobin types alpha-beta (CPX-2924, CPX-2922) in late pregnancy. It can be detected for a while in neonates.","predictedComplex":false,"interactors":[{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-8347246","identifier":"P06467","identifierLink":"https://www.uniprot.org/uniprotkb/P06467/entry","name":"Hbz","description":"Hemoglobin subunit zeta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9123514","identifier":"P02104","identifierLink":"https://www.uniprot.org/uniprotkb/P02104/entry","name":"Hbb-y","description":"Hemoglobin subunit epsilon-Y2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2420","complexName":"Dystrophin glycoprotein complex","organismName":"Drosophila melanogaster; 7227","description":"A plasma membrane transmembrane complex that links the actin cytoskeleton to the extracellular matrix. The complex is important for maintaining the integrity of skeletal and cardiac muscle cells. It also functions as a scaffold for proteins involved in signaling and accumulates at the neuromuscular junction and at a variety of synapses in the peripheral and central nervous system.","predictedComplex":false,"interactors":[{"ac":"EBI-110986","identifier":"Q9VDW6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VDW6/entry","name":"Dys","description":"Dystrophin, isoforms A/C/F/G/H","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11915","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-158358","identifier":"O76892","identifierLink":"https://www.uniprot.org/uniprotkb/O76892/entry","name":"Scgdelta","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12939","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26719883","identifier":"Q9VNY2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VNY2/entry","name":"Syn1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10554","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30874893","identifier":"A0A0C4DHF6","identifierLink":"https://www.uniprot.org/uniprotkb/A0A0C4DHF6/entry","name":"Dg","description":"Dystroglycan 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21559","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30874955","identifier":"A8DYB7","identifierLink":"https://www.uniprot.org/uniprotkb/A8DYB7/entry","name":"Dyb","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12268","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30874983","identifier":"M9PF78","identifierLink":"https://www.uniprot.org/uniprotkb/M9PF78/entry","name":"Scgalpha","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10132","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30875003","identifier":"Q9VG77","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VG77/entry","name":"Scgbeta","description":"Beta-sarcoglycan","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21142","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3410295","identifier":"A1ZAH3","identifierLink":"https://www.uniprot.org/uniprotkb/A1ZAH3/entry","name":"Syn2","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10554","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2421","complexName":"DNA polymerase delta complex","organismName":"Drosophila melanogaster; 7227","description":"Believed to be the major polymerase for the elongation of both leading and lagging strands of chromosomal DNA in eukaryotic cells duringDNA synthesis. A multi-subunit enzyme in which PolD1 encodes the catalytic subunit with polymerase and 3'-5' exonuclease proofreading activities.","predictedComplex":false,"interactors":[{"ac":"EBI-11708226","identifier":"CHEBI:33723","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:33723","name":"tetra-mu3-sulfido-tetrairon(1+)","description":"tetra-mu3-sulfido-tetrairon(1+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-131791","identifier":"P54358","identifierLink":"https://www.uniprot.org/uniprotkb/P54358/entry","name":"PolD1","description":"DNA polymerase delta catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10322","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-194173","identifier":"Q9W088","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W088/entry","name":"PolD2","description":"DNA polymerase delta subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-89582","identifier":"Q9Y118","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y118/entry","name":"PolD3","description":"DNA polymerase delta subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]}]},{"complexAC":"CPX-2422","complexName":"DNA polymerase epsilon complex","organismName":"Drosophila melanogaster; 7227","description":"Functions as a leading strand polymerase during nuclear DNA synthesis, moving along DNA with the replication fork. The complex  also has 3'-5' proofreading exonuclease activity that corrects errors arising during DNA replication","predictedComplex":false,"interactors":[{"ac":"EBI-11708226","identifier":"CHEBI:33723","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:33723","name":"tetra-mu3-sulfido-tetrairon(1+)","description":"tetra-mu3-sulfido-tetrairon(1+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-135887","identifier":"Q9VRQ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VRQ7/entry","name":"PolE2","description":"DNA polymerase epsilon subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12708","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-138718","identifier":"Q9V444","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V444/entry","name":"Chrac-14","description":"DNA polymerase epsilon subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46172","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-156665","identifier":"Q9W256","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W256/entry","name":"PolE4","description":"DNA polymerase epsilon subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10252","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-173478","identifier":"Q9VCN1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VCN1/entry","name":"PolE1","description":"DNA polymerase epsilon catalytic subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10670","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2423","complexName":"SWR1 chromatin remodelling complex","organismName":"Drosophila melanogaster; 7227","description":"ATP-dependent chromatin-remodeling complex. SWR1 replaces the canonical H2A/H2B dimer at nucleosomes flanking histone-depleted regions, such as promoters, with a variant histone H2A.V/H2B dimer.","predictedComplex":false,"interactors":[{"ac":"EBI-102665","identifier":"Q9Y0I1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y0I1/entry","name":"MRG15","description":"NuA4 complex subunit EAF3 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10880","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-103202","identifier":"Q9VAM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VAM5/entry","name":"Brd8","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15398","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-105997","identifier":"Q7K3D8","identifierLink":"https://www.uniprot.org/uniprotkb/Q7K3D8/entry","name":"DMAP1","description":"DNA methyltransferase 1-associated protein 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12855","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-116977","identifier":"Q9VKM6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VKM6/entry","name":"YL-1","description":"Vacuolar protein sorting-associated protein 72 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13275","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-123863","identifier":"Q7K012","identifierLink":"https://www.uniprot.org/uniprotkb/Q7K012/entry","name":"Bap55","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-163314","identifier":"P45890","identifierLink":"https://www.uniprot.org/uniprotkb/P45890/entry","name":"Arp6","description":"Actin-related protein 6","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1866001","identifier":"Q9NDJ2-2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NDJ2-2/entry","name":"dom","description":"Helicase domino","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-187741","identifier":"Q9VM63","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VM63/entry","name":"Gas41","description":"YEATS domain-containing protein 4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23195","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-192924","identifier":"Q9V3K3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V3K3/entry","name":"rept","description":"RuvB-like helicase 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-234957","identifier":"Q9VH07","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VH07/entry","name":"pont","description":"RuvB-like helicase 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2912878","identifier":"Q9V4C8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V4C8/entry","name":"Hcf","description":"Host cell factor","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46003","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34614390","identifier":"Q7K003","identifierLink":"https://www.uniprot.org/uniprotkb/Q7K003/entry","name":"MrgBP","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13581","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2424","complexName":"Dystrophin glycoprotein complex, skeletal muscle variant","organismName":"Homo sapiens; 9606","description":"A plasma membrane transmembrane complex that links the actin cytoskeleton to the extracellular matrix. In skeletal muscle, it limits mechanical damage during contraction and thus prevents muscle degeneration. The complex also functions as a scaffold for proteins involved in signaling such as neuronal nitric oxide synthase (NOS1, P29475).","predictedComplex":false,"interactors":[{"ac":"EBI-20738802","identifier":"Q14118-PRO_0000021066","identifierLink":"https://www.uniprot.org/uniprotkb/Q14118-PRO_0000021066/entry","name":"DAG1","description":"Beta-dystroglycan","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-20738807","identifier":"Q14118-PRO_0000021065","identifierLink":"https://www.uniprot.org/uniprotkb/Q14118-PRO_0000021065/entry","name":"DAG1","description":"Alpha-dystroglycan","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-20811995","identifier":"Q14714","identifierLink":"https://www.uniprot.org/uniprotkb/Q14714/entry","name":"SSPN","description":"Sarcospan","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15260","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-295843","identifier":"Q13884","identifierLink":"https://www.uniprot.org/uniprotkb/Q13884/entry","name":"SNTB1","description":"Beta-1-syntrophin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 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Catalyzes both histone H2A(P84051)  Lys-119 ubiquitination, thus adding a specific tag for epigenetic transcriptional repression and also demethylates Lys-36 of histone H3, regulating DNA accessibility to the cellular machineries which require DNA as a template.","predictedComplex":false,"interactors":[{"ac":"EBI-145507","identifier":"Q9VB08","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VB08/entry","name":"Sce","description":"E3 ubiquitin-protein ligase RING1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-158813","identifier":"Q9VHH9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VHH9/entry","name":"Kdm2","description":"JmjC domain-containing histone demethylation protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23123","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2929936","identifier":"CHEBI:29033","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29033","name":"iron2plus","description":"iron(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-84600","identifier":"P35820","identifierLink":"https://www.uniprot.org/uniprotkb/P35820/entry","name":"Psc","description":"Polycomb group protein Psc","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10825","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2428","complexName":"Casein kinase II complex, CSNK2A2 variant","organismName":"Homo sapiens; 9606","description":"Serine/threonine-protein kinase that phosphorylates  substrates containing acidic residues C-terminal to the phosphorylated serine or threonine.","predictedComplex":false,"interactors":[{"ac":"EBI-347451","identifier":"P19784","identifierLink":"https://www.uniprot.org/uniprotkb/P19784/entry","name":"CSNK2A2","description":"Casein kinase II subunit alpha'","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24054","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348169","identifier":"P67870","identifierLink":"https://www.uniprot.org/uniprotkb/P67870/entry","name":"CSNK2B","description":"Casein kinase II subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2429","complexName":"DSIF transcription elongation complex","organismName":"Drosophila melanogaster; 7227","description":"An essential RNA polymerase II elongation factor which functions in the control of RNAP II processivity. Mediates both activation and inhibition of transcription elongation, and plays a role in pre-mRNA processing. Required for promoter-proximal pausing when elongating Pol II pauses near the promoter, about 20-60 base pairs downstream of the transcription start site, a key event in post-initiation regulation of transcription. spt5 docks DSIF to Pol II near the RNA exit channel where it facilitates capping of the nascent RNA. The negative elongation factor (NELF) complex then recognizes the Pol II-spt5 interface and associates with the elongation complex as it transcribes through the promoter-proximal region. Phosphorylation of spt5 by P-TEFb appears to trigger dissociation of NELF from Pol II, enabling Pol II reactivation and resumption of elongation.","predictedComplex":false,"interactors":[{"ac":"EBI-134850","identifier":"Q9V460","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V460/entry","name":"Spt5","description":"Transcription elongation factor SPT5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11125","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-165626","identifier":"Q9TVQ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9TVQ5/entry","name":"spt4","description":"Transcription elongation factor SPT4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12882","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2430","complexName":"NELF negative elongation factor complex","organismName":"Drosophila melanogaster; 7227","description":"Negatively regulates the elongation of transcription by RNA polymerase II. Required for promoter-proximal pausing when elongating Pol II pauses near the promoter, about 20-60 base pairs downstream of the transcription start site, a key event in post-initiation regulation of transcription. SUPT5H (Q9V460) docks the DSIF complex (CPX-2429) to Pol II near the RNA exit channel where it facilitates capping of the nascent RNA. NELF then recognizes the Pol II-SUPT5H interface and associates with the elongation complex as it transcribes through the promoter-proximal region. Binding of newly synthesized RNA by NELF may stabilize its interactions with elongating Pol II at specific loci. Phosphorylation of SUPT5H by P-TEFb appears to trigger dissociation of NELF from Pol II, enabling Pol II reactivation and resumption of elongation.","predictedComplex":false,"interactors":[{"ac":"EBI-144590","identifier":"Q24134","identifierLink":"https://www.uniprot.org/uniprotkb/Q24134/entry","name":"TH1","description":"Negative elongation factor D","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12144","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-194490","identifier":"P92204","identifierLink":"https://www.uniprot.org/uniprotkb/P92204/entry","name":"Nelf-E","description":"Negative elongation factor E","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR17250","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3411985","identifier":"Q9Y113","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y113/entry","name":"NELF-B","description":"Negative elongation factor B","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13503","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-82217","identifier":"Q86NP2","identifierLink":"https://www.uniprot.org/uniprotkb/Q86NP2/entry","name":"Nelf-A","description":"Negative elongation factor A","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13328","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2431","complexName":"LKB1-STRAD-MO25 serine/threonine protein kinase complex, CAB39L-STRADA variant","organismName":"Homo sapiens; 9606","description":"Serine/threonine protein kinase complex which directly phosphorylates adenosine monophosphate-activated protein kinase (AMPK) family members on the T-loop thereby activating them.  Couples cellular growth and division to the availability of cellular energy. by activating the AMP kinases when energy levels are low, inhibiting signalling pathways that promote proliferation","predictedComplex":false,"interactors":[{"ac":"EBI-1047244","identifier":"Q9H9S4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H9S4/entry","name":"CAB39L","description":"Calcium-binding protein 39-like","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10182","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1109114","identifier":"Q7RTN6","identifierLink":"https://www.uniprot.org/uniprotkb/Q7RTN6/entry","name":"STRADA","description":"STE20-related kinase adapter protein alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48014","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-306838","identifier":"Q15831","identifierLink":"https://www.uniprot.org/uniprotkb/Q15831/entry","name":"STK11","description":"Serine/threonine-protein kinase STK11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43895","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2432","complexName":"Positive transcription elongation factor B complex","organismName":"Drosophila melanogaster; 7227","description":"A serine kinase complex that phosphorylates elongation pausing factors such as DSIF (CPX-2429) and NELF (CPX-2430) and Ser-2 and Ser-5 of RNA polymerase II (RNA Pol II) heptapeptide repeat, thus positively regulating productive mRNA elongation through the gene body after promoter-proximal pausing of RNA Pol II. Involved in cotranscriptional histone modification, mRNA processing and mRNA export.","predictedComplex":false,"interactors":[{"ac":"EBI-100284","identifier":"O17432","identifierLink":"https://www.uniprot.org/uniprotkb/O17432/entry","name":"Cdk9","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-191577","identifier":"O96433","identifierLink":"https://www.uniprot.org/uniprotkb/O96433/entry","name":"CycT","description":"Cyclin-T","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2433","complexName":"NXF5-NXT1 mRNA nuclear export factor complex","organismName":"Homo sapiens; 9606","description":"Mediates the export of bulk mRNA through direct interactions with both the mRNA cargo and nuclear pore proteins that contain characteristic phenylalanine-glycine repeating sequence motifs (FG-nucleoporins or FG-nups).","predictedComplex":false,"interactors":[{"ac":"EBI-20868263","identifier":"Q9H1B4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H1B4/entry","name":"NXF5","description":"Nuclear RNA export factor 5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 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7227","xrefs":[{"identifier":"PTHR15346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-137897","identifier":"Q9VJQ6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VJQ6/entry","name":"DCTN5-p25","description":"Dynactin subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46126","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-137955","identifier":"P45889","identifierLink":"https://www.uniprot.org/uniprotkb/P45889/entry","name":"Arp1","description":"Actin-related protein 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-148402","identifier":"Q9W1V8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W1V8/entry","name":"DCTN3-p24","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 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Associates with the asymmetric site 'CCAATAAG' in the Fab-7 insulator element.","predictedComplex":false,"interactors":[{"ac":"EBI-174123","identifier":"Q9VQD6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VQD6/entry","name":"Elba2","description":"Early boundary activity protein 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-180015","identifier":"Q9VR19","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VR19/entry","name":"Elba3","description":"Early boundary activity protein 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-188202","identifier":"Q9VR17","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VR17/entry","name":"Elba1","description":"Early boundary activity protein 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]}]},{"complexAC":"CPX-2440","complexName":"FLCN-FNIP GTPase-activating complex, FNIP2 variant","organismName":"Homo sapiens; 9606","description":"GTPase-activating complex which specifically stimulates GTP hydrolysis by RRAGC or RRAGD in the RAG guanosine triphosphatase complexes (CPX-2542, CPX-2513, CPX-2514, CPX-767) promoting the conversion to the GDP-bound state of RRAGC or RRAGD and thereby activating the kinase activity of mTORC1. Membrane sequestration of the FLCN-FNIP complex by GABARAP family members uncouples its regulation of RRAGC/RRAGD resulting in impaired substrate-specific mTOR-dependent phosphorylation of transcription factor TFE3 (P19532) and TFEB (P19484) which act as master regulators of lysosomal biogenesis, autophagy, lysosomal exocytosis, lipid catabolism, energy metabolism and immune response.","predictedComplex":false,"interactors":[{"ac":"EBI-2970160","identifier":"Q8NFG4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NFG4/entry","name":"FLCN","description":"Folliculin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31441","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7597109","identifier":"Q9P278","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P278/entry","name":"FNIP2","description":"Folliculin-interacting protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21634","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2441","complexName":"DNA replication factor C complex, elg1 variant","organismName":"Drosophila melanogaster; 7227","description":"DNA-dependent ATPase clamp-unloader complex that acts to remove PCNA (P1791, CPX-543) remaining on DNA after the completion of DNA replication and repair during the S phase of the cell cycle. The complex binds to DNA-loaded PCNA to induce opening of the PCNA ring, leading to the release of elg1-RFC bound-PCNA. Role in sister chromatid cohesion, unloading both unmodified and SUMOylated PCNA from DNA following replication. This is a genome-wide process and follows Okazaki fragment ligation.","predictedComplex":false,"interactors":[{"ac":"EBI-118156","identifier":"Q9VKW3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VKW3/entry","name":"RfC3","description":"Activator 1 subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-184606","identifier":"P53034","identifierLink":"https://www.uniprot.org/uniprotkb/P53034/entry","name":"RfC4","description":"Replication factor C subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-189726","identifier":"Q9U9Q1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9U9Q1/entry","name":"RfC38","description":"Replication factor C subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-88723","identifier":"Q9VX15","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VX15/entry","name":"Rfc37","description":"Replication factor C subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-94021","identifier":"Q86BP6","identifierLink":"https://www.uniprot.org/uniprotkb/Q86BP6/entry","name":"elg1","description":"Enhanced level of genomic instability 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23389","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2442","complexName":"Enok histone acetyltransferase complex","organismName":"Drosophila melanogaster; 7227","description":"Histone lysine acetyltransferase 6 complex which preferentially acetylates histone H3 residues in nucleosomes. May modulate PCNA levels on chromatin during cell cycle progression via an interaction with the Elg1-RFC-like complex (CPX-2441).","predictedComplex":false,"interactors":[{"ac":"EBI-100887","identifier":"Q9VJY8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VJY8/entry","name":"Ing5","description":"Inhibitor of growth protein 5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-111644","identifier":"Q7JVP4","identifierLink":"https://www.uniprot.org/uniprotkb/Q7JVP4/entry","name":"Br140","description":"Bromodomain-containing protein homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13793","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-140042","identifier":"Q9VRN3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VRN3/entry","name":"Eaf6","description":"Chromatin modification-related protein MEAF6","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-194800","identifier":"Q9W1A9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W1A9/entry","name":"enok","description":"histone acetyltransferase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2443","complexName":"Dystrophin glycoprotein complex, neuromuscular junction variant","organismName":"Homo sapiens; 9606","description":"A plasma membrane transmembrane complex that links the actin cytoskeleton to the extracellular matrix. At the post-synaptic neuromuscular junction (NMJ) is involved in receptor clustering and synaptic transmission, stabilizing neurotransmitter acetylcholine receptors. It also plays a role in a number of important signaling cascades acting at the NMJ, such as the agrin/muscle-specific kinase MUSK  (O15146), NOS1 (P29475), and Ca2+/calmodulin-dependent protein kinase II (CAMKII)-mediated signaling pathways.","predictedComplex":false,"interactors":[{"ac":"EBI-20738802","identifier":"Q14118-PRO_0000021066","identifierLink":"https://www.uniprot.org/uniprotkb/Q14118-PRO_0000021066/entry","name":"DAG1","description":"Beta-dystroglycan","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-20738807","identifier":"Q14118-PRO_0000021065","identifierLink":"https://www.uniprot.org/uniprotkb/Q14118-PRO_0000021065/entry","name":"DAG1","description":"Alpha-dystroglycan","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-20811995","identifier":"Q14714","identifierLink":"https://www.uniprot.org/uniprotkb/Q14714/entry","name":"SSPN","description":"Sarcospan","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 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9606","xrefs":[{"identifier":"PTHR21142","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-717191","identifier":"Q13424","identifierLink":"https://www.uniprot.org/uniprotkb/Q13424/entry","name":"SNTA1","description":"Alpha-1-syntrophin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10554","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2444","complexName":"Elongin transcription elongation complex","organismName":"Drosophila melanogaster; 7227","description":"A transcription elongation factor that increases RNA polymerase II elongation rate by suppressing transient pausing.","predictedComplex":false,"interactors":[{"ac":"EBI-108863","identifier":"Q9VCP0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VCP0/entry","name":"EloA","description":"Transcription elongation factor B polypeptide 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 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The complex reduces the energetic cost of insertion by inducing a local thinning of the membrane by approximately 10A, thus decreasing the distance that a substrate's soluble lumenal domain must travel through the hydrophobic bilayer, and also by creating a positively charged patch in the bilayer.","predictedComplex":false,"interactors":[{"ac":"EBI-136831","identifier":"Q9VEQ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VEQ1/entry","name":"EMC2A","description":"ER membrane protein complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12760","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-189387","identifier":"Q9W1Y1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W1Y1/entry","name":"EMC8-9","description":"ER membrane protein complex subunit 8/9 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12941","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26696716","identifier":"Q9VJ25","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VJ25/entry","name":"EMC5","description":"Membrane magnesium transporter","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21181","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26795128","identifier":"Q9VNQ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VNQ3/entry","name":"EMC4","description":"ER membrane protein complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19315","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30876338","identifier":"Q9VKR0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VKR0/entry","name":"EMC3","description":"ER membrane protein complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13116","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30876358","identifier":"Q9VBZ8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VBZ8/entry","name":"EMC6","description":"ER membrane protein complex subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR20994","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30876373","identifier":"A1ZA83","identifierLink":"https://www.uniprot.org/uniprotkb/A1ZA83/entry","name":"EMC7","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13605","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30876389","identifier":"Q8IPT0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IPT0/entry","name":"EMC10","description":"ER membrane protein complex subunit 10","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21397","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3415376","identifier":"Q9VHY6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VHY6/entry","name":"EMC1","description":"ER membrane protein complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21573","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2450","complexName":"UTP-A complex","organismName":"Homo sapiens; 9606","description":"Required for early co-transcriptional events in ribosome biogenesis, acting as an RNA chaperone to initiate ribosome assembly. At the earliest stages of transcription, three subunits of UTPA (UTP8, UTP9 and UTP17) bind to nascent pre-rRNA at the very 5′ end while the remaining four subunits (UTP10, UTP4, UTP5 and UTP15) interact with nucleotides further downstream in the 5'-external transcribed spacer (ETS). May also act to stimulate U3 snoRNP recruitment. A sub-unit of the small subunit (SSU) processome, a 2.2 MDa ribonucleoprotein complex involved in the processing, assembly and maturation of nascent pre-ribosomal RNA to form the small ribosomal subunit. The SSU processome is a giant particle composed of numerous ribosome assembly factors, including the UTP-A, UTP-B (CPX-2688) and MPP10 (CPX-2478) complexes, the U3 small nucleolar ribonucleoprotein (snoRNP) and many individual proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-1048301","identifier":"Q8TED0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TED0/entry","name":"UTP15","description":"U3 small nucleolar RNA-associated protein 15 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19924","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1048716","identifier":"Q9H583","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H583/entry","name":"HEATR1","description":"HEAT repeat-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13457","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2515097","identifier":"Q8IWA0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IWA0/entry","name":"WDR75","description":"WD repeat-containing protein 75","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44215","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2563523","identifier":"Q15061","identifierLink":"https://www.uniprot.org/uniprotkb/Q15061/entry","name":"WDR43","description":"WD repeat-containing protein 43","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44267","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2602591","identifier":"Q969X6","identifierLink":"https://www.uniprot.org/uniprotkb/Q969X6/entry","name":"UTP4","description":"U3 small nucleolar RNA-associated protein 4 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44163","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-725885","identifier":"Q9H8H0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H8H0/entry","name":"NOL11","description":"Nucleolar protein 11","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2451","complexName":"Endoplasmic reticulum membrane complex, EMC2B variant","organismName":"Drosophila melanogaster; 7227","description":"Insertase complex required for the post-translational integration of tail-anchored proteins and co-translational insertion of some multi-pass membrane proteins into the endoplasmic reticulum membrane. The complex reduces the energetic cost of insertion by inducing a local thinning of the membrane by approximately 10A, thus decreasing the distance that a substrate's soluble lumenal domain must travel through the hydrophobic bilayer, and also by creating a positively charged patch in the bilayer.","predictedComplex":false,"interactors":[{"ac":"EBI-101183","identifier":"Q9VEQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VEQ2/entry","name":"EMC2B","description":"ER membrane protein complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12760","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-189387","identifier":"Q9W1Y1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W1Y1/entry","name":"EMC8-9","description":"ER membrane protein complex subunit 8/9 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12941","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26696716","identifier":"Q9VJ25","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VJ25/entry","name":"EMC5","description":"Membrane magnesium transporter","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21181","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26795128","identifier":"Q9VNQ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VNQ3/entry","name":"EMC4","description":"ER membrane protein complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19315","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30876338","identifier":"Q9VKR0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VKR0/entry","name":"EMC3","description":"ER membrane protein complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13116","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30876358","identifier":"Q9VBZ8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VBZ8/entry","name":"EMC6","description":"ER membrane protein complex subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR20994","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30876373","identifier":"A1ZA83","identifierLink":"https://www.uniprot.org/uniprotkb/A1ZA83/entry","name":"EMC7","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13605","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30876389","identifier":"Q8IPT0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IPT0/entry","name":"EMC10","description":"ER membrane protein complex subunit 10","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21397","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3415376","identifier":"Q9VHY6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VHY6/entry","name":"EMC1","description":"ER membrane protein complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21573","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2452","complexName":"ESCRT-0 complex","organismName":"Drosophila melanogaster; 7227","description":"The ESCRT machinery, consisting of ESCRT-0 (this complex), -I (CPX-2457/CPX-2460), -II (CPX-2458), -III (CPX-2459) and -IV (VPS4-VTA1 complex, CPX-2462) has been implicated in membrane scission steps, transforming a single, continuous bilayer into two distinct bilayers, either from within the neck of a vesicle budding away from the cytoplasm or from within a membrane tubule, while segregating cargo throughout the process. ESCRT-0 binds to and clusters ubiquitinated cargo for delivery into  multivesicular bodies, and recruits clathrin, ubiquitin ligases, and deubiquitinating enzymes. ESCRT-0 recruits ESCRT-I which engages ESCRT-II to nucleate ESCRT-III polymerization. VPS4-VTA1 complex, also known as ESCRT-IV, disassembles ESCRT-III to recycle its subunits. The ESCRT-III complex facilitates changes in membrane architecture by oligomerizing to form spiral, filament-like tubules, accumulation of which is associated with membrane constriction and fission. Disassembly of ESCRT-III by VPS4-VTA1 may be a required step for fission.","predictedComplex":false,"interactors":[{"ac":"EBI-87548","identifier":"Q9XTL2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XTL2/entry","name":"Stam","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45929","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-90175","identifier":"Q960X8","identifierLink":"https://www.uniprot.org/uniprotkb/Q960X8/entry","name":"Hrs","description":"Hepatocyte growth factor-regulated tyrosine kinase substrate","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46275","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2453","complexName":"Dystrophin glycoprotein complex, CNS variant","organismName":"Homo sapiens; 9606","description":"A plasma membrane transmembrane complex that links the actin cytoskeleton to the extracellular matrix. Essential for cognition and memory involving hippocampal and forebrain function. Also plays a role in modulating synapse function at inhibitory GABAergic synapses in the cerebellum, the amygdala, and the hippocampus where it is present in the post-synapse.","predictedComplex":false,"interactors":[{"ac":"EBI-19763427","identifier":"Q9NSN8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NSN8/entry","name":"SNTG1","description":"Gamma-1-syntrophin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10554","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20738802","identifier":"Q14118-PRO_0000021066","identifierLink":"https://www.uniprot.org/uniprotkb/Q14118-PRO_0000021066/entry","name":"DAG1","description":"Beta-dystroglycan","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-20738807","identifier":"Q14118-PRO_0000021065","identifierLink":"https://www.uniprot.org/uniprotkb/Q14118-PRO_0000021065/entry","name":"DAG1","description":"Alpha-dystroglycan","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-30876505","identifier":"P11532-4","identifierLink":"https://www.uniprot.org/uniprotkb/P11532-4/entry","name":"DMD","description":"Dystrophin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-30876519","identifier":"Q96LD1","identifierLink":"https://www.uniprot.org/uniprotkb/Q96LD1/entry","name":"SGCZ","description":"Zeta-sarcoglycan","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12939","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-717191","identifier":"Q13424","identifierLink":"https://www.uniprot.org/uniprotkb/Q13424/entry","name":"SNTA1","description":"Alpha-1-syntrophin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10554","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-718097","identifier":"O43556","identifierLink":"https://www.uniprot.org/uniprotkb/O43556/entry","name":"SGCE","description":"Epsilon-sarcoglycan","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10132","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-740402","identifier":"O60941","identifierLink":"https://www.uniprot.org/uniprotkb/O60941/entry","name":"DTNB","description":"Dystrobrevin beta","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12268","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2454","complexName":"Dystrophin glycoprotein complex, retinal outer plexiform layer variant","organismName":"Homo sapiens; 9606","description":"A plasma membrane transmembrane complex that links the actin cytoskeleton to the extracellular matrix. In the retina the complex is  required for correct electrical activity and retina formation and is present in the presynapse.","predictedComplex":false,"interactors":[{"ac":"EBI-20738802","identifier":"Q14118-PRO_0000021066","identifierLink":"https://www.uniprot.org/uniprotkb/Q14118-PRO_0000021066/entry","name":"DAG1","description":"Beta-dystroglycan","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-20738807","identifier":"Q14118-PRO_0000021065","identifierLink":"https://www.uniprot.org/uniprotkb/Q14118-PRO_0000021065/entry","name":"DAG1","description":"Alpha-dystroglycan","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-20811995","identifier":"Q14714","identifierLink":"https://www.uniprot.org/uniprotkb/Q14714/entry","name":"SSPN","description":"Sarcospan","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15260","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-295843","identifier":"Q13884","identifierLink":"https://www.uniprot.org/uniprotkb/Q13884/entry","name":"SNTB1","description":"Beta-1-syntrophin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10554","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30876569","identifier":"P11532-2","identifierLink":"https://www.uniprot.org/uniprotkb/P11532-2/entry","name":"DMD","description":"Dystrophin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-3904504","identifier":"Q92629","identifierLink":"https://www.uniprot.org/uniprotkb/Q92629/entry","name":"SGCD","description":"Delta-sarcoglycan","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12939","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5357343","identifier":"Q13326","identifierLink":"https://www.uniprot.org/uniprotkb/Q13326/entry","name":"SGCG","description":"Gamma-sarcoglycan","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12939","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5663553","identifier":"Q16586","identifierLink":"https://www.uniprot.org/uniprotkb/Q16586/entry","name":"SGCA","description":"Alpha-sarcoglycan","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10132","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5663627","identifier":"Q16585","identifierLink":"https://www.uniprot.org/uniprotkb/Q16585/entry","name":"SGCB","description":"Beta-sarcoglycan","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21142","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-717191","identifier":"Q13424","identifierLink":"https://www.uniprot.org/uniprotkb/Q13424/entry","name":"SNTA1","description":"Alpha-1-syntrophin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10554","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-740402","identifier":"O60941","identifierLink":"https://www.uniprot.org/uniprotkb/O60941/entry","name":"DTNB","description":"Dystrobrevin beta","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12268","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-73","complexName":"Phosphatidylinositol 3-kinase complex, class III, ATG14 variant","organismName":"Homo sapiens; 9606","description":"A phosphatidylinositol 3-kinase complex that specifically phosphorylates 1-phosphatidyl-1D-myo-inositol(1-) (CHEBI:57880) in an ATP- and Mn(2+)-dependent manner. Plays a key role in initiation and maturation of autophagosomes, involved in the transport of lysosomal enzyme precursors to lysosomes, required for transport from early to late endosomes.","predictedComplex":false,"interactors":[{"ac":"EBI-1046979","identifier":"Q99570","identifierLink":"https://www.uniprot.org/uniprotkb/Q99570/entry","name":"PIK3R4","description":"Phosphoinositide 3-kinase regulatory subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR17583","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1056470","identifier":"Q8NEB9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NEB9/entry","name":"PIK3C3","description":"Phosphatidylinositol 3-kinase catalytic subunit type 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2690371","identifier":"Q6ZNE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6ZNE5/entry","name":"ATG14","description":"Beclin 1-associated autophagy-related key regulator","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13664","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-949378","identifier":"Q14457","identifierLink":"https://www.uniprot.org/uniprotkb/Q14457/entry","name":"BECN1","description":"Beclin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12768","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-74","complexName":"Phosphatidylinositol 3-kinase complex, class III, UVRAG variant","organismName":"Homo sapiens; 9606","description":"A phosphatidylinositol 3-kinase complex that specifically phosphorylates 1-phosphatidyl-1D-myo-inositol(1−) (CHEBI:57880) in an ATP- and Mn(2+)-dependent manner. Plays a role in later stages of autophagy.","predictedComplex":false,"interactors":[{"ac":"EBI-1046979","identifier":"Q99570","identifierLink":"https://www.uniprot.org/uniprotkb/Q99570/entry","name":"PIK3R4","description":"Phosphoinositide 3-kinase regulatory subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR17583","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1056470","identifier":"Q8NEB9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NEB9/entry","name":"PIK3C3","description":"Phosphatidylinositol 3-kinase catalytic subunit type 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2952704","identifier":"Q9P2Y5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P2Y5/entry","name":"UVRAG","description":"UV radiation resistance-associated gene protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15157","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-949378","identifier":"Q14457","identifierLink":"https://www.uniprot.org/uniprotkb/Q14457/entry","name":"BECN1","description":"Beclin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12768","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-75","complexName":"Phosphatidylinositol 3-kinase complex, class III, ATG14 variant","organismName":"Mus musculus; 10090","description":"A phosphatidylinositol 3-kinase complex that specifically phosphorylates 1-phosphatidyl-1D-myo-inositol(1-) (CHEBI:57880 ) in an ATP- and Mn(2+)-dependent manner. Plays a key role in initiation and maturation of autophagosomes, involved in the transport of lysosomal enzyme precursors to lysosomes, required for transport from early to late endosomes.","predictedComplex":false,"interactors":[{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-3506699","identifier":"Q8CDJ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CDJ3/entry","name":"Atg14","description":"Beclin 1-associated autophagy-related key regulator","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13664","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-643716","identifier":"O88597","identifierLink":"https://www.uniprot.org/uniprotkb/O88597/entry","name":"Becn1","description":"Beclin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12768","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6678149","identifier":"Q6PF93","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PF93/entry","name":"Pik3c3","description":"Phosphatidylinositol 3-kinase catalytic subunit type 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6678184","identifier":"Q8VD65","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VD65/entry","name":"Pik3r4","description":"Phosphoinositide 3-kinase regulatory subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR17583","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-76","complexName":"Phosphatidylinositol 3-kinase complex, class III, UVRAG variant","organismName":"Mus musculus; 10090","description":"A phosphatidylinositol 3-kinase complex that specifically phosphorylates 1-phosphatidyl-1D-myo-inositol(1-) (CHEBI:57880) in an ATP- and Mn(2+)-dependent manner. Plays a role in later stages of autophagy.","predictedComplex":false,"interactors":[{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-643716","identifier":"O88597","identifierLink":"https://www.uniprot.org/uniprotkb/O88597/entry","name":"Becn1","description":"Beclin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12768","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6678149","identifier":"Q6PF93","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PF93/entry","name":"Pik3c3","description":"Phosphatidylinositol 3-kinase catalytic subunit type 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6678184","identifier":"Q8VD65","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VD65/entry","name":"Pik3r4","description":"Phosphoinositide 3-kinase regulatory subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR17583","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6678333","identifier":"Q8K245","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K245/entry","name":"Uvrag","description":"UV radiation resistance-associated protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15157","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-77","complexName":"DNA mismatch repair MutSbeta complex","organismName":"Homo sapiens; 9606","description":"Mismatch repair complex, involved in the recognition and repair of base-base and small insertion/deletion mismatches that appear as a consequence of DNA polymerase errors during DNA synthesis. MutSbeta recognises insertions or deletions loops 1-15 nucleotides as well as DNA with a 3prime single-stranded overhang. Also required for the mutagenic expansion of trinucleotide repeats.","predictedComplex":false,"interactors":[{"ac":"EBI-1164205","identifier":"P20585","identifierLink":"https://www.uniprot.org/uniprotkb/P20585/entry","name":"MSH3","description":"DNA mismatch repair protein Msh3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11361","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355888","identifier":"P43246","identifierLink":"https://www.uniprot.org/uniprotkb/P43246/entry","name":"MSH2","description":"DNA mismatch repair protein Msh2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11361","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-78","complexName":"DNA mismatch repair MutSbeta complex","organismName":"Mus musculus; 10090","description":"Mismatch repair complex, involved in the recognition and repair of base-base and small insertion/deletion mismatches that appear as a consequence of DNA polymerase errors during DNA synthesis. MutSbeta recognises insertions or deletions of more than 2 nucleotides. Also required for the mutagenic expansion of trinucleotide repeats.","predictedComplex":false,"interactors":[{"ac":"EBI-10691005","identifier":"P13705","identifierLink":"https://www.uniprot.org/uniprotkb/P13705/entry","name":"Msh3","description":"DNA mismatch repair protein Msh3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11361","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2549940","identifier":"P43247","identifierLink":"https://www.uniprot.org/uniprotkb/P43247/entry","name":"Msh2","description":"DNA mismatch repair protein Msh2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11361","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-80","complexName":"DNA mismatch repair MutSalpha complex","organismName":"Homo sapiens; 9606","description":"Mismatch repair complex, involved in the recognition and repair of base-base and small insertion/deletion mismatches that appear as a consequence of DNA polymerase errors during DNA synthesis. MutSalpha recognizes single base mismatches and 1- or 2- nucleotide insertion or deletion mis-pairs.","predictedComplex":false,"interactors":[{"ac":"EBI-355888","identifier":"P43246","identifierLink":"https://www.uniprot.org/uniprotkb/P43246/entry","name":"MSH2","description":"DNA mismatch repair protein Msh2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11361","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395529","identifier":"P52701","identifierLink":"https://www.uniprot.org/uniprotkb/P52701/entry","name":"MSH6","description":"DNA mismatch repair protein Msh6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11361","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-79","complexName":"General transcription factor TFIIF complex","organismName":"Homo sapiens; 9606","description":"TFIIF is a general transcription factor associated with RNA polymerase II (CPX-2387/CPX-7481). It prevents the non-specific interaction of RNA Pol II with DNA and stabilizes the pre-initiation complex (PIC), in particular stabilizing TFIIB within the PIC and stimulating the recruitment of TFIIH, thus promoting initiation and elongation. May also interact with paused Pol II causing a conformational change that facilitates the re-entry into elongation mode.","predictedComplex":false,"interactors":[{"ac":"EBI-1030560","identifier":"P13984","identifierLink":"https://www.uniprot.org/uniprotkb/P13984/entry","name":"GTF2F2","description":"General transcription factor IIF subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10445","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-457886","identifier":"P35269","identifierLink":"https://www.uniprot.org/uniprotkb/P35269/entry","name":"GTF2F1","description":"General transcription factor IIF subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13011","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-81","complexName":"DNA mismatch repair MutSalpha complex","organismName":"Mus musculus; 10090","description":"Mismatch repair complex, involved in the recognition and repair of base-base and small insertion/deletion mismatches that appear as a consequence of DNA polymerase errors during DNA synthesis. MutSalpha recognises single base mismatches and 1- or 2- nucleotide insertion or deletion mis-pairs.","predictedComplex":false,"interactors":[{"ac":"EBI-2549940","identifier":"P43247","identifierLink":"https://www.uniprot.org/uniprotkb/P43247/entry","name":"Msh2","description":"DNA mismatch repair protein Msh2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11361","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2549976","identifier":"P54276","identifierLink":"https://www.uniprot.org/uniprotkb/P54276/entry","name":"Msh6","description":"DNA mismatch repair protein Msh6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11361","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-82","complexName":"Mitotic spindle assembly checkpoint Mad1 complex","organismName":"Homo sapiens; 9606","description":"Downstream component of the kinetochore-targeting hierarchy. Stimulates assembly of the mitotic checkpoint complex which prevents premature chromosome segregation until all kinetochores have obtained connections to spindle microtubules.","predictedComplex":false,"interactors":[{"ac":"EBI-742610","identifier":"Q9Y6D9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6D9/entry","name":"MAD1L1","description":"Mitotic spindle assembly checkpoint protein MAD1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23168","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-83","complexName":"General transcription factor TFIIF complex","organismName":"Mus musculus; 10090","description":"TFIIF is a general transription factor associated with RNA polymerase II. It  promotes inititation and elongation.","predictedComplex":false,"interactors":[{"ac":"EBI-8391657","identifier":"Q3THK3","identifierLink":"https://www.uniprot.org/uniprotkb/Q3THK3/entry","name":"Gtf2f1","description":"General transcription factor IIF subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13011","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8458632","identifier":"Q8R0A0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R0A0/entry","name":"Gtf2f2","description":"General transcription factor IIF subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10445","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-84","complexName":"Mitotic spindle assembly checkpoint Mad1 complex","organismName":"Mus musculus; 10090","description":"Stimulates assembly of the mitotic checkpoint complex. which prevents premature chromosome segregation until all kinetochores have obtained connections to spindle microtubules.","predictedComplex":false,"interactors":[{"ac":"EBI-4285225","identifier":"Q9WTX8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WTX8/entry","name":"Mad1l1","description":"Mitotic spindle assembly checkpoint protein MAD1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23168","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-85","complexName":"Mitotic spindle assembly checkpoint MAD1-MAD2 complex","organismName":"Homo sapiens; 9606","description":"Acts at the spindle checkpoint, in a surveillance mechanism that mediates a delay in the onset of anaphase, until all chromosomes are properly attached to the mitotic or meiotic spindle.  Inhibits Cdc20, the mitotic co-activator of the anaphase-promoting complex/cyclosome (APC/C), an E3 ubiquitin ligase. Mad2 adopts two distinct conformations; when unbound, it adopts an open conformation (O-Mad2) but upon binding to Mad1, the Mad2 C-terminal tail crosses the entire surface of the beta-sheet and locks Mad1. Upon mitotic entry, the Mad1-C-Mad2 core complex is recruited to kinetochores. Because Mad2 can dimerise, O-Mad2 from the cytosol can then be recruited to kinetochore-bound Mad1-C-Mad2. C-Mad2 within the Mad1-C-Mad2 core complex acts as a prion-like template, catalysing the conversion of additional O-Mad2 proteins to the closed conformation and in doing so binding Cdc20.","predictedComplex":false,"interactors":[{"ac":"EBI-742610","identifier":"Q9Y6D9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6D9/entry","name":"MAD1L1","description":"Mitotic spindle assembly checkpoint protein MAD1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23168","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-78203","identifier":"Q13257","identifierLink":"https://www.uniprot.org/uniprotkb/Q13257/entry","name":"MAD2L1","description":"Mitotic spindle assembly checkpoint protein MAD2A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-87","complexName":"Mitotic spindle assembly checkpoint Mad1-Mad2 complex","organismName":"Mus musculus; 10090","description":"Acts at the spindle checkpoint, in a surveillance mechanism that mediates a delay in the onset of anaphase, until all chromosomes are properly attached to the mitotic or meiotic spindle.  Inhibits Cdc20, the mitotic co-activator of the anaphase-promoting complex/cyclosome (APC/C), an E3 ubiquitin ligase. Mad2 adopts two distinct conformations; when unbound, it adopts an open conformation (O-Mad2) but upon binding to Mad1, the Mad2 C-terminal tail crosses the entire surface of the beta-sheet and locks Mad1. Upon mitotic entry, the Mad1-C-Mad2 core complex is recruited to kinetochores. Because Mad2 can dimerise, O-Mad2 from the cytosol can then be recruited to kinetochore-bound Mad1-C-Mad2. C-Mad2 within the Mad1-C-Mad2 core complex acts as a prion-like template, catalysing the conversion of additional O-Mad2 proteins to the closed conformation and in doing so binding Cdc20.","predictedComplex":false,"interactors":[{"ac":"EBI-2552918","identifier":"Q9Z1B5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z1B5/entry","name":"Mad2l1","description":"Mitotic spindle assembly checkpoint protein MAD2A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4285225","identifier":"Q9WTX8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WTX8/entry","name":"Mad1l1","description":"Mitotic spindle assembly checkpoint protein MAD1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23168","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-86","complexName":"Beta-catenin-ICAT complex","organismName":"Mus musculus; 10090","description":"Transcription factor complex that inhibits binding of Tcf to beta-catenin while preserving interaction of catenin with cadherin thus inhibiting transcription mediated by beta-catenin-Tcf complex.","predictedComplex":false,"interactors":[{"ac":"EBI-397872","identifier":"Q02248","identifierLink":"https://www.uniprot.org/uniprotkb/Q02248/entry","name":"Ctnnb1","description":"Catenin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45976","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7338912","identifier":"Q9JJN6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JJN6/entry","name":"Ctnnbip1","description":"Beta-catenin-interacting protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR47142","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-88","complexName":"Mitotic spindle assembly checkpoint complex MAD2","organismName":"Homo sapiens; 9606","description":"The Spindle Assembly complex ensures accurate chromosome segregation by delaying anaphase entry by inhibiting Cdc20, the mitotic co-activator of the anaphase-promoting complex/cyclosome (APC/C), an E3 ubiquitin ligase. Mad2 adopts two distinct conformations; when unbound, it adopts an open conformation (O-Mad2) but upon binding to Mad1, the Mad2 C‐terminal tail crosses the entire surface of the beta‐sheet and locks Mad1. Upon mitotic entry, the Mad1–C-Mad2 core complex is recruited to kinetochores. Because Mad2 can dimerise, O-Mad2 from the cytosol can then be recruited to kinetochore-bound Mad1–C-Mad2. C-Mad2 within the Mad1–C-Mad2 core complex acts as a prion-like template, catalysing the conversion of additional O-Mad2 proteins to the closed conformation and in doing so binding Cdc20.","predictedComplex":false,"interactors":[{"ac":"EBI-78203","identifier":"Q13257","identifierLink":"https://www.uniprot.org/uniprotkb/Q13257/entry","name":"MAD2L1","description":"Mitotic spindle assembly checkpoint protein MAD2A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-89","complexName":"CCAAT-binding factor complex","organismName":"Mus musculus; 10090","description":"Transcription factor which binds to the CCAAT box, which occurs in 30% of eukaryotic promoters and appears to be crucial for promoter activity. May also play a role in histone methylations and some acetylations through recruitment of relevant enzymes to active promoters.","predictedComplex":false,"interactors":[{"ac":"EBI-10705668","identifier":"P63139","identifierLink":"https://www.uniprot.org/uniprotkb/P63139/entry","name":"Nfyb","description":"Nuclear transcription factor Y subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11064","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3043934","identifier":"P70353","identifierLink":"https://www.uniprot.org/uniprotkb/P70353/entry","name":"Nfyc","description":"Nuclear transcription factor Y subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10252","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-862337","identifier":"P23708","identifierLink":"https://www.uniprot.org/uniprotkb/P23708/entry","name":"Nfya","description":"Nuclear transcription factor Y subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12632","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-90","complexName":"Mitotic spindle assembly checkpoint complex MAD2","organismName":"Mus musculus; 10090","description":"The Spindle Assembly complex ensures accurate chromosome segregation by delaying anaphase entry by inhibiting Cdc20, the mitotic co-activator of the anaphase-promoting complex/cyclosome (APC/C), an E3 ubiquitin ligase. Mad2 adopts two distinct conformations; when unbound, it adopts an open conformation (O-Mad2) but upon binding to Mad1, the Mad2 C‐terminal tail crosses the entire surface of the beta‐sheet and locks Mad1. Upon mitotic entry, the Mad1-C-Mad2 core complex is recruited to kinetochores. Because Mad2 can dimerise, O-Mad2 from the cytosol can then be recruited to kinetochore-bound Mad1-C-Mad2. C-Mad2 within the Mad1-C-Mad2 core complex acts as a prion-like template, catalysing the conversion of additional O-Mad2 proteins to the closed conformation and in doing so binding Cdc20","predictedComplex":false,"interactors":[{"ac":"EBI-2552918","identifier":"Q9Z1B5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z1B5/entry","name":"Mad2l1","description":"Mitotic spindle assembly checkpoint protein MAD2A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-91","complexName":"MYC-MAX transcriptional activator complex","organismName":"Homo sapiens; 9606","description":"Proto-oncogenic transcriptional activator recognizing E box hexanucleotides containing the DNA consensus sequence CACGTG within gene promoters. The MYC-MAX heterodimer upregulates gene transcription by interaction with TATA binding protein (TBP, P20226), which in turn upregulates RNA polymerase transcription of the gene. Role in cellular proliferation and division.","predictedComplex":false,"interactors":[{"ac":"EBI-447544","identifier":"P01106","identifierLink":"https://www.uniprot.org/uniprotkb/P01106/entry","name":"MYC","description":"Myc proto-oncogene protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45851","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-751711","identifier":"P61244","identifierLink":"https://www.uniprot.org/uniprotkb/P61244/entry","name":"MAX","description":"Protein max","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10328","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-92","complexName":"Galectin-1 complex","organismName":"Homo sapiens; 9606","description":"Galectin-1 complex binds a wide array of complex carbohydrates and takes part in several key cellular processes such as growth regulation, adhesion of cells, and release of mediator. It is a potential target of glycomimetics such as glycoclusters.","predictedComplex":false,"interactors":[{"ac":"EBI-1048875","identifier":"P09382","identifierLink":"https://www.uniprot.org/uniprotkb/P09382/entry","name":"LGALS1","description":"Galectin-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-93","complexName":"MutS DNA mismatch repair complex","organismName":"Escherichia coli (strain K12); 83333","description":"Mismatch repair complex, involved in the recognition and repair of base-base and small insertion/deletion mismatches that appear as a consequence of DNA polymerase errors during replication or homologous recombination. Strand recognition necessary for removal of DNA biosynthetic errors from the daughter strand is based on the transient absence of d(GATC) methylation in the newly synthesized DNA strand (hemimethylation). Repair is initiated by the binding of mutS to a mismatch or to a small insertion-deletion loop.","predictedComplex":false,"interactors":[{"ac":"EBI-554920","identifier":"P23909","identifierLink":"https://www.uniprot.org/uniprotkb/P23909/entry","name":"mutS","description":"DNA mismatch repair protein MutS","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11361","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-94","complexName":"Galectin-1 complex","organismName":"Mus musculus; 10090","description":"Galectin-1 complex binds a wide array of complex carbohydrates and takes part in several key cellular processes such as growth regulation, adhesion of cells, and release of mediator. High expression increases tumour survival and metastasis. Contributes to intestinal inflammation suppression by induction of apoptosis in activated T cells. It is a potential target of glycomimetics such as glycoclusters.","predictedComplex":false,"interactors":[{"ac":"EBI-1634185","identifier":"P16045","identifierLink":"https://www.uniprot.org/uniprotkb/P16045/entry","name":"Lgals1","description":"Galectin-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-95","complexName":"Galectin-2 complex","organismName":"Homo sapiens; 9606","description":"Sugar-binding protein complex specific for lactose and lactose related saccharides. Plays role in cell-cell and cell-matrix interactions based on sugar recognition. Induces apoptosis of mucosal T cells thus ameliorating intestinal inflammation.","predictedComplex":false,"interactors":[{"ac":"EBI-7181544","identifier":"P05162","identifierLink":"https://www.uniprot.org/uniprotkb/P05162/entry","name":"LGALS2","description":"Galectin-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-96","complexName":"Galectin-2 complex","organismName":"Mus musculus; 10090","description":"Sugar-binding protein complex specific for lactose and lactose related saccharides. Plays role in cell-cell and cell-matrix interactions based on sugar recognition. Induces apoptosis of mucosal T cells thus ameliorating intestinal inflammation.","predictedComplex":false,"interactors":[{"ac":"EBI-1184048","identifier":"Q9CQW5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQW5/entry","name":"Lgals2","description":"Galectin-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-97","complexName":"Myc-Max transcriptional activator complex","organismName":"Mus musculus; 10090","description":"Proto-oncogenic transcriptional activator recognizing E box hexanucleotide. E-boxes contain the DNA consensus sequence CACGTG3 and are located within gene promoters. The Myc-Max heterodimer upregulates gene transcriptions by interaction with\r\nTATA binding protein (TBP, P29037), which in turn upregulates RNA\r\npolymerase transcription of the gene. Role in cellular proliferation and division.","predictedComplex":false,"interactors":[{"ac":"EBI-1183003","identifier":"P28574","identifierLink":"https://www.uniprot.org/uniprotkb/P28574/entry","name":"Max","description":"Protein max","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10328","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1183114","identifier":"P01108","identifierLink":"https://www.uniprot.org/uniprotkb/P01108/entry","name":"Myc","description":"Myc proto-oncogene protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45851","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-98","complexName":"Cathepsin-B - cystatin-A complex","organismName":"Homo sapiens; 9606","description":"Complex of cathepsin-B with its inhibitor cystatin-A. Cystatin displaces the occluding loop in the catalytic cleft thus inhibiting the enzyme's peptidase activity.","predictedComplex":false,"interactors":[{"ac":"EBI-715062","identifier":"P07858","identifierLink":"https://www.uniprot.org/uniprotkb/P07858/entry","name":"CTSB","description":"Cathepsin B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724303","identifier":"P01040","identifierLink":"https://www.uniprot.org/uniprotkb/P01040/entry","name":"CSTA","description":"Cystatin-A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11414","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-99","complexName":"Beta-catenin destruction core complex, APC2-AXIN1-GSK3B variant","organismName":"Homo sapiens; 9606","description":"Phosphorylates cytoplasmic beta-catenin (CTNNB1, P35222) in the absence of WNT-signalling, thus positively controlling its continuous proteasome-mediated degradation. CSNK1A1 phosphorylates CTNNB1 on Ser-45 and primes successive phosphorylation of Thr-41, Ser-37, and Ser-33 by GSK3. Phosphorylation of CTNNB1 promotes its subsequent ubiquitination which targets the protein for degradation by the proteasome.  Without WNT, Axin is also phosphorylated by GSK3, and thereby kept in an active, open conformation for beta-catenin binding and degradation. Upon WNT stimulation, the  ternary WNT-FZ-LRP6 complex is formed, recruits the scaffold protein DVL and the beta-catenin destruction complex. As a result, GSK3 is inhibited, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activation of WNT responsive genes.","predictedComplex":false,"interactors":[{"ac":"EBI-1053045","identifier":"O95996","identifierLink":"https://www.uniprot.org/uniprotkb/O95996/entry","name":"APC2","description":"Adenomatous polyposis coli protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1383726","identifier":"P48729","identifierLink":"https://www.uniprot.org/uniprotkb/P48729/entry","name":"CSNK1A1","description":"Casein kinase I isoform alpha","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11909","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373586","identifier":"P49841","identifierLink":"https://www.uniprot.org/uniprotkb/P49841/entry","name":"GSK3B","description":"Glycogen synthase kinase-3 beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-710484","identifier":"O15169","identifierLink":"https://www.uniprot.org/uniprotkb/O15169/entry","name":"AXIN1","description":"Axin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-100","complexName":"Cathepsin-B - cystatin-A complex","organismName":"Mus musculus; 10090","description":"Complex of cathepsin-B with its inhibitor cystatin-A. Cystatin displaces the occluding loop in the catalytic cleft thus inhibiting the enzyme's peptidase activity.","predictedComplex":false,"interactors":[{"ac":"EBI-10711336","identifier":"P56567","identifierLink":"https://www.uniprot.org/uniprotkb/P56567/entry","name":"Csta","description":"Cystatin-A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11414","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2924871","identifier":"P10605","identifierLink":"https://www.uniprot.org/uniprotkb/P10605/entry","name":"Ctsb","description":"Cathepsin B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-101","complexName":"Titin-Telethonin complex","organismName":"Homo sapiens; 9606","description":"The complex between the N-terminus of the giant sarcomeric filament protein titin with the Z-disk ligand, telethonin is believed to anchor titin in the Z-disk of the skeletal and cardiac sarcomere. The extensive interactions between the two proteins indicate that Telethonin provides a 'bridge' that anchors the ends of two different Titin molecules to the Z disk. There is evidence that Telethonin binding to Titin might be essential for the initial assembly, stabilization and functional integrity of the Titin filament and hence important for muscle contraction relaxation in mature myofibrils.","predictedComplex":false,"interactors":[{"ac":"EBI-681210","identifier":"Q8WZ42","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WZ42/entry","name":"TTN","description":"Titin","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13817","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-954089","identifier":"O15273","identifierLink":"https://www.uniprot.org/uniprotkb/O15273/entry","name":"TCAP","description":"Telethonin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15143","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-102","complexName":"DAPK1 - calmodulin complex","organismName":"Homo sapiens; 9606","description":"A serine/threonine protein kinase complex involved in cell survival, apoptosis and autophagic cell death pathways. DAPK1 is activated by dephosphorylation of Ser-308 and calcium-calmodulin binding. Complex activity is regulated via various phosphorylation sites, two of which (Ser-298 and Ser-308) are located on the autoregulatory domain (ARD) of DAPK1.","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-358616","identifier":"P53355","identifierLink":"https://www.uniprot.org/uniprotkb/P53355/entry","name":"DAPK1","description":"Death-associated protein kinase 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24342","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397435","identifier":"P62158","identifierLink":"https://www.uniprot.org/uniprotkb/P62158/entry","name":"calm_human","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-103","complexName":"Beta-catenin destruction core complex, Apc-Axin1-Gsk3b variant","organismName":"Mus musculus; 10090","description":"Phosphorylates cytoplasmic beta-catenin (Ctnnb1, Q02248) in the absence of WNT-signalling, thus positively controlling its continuous proteasome-mediated degradation. Csnk1a1 phosphorylates Ctnnb1 on Ser-45 and primes successive phosphorylation of Thr-41, Ser-37, and Ser-33 by GSK3. Phosphorylation of Ctnnb1 promotes its subsequent ubiquitination which targets the protein for degradation by the proteasome.  Without Wnt, Axin is also phosphorylated by GSK3, and thereby kept in an active, open conformation for beta-catenin binding and degradation. Upon Wnt stimulation, the  ternary Wnt-Fz-Lrp6 complex is formed and recruits the scaffold protein Dvl and the beta-catenin destruction complex. As a result, GSK3 is inhibited, Ctnnb1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the Tcf/Lef family, leading to activation of Wnt responsive genes.","predictedComplex":false,"interactors":[{"ac":"EBI-2365912","identifier":"O35625","identifierLink":"https://www.uniprot.org/uniprotkb/O35625/entry","name":"Axin1","description":"Axin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-400793","identifier":"Q9WV60","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WV60/entry","name":"Gsk3b","description":"Glycogen synthase kinase-3 beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-771679","identifier":"Q8BK63","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BK63/entry","name":"Csnk1a1","description":"Casein kinase I isoform alpha","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11909","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7848277","identifier":"Q61315","identifierLink":"https://www.uniprot.org/uniprotkb/Q61315/entry","name":"Apc","description":"Adenomatous polyposis coli protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-104","complexName":"MAD-MAX transcriptional repressor complex","organismName":"Homo sapiens; 9606","description":"Transcriptional repressor which recognizes an E box hexanucleotide DNA consensus sequence 5'-CACGTG-3'  located within gene promoters. Antagonises transcriptional activation by MYC family members by competing for available MAX to form heterodimers, competiing with other heterodimers for E-box-binding sites, and also potentially directly repressing bound genes. MXD family members contain a short conserved amino acid sequence, which directly interacts with the SIN3A (CPX-3321.CPX-3323) or SIN3B (CPX-3322) histone deacetylase co-repressor complexes which mediate gene silencing.","predictedComplex":false,"interactors":[{"ac":"EBI-751711","identifier":"P61244","identifierLink":"https://www.uniprot.org/uniprotkb/P61244/entry","name":"MAX","description":"Protein max","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10328","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8833637","identifier":"Q05195","identifierLink":"https://www.uniprot.org/uniprotkb/Q05195/entry","name":"MXD1","description":"Max dimerization protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11969","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-105","complexName":"Mad-Max transcriptional repressor complex","organismName":"Mus musculus; 10090","description":"Transcriptional repressor which recognizes an E box hexanucleotide DNA consensus sequence 5'-CACGTG-3'  located within gene promoters. \r\nMXD family members  contain a short conserved amino acid sequence, which directly interacts with the SIN3A (CPX-3443.CPX-3441) or SIN3B (CPX-3444) histone deacetylase co-repressor complexes which mediate gene silencing.","predictedComplex":false,"interactors":[{"ac":"EBI-10713354","identifier":"P50538","identifierLink":"https://www.uniprot.org/uniprotkb/P50538/entry","name":"Mxd1","description":"Max dimerization protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11969","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1183003","identifier":"P28574","identifierLink":"https://www.uniprot.org/uniprotkb/P28574/entry","name":"Max","description":"Protein max","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10328","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-106","complexName":"DAPK1 - calmodulin complex","organismName":"Mus musculus; 10090","description":"Serine/threonine protein kinase associated with cell survival, apoptosis and autophagic cell death pathways. DAPK2 is activated by dephosphorylation of Ser-308 and calcium-calmodulin binding. Complex activity is regulated via various phosphorylation sites, two of which (Ser-298 and Ser-308) are located on the autoregulatory domain (ARD) of DAPK2.","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2584874","identifier":"Q80YE7","identifierLink":"https://www.uniprot.org/uniprotkb/Q80YE7/entry","name":"Dapk1","description":"Death-associated protein kinase 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24342","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397460","identifier":"P62204","identifierLink":"https://www.uniprot.org/uniprotkb/P62204/entry","name":"Calm1","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-107","complexName":"Beta-catenin destruction core complex, APC-AXIN1-GSK3A variant","organismName":"Homo sapiens; 9606","description":"Phosphorylates cytoplasmic beta-catenin (CTNNB1) by CSNK1A1 and glycogen synthase kinase 3 (GSK3) in the absence of WNT-signalling, thus positively controlling its continuous proteasome-mediated degradation. CSNK1A1 phosphorylates CTNNB1 on Ser-45 and primes successive phosphorylation of Thr-41, Ser-37, and Ser-33 by GSK3. Phosphorylation of CTNNB1 promotes its subsequent ubiquitination which targets the protein for degradation by the proteasome.  Without WNT, Axin is also phosphorylated by GSK3, and thereby kept in an active (‘open’) conformation for beta-catenin binding and degradation. Upon WNT stimulation, the  ternary WNT-FZ-LRP6 complex is formed and recruits the scaffold protein DVL and the beta-catenin destruction complex. As a result, GSK3 is inhibited, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activation of WNT responsive genes.\r\n\r\nGSK3A is normally excluded from the nucleus and appears to only accumulate there, and regulate CTNNB1 levels, following activation of calpain in response to calcium levels.","predictedComplex":false,"interactors":[{"ac":"EBI-1044067","identifier":"P49840","identifierLink":"https://www.uniprot.org/uniprotkb/P49840/entry","name":"GSK3A","description":"Glycogen synthase kinase-3 alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1383726","identifier":"P48729","identifierLink":"https://www.uniprot.org/uniprotkb/P48729/entry","name":"CSNK1A1","description":"Casein kinase I isoform alpha","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11909","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-710484","identifier":"O15169","identifierLink":"https://www.uniprot.org/uniprotkb/O15169/entry","name":"AXIN1","description":"Axin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727707","identifier":"P25054","identifierLink":"https://www.uniprot.org/uniprotkb/P25054/entry","name":"APC","description":"Adenomatous polyposis coli protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-108","complexName":"Nuclear export complex Frat1-Gsk3b","organismName":"Mus musculus; 10090","description":"Role in beta-catenin destruction complex disassembly. Gsk3b-Frat1 cannot bind to Axin and thus Gsk3b is inhibited from participating in the Axin-dependent phosphorylation of Ctnnb1. Initially forms a quaternary Frat1-Dvl-Gsk3b-AXIN complex which dissociates, with Gsk3b maintaining its association with Frat1. Gsk3b-Frat1 then translocates from the nucleus to the cytoplasm. The binding of Frat1 does not inhibit Gsk3b from phosphorylating glycogen synthase.","predictedComplex":false,"interactors":[{"ac":"EBI-10714242","identifier":"P70339","identifierLink":"https://www.uniprot.org/uniprotkb/P70339/entry","name":"Frat1","description":"Proto-oncogene FRAT1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR35154","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-400793","identifier":"Q9WV60","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WV60/entry","name":"Gsk3b","description":"Glycogen synthase kinase-3 beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-109","complexName":"Beta-catenin destruction core complex, APC-AXIN1-GSK3B variant","organismName":"Homo sapiens; 9606","description":"Phosphorylates cytoplasmic beta-catenin (CTNNB1, P35222) in the absence of WNT-signalling, thus positively controlling its continuous proteasome-mediated degradation. CSNK1A1 phosphorylates CTNNB1 on Ser-45 and primes successive phosphorylation of Thr-41, Ser-37, and Ser-33 by GSK3. Phosphorylation of CTNNB1 promotes its subsequent ubiquitination which targets the protein for degradation by the proteasome.  Without Wnt, Axin is also phosphorylated by GSK3, and thereby kept in an active, open conformation for beta-catenin binding and degradation. Upon Wnt stimulation, the  ternary WNT-FZ-LRP6 complex is formed, recruits the scaffold protein DVL and the beta-catenin destruction complex. As a result, GSK3 is inhibited, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activation of Wnt responsive genes.","predictedComplex":false,"interactors":[{"ac":"EBI-1383726","identifier":"P48729","identifierLink":"https://www.uniprot.org/uniprotkb/P48729/entry","name":"CSNK1A1","description":"Casein kinase I isoform alpha","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11909","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373586","identifier":"P49841","identifierLink":"https://www.uniprot.org/uniprotkb/P49841/entry","name":"GSK3B","description":"Glycogen synthase kinase-3 beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-710484","identifier":"O15169","identifierLink":"https://www.uniprot.org/uniprotkb/O15169/entry","name":"AXIN1","description":"Axin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727707","identifier":"P25054","identifierLink":"https://www.uniprot.org/uniprotkb/P25054/entry","name":"APC","description":"Adenomatous polyposis coli protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-110","complexName":"Nuclear export complex Frat2-Gsk3b","organismName":"Mus musculus; 10090","description":"Role in beta-catenin destruction complex disassembly. Gsk3b-Frat2 cannot bind to Axin and thus Gsk3b is inhibited from participating in the Axin-dependent phosphorylation of Ctnnb1. Initially forms a quaternary Frat2-Dvl-Gsk3b-AXIN complex which dissociates, with Gsk3b maintaining its association with Frat2. Gsk3b-Frat2 then translocates from the nucleus to the cytoplasm. The binding of Frat2 does not inhibit Gsk3b from phosphorylating glycogen synthase.","predictedComplex":false,"interactors":[{"ac":"EBI-11789326","identifier":"Q8K025","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K025/entry","name":"Frat2","description":"GSK-3-binding protein FRAT2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR35154","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-400793","identifier":"Q9WV60","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WV60/entry","name":"Gsk3b","description":"Glycogen synthase kinase-3 beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-111","complexName":"Survivin homodimer complex","organismName":"Homo sapiens; 9606","description":"An anti-apoptotic pre-assembly complex that provides one protomer to the chromosomal passenger complex (CPC). Survivin cycles through alternating monomer-dimer states that are capably of diverse functions.","predictedComplex":false,"interactors":[{"ac":"EBI-518823","identifier":"O15392","identifierLink":"https://www.uniprot.org/uniprotkb/O15392/entry","name":"BIRC5","description":"Baculoviral IAP repeat-containing protein 5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46771","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-112","complexName":"LSM1-7-PAT1 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Lsm1-7-Pat1 is a complex conserved in all eukaryotes. It is an important part of cytoplasmic mRNA degradation. It preferentially binds oligo-adenylated (but not poly-A) mRNAs at their 3' end and promotes decapping at the 5' end thereby directing the mRNA for degradation through the 5' to 3' pathway.  Lsm1-7-Pat1 complex might also be involved in protein-protein recognition in the nucleus in the context of the nuclear Lsm2-8 complex (CPX-44).","predictedComplex":false,"interactors":[{"ac":"EBI-10227","identifier":"P57743","identifierLink":"https://www.uniprot.org/uniprotkb/P57743/entry","name":"LSM3","description":"LSM complex subunit LSM3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13110","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10236","identifier":"P40089","identifierLink":"https://www.uniprot.org/uniprotkb/P40089/entry","name":"LSM5","description":"LSM complex subunit LSM5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR20971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-141","identifier":"P53905","identifierLink":"https://www.uniprot.org/uniprotkb/P53905/entry","name":"LSM7","description":"LSM complex subunit LSM7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-174","identifier":"P47017","identifierLink":"https://www.uniprot.org/uniprotkb/P47017/entry","name":"LSM1","description":"LSM1-LSM7 complex subunit LSM1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-180","identifier":"P38203","identifierLink":"https://www.uniprot.org/uniprotkb/P38203/entry","name":"LSM2","description":"LSM complex subunit LSM2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-188","identifier":"P40070","identifierLink":"https://www.uniprot.org/uniprotkb/P40070/entry","name":"LSM4","description":"LSM complex subunit LSM4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-196","identifier":"Q06406","identifierLink":"https://www.uniprot.org/uniprotkb/Q06406/entry","name":"LSM6","description":"LSM complex subunit LSM6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-204","identifier":"P25644","identifierLink":"https://www.uniprot.org/uniprotkb/P25644/entry","name":"PAT1","description":"Deadenylation-dependent mRNA-decapping factor PAT1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21551","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-113","complexName":"Survivin homodimer complex","organismName":"Mus musculus; 10090","description":"An anti-apoptotic pre-assembly complex that provides one protomer to the chromosomal passenger complex (CPC). Survivin cycles through alternating monomer-dimer states that are capably of diverse functions.","predictedComplex":false,"interactors":[{"ac":"EBI-10713673","identifier":"O70201","identifierLink":"https://www.uniprot.org/uniprotkb/O70201/entry","name":"Birc5","description":"Baculoviral IAP repeat-containing protein 5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-114","complexName":"Glycoprotein Ib-IX-V complex","organismName":"Homo sapiens; 9606","description":"Serves as a receptor for many proteins involved in hemostasis and thrombosis, such as von Willebrand factor (VWF). Through its interaction with VWF immobilized at the damaged blood vessel wall, the GPIb-IX-V complex mediates the initial tethering and rolling of circulating platelets to the injury site. The rolling reduces platelet velocity and prolongs the contact time with components of the cell matrix, facilitating platelet activation and subsequent integrin-mediated firm attachment. Ligation of VWF to the complex sends an activating signal into the platelet, which helps to activate platelet integrin alphaIIb-beta3 (CPX-1799), and induces calcium mobilization, the rearrangement of the cytoskeleton, granule release and platelet aggregation.","predictedComplex":false,"interactors":[{"ac":"EBI-10891395","identifier":"P40197","identifierLink":"https://www.uniprot.org/uniprotkb/P40197/entry","name":"GP5","description":"Platelet glycoprotein V","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45617","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1754109","identifier":"P14770","identifierLink":"https://www.uniprot.org/uniprotkb/P14770/entry","name":"GP9","description":"Platelet glycoprotein IX","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22650","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2833037","identifier":"P13224","identifierLink":"https://www.uniprot.org/uniprotkb/P13224/entry","name":"GP1BB","description":"Platelet glycoprotein Ib beta chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22650","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-297082","identifier":"P07359","identifierLink":"https://www.uniprot.org/uniprotkb/P07359/entry","name":"GP1BA","description":"Platelet glycoprotein Ib alpha chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24373","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-115","complexName":"Glycoprotein Ib-IX-V complex","organismName":"Mus musculus; 10090","description":"Serves as a receptor for many proteins involved in hemostasis and thrombosis, such as von Willebrand factor (VWF). Through its interaction with VWF immobilized at the damaged blood vessel wall, the GP Ib-IX-V complex mediates the initial tethering and rolling of circulating platelets to the injury site. The rolling reduces platelet velocity and prolongs the contact time with components of the cell matrix, facilitating platelet activation and subsequent integrin-mediated firm attachment. Ligation of VWF to the complex sends an activating signal into the platelet, which helps to activate platelet integrin alphaIIb-beta3 (CPX-1799), and induces calcium mobilization, the rearrangement of the cytoskeleton, granule release and platelet aggregation.","predictedComplex":false,"interactors":[{"ac":"EBI-10728095","identifier":"O35930","identifierLink":"https://www.uniprot.org/uniprotkb/O35930/entry","name":"Gp1ba","description":"Platelet glycoprotein Ib alpha chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24373","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10892292","identifier":"P56400","identifierLink":"https://www.uniprot.org/uniprotkb/P56400/entry","name":"Gp1bb","description":"Platelet glycoprotein Ib beta chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22650","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10892309","identifier":"O88186","identifierLink":"https://www.uniprot.org/uniprotkb/O88186/entry","name":"Gp9","description":"Platelet glycoprotein IX","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22650","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10892327","identifier":"O08742","identifierLink":"https://www.uniprot.org/uniprotkb/O08742/entry","name":"Gp5","description":"Platelet glycoprotein V","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45617","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-116","complexName":"Chromosomal passenger complex, AURKB variant","organismName":"Homo sapiens; 9606","description":"Serine/threonine kinase complex which ensures chromosome bi-orientation on the mitotic spindle during metaphase by phosphorylating multiple kinetochore components. It destabilizes monopolar attachments by phosphorylating key proteins at the kinetophore. The chromosomal passenger complex (CPC) regulates chromosome segregation and cytokinesis. Disruption of any of its four members from the complex results in structural impairment and subsequent mislocalization of the CPC.","predictedComplex":false,"interactors":[{"ac":"EBI-307907","identifier":"Q9NQS7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NQS7/entry","name":"INCENP","description":"Inner centromere protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13142","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-518823","identifier":"O15392","identifierLink":"https://www.uniprot.org/uniprotkb/O15392/entry","name":"BIRC5","description":"Baculoviral IAP repeat-containing protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46771","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-624291","identifier":"Q96GD4","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GD4/entry","name":"AURKB","description":"Aurora kinase B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24350","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-979174","identifier":"Q53HL2","identifierLink":"https://www.uniprot.org/uniprotkb/Q53HL2/entry","name":"CDCA8","description":"Borealin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-117","complexName":"Glycoprotein Ib-IX-V-Filamin-A complex","organismName":"Homo sapiens; 9606","description":"The cytoplasmic domain of GPIBA of the GPIb-IX-V complex (CPX-114) binds to actin filaments through Filamin A. This may serve to anchor the complex and help it to withstand high shear stress and also enable communication with the actin cytoskeleton. The complex plays an important role in mediating the initial tethering and rolling of circulating platelets to a damaged blood vessel wall, for maintaining normal platelet integrity and shape and regulating platelet activation.","predictedComplex":false,"interactors":[{"ac":"EBI-10891395","identifier":"P40197","identifierLink":"https://www.uniprot.org/uniprotkb/P40197/entry","name":"GP5","description":"Platelet glycoprotein V","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45617","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1754109","identifier":"P14770","identifierLink":"https://www.uniprot.org/uniprotkb/P14770/entry","name":"GP9","description":"Platelet glycoprotein IX","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22650","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2833037","identifier":"P13224","identifierLink":"https://www.uniprot.org/uniprotkb/P13224/entry","name":"GP1BB","description":"Platelet glycoprotein Ib beta chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22650","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-297082","identifier":"P07359","identifierLink":"https://www.uniprot.org/uniprotkb/P07359/entry","name":"GP1BA","description":"Platelet glycoprotein Ib alpha chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24373","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350432","identifier":"P21333","identifierLink":"https://www.uniprot.org/uniprotkb/P21333/entry","name":"FLNA","description":"Filamin-A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR38537","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-118","complexName":"Glycoprotein Ib-IX-V-Filamin-A complex","organismName":"Mus musculus; 10090","description":"The cytoplasmic domain of GPIBA of the GPIb-IX-V complex (CPX-115) binds to actin filaments through Filamin A. This may serve to anchor the complex and help it to withstand high shear stress and also enable communication with the actin cytoskeleton. The complex plays an important role in mediating the initial tethering and rolling of circulating platelets to a damaged blood vessel wall, for maintaining normal platelet integrity and shape and regulating platelet activation.","predictedComplex":false,"interactors":[{"ac":"EBI-10728095","identifier":"O35930","identifierLink":"https://www.uniprot.org/uniprotkb/O35930/entry","name":"Gp1ba","description":"Platelet glycoprotein Ib alpha chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24373","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10892292","identifier":"P56400","identifierLink":"https://www.uniprot.org/uniprotkb/P56400/entry","name":"Gp1bb","description":"Platelet glycoprotein Ib beta chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22650","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10892309","identifier":"O88186","identifierLink":"https://www.uniprot.org/uniprotkb/O88186/entry","name":"Gp9","description":"Platelet glycoprotein IX","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22650","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10892327","identifier":"O08742","identifierLink":"https://www.uniprot.org/uniprotkb/O08742/entry","name":"Gp5","description":"Platelet glycoprotein V","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45617","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-641991","identifier":"Q8BTM8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BTM8/entry","name":"Flna","description":"Filamin-A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR38537","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-119","complexName":"Chromosomal passenger complex","organismName":"Mus musculus; 10090","description":"Serine/threonine kinase complex which ensures chromosome bi-orientation on the mitotic spindle during metaphase by phosphorylating multiple kinetochore components. It destabilizes monopolar attachments by phosphorylating key proteins at the kinetophore. The chromosomal passenger complex (CPC) regulates chromosome segregation and cytokinesis. Disruption of any of its four members from the complex results in structural impairment and subsequent mislocalization of the CPC.","predictedComplex":false,"interactors":[{"ac":"EBI-10713673","identifier":"O70201","identifierLink":"https://www.uniprot.org/uniprotkb/O70201/entry","name":"Birc5","description":"Baculoviral IAP repeat-containing protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2551837","identifier":"O70126","identifierLink":"https://www.uniprot.org/uniprotkb/O70126/entry","name":"Aurkb","description":"Aurora kinase B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24350","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2552254","identifier":"Q9WU62","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WU62/entry","name":"Incenp","description":"Inner centromere protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13142","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2552833","identifier":"Q8BHX3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BHX3/entry","name":"Cdca8","description":"Borealin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-120","complexName":"Prostatic acid phosphatase complex","organismName":"Homo sapiens; 9606","description":"Dephosphorylates orthophosphate monoesters and phosphorylated proteins, primaryly on tyrosine. Optimal activity in acidic environment (pH 4-6). Prediminantly expressed in and secreted from prostate but also found in many other tissues at lower concentration. TM-PAP splice variant is membrane bound. Modulates nociception at the dorsal root ganglia.","predictedComplex":false,"interactors":[{"ac":"EBI-10765575","identifier":"P15309-PRO_0000023963","identifierLink":"https://www.uniprot.org/uniprotkb/P15309-PRO_0000023963/entry","name":"ACP3","description":"Prostatic acid phosphatase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-121","complexName":"Prostatic acid phosphatase complex","organismName":"Mus musculus; 10090","description":"Dephosphorylates orthophosphate monoesters and phosphorylated proteins, primaryly on tyrosine. Optimal activity in acidic environment (pH 4-6). Prediminantly expressed in and secreted from prostate but also found in many other tissues at lower concentration. TM-PAP splice variant is membrane bound. Modulates nociception at the dorsal root ganglia.","predictedComplex":false,"interactors":[{"ac":"EBI-10765664","identifier":"Q8CE08-PRO_0000356293","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CE08-PRO_0000356293/entry","name":"Acp3","description":"Prostatic acid phosphatase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-122","complexName":"Filamin A homodimer","organismName":"Homo sapiens; 9606","description":"Homodimeric actin cross-linking proteins that organize the actin cytoskeleton and maintain extracellular matrix connections by anchoring actin filaments to transmembrane receptors. By cross-linking and anchoring actin filaments, filamins stabilize the plasma membrane, provide cellular cortical rigidity, and contribute to the mechanical stability of the plasma membrane and the cell cortex. FLNa-actin networks behave as weak elastic solids under low shear stress due to the flexible nature of actin-FLNa crosslinks, yet can support large shear stresses and have pronounced nonlinear strain-stiffening behaviors. High avidity binding to F-actin due to dimerization and multiple binding to F-actin through FLNa ABD and rod 1 confers strain-stiffening on actin networks. FLNa dimers also interact with transmembrane proteins, cytoskeletal proteins, and intracellular signaling proteins and are therefore  involved in stabilization and regulation of plasma membrane and intracellular signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-350432","identifier":"P21333","identifierLink":"https://www.uniprot.org/uniprotkb/P21333/entry","name":"FLNA","description":"Filamin-A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR38537","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-123","complexName":"Filamin A homodimer","organismName":"Mus musculus; 10090","description":"Homodimeric actin cross-linking proteins that organize the actin cytoskeleton and maintain extracellular matrix connections by anchoring actin filaments to transmembrane receptors. By cross-linking and anchoring actin filaments, filamins stabilize the plasma membrane, provide cellular cortical rigidity, and contribute to the mechanical stability of the plasma membrane and the cell cortex. FLNa-actin networks behave as weak elastic solids under low shear stress due to the flexible nature of actin-FLNa crosslinks, yet can support large shear stresses and have pronounced nonlinear strain-stiffening behaviors. High avidity binding to F-actin due to dimerization and multiple binding to F-actin through FLNa ABD and rod 1 confers strain-stiffening on actin networks. FLNa dimers also interact with transmembrane proteins, cytoskeletal proteins, and intracellular signaling proteins and are therefore  involved in stabilization and regulation of plasma membrane and intracellular signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-641991","identifier":"Q8BTM8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BTM8/entry","name":"Flna","description":"Filamin-A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR38537","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-124","complexName":"HIR histone chaperone complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Histone chaperone complex which promotes nucleosome assembly. Cooperates with the ASF1 (P32447) co-chaperone to deposit histone (H3/H4)2 tetramers on DNA for replication-independent chromatin assembly. Prevents SWI/SNF chromatin remodeling activity. Binds to and represses transcription of histone genes throughout the cell cycle, but does not repress transcription in G1/S phase.","predictedComplex":false,"interactors":[{"ac":"EBI-25715","identifier":"P47171","identifierLink":"https://www.uniprot.org/uniprotkb/P47171/entry","name":"HIR3","description":"Histone transcription regulator 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15502","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8316","identifier":"P32479","identifierLink":"https://www.uniprot.org/uniprotkb/P32479/entry","name":"HIR1","description":"Protein HIR1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13831","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8323","identifier":"P32480","identifierLink":"https://www.uniprot.org/uniprotkb/P32480/entry","name":"HIR2","description":"Protein HIR2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13831","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8520","identifier":"Q01448","identifierLink":"https://www.uniprot.org/uniprotkb/Q01448/entry","name":"HPC2","description":"Histone promoter control protein 2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-125","complexName":"Sodium:potassium-exchanging ATPase complex, FXYD2 variant","organismName":"Homo sapiens; 9606","description":"An ATPase-dependent transmembrane transport complex capable of generating electrochemical gradients by exchanging three intracellular sodium ions for two extracellular potassium ions during each cycle of ATP hydrolysis. Na+/K+ pumps can also generate an inward current of protons.  \r\n\r\nEach transport cycle comprises a sequence of conformational transitions that permit extracellular K+ ions to access the binding sites in phosphorylated pumps and cytoplasmic Na+ ions to access the sites after dephosphorylation . Binding of the third Na+ ion triggers autophosphorylation, and binding of the second K+ ion prompts auto-dephosphorylation. This coupling of alternating ion access to ATP hydrolysis ensures forward, energetically uphill, progress of the Na+/K+ transport cycle. The larger pumped Na+ efflux than K+ influx constitutes outward current, a direction tending to make the membrane potential more negative. However, because each step in the cycle is reversible , if the normally transported intracellular Na+ and extracellular K+ are both scarce, the cycle can run backward, thus synthesizing ATP and generating inward, depolarizing current. Variants containing ATP1A1-ATP1B1 appear to be most widely expressed.","predictedComplex":false,"interactors":[{"ac":"EBI-10765115","identifier":"P54710","identifierLink":"https://www.uniprot.org/uniprotkb/P54710/entry","name":"FXYD2","description":"Sodium/potassium-transporting ATPase subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14132","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358778","identifier":"P05023","identifierLink":"https://www.uniprot.org/uniprotkb/P05023/entry","name":"ATP1A1","description":"Sodium/potassium-transporting ATPase subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714630","identifier":"P05026","identifierLink":"https://www.uniprot.org/uniprotkb/P05026/entry","name":"ATP1B1","description":"Sodium/potassium-transporting ATPase subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11523","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-126","complexName":"Sodium:potassium-exchanging ATPase complex, FXYD2 variant","organismName":"Mus musculus; 10090","description":"An ATPase-dependent transmembrane transport complex capable of generating electrochemical gradients by exchanging three intracellular sodium ions for two extracellular potassium ions during each cycle of ATP hydrolysis. Na+/K+ pumps can also generate an inward current of protons.  \r\n\r\nEach transport cycle comprises a sequence of conformational transitions that permit extracellular K+ ions to access the binding sites in phosphorylated pumps and cytoplasmic Na+ ions to access the sites after dephosphorylation . Binding of the third Na+ ion triggers autophosphorylation, and binding of the second K+ ion prompts auto-dephosphorylation. This coupling of alternating ion access to ATP hydrolysis ensures forward, energetically uphill, progress of the Na+/K+ transport cycle. The larger pumped Na+ efflux than K+ influx constitutes outward current, a direction tending to make the membrane potential more negative. However, because each step in the cycle is reversible , if the normally transported intracellular Na+ and extracellular K+ are both scarce, the cycle can run backward, thus synthesizing ATP and generating inward, depolarizing current.","predictedComplex":false,"interactors":[{"ac":"EBI-10765152","identifier":"Q04646","identifierLink":"https://www.uniprot.org/uniprotkb/Q04646/entry","name":"Fxyd2","description":"Sodium/potassium-transporting ATPase subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14132","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-444536","identifier":"Q8VDN2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VDN2/entry","name":"Atp1a1","description":"Sodium/potassium-transporting ATPase subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR43294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-770851","identifier":"P14094","identifierLink":"https://www.uniprot.org/uniprotkb/P14094/entry","name":"Atp1b1","description":"Sodium/potassium-transporting ATPase subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11523","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-127","complexName":"Titin-Telethonin complex","organismName":"Mus musculus; 10090","description":"The complex between the N-terminus of the giant sarcomeric filament protein titin with the Z-disk ligand, telethonin  is believed to anchor titin in the Z-disk of the skeletal and cardiac sarcomere. The extensive interactions between the two proteins indicate that Telethonin provides a 'bridge' that anchors the ends of two different Titin molecules to the Z disk. There is evidence that Telethonin binding to Titin might be essential for the initial assembly, stabilization and functional integrity of the Titin filament and hence important for muscle contraction relaxation in mature myofibrils.","predictedComplex":false,"interactors":[{"ac":"EBI-10767826","identifier":"O70548","identifierLink":"https://www.uniprot.org/uniprotkb/O70548/entry","name":"Tcap","description":"Telethonin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15143","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9672947","identifier":"A2ASS6","identifierLink":"https://www.uniprot.org/uniprotkb/A2ASS6/entry","name":"Ttn","description":"Titin","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14340","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-128","complexName":"LDLR-PCSK9 complex","organismName":"Homo sapiens; 9606","description":"The formation of the LDLR-PCSK9 complex at neutral pH prevents a conformational change and normal recycling of the low density lipoprotein receptor LDLR following receptor internalization, instead directing LDLR to lysosomal degradation. This results in an increase in levels of low-density lipoprotein cholesterol  in peripheral blood","predictedComplex":false,"interactors":[{"ac":"EBI-10824267","identifier":"Q8NBP7-PRO_0000027120","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NBP7-PRO_0000027120/entry","name":"PCSK9","description":"","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-10824281","identifier":"Q8NBP7-PRO_0000027121","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NBP7-PRO_0000027121/entry","name":"PCSK9","description":"Proprotein convertase subtilisin/kexin type 9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-988319","identifier":"P01130","identifierLink":"https://www.uniprot.org/uniprotkb/P01130/entry","name":"LDLR","description":"Low-density lipoprotein receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24270","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-129","complexName":"LDLR-PCSK9 complex","organismName":"Mus musculus; 10090","description":"The formation of the LDLR- PCSK9 complex at neutral pH promotes degradation of the low density lipoprotein receptor (LDLR) component, the major clearance route of circulating cholesterol through the endosome/lysosome pathway. Consequently, a reduction in the internalisation of circulating low density lipoproteins (LDLs) occurs, leading to high plasma levels of LDLs, causing familial hypercholesterolemia type 3. \r\nFormation of the complex interferes with an acid-dependent conformational change of LDLR required for receptor recycling via the endosome. Instead, PCSK9 binding to LDLR can induce its ubiquitination leading to rerouteing of LDLR to the lysosome where it is degraded.","predictedComplex":false,"interactors":[{"ac":"EBI-10824479","identifier":"Q80W65-PRO_0000027122","identifierLink":"https://www.uniprot.org/uniprotkb/Q80W65-PRO_0000027122/entry","name":"Pcsk9","description":"","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-10824489","identifier":"Q80W65-PRO_0000027123","identifierLink":"https://www.uniprot.org/uniprotkb/Q80W65-PRO_0000027123/entry","name":"Pcsk9","description":"Proprotein convertase subtilisin/kexin type 9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-301050","identifier":"P35951","identifierLink":"https://www.uniprot.org/uniprotkb/P35951/entry","name":"Ldlr","description":"Low-density lipoprotein receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24270","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-130","complexName":"ANXA2-PCSK9 complex","organismName":"Homo sapiens; 9606","description":"The formation of the AnxA2-PCSK9 complex reduces the degradation of the LDLR (low density lipoprotein receptor, P01130), leading to increased clearance of LDLs (low density lipoproteins). The reduced levels of circulating LDLs in plasma could lead to protection from coronary heart disease and premature atherosclorosis. This activity opposes that of a closely related complex the LDLR-PCSK9 complex CPX-128.","predictedComplex":false,"interactors":[{"ac":"EBI-352622","identifier":"P07355","identifierLink":"https://www.uniprot.org/uniprotkb/P07355/entry","name":"ANXA2","description":"Annexin A2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10502","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7539251","identifier":"Q8NBP7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NBP7/entry","name":"PCSK9","description":"Proprotein convertase subtilisin/kexin type 9","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43806","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-131","complexName":"HCN4 channel complex","organismName":"Homo sapiens; 9606","description":"Hyperpolarization-activated cyclic nucleotide-gated (HCN) ion channel that is dually activated by hyperpolarization and binding of cAMP to their cyclic nucleotide binding domain (CNBD) thereby releasing the tonic inhibition exerted by the cytoplasmic CNBD on the channel pore. Exhibits weak selectivity for potassium over sodium ions and contributes to the native pacemaker currents in heart (If) and possibly in neurons (Ih). Together with HCN2 (Q9UL51, CPX-143), HCN4 is the dominant form of HCN expressed in the heart, especially in the sinoatrial node. \r\n\r\nContrary to other ion-gated channels, HCN channels do not require an accessory unit but depolarisation activity is affected by optional accessory proteins such as TRIP8b (PEX5L, Q8IYB4). \r\n\r\nMutations in the C-terminus containing the C-linker and CNBD domain, which affect the expression or function of the HCN4 channel, are known to cause arrhythmia or bradycardia or lipids such as phosphatidylinositol-4,5-biphosphate.","predictedComplex":false,"interactors":[{"ac":"EBI-1753521","identifier":"Q9Y3Q4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3Q4/entry","name":"HCN4","description":"Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45689","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-983884","identifier":"CHEBI:17489","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:17489","name":"3',5'-cyclic amp","description":"3',5'-cyclic AMP","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-132","complexName":"BAT3 complex","organismName":"Homo sapiens; 9606","description":"BAT3 complex is recruited to ribosomes synthesizing tail-anchored (TA) proteins or polypeptides bearing hydrophobic transmembrane domains (TMDs). BAT3 complex sequesters TA proteins into a soluble form which prevents aggregation or inappropriate interactions, thus facilitating their targeting through the cytosol to GET3. It acts during retrotranslocation as part of the transmembrane recognition complex (TRC) pathway, the mislocalized protein degradation pathway, and the ER-associated protein degradation (ERAD) pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-347552","identifier":"P46379","identifierLink":"https://www.uniprot.org/uniprotkb/P46379/entry","name":"BAG6","description":"Large proline-rich protein BAG6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15204","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356983","identifier":"P11441","identifierLink":"https://www.uniprot.org/uniprotkb/P11441/entry","name":"UBL4A","description":"Ubiquitin-like protein 4A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46555","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-711823","identifier":"Q7L5D6","identifierLink":"https://www.uniprot.org/uniprotkb/Q7L5D6/entry","name":"GET4","description":"Golgi to ER traffic protein 4 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12875","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-133","complexName":"BAT3 complex","organismName":"Mus musculus; 10090","description":"BAT3 complex is recruited to ribosomes synthesizing tail-anchored (TA) proteins or polypeptides bearing hydrophobic transmembrane domains (TMDs). BAT3 complex sequesters TA proteins into a soluble form which prevents aggregation or inappropriate interactions, thus facilitating their targeting through the cytosol to Get3. It acts during retrotranslocation as part of the transmembrane recognition complex (TRC) pathway, the mislocalized protein degradation pathway, and the ER-associated protein degradation (ERAD) pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-10815236","identifier":"Q9D1H7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D1H7/entry","name":"Get4","description":"Golgi to ER traffic protein 4 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12875","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10815268","identifier":"P21126","identifierLink":"https://www.uniprot.org/uniprotkb/P21126/entry","name":"Ubl4a","description":"Ubiquitin-like protein 4A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46555","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-644645","identifier":"Q9Z1R2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z1R2/entry","name":"Bag6","description":"Large proline-rich protein BAG6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15204","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-136","complexName":"Vcp-Npl4-Ufd1 AAA ATPase complex","organismName":"Mus musculus; 10090","description":"A type II AAA ATPase that is involved in the dislocation/extraction step of retrotranslocation of misfolded proteins from the endoplasmic reticulum (ER) into the cytosol where they are polyubiquitinated and degraded by the proteasome as part of the ER-associated protein degradation (ERAD) pathway. The AAA+ ATPase VCP is essential to a wide range of cellular functions which are regulated by ubiquitination, extracting its substrate proteins from cellular structures or multiprotein complexes in an ATP hydrolysis-dependent process. Substrate-recruiting components determine the specificity of each complex.","predictedComplex":false,"interactors":[{"ac":"EBI-10817650","identifier":"P60670","identifierLink":"https://www.uniprot.org/uniprotkb/P60670/entry","name":"Nploc4","description":"Nuclear protein localization protein 4 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12710","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7961331","identifier":"P70362","identifierLink":"https://www.uniprot.org/uniprotkb/P70362/entry","name":"Ufd1","description":"Ubiquitin recognition factor in ER-associated degradation protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12555","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-80597","identifier":"Q01853","identifierLink":"https://www.uniprot.org/uniprotkb/Q01853/entry","name":"Vcp","description":"Transitional endoplasmic reticulum ATPase","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-137","complexName":"VCP-NPL4-UFD1 AAA ATPase complex","organismName":"Homo sapiens; 9606","description":"A type II AAA ATPase that is involved in the dislocation/extraction step of retrotranslocation of misfolded proteins from the endoplasmic reticulum (ER) into the cytosol where they are polyubiquitinated and degraded by the proteasome as part of the ER-associated protein degradation (ERAD) pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-1994090","identifier":"Q92890","identifierLink":"https://www.uniprot.org/uniprotkb/Q92890/entry","name":"UFD1","description":"Ubiquitin recognition factor in ER-associated degradation protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12555","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1994109","identifier":"Q8TAT6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAT6/entry","name":"NPLOC4","description":"Nuclear protein localization protein 4 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12710","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355164","identifier":"P55072","identifierLink":"https://www.uniprot.org/uniprotkb/P55072/entry","name":"VCP","description":"Transitional endoplasmic reticulum ATPase","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-138","complexName":"Vcp-Npl4-Ufd1 AAA ATPase complex","organismName":"Rattus norvegicus; 10116","description":"A type II AAA ATPase that is involved in the dislocation/extraction step of retrotranslocation of misfolded proteins from the endoplasmic reticulum (ER) into the cytosol where they are polyubiquitinated and degraded by the proteasome as part of the ER-associated protein degradation (ERAD) pathway. The AAA+ ATPase Vcp is essential to a wide range of cellular functions which are regulated by ubiquitination, extracting its substrate proteins from cellular structures or multiprotein complexes in an ATP hydrolysis-dependent process. Substrate-recruiting components determine the specificity of each complex.","predictedComplex":false,"interactors":[{"ac":"EBI-1993990","identifier":"Q9ES54","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ES54/entry","name":"Nploc4","description":"Nuclear protein localization protein 4 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR12710","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-399011","identifier":"P46462","identifierLink":"https://www.uniprot.org/uniprotkb/P46462/entry","name":"Vcp","description":"Transitional endoplasmic reticulum ATPase","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-399031","identifier":"Q9ES53","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ES53/entry","name":"Ufd1","description":"Ubiquitin recognition factor in ER-associated degradation protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR12555","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-139","complexName":"HCN4 channel complex","organismName":"Mus musculus; 10090","description":"Hyperpolarization-activated cyclic nucleotide-gated (HCN) ion channel that is dually activated by hyperpolarization and binding of cAMP to their cyclic nucleotide binding domain (CNBD) thereby releasing the tonic inhibition exerted by the cytoplasmic CNBD on the channel pore. Exhibits weak selectivity for potassium over sodium ions and contributes to the native pacemaker currents in heart (If) and possibly in neurons (Ih). Together with HCN2 (O88703, CPX-142), HCN4 is the dominant form of HCN expressed in the heart, especially in the sinoatrial node. \r\n\r\nContrary to other ion-gated channels, HCN channels do not require an accessory unit but depolarisation activity is affected by optional accessory proteins such as TRIP8b (Pex5l, Q8C437) or lipids such as phosphatidylinositol-4,5-biphosphate.","predictedComplex":false,"interactors":[{"ac":"EBI-10820097","identifier":"O70507","identifierLink":"https://www.uniprot.org/uniprotkb/O70507/entry","name":"Hcn4","description":"Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45689","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-983884","identifier":"CHEBI:17489","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:17489","name":"3',5'-cyclic amp","description":"3',5'-cyclic AMP","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-140","complexName":"MICOS mitochondrial contact site and cristae organizing system complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"MICOS (MItochondrial contact site and Cristae Organizing System) is a mitochondrial inner membrane complex that extends into the intermembrane space and has a role in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane. The Mic60 subunit also has a role in import of inter-membrane space proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-21120","identifier":"P38341","identifierLink":"https://www.uniprot.org/uniprotkb/P38341/entry","name":"MIC12","description":"MICOS complex subunit MIC12","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-22936","identifier":"P43594","identifierLink":"https://www.uniprot.org/uniprotkb/P43594/entry","name":"MIC19","description":"MICOS complex subunit MIC19","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-23537","identifier":"P50087","identifierLink":"https://www.uniprot.org/uniprotkb/P50087/entry","name":"MIC26","description":"MICOS subunit MIC26","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28268","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27078","identifier":"P36112","identifierLink":"https://www.uniprot.org/uniprotkb/P36112/entry","name":"MIC60","description":"MICOS complex subunit MIC60","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15415","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28819","identifier":"P50945","identifierLink":"https://www.uniprot.org/uniprotkb/P50945/entry","name":"MIC27","description":"MICOS complex subunit MIC27","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-7486587","identifier":"Q96VH5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96VH5/entry","name":"MIC10","description":"MICOS complex subunit MIC10","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-141","complexName":"ANXA2-PCSK9 complex","organismName":"Mus musculus; 10090","description":"The formation of the AnxA2-PCSK9 complex reduces the degradation of the LDLR (low density lipoprotein receptor, P35951), leading to increased clearance of LDLs (low density lipoproteins) in plasma. This activity opposes that of a closely related complex the LDLR-PCSK9 complex CPX-129.","predictedComplex":false,"interactors":[{"ac":"EBI-10634657","identifier":"Q80W65","identifierLink":"https://www.uniprot.org/uniprotkb/Q80W65/entry","name":"Pcsk9","description":"Proprotein convertase subtilisin/kexin type 9","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR43806","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-738510","identifier":"P07356","identifierLink":"https://www.uniprot.org/uniprotkb/P07356/entry","name":"Anxa2","description":"Annexin A2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10502","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-142","complexName":"HCN2 channel complex","organismName":"Mus musculus; 10090","description":"Hyperpolarization-activated cyclic nucleotide-gated (HCN) ion channel that is dually activated by hyperpolarization and binding of cAMP to their cyclic nucleotide binding domain (CNBD) thereby releasing the tonic inhibition exerted by the cytoplasmic CNBD on the channel pore. Exhibits weak selectivity for potassium over sodium ions and contributes to the native pacemaker currents in heart (If) and in neurons (Ih). Together with HCN4 (O70507, CPX-139), HCN2 is the dominant form of HCN expressed in the heart. Produces a large instantaneous current. Modulated by intracellular chloride ions and pH; acidic pH shifts the activation to more negative voltages. \r\n\r\nContrary to other ion-gated channels, HCN channels do not require an accessory unit but depolarisation activity is affected by optional accessory proteins such as TRIP8b (Pex5l, Q8C437) or lipids such as phosphatidylinositol-4,5-biphosphate.","predictedComplex":false,"interactors":[{"ac":"EBI-771231","identifier":"O88703","identifierLink":"https://www.uniprot.org/uniprotkb/O88703/entry","name":"Hcn2","description":"Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45689","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-983884","identifier":"CHEBI:17489","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:17489","name":"3',5'-cyclic amp","description":"3',5'-cyclic AMP","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-143","complexName":"HCN2 channel complex","organismName":"Homo sapiens; 9606","description":"Hyperpolarization-activated cyclic nucleotide-gated (HCN) ion channel that is dually activated by hyperpolarization and binding of cAMP to their cyclic nucleotide binding domain (CNBD) thereby releasing the tonic inhibition exerted by the cytoplasmic CNBD on the channel pore. Exhibits weak selectivity for potassium over sodium ions and contributes to the native pacemaker currents in heart (If) and in neurons (Ih). Together with HCN4 (Q9Y3Q4, CPX-131), HCN2 is the dominant form of HCN expressed in the heart. Produces a large instantaneous current. Modulated by intracellular chloride ions and pH; acidic pH shifts the activation to more negative voltages. \r\n\r\nContrary to other ion-gated channels, HCN channels do not require an accessory unit but depolarisation activity is affected by optional accessory proteins such as TRIP8b (PEX5L, Q8IYB4) or lipids such as phosphatidylinositol-4,5-biphosphate.","predictedComplex":false,"interactors":[{"ac":"EBI-1751885","identifier":"Q9UL51","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UL51/entry","name":"HCN2","description":"Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45689","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-983884","identifier":"CHEBI:17489","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:17489","name":"3',5'-cyclic amp","description":"3',5'-cyclic AMP","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-144","complexName":"SMAD1 homotrimer","organismName":"Homo sapiens; 9606","description":"In the absence of Smad4, R-Smad phosphorylation results in homotrimerization, however, this complex does not appear to import into the nucleus and is assumed to be transcriptionally inactive.","predictedComplex":false,"interactors":[{"ac":"EBI-1567153","identifier":"Q15797","identifierLink":"https://www.uniprot.org/uniprotkb/Q15797/entry","name":"SMAD1","description":"Mothers against decapentaplegic homolog 1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13703","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-145","complexName":"Smad1 homotrimer","organismName":"Mus musculus; 10090","description":"In the absence of Smad4, R-Smad phosphorylation results in homotrimerization, however, this complex does not appear to import into the nucleus and is assumed to be transcriptionally inactive.","predictedComplex":false,"interactors":[{"ac":"EBI-6992047","identifier":"P70340","identifierLink":"https://www.uniprot.org/uniprotkb/P70340/entry","name":"Smad1","description":"Mothers against decapentaplegic homolog 1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13703","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-146","complexName":"SMAD1-SMAD4 complex","organismName":"Mus musculus; 10090","description":"A transcription factor complex which binds to the promoters of target genes and recruits co-activators and histone acetyltransferases, such as p300, CBP and P300/CBP-associated factor, facilitating transcription. In response to TGF-beta/activin-family protein binding, primarily  BMP (bone morphogenetic proteins), TGF-beta type II receptors phosphorylate TGF-beta type I receptors (ALK1, 2, 3 and 6) which in turn phosphorylates SMAD1 on Ser-463 and Ser-465. This enables binding to SMAD4 to form heteromeric SMAD complexes that enter the nucleus to initiate gene transcription.\r\nBecause of their relatively low DNA-binding affinity, SMAD complexes interact with a wide variety of DNA-binding proteins. Crosstalk with other signalling pathways and interaction with other DNA-binding cofactors define the specific binding patterns of SMADs; in addition, interaction with coactivators/corepressors modulates their transcriptional activity.","predictedComplex":false,"interactors":[{"ac":"EBI-5259270","identifier":"P97471","identifierLink":"https://www.uniprot.org/uniprotkb/P97471/entry","name":"Smad4","description":"Mothers against decapentaplegic homolog 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13703","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6992047","identifier":"P70340","identifierLink":"https://www.uniprot.org/uniprotkb/P70340/entry","name":"Smad1","description":"Mothers against decapentaplegic homolog 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13703","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-147","complexName":"GLI1-SUFU complex","organismName":"Mus musculus; 10090","description":"Transcriptional modulator complex, the formation of which regulates the activity of GLI transcription factors. Role as a negative regulator of the hedgehog-signalling network and plays a fundamental role in the control of development, cell proliferation and differentiation.","predictedComplex":false,"interactors":[{"ac":"EBI-3508336","identifier":"Q9Z0P7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0P7/entry","name":"Sufu","description":"Suppressor of fused homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10928","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3871446","identifier":"P47806","identifierLink":"https://www.uniprot.org/uniprotkb/P47806/entry","name":"Gli1","description":"Zinc finger protein GLI1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45718","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-148","complexName":"GLI2-SUFU complex","organismName":"Homo sapiens; 9606","description":"Transcriptional modulator complex, the formation of which regulates the activity of GLI transcription factors. Role as a negative regulator of the hedgehog-signalling network and plays a fundamental role in the control of development, cell proliferation and differentiation.","predictedComplex":false,"interactors":[{"ac":"EBI-10821567","identifier":"P10070","identifierLink":"https://www.uniprot.org/uniprotkb/P10070/entry","name":"GLI2","description":"Zinc finger protein GLI2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45718","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-740595","identifier":"Q9UMX1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UMX1/entry","name":"SUFU","description":"Suppressor of fused homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10928","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-149","complexName":"GLI2-SUFU complex","organismName":"Mus musculus; 10090","description":"Transcriptional modulator complex, the formation of which regulates the activity of GLI transcription factors. Role as a negative regulator of the hedgehog-signalling network and plays a fundamental role in the control of development, cell proliferation and differentiation.","predictedComplex":false,"interactors":[{"ac":"EBI-3508336","identifier":"Q9Z0P7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0P7/entry","name":"Sufu","description":"Suppressor of fused homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10928","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9344284","identifier":"Q0VGT2","identifierLink":"https://www.uniprot.org/uniprotkb/Q0VGT2/entry","name":"Gli2","description":"Zinc finger protein GLI2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45718","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-150","complexName":"GLI3-SUFU complex","organismName":"Homo sapiens; 9606","description":"Transcriptional modulator complex, the formation of which regulates the activity of GLI transcription factors. Role as a negative regulator of the hedgehog-signalling network and plays a fundamental role in the control of development, cell proliferation and differentiation.","predictedComplex":false,"interactors":[{"ac":"EBI-308055","identifier":"P10071","identifierLink":"https://www.uniprot.org/uniprotkb/P10071/entry","name":"GLI3","description":"Transcriptional activator GLI3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45718","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-740595","identifier":"Q9UMX1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UMX1/entry","name":"SUFU","description":"Suppressor of fused homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10928","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-151","complexName":"GLI3-SUFU complex","organismName":"Mus musculus; 10090","description":"Transcriptional modulator complex, the formation of which regulates the activity of GLI transcription factors. Role as a negative regulator of the hedgehog-signalling network and plays a fundamental role in the control of  development, cell proliferation and differentiation.","predictedComplex":false,"interactors":[{"ac":"EBI-10829058","identifier":"Q61602","identifierLink":"https://www.uniprot.org/uniprotkb/Q61602/entry","name":"Gli3","description":"Transcriptional activator GLI3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45718","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3508336","identifier":"Q9Z0P7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0P7/entry","name":"Sufu","description":"Suppressor of fused homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10928","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-152","complexName":"Shelterin complex","organismName":"Homo sapiens; 9606","description":"The Shelterin (Telosome) complex is a DNA-binding protein complex that associates with the telomeres that cap the ends of eukaryotic chromosomes and distinguishes them from sites of DNA damage thus sheltering chromosome ends from being inappropriately processed by the DNA repair machinery. Consequently it plays an essential role in maintaining telomere structure and integrity. Three subunits can interact directly either with single-stranded (POT1) or double-stranded telomeric DNA (TERF1 and TERF2).","predictedComplex":false,"interactors":[{"ac":"EBI-706637","identifier":"Q15554","identifierLink":"https://www.uniprot.org/uniprotkb/Q15554/entry","name":"TERF2","description":"Telomeric repeat-binding factor 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46833","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-710997","identifier":"P54274","identifierLink":"https://www.uniprot.org/uniprotkb/P54274/entry","name":"TERF1","description":"Telomeric repeat-binding factor 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46734","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-717399","identifier":"Q9BSI4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BSI4/entry","name":"TINF2","description":"TERF1-interacting nuclear factor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15512","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-717666","identifier":"Q96AP0","identifierLink":"https://www.uniprot.org/uniprotkb/Q96AP0/entry","name":"ACD","description":"Adrenocortical dysplasia protein homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14487","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-750109","identifier":"Q9NYB0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NYB0/entry","name":"TERF2IP","description":"Telomeric repeat-binding factor 2-interacting protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16466","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752420","identifier":"Q9NUX5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NUX5/entry","name":"POT1","description":"Protection of telomeres protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14513","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-153","complexName":"Shelterin complex","organismName":"Mus musculus; 10090","description":"The Shelterin (Telosome) complex is a DNA-binding protein complex that associates with the telomeres that cap the ends of eukaryotic chromosomes and distinguishes them from sites of DNA damage thus sheltering chromosome ends from being inappropriately processed by the DNA repair machinery. Consequently it plays an essential role in maintaining telomere structure and integrity. Three subunits can interact directly either with single-stranded (Pot1) or double-stranded telomeric DNA (Terf1 and Terf2).","predictedComplex":false,"interactors":[{"ac":"EBI-6258642","identifier":"Q5EE38","identifierLink":"https://www.uniprot.org/uniprotkb/Q5EE38/entry","name":"Acd","description":"Adrenocortical dysplasia protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14487","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6919183","identifier":"P70371","identifierLink":"https://www.uniprot.org/uniprotkb/P70371/entry","name":"Terf1","description":"Telomeric repeat-binding factor 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46734","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6919263","identifier":"O35144","identifierLink":"https://www.uniprot.org/uniprotkb/O35144/entry","name":"Terf2","description":"Telomeric repeat-binding factor 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46833","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7051001","identifier":"Q91WC1","identifierLink":"https://www.uniprot.org/uniprotkb/Q91WC1/entry","name":"Pot1","description":"Protection of telomeres protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14513","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8341040","identifier":"Q91VL8","identifierLink":"https://www.uniprot.org/uniprotkb/Q91VL8/entry","name":"Terf2ip","description":"Telomeric repeat-binding factor 2-interacting protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16466","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8788053","identifier":"Q9QXG9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9QXG9/entry","name":"Tinf2","description":"TERF1-interacting nuclear factor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15512","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-154","complexName":"BUB1-BUB3 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Present throughout the cell cycle, this complex promotes spindle assembly checkpoint signalling. The spindle checkpoint ensures accurate chromosome segregation by sending a signal from an unattached kinetochore to inhibit anaphase onset. BUB3 localizes and binds to to kinetochore protein SPC105 via its phosphorylated MELT motif (a motif conforming to the consensus M-[E/D]-[L/I/V/M]-T). The presence of BUB1 positively contributes to the interaction by reducing the BUB3-SPC105 binding affinity.","predictedComplex":false,"interactors":[{"ac":"EBI-3816","identifier":"P41695","identifierLink":"https://www.uniprot.org/uniprotkb/P41695/entry","name":"BUB1","description":"Spindle assembly checkpoint serine/threonine-protein kinase BUB1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14030","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3830","identifier":"P26449","identifierLink":"https://www.uniprot.org/uniprotkb/P26449/entry","name":"BUB3","description":"Spindle assembly checkpoint protein BUB3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-155","complexName":"RB1-E2F1-DP1 transcriptional repressor complex","organismName":"Homo sapiens; 9606","description":"Formation of this complex, by binding to RB1 to the E2F1-DP1 transcription factor complex (CPX-175), negatively regulates the G1-S transition by blocking the transactivation domain of E2F1. RB1 dissociates from the complex following hyperphosphorylation by cyclin-dependent kinases.","predictedComplex":false,"interactors":[{"ac":"EBI-448924","identifier":"Q01094","identifierLink":"https://www.uniprot.org/uniprotkb/Q01094/entry","name":"E2F1","description":"Transcription factor E2F1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12081","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-491274","identifier":"P06400","identifierLink":"https://www.uniprot.org/uniprotkb/P06400/entry","name":"RB1","description":"Retinoblastoma-associated protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749713","identifier":"Q14186","identifierLink":"https://www.uniprot.org/uniprotkb/Q14186/entry","name":"TFDP1","description":"Transcription factor Dp-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12548","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-156","complexName":"PPP4C-PPP4R2 protein phosphatase 4 complex","organismName":"Homo sapiens; 9606","description":"PP2A-type phosphatase implicated in a variety of critical biological processes.","predictedComplex":false,"interactors":[{"ac":"EBI-1046072","identifier":"P60510","identifierLink":"https://www.uniprot.org/uniprotkb/P60510/entry","name":"PPP4C","description":"Serine/threonine-protein phosphatase 4 catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1048740","identifier":"Q9NY27","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NY27/entry","name":"PPP4R2","description":"Serine/threonine-protein phosphatase 4 regulatory subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16487","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-157","complexName":"PPP4C-PPP4R1 protein phosphatase 4 complex","organismName":"Mus musculus; 10090","description":"PP2A-type phosphatase implicated in a variety of critical biological processes including regulation of histone deacetylase 3 activity and microtubule growth at the centrosome via dephosphorylation of Ndel1.","predictedComplex":false,"interactors":[{"ac":"EBI-10900513","identifier":"Q8K2V1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K2V1/entry","name":"Ppp4r1","description":"Serine/threonine-protein phosphatase 4 regulatory subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2476073","identifier":"P97470","identifierLink":"https://www.uniprot.org/uniprotkb/P97470/entry","name":"Ppp4c","description":"Serine/threonine-protein phosphatase 4 catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-158","complexName":"PPP4C-PPP4R2-PPP4R3A protein phosphatase 4 complex","organismName":"Mus musculus; 10090","description":"PP2A-type phosphatase implicated in a variety of critical biological processes. Specifically dephosphorylates H2AFX phosphorylated on 'Ser-140' (gamma-H2AFX) generated during DNA replication and required for DNA DSB repair.","predictedComplex":false,"interactors":[{"ac":"EBI-10900543","identifier":"Q0VGB7","identifierLink":"https://www.uniprot.org/uniprotkb/Q0VGB7/entry","name":"Ppp4r2","description":"Serine/threonine-protein phosphatase 4 regulatory subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16487","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10901557","identifier":"Q6P2K6","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P2K6/entry","name":"Ppp4r3a","description":"Serine/threonine-protein phosphatase 4 regulatory subunit 3A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23318","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2476073","identifier":"P97470","identifierLink":"https://www.uniprot.org/uniprotkb/P97470/entry","name":"Ppp4c","description":"Serine/threonine-protein phosphatase 4 catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-159","complexName":"E2F1-DP1 transcription factor complex","organismName":"Mus musculus; 10090","description":"Transcription factor complex which binds DNA through the E2 recognition site, 5'-TTTC[CG]CGC-3', typically associated with the promoters of genes active in S phase. Activates genes that stimulate DNA synthesis and cell cycle advancement.","predictedComplex":false,"interactors":[{"ac":"EBI-1025536","identifier":"Q61501","identifierLink":"https://www.uniprot.org/uniprotkb/Q61501/entry","name":"E2f1","description":"Transcription factor E2F1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12081","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1216575","identifier":"Q08639","identifierLink":"https://www.uniprot.org/uniprotkb/Q08639/entry","name":"Tfdp1","description":"Transcription factor Dp-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12548","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-160","complexName":"RB1-E2F1-DP1 transcriptional repressor complex","organismName":"Mus musculus; 10090","description":"Formation of this complex, by binding to Rb1 to the E2F1-DP1 transcription factor complex (CPX-159), negatively regulates the G1-S transition by blocking the transactivation domain of E2F1. RB1 dissociates from the complex following hyperphosphorylation by cyclin-dependent kinases.","predictedComplex":false,"interactors":[{"ac":"EBI-1025536","identifier":"Q61501","identifierLink":"https://www.uniprot.org/uniprotkb/Q61501/entry","name":"E2f1","description":"Transcription factor E2F1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12081","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1216575","identifier":"Q08639","identifierLink":"https://www.uniprot.org/uniprotkb/Q08639/entry","name":"Tfdp1","description":"Transcription factor Dp-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12548","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-971782","identifier":"P13405","identifierLink":"https://www.uniprot.org/uniprotkb/P13405/entry","name":"Rb1","description":"Retinoblastoma-associated protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-161","complexName":"FZO1-MGM1-UGO1 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Spans the outer and inner membranes of mitochondria and mediates fusion of membranes. Required to control mitochondria shape, maintain mitochondrial DNA and plays a role in mitochondrial membrane fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-10865","identifier":"P32266","identifierLink":"https://www.uniprot.org/uniprotkb/P32266/entry","name":"MGM1","description":"Dynamin-like GTPase MGM1, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11566","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20900","identifier":"P38297","identifierLink":"https://www.uniprot.org/uniprotkb/P38297/entry","name":"FZO1","description":"Mitofusin FZO1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10465","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32955","identifier":"Q03327","identifierLink":"https://www.uniprot.org/uniprotkb/Q03327/entry","name":"UGO1","description":"Mitochondrial fusion and transport protein UGO1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24089","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-162","complexName":"Dehydrodolichyl diphosphate synthase complex variant RER2","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"One of two complexes involved in dolichol synthesis. An essential part of the dolichol monophosphate biosynthetic machinery; creates dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol, by adding multiple isopentenyl pyrophosphates (IPP) to farnesyl pyrophosphate (FPP). Predominate product is 16 IPP units.","predictedComplex":false,"interactors":[{"ac":"EBI-14943","identifier":"P35196","identifierLink":"https://www.uniprot.org/uniprotkb/P35196/entry","name":"RER2","description":"Dehydrodolichyl diphosphate synthase complex subunit RER2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10291","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34546","identifier":"Q12063","identifierLink":"https://www.uniprot.org/uniprotkb/Q12063/entry","name":"NUS1","description":"Dehydrodolichyl diphosphate synthase complex subunit NUS1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21528","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-163","complexName":"PPP4C-PPP4R2 protein phosphatase 4 complex","organismName":"Mus musculus; 10090","description":"PP2A-type phosphatase implicated in a variety of critical biological processes.","predictedComplex":false,"interactors":[{"ac":"EBI-10900543","identifier":"Q0VGB7","identifierLink":"https://www.uniprot.org/uniprotkb/Q0VGB7/entry","name":"Ppp4r2","description":"Serine/threonine-protein phosphatase 4 regulatory subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16487","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2476073","identifier":"P97470","identifierLink":"https://www.uniprot.org/uniprotkb/P97470/entry","name":"Ppp4c","description":"Serine/threonine-protein phosphatase 4 catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-164","complexName":"PPP4C-PPP4R2-PPP4R3B protein phosphatase 4 complex","organismName":"Mus musculus; 10090","description":"PP2A-type phosphatase implicated in a variety of critical biological processes.  Specifically dephosphorylates ATR-mediated gamma-H2AX generated during DNA replication.","predictedComplex":false,"interactors":[{"ac":"EBI-10900543","identifier":"Q0VGB7","identifierLink":"https://www.uniprot.org/uniprotkb/Q0VGB7/entry","name":"Ppp4r2","description":"Serine/threonine-protein phosphatase 4 regulatory subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16487","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10901583","identifier":"Q922R5","identifierLink":"https://www.uniprot.org/uniprotkb/Q922R5/entry","name":"Ppp4r3b","description":"Serine/threonine-protein phosphatase 4 regulatory subunit 3B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23318","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2476073","identifier":"P97470","identifierLink":"https://www.uniprot.org/uniprotkb/P97470/entry","name":"Ppp4c","description":"Serine/threonine-protein phosphatase 4 catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-165","complexName":"PPP4C-PPP4R4 protein phosphatase 4 complex","organismName":"Mus musculus; 10090","description":"PP2A-type phosphatase implicated in a variety of critical biological processes.","predictedComplex":false,"interactors":[{"ac":"EBI-2476041","identifier":"Q8C0Y0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C0Y0/entry","name":"Ppp4r4","description":"Serine/threonine-protein phosphatase 4 regulatory subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21467","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2476073","identifier":"P97470","identifierLink":"https://www.uniprot.org/uniprotkb/P97470/entry","name":"Ppp4c","description":"Serine/threonine-protein phosphatase 4 catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-166","complexName":"Dehydrodolichyl diphosphate synthase complex variant SRT1","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"One of two complexes involved in dolichol synthesis. An essential part of the dolichol monophosphate biosynthetic machinery; creates dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol, by adding multiple isopentenyl pyrophosphates (IPP) to farnesyl pyrophosphate (FPP). Predominate product is 17-19 IPP units.","predictedComplex":false,"interactors":[{"ac":"EBI-18117","identifier":"Q03175","identifierLink":"https://www.uniprot.org/uniprotkb/Q03175/entry","name":"SRT1","description":"Dehydrodolichyl diphosphate synthase complex subunit SRT1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10291","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34546","identifier":"Q12063","identifierLink":"https://www.uniprot.org/uniprotkb/Q12063/entry","name":"NUS1","description":"Dehydrodolichyl diphosphate synthase complex subunit NUS1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21528","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-167","complexName":"Neuronal nicotinic acetylcholine receptor complex, 3xalpha4-2xbeta2","organismName":"Mus musculus; 10090","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived, mainly pre-synaptic transmission of neurotransmitters. Major receptor in Central Nervous System and predominantly found in cerebellum, cortex, forebrain, hippocampus, mesencephalon, striatum, superior colliculus and thalamus. Up-regulated by pro-inflammatory cytokines, for example TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10916254","identifier":"O70174-PRO_0000000352","identifierLink":"https://www.uniprot.org/uniprotkb/O70174-PRO_0000000352/entry","name":"Chrna4","description":"Neuronal acetylcholine receptor subunit alpha-4","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-10916261","identifier":"Q9ERK7-PRO_0000000380","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ERK7-PRO_0000000380/entry","name":"Chrnb2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-168","complexName":"Neuronal nicotinic acetylcholine receptor complex, 3xalpha4-2xbeta2","organismName":"Homo sapiens; 9606","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. 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Up-regulated by pro-inflammatory cytokines, for example TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10899398","identifier":"P43681-PRO_0000000351","identifierLink":"https://www.uniprot.org/uniprotkb/P43681-PRO_0000000351/entry","name":"CHRNA4","description":"Neuronal acetylcholine receptor subunit alpha-4","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-10899404","identifier":"P17787-PRO_0000000379","identifierLink":"https://www.uniprot.org/uniprotkb/P17787-PRO_0000000379/entry","name":"CHRNB2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-169","complexName":"Neuronal nicotinic acetylcholine receptor complex, 2xalpha4-3xbeta2","organismName":"Mus musculus; 10090","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. 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Up-regulated by pro-inflammatory cytokines, for example TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10916254","identifier":"O70174-PRO_0000000352","identifierLink":"https://www.uniprot.org/uniprotkb/O70174-PRO_0000000352/entry","name":"Chrna4","description":"Neuronal acetylcholine receptor subunit alpha-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-10916261","identifier":"Q9ERK7-PRO_0000000380","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ERK7-PRO_0000000380/entry","name":"Chrnb2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-170","complexName":"Neuronal nicotinic acetylcholine receptor complex, 2xalpha4-3xbeta2","organismName":"Rattus norvegicus; 10116","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived, mainly pre-synaptic transmission of neurotransmitters. Major receptor in Central Nervous System and predominantly found in cerebellum, cortex, forebrain, hippocampus, mesencephalon, striatum, superior colliculus and thalamus. Up-regulated by pro-inflammatory cytokines, for example TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10916765","identifier":"P09483-PRO_0000000354","identifierLink":"https://www.uniprot.org/uniprotkb/P09483-PRO_0000000354/entry","name":"Chrna4","description":"Neuronal acetylcholine receptor subunit alpha-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-10916775","identifier":"P12390-PRO_0000000381","identifierLink":"https://www.uniprot.org/uniprotkb/P12390-PRO_0000000381/entry","name":"Chrnb2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-171","complexName":"Neuronal nicotinic acetylcholine receptor complex, 3xalpha4-2xbeta2","organismName":"Rattus norvegicus; 10116","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. 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Up-regulated by pro-inflammatory cytokines, for example TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10916765","identifier":"P09483-PRO_0000000354","identifierLink":"https://www.uniprot.org/uniprotkb/P09483-PRO_0000000354/entry","name":"Chrna4","description":"Neuronal acetylcholine receptor subunit alpha-4","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-10916775","identifier":"P12390-PRO_0000000381","identifierLink":"https://www.uniprot.org/uniprotkb/P12390-PRO_0000000381/entry","name":"Chrnb2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-172","complexName":"Neuronal nicotinic acetylcholine receptor complex, 3xalpha4-2xbeta2","organismName":"Gallus gallus; 9031","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived, mainly pre-synaptic transmission of neurotransmitters. Major receptor in Central Nervous System and predominantly found in cerebellum, cortex, forebrain, hippocampus, mesencephalon, striatum, superior colliculus and thalamus. Up-regulated by pro-inflammatory cytokines, for example TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10916921","identifier":"P09482-PRO_0000000355","identifierLink":"https://www.uniprot.org/uniprotkb/P09482-PRO_0000000355/entry","name":"CHRNA4","description":"Neuronal acetylcholine receptor subunit alpha-4","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]},{"ac":"EBI-10916933","identifier":"P09484-PRO_0000000382","identifierLink":"https://www.uniprot.org/uniprotkb/P09484-PRO_0000000382/entry","name":"CHRNB2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]}]},{"complexAC":"CPX-173","complexName":"Neuronal nicotinic acetylcholine receptor complex, 2xalpha4-3xbeta2","organismName":"Gallus gallus; 9031","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived, mainly pre-synaptic transmission of neurotransmitters. Major receptor in Central Nervous System and predominantly found in cerebellum, cortex, forebrain, hippocampus, mesencephalon, striatum, superior colliculus and thalamus. Up-regulated by pro-inflammatory cytokines, for example TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10916921","identifier":"P09482-PRO_0000000355","identifierLink":"https://www.uniprot.org/uniprotkb/P09482-PRO_0000000355/entry","name":"CHRNA4","description":"Neuronal acetylcholine receptor subunit alpha-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]},{"ac":"EBI-10916933","identifier":"P09484-PRO_0000000382","identifierLink":"https://www.uniprot.org/uniprotkb/P09484-PRO_0000000382/entry","name":"CHRNB2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]}]},{"complexAC":"CPX-174","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha2-beta2","organismName":"Mus musculus; 10090","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. Mainly found in optic lobe. Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10916261","identifier":"Q9ERK7-PRO_0000000380","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ERK7-PRO_0000000380/entry","name":"Chrnb2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-10950438","identifier":"Q91X60-PRO_0000000341","identifierLink":"https://www.uniprot.org/uniprotkb/Q91X60-PRO_0000000341/entry","name":"Chrna2","description":"Neuronal acetylcholine receptor subunit alpha-2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-379","complexName":"Cyclin Y-CDK16 complex","organismName":"Homo sapiens; 9606","description":"Cyclin-dependent protein kinase complex which appears to play an essential role in spermatogenesis. The AMPK complex activates Cyclin Y/CDK16 to initiate an early step in the formation of autophagosomes.","predictedComplex":false,"interactors":[{"ac":"EBI-1049189","identifier":"Q8ND76","identifierLink":"https://www.uniprot.org/uniprotkb/Q8ND76/entry","name":"CCNY","description":"Cyclin-Y","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14248","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-726261","identifier":"Q00536","identifierLink":"https://www.uniprot.org/uniprotkb/Q00536/entry","name":"CDK16","description":"Cyclin-dependent kinase 16","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-380","complexName":"ULK1-ATG13-RB1CC1-ATG101 autophagy initiation complex","organismName":"Mus musculus; 10090","description":"Serine/threonine-protein kinase complex required for pre-autophagosomal structure assembly in response to starvation. Ultimately facilitates sequestration of cytoplasmic proteins and organelles for bulk degradation via autophagy and mitophagy, respectively. \r\n\r\nUnder glucose starvation conditions activated through phosphorylation of Ulk1 on Ser-317 and Ser-777 by AMPK complex. Under amino acid starvation conditions ULK1 and ATG13 are phosphorylated by mTorc1. Activated Ulk1 represses mTorc1 kinase activity via phosphorylation of Rptor(Q8K4Q0, subunit of mTORC1 complex) and phosphorylates ATG13, Rb1cc1 and itself. \r\n\r\nUnder nutrient-rich conditions inhibited through phosphorylation of Atg13 and Ulk1 on Ser-757 by Rptor (subunit of mTORC1 complex), leading to cell proliferation and cell mass increase.","predictedComplex":false,"interactors":[{"ac":"EBI-6396649","identifier":"Q9D8Z6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D8Z6/entry","name":"Atg101","description":"Autophagy-related protein 101","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13292","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-647302","identifier":"Q9ESK9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ESK9/entry","name":"Rb1cc1","description":"RB1-inducible coiled-coil protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8390771","identifier":"O70405","identifierLink":"https://www.uniprot.org/uniprotkb/O70405/entry","name":"Ulk1","description":"Serine/threonine-protein kinase ULK1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24348","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8391007","identifier":"Q91YI1","identifierLink":"https://www.uniprot.org/uniprotkb/Q91YI1/entry","name":"Atg13","description":"Autophagy-related protein 13","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13430","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-381","complexName":"Interleukin-12 complex","organismName":"Homo sapiens; 9606","description":"Cytokine complex that activates and stimulates proliferation of a wide range of lymphocytes, in particular natural killer cells and T helper 1 (Th1) cells, upon binding to its receptor subunits IL12RB1 (P42701) and IL12RB2 (Q99665). Formation of the ligand-receptor complex (CPX-382) initiates the JAK-STAT signaling pathway which ultimately activates transcription of interferon (IFN)-gamma which, in turn, stimulates production of IL12 leading to a positive regulation loop. Produced by antigen-presenting cells in response to Interleukin-18 and/or the related Interleukin-23 (CPX-3290). Anti-inflammatory agent that counteracts Interleukin-23 and inhibits Interleukin-17 secretion by activated T cells. Mutations in IL12B can lead to mycobacterial diseases of varying severity, primarily bacillus Calmette-Guerin and Salmonella infections.","predictedComplex":false,"interactors":[{"ac":"EBI-11665075","identifier":"P29460-PRO_0000010930","identifierLink":"https://www.uniprot.org/uniprotkb/P29460-PRO_0000010930/entry","name":"IL12B","description":"Interleukin-12 subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-11665081","identifier":"P29459-PRO_0000015604","identifierLink":"https://www.uniprot.org/uniprotkb/P29459-PRO_0000015604/entry","name":"IL12A","description":"Interleukin-12 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-384","complexName":"CBP3-CBP6 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Role in both the efficient synthesis of cytochrome b and protection of the newly synthesized protein from proteolysis. Associates with mitochondrial ribosomes at the polypeptide tunnel exit and is necessary for efficient translation of cytochrome b transcript. Also interacts directly with newly synthesized cytochrome b in an assembly intermediate that is not ribosome bound and coordinates cytochrome b synthesis with mitochondrial electron transport complex III (CPX-567) assembly.","predictedComplex":false,"interactors":[{"ac":"EBI-4134","identifier":"P21560","identifierLink":"https://www.uniprot.org/uniprotkb/P21560/entry","name":"CBP3","description":"Protein CBP3, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12184","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4142","identifier":"P07253","identifierLink":"https://www.uniprot.org/uniprotkb/P07253/entry","name":"CBP6","description":"Cytochrome B pre-mRNA-processing protein 6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28250","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-385","complexName":"CFD1-NBP35 Fe-S cluster assembly complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Scaffold complex that assembles nascent FeS clusters as part of the iron-sulfur cluster (ISC) assembly system, for transfer to FeS-requiring enzymes. NBP35 appears to bind the major portion of FeS clusters in the complex whereas CFD1 enhances this binding and drives the release of FeS to target apo-FeS proteins. The complex appears to have low level ATPase activity.","predictedComplex":false,"interactors":[{"ac":"EBI-11880","identifier":"P52920","identifierLink":"https://www.uniprot.org/uniprotkb/P52920/entry","name":"NBP35","description":"Cytosolic Fe-S cluster assembly factor NBP35","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-24924","identifier":"P40558","identifierLink":"https://www.uniprot.org/uniprotkb/P40558/entry","name":"CFD1","description":"Cytosolic Fe-S cluster assembly factor CFD1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-386","complexName":"TAH18-DRE2 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Protein complex that supplies reducing equivalents to the early steps of the cytosolic Fe-S assembly (CIA) pathway and also functions in ribonucleotide reductase cluster assembly, potentially also supplying reducing equivalents to the di-iron cluster. Electrons from NADPH are transferred via FAD and FMN, the two flavin cofactors in TAH18, to the Fe-S cluster(s) in DRE2, which subsequently deliver the electrons to proteins in the CIA pathway and RNR2 (P09938).","predictedComplex":false,"interactors":[{"ac":"EBI-11172266","identifier":"CHEBI:49601","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49601","name":"fe2s2 iron-sulfur cluster","description":"Fe2S2 iron-sulfur cluster","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-26482","identifier":"P36152","identifierLink":"https://www.uniprot.org/uniprotkb/P36152/entry","name":"DRE2","description":"Fe-S cluster assembly protein DRE2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13273","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-37624","identifier":"Q12181","identifierLink":"https://www.uniprot.org/uniprotkb/Q12181/entry","name":"TAH18","description":"NADPH-dependent diflavin oxidoreductase 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19384","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9663515","identifier":"CHEBI:58210","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58210","name":"fmn(3-)","description":"FMN(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-387","complexName":"Interleukin-12 complex","organismName":"Mus musculus; 10090","description":"Cytokine complex that activates and stimulates proliferation of a wide range of lymphocytes, in particular natural killer cells and T helper 1 (Th1) cells, upon binding to its receptor subunits Il12rb1 (Q60837) and Il12rb2 (P97378). Formation of the ligand-receptor complex (CPX-388) initiates the JAK-STAT signaling pathway which ultimately activates transcription of interferon (IFN)-gamma which, in turn, stimulates production of IL12 leading to a positive regulation loop. Produced by antigen-presenting cells in response to Interleukin-18 and/or the related Interleukin-23 (CPX-3293). Anti-inflammatory agent that counteracts Interleukin-23 and inhibits Interleukin-17 secretion by activated T cells.","predictedComplex":false,"interactors":[{"ac":"EBI-11682051","identifier":"P43431-PRO_0000015608","identifierLink":"https://www.uniprot.org/uniprotkb/P43431-PRO_0000015608/entry","name":"Il12a","description":"Interleukin-12 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-11682058","identifier":"P43432-PRO_0000010933","identifierLink":"https://www.uniprot.org/uniprotkb/P43432-PRO_0000010933/entry","name":"Il12b","description":"Interleukin-12 subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-388","complexName":"Interleukin-12-receptor complex","organismName":"Mus musculus; 10090","description":"Receptor complex that activates and stimulates proliferation of a wide range of lymphocytes, in particular natural killer cells and T helper 1 (Th1) cells. The IL12 ligand complex (CPX-387) binds the receptors chains Il12rb1 and Il12rb2 which are associated with the kinases Tyk2 and Jak2, respectively. Transphosphorylation of Il12rb2 and the JAK-family kinases initiates the JAK-STAT signaling cascade via phosphorylation and homodimerisation of Stat3/Stat4 (P42227/P42228). This ultimately leads to the activation of transcription of interferon-gamma which, in turn, stimulates production of IL12 leading to a positive regulation loop.","predictedComplex":false,"interactors":[{"ac":"EBI-11682051","identifier":"P43431-PRO_0000015608","identifierLink":"https://www.uniprot.org/uniprotkb/P43431-PRO_0000015608/entry","name":"Il12a","description":"Interleukin-12 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-11682058","identifier":"P43432-PRO_0000010933","identifierLink":"https://www.uniprot.org/uniprotkb/P43432-PRO_0000010933/entry","name":"Il12b","description":"Interleukin-12 subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-11682068","identifier":"Q60837-PRO_0000010918","identifierLink":"https://www.uniprot.org/uniprotkb/Q60837-PRO_0000010918/entry","name":"Il12rb1","description":"Interleukin-12 receptor subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-11682074","identifier":"P97378-PRO_0000010921","identifierLink":"https://www.uniprot.org/uniprotkb/P97378-PRO_0000010921/entry","name":"Il12rb2","description":"Interleukin-12 receptor subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-11683202","identifier":"Q9R117","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R117/entry","name":"Tyk2","description":"Non-receptor tyrosine-protein kinase TYK2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45807","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-646604","identifier":"Q62120","identifierLink":"https://www.uniprot.org/uniprotkb/Q62120/entry","name":"Jak2","description":"Tyrosine-protein kinase JAK2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45807","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-389","complexName":"Interleukin-23-receptor complex","organismName":"Mus musculus; 10090","description":"Receptor complex that activates and stimulates proliferation of a wide range of lymphocytes, in particular memory T cells and Th17 cells. The IL23 ligand complex (CPX-3293) binds the receptors chains Il12rb1 and Il23r which are associated with the kinases Tyk2 and Jak2, respectively. Transphosphorylation of Il23r and the JAK-family kinases initiates the JAK-STAT signaling cascade via phosphorylation and heterodimerisation of STAT3 and STAT4 (P42227/P42228). This ultimately leads to the activation of transcription of interferon-gamma or Interleukin-17.","predictedComplex":false,"interactors":[{"ac":"EBI-11682058","identifier":"P43432-PRO_0000010933","identifierLink":"https://www.uniprot.org/uniprotkb/P43432-PRO_0000010933/entry","name":"Il12b","description":"Interleukin-12 subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-11682068","identifier":"Q60837-PRO_0000010918","identifierLink":"https://www.uniprot.org/uniprotkb/Q60837-PRO_0000010918/entry","name":"Il12rb1","description":"Interleukin-12 receptor subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-11682079","identifier":"Q9EQ14-PRO_0000259489","identifierLink":"https://www.uniprot.org/uniprotkb/Q9EQ14-PRO_0000259489/entry","name":"Il23a","description":"Interleukin-23 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-11682109","identifier":"Q8K4B4-PRO_0000268663","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K4B4-PRO_0000268663/entry","name":"Il23r","description":"Interleukin-23 receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-11683202","identifier":"Q9R117","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R117/entry","name":"Tyk2","description":"Non-receptor tyrosine-protein kinase TYK2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45807","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-646604","identifier":"Q62120","identifierLink":"https://www.uniprot.org/uniprotkb/Q62120/entry","name":"Jak2","description":"Tyrosine-protein kinase JAK2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45807","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-390","complexName":"Collagen type XXV trimer, variant 2","organismName":"Homo sapiens; 9606","description":"Type II orientated transmembrane collagen. Inhibits fibrillization of beta amyloid peptide during the elongation phase. Has also been shown to assemble amyloid fibrils into protease-resistant aggregates. Binds heparin.","predictedComplex":false,"interactors":[{"ac":"EBI-11682395","identifier":"Q9BXS0-2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BXS0-2/entry","name":"COL25A1","description":"Collagen alpha-1(XXV) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-391","complexName":"Collagen type XXV trimer, variant 3","organismName":"Homo sapiens; 9606","description":"Type II orientated transmembrane collagen. Inhibits fibrillization of beta amyloid peptide during the elongation phase. Has also been shown to assemble amyloid fibrils into protease-resistant aggregates. Binds heparin.","predictedComplex":false,"interactors":[{"ac":"EBI-11682418","identifier":"Q9BXS0-3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BXS0-3/entry","name":"COL25A1","description":"Collagen alpha-1(XXV) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-393","complexName":"Phosphopantothenoylcysteine decarboxylase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyses the third step of the coenzyme A (CoA) biosynthetic pathway, namely the decarboxylation of 4'-phosphopantothenoylcysteine to form 4′-phosphopantetheine. May potentially be part of a larger Coenzyme A-synthesizing protein complex (CPX-396) but this is not yet clear.\r\n\r\nThe synthesis of CoA involves the phosphorylation of pantothenate (vitamin B5) to 4'-phosphopantothenate, to which a cysteine is then added to form \r\n4'-phospho-N-pantothenoylcysteine (PCC). PPC is decarboxylated to 4'-phosphopantetheine by phosphopantothenoylcysteine decarboxylase (this complex). 4'-phosphopantetheine is adenylylated to form dephospho-CoA which is then phosphorylated to form coenzyme A.","predictedComplex":false,"interactors":[{"ac":"EBI-17250","identifier":"P36024","identifierLink":"https://www.uniprot.org/uniprotkb/P36024/entry","name":"SIS2","description":"Phosphopantothenoylcysteine decarboxylase subunit SIS2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14359","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26778","identifier":"P36076","identifierLink":"https://www.uniprot.org/uniprotkb/P36076/entry","name":"CAB3","description":"Coenzyme A biosynthesis protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14359","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30482","identifier":"Q08438","identifierLink":"https://www.uniprot.org/uniprotkb/Q08438/entry","name":"VHS3","description":"Phosphopantothenoylcysteine decarboxylase subunit VHS3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14359","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-394","complexName":"YAP1-TEAD1 transcription factor complex","organismName":"Mus musculus; 10090","description":"Transcription factor complex of enhancer factor TEF-1 (Tead) and coactivator Yap1. Plays key role in Hippo signaling pathway involved in organ size control and tumor supression by restricting proliferation and promoting apoptosis. Connective tissue growth factor (Ctgf) has been identified as a direct target gene.","predictedComplex":false,"interactors":[{"ac":"EBI-1211949","identifier":"P46938","identifierLink":"https://www.uniprot.org/uniprotkb/P46938/entry","name":"Yap1","description":"Transcriptional coactivator YAP1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR17616","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3953905","identifier":"P30051","identifierLink":"https://www.uniprot.org/uniprotkb/P30051/entry","name":"Tead1","description":"Transcriptional enhancer factor TEF-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11834","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-395","complexName":"GTPase HRAS - Son of sevenless homolog 1 complex","organismName":"Homo sapiens; 9606","description":"A RAS GTPase complex responsible for intracellular transduction of signals received through cell-surface receptor tyrosine kinases. \r\n\r\nActivated HRAS.GTP promotes cell growth and survival. HRAS and SOS1 allosterically activate each other: binding of inactive HRAS.GDP to SOS1 stimulates SOS1 nucleotide exchange activity which in turn leads to HRAS binding GTP in place of GDP.","predictedComplex":false,"interactors":[{"ac":"EBI-297487","identifier":"Q07889","identifierLink":"https://www.uniprot.org/uniprotkb/Q07889/entry","name":"SOS1","description":"Son of sevenless homolog 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23113","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350145","identifier":"P01112","identifierLink":"https://www.uniprot.org/uniprotkb/P01112/entry","name":"HRAS","description":"GTPase HRas","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24070","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-989053","identifier":"CHEBI:15996","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15996","name":"gtp","description":"guanosine triphosphate - GTP","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-396","complexName":"Coenzyme A-synthesizing protein complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyses multiple steps in the coenzyme A (CoA) biosynthetic pathway, with the CAB3 protein potentially acting as a scaffold to which other enzymes bind. This may be a larger complex, also incorporating the Phosphopantothenoylcysteine decarboxylase complex (CPX-393) but this is not yet clear.\r\n\r\nThe synthesis of CoA involves the phosphorylation of pantothenate (vitamin B5) to 4'-phosphopantothenate, to which a cysteine is then added to form \r\n4'-phospho-N-pantothenoylcysteine (PCC). PPC is decarboxylated to 4'-phosphopantetheine by phosphopantothenoylcysteine decarboxylase (CPX-393). 4'-phosphopantetheine is adenylylated to form dephospho-CoA which is then phosphorylated to form coenzyme A.","predictedComplex":false,"interactors":[{"ac":"EBI-22174","identifier":"Q03941","identifierLink":"https://www.uniprot.org/uniprotkb/Q03941/entry","name":"CAB5","description":"Dephospho-CoA kinase CAB5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10695","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23648","identifier":"P53332","identifierLink":"https://www.uniprot.org/uniprotkb/P53332/entry","name":"CAB4","description":"Phosphopantetheine adenylyltransferase","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10695","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25089","identifier":"P40506","identifierLink":"https://www.uniprot.org/uniprotkb/P40506/entry","name":"CAB2","description":"Phosphopantothenate--cysteine ligase CAB2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12290","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26778","identifier":"P36076","identifierLink":"https://www.uniprot.org/uniprotkb/P36076/entry","name":"CAB3","description":"Coenzyme A biosynthesis protein 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14359","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-397","complexName":"Atg17-Atg31-Atg29 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Scaffolding complex required for the assembly of the preautophagosomal structure (PAS), the first step of autophagosome formation. Constructively present under both growing and starvation conditions. Under conditions of nutrient starvation, it forms a complex with ATG1 and ATG13 to enhance the kinase activity of ATG1 (CPX-1676).","predictedComplex":false,"interactors":[{"ac":"EBI-30856","identifier":"Q06410","identifierLink":"https://www.uniprot.org/uniprotkb/Q06410/entry","name":"ATG17","description":"Autophagy-related protein 17","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28005","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34768","identifier":"Q12421","identifierLink":"https://www.uniprot.org/uniprotkb/Q12421/entry","name":"ATG31","description":"Autophagy-related protein 31","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-38752","identifier":"Q12092","identifierLink":"https://www.uniprot.org/uniprotkb/Q12092/entry","name":"ATG29","description":"Autophagy-related protein 29","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR40012","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-398","complexName":"ced-9-egl-1 complex","organismName":"Caenorhabditis elegans; 6239","description":"Complex plays a major role in programmed cell death (apoptosis). Egl-1 binds to and directly inhibits the activity of ced-9, releasing the cell death activator ced-4 from the ced-9-ced-4 complex and allowing ced-4 to activate the cell-killing caspase ced-3.","predictedComplex":false,"interactors":[{"ac":"EBI-494110","identifier":"P41958","identifierLink":"https://www.uniprot.org/uniprotkb/P41958/entry","name":"ced-9","description":"Apoptosis regulator ced-9","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11256","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-495949","identifier":"O61667","identifierLink":"https://www.uniprot.org/uniprotkb/O61667/entry","name":"egl-1","description":"Programmed cell death activator egl-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]}]},{"complexAC":"CPX-399","complexName":"ced-9-ced-4 complex","organismName":"Caenorhabditis elegans; 6239","description":"Complex plays a major role in programmed cell death (apoptosis), by causing the sequestration and inhibition of ced-4. egl-1 binds to and directly inhibits the activity of ced-9, releasing the cell death activator ced-4 from the ced-9-ced-4 complex and allowing ced-4 to activate the cell-killing caspase ced-3.","predictedComplex":false,"interactors":[{"ac":"EBI-494110","identifier":"P41958","identifierLink":"https://www.uniprot.org/uniprotkb/P41958/entry","name":"ced-9","description":"Apoptosis regulator ced-9","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11256","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-494118","identifier":"P30429","identifierLink":"https://www.uniprot.org/uniprotkb/P30429/entry","name":"ced-4","description":"Cell death protein 4","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]}]},{"complexAC":"CPX-400","complexName":"Bub-1-Bub-3 complex","organismName":"Caenorhabditis elegans; 6239","description":"Present throughout the cell cycle, this complex promotes spindle assembly checkpoint signalling. The spindle checkpoint ensures accurate chromosome segregation by sending a signal from an unattached kinetochore to inhibit anaphase onset.\r\n\r\nLocalises to the kinetochore region of mitotic chromosomes to promote the onset of anaphase in a fashion that is independent of its function in spindle assembly checkpoint signalling and chromosome alignment. The complex also recruits other spindle components to the kinetochore region.","predictedComplex":false,"interactors":[{"ac":"EBI-331258","identifier":"Q9XWH0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XWH0/entry","name":"bub-3","description":"Mitotic checkpoint protein bub-3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-331300","identifier":"Q21776","identifierLink":"https://www.uniprot.org/uniprotkb/Q21776/entry","name":"bub-1","description":"Mitotic checkpoint serine/threonine-protein kinase bub-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR14030","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-401","complexName":"Mitotic checkpoint complex, Mad-1-Mad-2-Bub-1-Bub-3 subcomplex","organismName":"Caenorhabditis elegans; 6239","description":"This complex forms during mitosis, as a result of the activation of the spindle checkpoint. bub-3 and bub-1 are associated through the cell cycle, however, the addition of mdf-1 is cell cycle dependent.\r\n\r\nThe interaction of bub-1 and mdf-1 recruits mdf-1 to unattached kinetochores during mitosis and between homologous chromosomes in early anaphase of meiosis I.","predictedComplex":false,"interactors":[{"ac":"EBI-316684","identifier":"G5EFM0","identifierLink":"https://www.uniprot.org/uniprotkb/G5EFM0/entry","name":"mdf-1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR23168","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-328699","identifier":"Q9NGT3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NGT3/entry","name":"mdf-2","description":"Mitotic spindle assembly checkpoint protein MAD2A","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-331258","identifier":"Q9XWH0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XWH0/entry","name":"bub-3","description":"Mitotic checkpoint protein bub-3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-331300","identifier":"Q21776","identifierLink":"https://www.uniprot.org/uniprotkb/Q21776/entry","name":"bub-1","description":"Mitotic checkpoint serine/threonine-protein kinase bub-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR14030","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-402","complexName":"Mitotic spindle assembly checkpoint mad-1-mad-2 complex","organismName":"Caenorhabditis elegans; 6239","description":"Acts at the spindle checkpoint, in a surveillance mechanism that mediates a delay in the onset of anaphase, until all chromosomes are properly attached to the mitotic or meiotic spindle. Required for the checkpoint response to absence of spindle tension, localising only to unattached kinetochores but not to attached kinetochores that lack tension, and participate in a bipolar orientation defect signalling pathway.\r\n\r\nInteraction between mdf-1 and bub-1 recruits the mad-1-mad-2 complex to unattached kinetochores.","predictedComplex":false,"interactors":[{"ac":"EBI-316684","identifier":"G5EFM0","identifierLink":"https://www.uniprot.org/uniprotkb/G5EFM0/entry","name":"mdf-1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR23168","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-328699","identifier":"Q9NGT3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NGT3/entry","name":"mdf-2","description":"Mitotic spindle assembly checkpoint protein MAD2A","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-404","complexName":"GABA-B receptor complex","organismName":"Rattus norvegicus; 10116","description":"G-protein-coupled, metabotropic transmembrane receptor for gamma-aminobutyric acid (GABA), the major inhibitory neurotransmitter in the vertebrate brain. Linked via G-proteins to potassium channels.\r\n\r\nLigand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis. Calcium is required for high affinity binding to GABA. Plays a critical role in the fine-tuning of inhibitory synaptic transmission. Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials. Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception.","predictedComplex":false,"interactors":[{"ac":"EBI-7090239","identifier":"O88871","identifierLink":"https://www.uniprot.org/uniprotkb/O88871/entry","name":"Gabbr2","description":"Gamma-aminobutyric acid type B receptor subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR10519","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7090268","identifier":"Q9Z0U4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0U4/entry","name":"Gabbr1","description":"Gamma-aminobutyric acid type B receptor subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR10519","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-405","complexName":"GABA-A receptor, alpha6-beta3-gamma2","organismName":"Rattus norvegicus; 10116","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-11693649","identifier":"P30191","identifierLink":"https://www.uniprot.org/uniprotkb/P30191/entry","name":"Gabra6","description":"Gamma-aminobutyric acid receptor subunit alpha-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6257937","identifier":"P63079","identifierLink":"https://www.uniprot.org/uniprotkb/P63079/entry","name":"Gabrb3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8601559","identifier":"P18508","identifierLink":"https://www.uniprot.org/uniprotkb/P18508/entry","name":"Gabrg2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-406","complexName":"GABA-A receptor, alpha6-beta3-delta","organismName":"Rattus norvegicus; 10116","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.","predictedComplex":false,"interactors":[{"ac":"EBI-11296683","identifier":"P18506","identifierLink":"https://www.uniprot.org/uniprotkb/P18506/entry","name":"Gabrd","description":"Gamma-aminobutyric acid receptor subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11693649","identifier":"P30191","identifierLink":"https://www.uniprot.org/uniprotkb/P30191/entry","name":"Gabra6","description":"Gamma-aminobutyric acid receptor subunit alpha-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6257937","identifier":"P63079","identifierLink":"https://www.uniprot.org/uniprotkb/P63079/entry","name":"Gabrb3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-407","complexName":"GABA-A receptor, alpha6-beta2-delta","organismName":"Rattus norvegicus; 10116","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-11296683","identifier":"P18506","identifierLink":"https://www.uniprot.org/uniprotkb/P18506/entry","name":"Gabrd","description":"Gamma-aminobutyric acid receptor subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11693649","identifier":"P30191","identifierLink":"https://www.uniprot.org/uniprotkb/P30191/entry","name":"Gabra6","description":"Gamma-aminobutyric acid receptor subunit alpha-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6258047","identifier":"P63138","identifierLink":"https://www.uniprot.org/uniprotkb/P63138/entry","name":"Gabrb2","description":"Gamma-aminobutyric acid receptor subunit beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-408","complexName":"GABA-A receptor, alpha4-beta2-delta","organismName":"Rattus norvegicus; 10116","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-11296648","identifier":"P28471","identifierLink":"https://www.uniprot.org/uniprotkb/P28471/entry","name":"Gabra4","description":"Gamma-aminobutyric acid receptor subunit alpha-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11296683","identifier":"P18506","identifierLink":"https://www.uniprot.org/uniprotkb/P18506/entry","name":"Gabrd","description":"Gamma-aminobutyric acid receptor subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6258047","identifier":"P63138","identifierLink":"https://www.uniprot.org/uniprotkb/P63138/entry","name":"Gabrb2","description":"Gamma-aminobutyric acid receptor subunit beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-409","complexName":"GABA-A receptor, alpha3-beta3-gamma2","organismName":"Rattus norvegicus; 10116","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets..","predictedComplex":false,"interactors":[{"ac":"EBI-5273284","identifier":"P20236","identifierLink":"https://www.uniprot.org/uniprotkb/P20236/entry","name":"Gabra3","description":"Gamma-aminobutyric acid receptor subunit alpha-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6257937","identifier":"P63079","identifierLink":"https://www.uniprot.org/uniprotkb/P63079/entry","name":"Gabrb3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8601559","identifier":"P18508","identifierLink":"https://www.uniprot.org/uniprotkb/P18508/entry","name":"Gabrg2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-410","complexName":"GABA-A receptor, alpha1-beta3-gamma2","organismName":"Rattus norvegicus; 10116","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-6257937","identifier":"P63079","identifierLink":"https://www.uniprot.org/uniprotkb/P63079/entry","name":"Gabrb3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6258192","identifier":"P62813","identifierLink":"https://www.uniprot.org/uniprotkb/P62813/entry","name":"Gabra1","description":"Gamma-aminobutyric acid receptor subunit alpha-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8601559","identifier":"P18508","identifierLink":"https://www.uniprot.org/uniprotkb/P18508/entry","name":"Gabrg2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-411","complexName":"GABA-A receptor, alpha5-beta3-gamma2","organismName":"Rattus norvegicus; 10116","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-6257937","identifier":"P63079","identifierLink":"https://www.uniprot.org/uniprotkb/P63079/entry","name":"Gabrb3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8069330","identifier":"P19969","identifierLink":"https://www.uniprot.org/uniprotkb/P19969/entry","name":"Gabra5","description":"Gamma-aminobutyric acid receptor subunit alpha-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8601559","identifier":"P18508","identifierLink":"https://www.uniprot.org/uniprotkb/P18508/entry","name":"Gabrg2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-412","complexName":"GABA-A receptor, alpha2-beta3-gamma2","organismName":"Rattus norvegicus; 10116","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-11694968","identifier":"P23576","identifierLink":"https://www.uniprot.org/uniprotkb/P23576/entry","name":"Gabra2","description":"Gamma-aminobutyric acid receptor subunit alpha-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6257937","identifier":"P63079","identifierLink":"https://www.uniprot.org/uniprotkb/P63079/entry","name":"Gabrb3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8601559","identifier":"P18508","identifierLink":"https://www.uniprot.org/uniprotkb/P18508/entry","name":"Gabrg2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-413","complexName":"GTPase Hras - Son of sevenless homolog 1 complex","organismName":"Mus musculus; 10090","description":"A RAS GTPase complex responsible for intracellular transduction of signals received through cell-surface receptor tyrosine kinases. \r\n\r\nActivated Hras.GTP promotes cell growth and survival. Ras and Sos1 allosterically activate each other: binding of inactive Hras.GDP to Sos1 stimulates Sos1 nucleotide exchange activity which in turn leads to Hras binding GTP in place of GDP.","predictedComplex":false,"interactors":[{"ac":"EBI-1693","identifier":"Q62245","identifierLink":"https://www.uniprot.org/uniprotkb/Q62245/entry","name":"Sos1","description":"Son of sevenless homolog 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23113","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-400273","identifier":"Q61411","identifierLink":"https://www.uniprot.org/uniprotkb/Q61411/entry","name":"Hras","description":"GTPase HRas","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24070","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-989053","identifier":"CHEBI:15996","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15996","name":"gtp","description":"guanosine triphosphate - GTP","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-414","complexName":"PR-DUB complex","organismName":"Homo sapiens; 9606","description":"A polycomb repressive deubiquitinase complex that specifically mediates deubiquitination of histone H2A (but not H2B) monoubiquitinated at Lys-119 (H2AK119ub1) in nucleosomes.","predictedComplex":false,"interactors":[{"ac":"EBI-1646500","identifier":"Q8IXJ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IXJ9/entry","name":"ASXL1","description":"Polycomb group protein ASXL1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13578","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1791447","identifier":"Q92560","identifierLink":"https://www.uniprot.org/uniprotkb/Q92560/entry","name":"BAP1","description":"Ubiquitin carboxyl-terminal hydrolase BAP1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10589","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-416","complexName":"Glutamyl-tRNA(Gln) amidotransferase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Generates glutaminyl-tRNA(Gln) in the mitochondrion. Cytosolic glutamyl-tRNA synthetase (ERS) is imported into mitochondria, where it constitutes the mitochondrial nondiscriminating ERS that generates the mitochondrial misacylated glutamyl-tRNA(Gln) substrate for the Glutamyl-tRNA(Gln) amidotransferase complex. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).","predictedComplex":false,"interactors":[{"ac":"EBI-23248","identifier":"P53260","identifierLink":"https://www.uniprot.org/uniprotkb/P53260/entry","name":"GTF1","description":"Glutamyl-tRNA(Gln) amidotransferase subunit F, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-7364","identifier":"P33893","identifierLink":"https://www.uniprot.org/uniprotkb/P33893/entry","name":"PET112","description":"Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11659","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7372","identifier":"Q03557","identifierLink":"https://www.uniprot.org/uniprotkb/Q03557/entry","name":"HER2","description":"Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11895","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-417","complexName":"Glucosidase II complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Glycoprotein-processing enzyme that successively cleaves the innermost two alpha1,3-linked glucose residues from N-linked oligosaccharides in the endoplasmic reticulum during glycoprotein biogenesis. The enzyme has dual activity, cleaving two alpha1,3-linked glucose residues in succession from Glc2Man9GlcNAc2 (G2M9) to Glc1Man9GlcNAc2 (G1M9) (cleavage-1), and then to Man9GlcNAc2 (M9) (cleavage-2). G1M9 plays a key role in glycoprotein quality control in the ER, because it is a primary ligand of the lectin chaperones calnexin (CNX) and calreticulin (CRT). Therefore, the cleavage-2 activity provides an exit for correctly folded glycoproteins from the CNX/CRT cycle, while the cleavage-1 activity provides an entry for immature glycoproteins into the cycle.","predictedComplex":false,"interactors":[{"ac":"EBI-21021","identifier":"P38138","identifierLink":"https://www.uniprot.org/uniprotkb/P38138/entry","name":"ROT2","description":"Glucosidase 2 subunit alpha","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22762","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-37493","identifier":"Q04924","identifierLink":"https://www.uniprot.org/uniprotkb/Q04924/entry","name":"GTB1","description":"Glucosidase 2 subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-418","complexName":"MTQ2-TRM112 eRF1 methyltransferase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"S-adenosylmethionine-dependent methyltransferase  responsible for methylating Gln-182 present in the conserved GGQ motif of the eRF1 subunit of the class 1 peptide chain release factor eRF1-eRF3 complex. Methylation occurs in the presence of GTP. This terminates the translation of nascent peptides in response to the termination codons UAA, UAG and UGA. Uses S-adenosyl L-methionine as methyl donor.","predictedComplex":false,"interactors":[{"ac":"EBI-28520","identifier":"P53738","identifierLink":"https://www.uniprot.org/uniprotkb/P53738/entry","name":"TRM112","description":"Multifunctional methyltransferase subunit TRM112","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12773","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31378","identifier":"Q03920","identifierLink":"https://www.uniprot.org/uniprotkb/Q03920/entry","name":"MTQ2","description":"eRF1 methyltransferase catalytic subunit MTQ2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45875","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-419","complexName":"FACT complex","organismName":"Homo sapiens; 9606","description":"FACT is an H2A-H2B histone chaperon complex that helps reorganize nucleosomes in an ATP-independent fashion. It is involved in various processes related to chromatin dynamics: DNA replication, DNA damage and repair, transcription initiation and elongation. Binds histone H2A-H2B dimers and possibly small amounts of H3H4. Facilitates RNAPol II driven transcription through chromatin by destabilizing nucleosomal structure so that one of the H2A-H2B dimers is removed upon RNA Pol II passage. Subsequently brings back the histones and thereby maintains nucleosome integrity after RNA Pol II passage. Interacts with the active forms of the MCM complexes facilitating its unwinding activity.","predictedComplex":false,"interactors":[{"ac":"EBI-1046849","identifier":"Q9Y5B9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5B9/entry","name":"SUPT16H","description":"FACT complex subunit SPT16","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13980","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353771","identifier":"Q08945","identifierLink":"https://www.uniprot.org/uniprotkb/Q08945/entry","name":"SSRP1","description":"FACT complex subunit SSRP1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45849","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-420","complexName":"xtbd-paxt-1 complex","organismName":"Caenorhabditis elegans; 6239","description":"5'-3' exonuclease complex that maintains the steady-state concentration and turnover of microRNAs (miRNA) by degradation of mature miRNA.\r\n\r\nPaxt-1 stabilizes and enhances the activity of xrn-2 within the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-11705385","identifier":"Q21738","identifierLink":"https://www.uniprot.org/uniprotkb/Q21738/entry","name":"paxt-1","description":"Partner of xrn-2 protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR48430","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-320499","identifier":"Q9U299","identifierLink":"https://www.uniprot.org/uniprotkb/Q9U299/entry","name":"xrn-2","description":"5'-3' exoribonuclease 2 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12341","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-421","complexName":"EMILIN-1 complex","organismName":"Homo sapiens; 9606","description":"Glycoprotein complex of the C1q/TNF superfamily found in the extracellular matrix (ECM) where it is an important component of the elastic fiber system. It is involved in cell adhesion, migration and proliferation, angiogenesis, blood pressure control and blood coagulation, apoptosis, platelet aggregation and possibly anti-microbial activities. Its function is strongly linked to its ability to bind integrins alpha4-beta1 (CPX-1802) and alpha9-beta1 (CPX-1816) via its gC1q domain.","predictedComplex":false,"interactors":[{"ac":"EBI-744586","identifier":"Q9Y6C2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6C2/entry","name":"EMILIN1","description":"EMILIN-1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15427","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-422","complexName":"DNA replication factor C complex, ELG1 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"DNA-dependent ATPase clamp-unloader complex that acts to remove PCNA (P15873, CPX-544) remaining on DNA after the completion of DNA replication and repair during the S phase of the cell cycle. The complex binds to DNA-loaded PCNA to induce opening of the PCNA ring, leading to the release of ELG1-RFC bound-PCNA.Role in sister chromatid cohesion, unloading both unmodified and SUMOylated PCNA from DNA following replication. This is a genome-wide process and follows Okazaki fragment ligation.","predictedComplex":false,"interactors":[{"ac":"EBI-14992","identifier":"P40348","identifierLink":"https://www.uniprot.org/uniprotkb/P40348/entry","name":"RFC2","description":"Replication factor C subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15000","identifier":"P38629","identifierLink":"https://www.uniprot.org/uniprotkb/P38629/entry","name":"RFC3","description":"Replication factor C subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15009","identifier":"P40339","identifierLink":"https://www.uniprot.org/uniprotkb/P40339/entry","name":"RFC4","description":"Replication factor C subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15016","identifier":"P38251","identifierLink":"https://www.uniprot.org/uniprotkb/P38251/entry","name":"RFC5","description":"Replication factor C subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32195","identifier":"Q12050","identifierLink":"https://www.uniprot.org/uniprotkb/Q12050/entry","name":"ELG1","description":"Telomere length regulation protein ELG1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23389","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-423","complexName":"PR-DUB complex","organismName":"Mus musculus; 10090","description":"A polycomb repressive deubiquitinase complex that specifically mediates deubiquitination of histone H2A (but not H2B) monoubiquitinated at Lys-119 (H2AK119ub1) in nucleosomes.","predictedComplex":false,"interactors":[{"ac":"EBI-1791471","identifier":"Q99PU7","identifierLink":"https://www.uniprot.org/uniprotkb/Q99PU7/entry","name":"Bap1","description":"Ubiquitin carboxyl-terminal hydrolase BAP1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10589","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5743705","identifier":"P59598","identifierLink":"https://www.uniprot.org/uniprotkb/P59598/entry","name":"Asxl1","description":"Polycomb group protein ASXL1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13578","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-424","complexName":"NoRC chromatin remodelling complex","organismName":"Mus musculus; 10090","description":"ATP-dependent nucleosome remodeling complex that represses ribosomal gene transcription. NoRC is targeted to rDNA by the interaction of its subunit Baz2a with Ttf1 (P50220) bound to the promoter-proximal target site. NoRC also binds to 150-300 nt RNAs that are complementary to the rDNA promoter (transcripts originating from the intergenic spacer that separates rRNA genes). NoRC remodels nucleosomes at the rDNA promoter and recruits histone deacetylases (e.g. Hdac1, Hdac2), histone methyltransferase and DNA methyltransferases (e.g. Dnmt1, Dnmt3b) leading to heterochromatin formation and transcriptional silencing.  The interaction of NoRC with the short RNA transcripts is mediated by the TAM domain of Baz2a and it is required for NoRC binding to chromatin and heterochromatin formation.","predictedComplex":false,"interactors":[{"ac":"EBI-11705475","identifier":"Q91YE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q91YE5/entry","name":"Baz2a","description":"Bromodomain adjacent to zinc finger domain protein 2A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45915","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-927547","identifier":"Q91ZW3","identifierLink":"https://www.uniprot.org/uniprotkb/Q91ZW3/entry","name":"Smarca5","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-425","complexName":"Elongation Factor eEF1 complex, variant TEF4","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Transports an aminoacylated-tRNA (aa-tRNA) to the ribosomal A-site during the elongation phase of protein synthesis. GTP bound to eEF1A (TEF1/2) is hydrolyzed upon codon-anticodon match between an aa-tRNA in the ribosomal RNA A-site and mRNA bound to the ribosome. Inactive eEF1A-GDP leaves the ribosome and must be recycled to eEF1A-GTP before binding another molecule of aa-tRNA. The guanine nucleotide exchange factor eEF1B catalyzes the exchange of GDP for GTP.","predictedComplex":false,"interactors":[{"ac":"EBI-6314","identifier":"P02994","identifierLink":"https://www.uniprot.org/uniprotkb/P02994/entry","name":"TEF1","description":"Elongation factor 1-alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6319","identifier":"P32471","identifierLink":"https://www.uniprot.org/uniprotkb/P32471/entry","name":"EFB1","description":"Elongation factor 1-beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11595","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6329","identifier":"P36008","identifierLink":"https://www.uniprot.org/uniprotkb/P36008/entry","name":"TEF4","description":"Elongation factor 1-gamma 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43986","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-426","complexName":"PAN1 actin cytoskeleton-regulatory complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Actin cytoskeleton-regulatory complex which is believed to be required for the internalization of endosomes during actin-coupled endocytosis. The complex links the site of endocytosis to the cell membrane-associated actin cytoskeleton, coordinating ARP2/3 stimulation at the later stages of endocytosis. Present in the late endocytic coat.","predictedComplex":false,"interactors":[{"ac":"EBI-12875","identifier":"P32521","identifierLink":"https://www.uniprot.org/uniprotkb/P32521/entry","name":"PAN1","description":"Actin cytoskeleton-regulatory complex protein PAN1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11216","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17313","identifier":"P32790","identifierLink":"https://www.uniprot.org/uniprotkb/P32790/entry","name":"SLA1","description":"Actin cytoskeleton-regulatory complex protein SLA1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15735","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6460","identifier":"P39013","identifierLink":"https://www.uniprot.org/uniprotkb/P39013/entry","name":"END3","description":"Actin cytoskeleton-regulatory complex protein END3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11216","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-427","complexName":"Eukaryotic translation initiation factor 2 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Delivers initiator methionyl-tRNA to the 40S ribosomal subunit in a eukaryotic translation initiation factor 2 (eIF2).GTP.Met-tRNA(Met) ternary complex. The resulting 43S complex, which also includes eIF3 and eIF1A, binds at or near the 5-prime end of capped eukaryotic messenger RNAs. Recognition of the AUG codon translational start site is accompanied by GTP hydrolysis (stimulated by the eIF5 complex), which releases Met-tRNA to the ribosomal peptidyl site and converts eIF2-GTP to eIF2-GDP. Binding of nucleotide exchange factor eIF2B complex (CPX-429) replaces GDP again for GTP. This activity is inhibited when phosphorylated eIF2 (alpha subunit) binds to eIF2B.  Phosphorylation of eIF2 occurs in response to nutrient starvation and thus prevents further protein synthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-8915","identifier":"P20459","identifierLink":"https://www.uniprot.org/uniprotkb/P20459/entry","name":"SUI2","description":"Eukaryotic translation initiation factor 2 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10602","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8920","identifier":"P09064","identifierLink":"https://www.uniprot.org/uniprotkb/P09064/entry","name":"SUI3","description":"Eukaryotic translation initiation factor 2 subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23001","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8924","identifier":"P32481","identifierLink":"https://www.uniprot.org/uniprotkb/P32481/entry","name":"GCD11","description":"Eukaryotic translation initiation factor 2 subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR42854","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-428","complexName":"BBSome complex","organismName":"Caenorhabditis elegans; 6239","description":"The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function.\r\n\r\nbbs-1, bbs-2, bbs-4, osm-12, bbs-8 and bbs-9 are required for proper BBSome complex assembly and its ciliary localization. bbs-5 is required for BBSome localization only.","predictedComplex":false,"interactors":[{"ac":"EBI-11712144","identifier":"Q9NEZ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NEZ7/entry","name":"bbs-1","description":"BBSome complex member BBS1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR20870","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11712162","identifier":"Q19640","identifierLink":"https://www.uniprot.org/uniprotkb/Q19640/entry","name":"bbs-2","description":"BBSome complex member bbs-2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR32465","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11712182","identifier":"Q5CZ52","identifierLink":"https://www.uniprot.org/uniprotkb/Q5CZ52/entry","name":"bbs-4","description":"BBSome complex member bbs-4","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR44186","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11712204","identifier":"O01514","identifierLink":"https://www.uniprot.org/uniprotkb/O01514/entry","name":"bbs-9","description":"Protein pthb1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR20991","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-314335","identifier":"Q21626","identifierLink":"https://www.uniprot.org/uniprotkb/Q21626/entry","name":"bbs-5","description":"BBSome complex member bbs-5","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR21351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-329026","identifier":"Q23049","identifierLink":"https://www.uniprot.org/uniprotkb/Q23049/entry","name":"bbs-8","description":"Tetratricopeptide repeat protein 8","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR44177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-331722","identifier":"Q9XW70","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XW70/entry","name":"osm-12","description":"BBSome complex member bbs-7","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR16074","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-429","complexName":"Eukaryotic translation initiation factor 2B complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Plays a critical regulatory role in eukaryotic translation initiation. Acts as a guanine nucleotide exchange factor (GEF) catalyzing the exchange of GDP on eIF2-GDP for GTP, thus reactivating eIF2 (CPX-427) and allowing subsequent rounds of translation initiation. This activity is inhibited by the when phosphorylated eIF2 (alpha subunit) binds to eIF2B. Phosphorylation of eIF2 occurs in response to nutrient starvation and thus prevents further protein synthesis. eIF2B also acts as a GDP dissociation inhibitor (GDI) displacement factor that can recruit eIF2 from the eIF2.GDP/eIF5 GDI complex prior to GEF action.","predictedComplex":false,"interactors":[{"ac":"EBI-6253","identifier":"P14741","identifierLink":"https://www.uniprot.org/uniprotkb/P14741/entry","name":"GCN3","description":"Translation initiation factor eIF2B subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45860","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6260","identifier":"P32502","identifierLink":"https://www.uniprot.org/uniprotkb/P32502/entry","name":"GCD7","description":"Translation initiation factor eIF2B subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6265","identifier":"P12754","identifierLink":"https://www.uniprot.org/uniprotkb/P12754/entry","name":"GCD2","description":"Translation initiation factor eIF2B subunit delta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10233","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6270","identifier":"P32501","identifierLink":"https://www.uniprot.org/uniprotkb/P32501/entry","name":"GCD6","description":"Translation initiation factor eIF2B subunit epsilon","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45887","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6275","identifier":"P09032","identifierLink":"https://www.uniprot.org/uniprotkb/P09032/entry","name":"GCD1","description":"Translation initiation factor eIF2B subunit gamma","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45989","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-430","complexName":"Eukaryotic translation initiation factor 4F complex, variant TIF4631","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Binds the 5-prime cap of messenger RNAs to recruit mRNA to the ribosome during translation initiation. During cap-dependent translation, eIF4G1 (TIF4631) brings the 5' end of the mRNA in proximity with the helicase eIF4A (TIF1,TIF2) through interactions with eIF4E (CDC33). Facilitates 48S pre-initiation complex formation through interaction with eIF3 (CPX-1831) in the 43S pre-initiation complex. The relatively weak helicase activity of eIF4A is presumed to be required for unwinding mRNA secondary structures. The poly(A) binding protein PAB1 can bind to eIF4G1 act to stimulate cap-dependent translation initiation, even in the absence of a poly(A) tail.","predictedComplex":false,"interactors":[{"ac":"EBI-150","identifier":"P07260","identifierLink":"https://www.uniprot.org/uniprotkb/P07260/entry","name":"CDC33","description":"Eukaryotic translation initiation factor 4E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9002","identifier":"P39935","identifierLink":"https://www.uniprot.org/uniprotkb/P39935/entry","name":"TIF4631","description":"Eukaryotic initiation factor 4F subunit p150","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23253","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9017","identifier":"P10081","identifierLink":"https://www.uniprot.org/uniprotkb/P10081/entry","name":"TIF1","description":"ATP-dependent RNA helicase eIF4A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-431","complexName":"Eukaryotic translation initiation factor 4F complex, variant TIF4632","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Binds the 5-prime cap of messenger RNAs to recruit mRNA to the ribosome during translation initiation. During cap-dependent translation, eIF4G2 (TIF4632) brings the 5' end of the mRNA in proximity with the helicase eIF4A (TIF1,TIF2) through interactions with eIF4E (CDC33). Facilitates 48S pre-initiation complex formation through interaction with eIF3 (CPX-1831) in the 43S pre-initiation complex. The relatively weak helicase activity of eIF4A is presumed to be required for unwinding mRNA secondary structures. The poly(A) binding protein PAB1 can bind to eIF4G2 act to stimulate cap-dependent translation initiation, even in the absence of a poly(A) tail.","predictedComplex":false,"interactors":[{"ac":"EBI-150","identifier":"P07260","identifierLink":"https://www.uniprot.org/uniprotkb/P07260/entry","name":"CDC33","description":"Eukaryotic translation initiation factor 4E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9006","identifier":"P39936","identifierLink":"https://www.uniprot.org/uniprotkb/P39936/entry","name":"TIF4632","description":"Eukaryotic initiation factor 4F subunit p130","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23253","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9017","identifier":"P10081","identifierLink":"https://www.uniprot.org/uniprotkb/P10081/entry","name":"TIF1","description":"ATP-dependent RNA helicase eIF4A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-432","complexName":"NoRC chromatin remodelling complex","organismName":"Homo sapiens; 9606","description":"ATP-dependent nucleosome remodeling complex that represses ribosomal gene transcription. NoRC is targeted to rDNA by the interaction of its subunit BAZ2A with TTF1 [P43699] bound to the promoter-proximal target site. NoRC also binds to 150-300 nt RNAs that are complementary to the rDNA promoter (transcripts originating from the intergenic spacer that separates rRNA genes). NoRC remodels nucleosomes at the rDNA promoter and recruits histone deacetylases (e.g. Hdac1, Hdac2), histone methyltransferase and DNA methyltransferases (e.g. Dnmt1, Dnmt3b) leading to heterochromatin formation and transcriptional silencing.  The interaction of NoRC with the  short RNA transcripts  is mediated by the TAM domain of BAZ2A and it is required for NoRC binding to chromatin and  heterochromatin  formation.","predictedComplex":false,"interactors":[{"ac":"EBI-352588","identifier":"O60264","identifierLink":"https://www.uniprot.org/uniprotkb/O60264/entry","name":"SMARCA5","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-934890","identifier":"Q9UIF9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UIF9/entry","name":"BAZ2A","description":"Bromodomain adjacent to zinc finger domain protein 2A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45915","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-433","complexName":"FACT complex","organismName":"Mus musculus; 10090","description":"FACT is an H2A-H2B histone chaperon complex that helps reorganize nucleosomes in an ATP-independent fashion. It is involved in various processes related to chromatin dynamics: DNA replication, DNA damage and repair, transcription initiation and elongation. Binds histone H2A-H2B dimers and possibly small amounts of H3H4. Facilitates RNA Pol II driven transcription through chromatin by destabilizing nucleosomal structure so that one of the H2A-H2B dimers is removed upon RNA Pol II passage. Subsequently brings back the histones and thereby maintains nucleosome integrity after RNA Pol II passage. Interacts with the active forms of the MCM complexes facilitating its unwinding activity.","predictedComplex":false,"interactors":[{"ac":"EBI-2549823","identifier":"Q920B9","identifierLink":"https://www.uniprot.org/uniprotkb/Q920B9/entry","name":"Supt16h","description":"FACT complex subunit SPT16","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13980","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2657613","identifier":"Q08943","identifierLink":"https://www.uniprot.org/uniprotkb/Q08943/entry","name":"Ssrp1","description":"FACT complex subunit SSRP1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45849","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-434","complexName":"ACF chromatin remodeling complex","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex, that regulates the even spacing of nucleosomes along the chromatin thus promoting chromatin assembly and the repression of transcription. The BAZ1A subunit can enhance and direct the process provided by the ATPase subunit, SMARCA5, probably through targeting pericentromeric heterochromatin in late S phase. Moves end-positioned nucleosomes to a predominantly central position. The ATPase activity of the complex is regulated by the length of flanking DNA. Also involved in facilitating the DNA replication process.","predictedComplex":false,"interactors":[{"ac":"EBI-352588","identifier":"O60264","identifierLink":"https://www.uniprot.org/uniprotkb/O60264/entry","name":"SMARCA5","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-927511","identifier":"Q9NRL2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NRL2/entry","name":"BAZ1A","description":"Bromodomain adjacent to zinc finger domain protein 1A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46510","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-435","complexName":"ERF1-ERF3 translation release factor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for the termination of protein synthesis which occurs when one of three stop codons (UAA, UAG or UGA) enters the ribosomal A site. eRF1 stimulates GTP binding to eRF3, inducing the GTPase activity of eRF3 that couples codon recognition and eRF1 peptidyl-tRNA hydrolysis to ensure rapid and efficient peptide release from the ribosome.","predictedComplex":false,"interactors":[{"ac":"EBI-25820308","identifier":"CHEBI:37565","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:37565","name":"gtp(4-)","description":"GTP(4-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-6533","identifier":"P12385","identifierLink":"https://www.uniprot.org/uniprotkb/P12385/entry","name":"SUP45","description":"Eukaryotic peptide chain release factor subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10113","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6540","identifier":"P05453","identifierLink":"https://www.uniprot.org/uniprotkb/P05453/entry","name":"SUP35","description":"Eukaryotic peptide chain release factor GTP-binding subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-436","complexName":"EMILIN-2 complex","organismName":"Homo sapiens; 9606","description":"Glycoprotein complex of the C1q/TNF superfamily found in the extracellular matrix (ECM) where it is an important component of the elastic fiber system. It is involved in cell adhesion, migration and proliferation, angiogenesis, blood pressure control and blood coagulation, apoptosis, platelet aggregation and possibly anti-microbial activities. Its function is strongly linked to its ability to bind integrins alpha4-beta1 (CPX-1802) and alpha9-beta1 (CPX-1816) via its gC1q domain. Also detected outside blood vessels in central nervous cell cells.","predictedComplex":false,"interactors":[{"ac":"EBI-11740176","identifier":"Q9BXX0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BXX0/entry","name":"EMILIN2","description":"EMILIN-2","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15427","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-437","complexName":"EMILIN-1 complex","organismName":"Mus musculus; 10090","description":"Glycoprotein complex of the C1q/TNF superfamily found in the extracellular matrix (ECM) where it is an important component of the elastic fiber system. It is involved in cell adhesion, migration and proliferation, angiogenesis, blood pressure control and blood coagulation, apoptosis, platelet aggregation and possibly anti-microbial activities. Its function is strongly linked to its ability to bind integrins alpha4-beta1 (CPX-3118) and alpha9-beta1 (CPX-3123) via its gC1q domain.","predictedComplex":false,"interactors":[{"ac":"EBI-906561","identifier":"Q99K41","identifierLink":"https://www.uniprot.org/uniprotkb/Q99K41/entry","name":"Emilin1","description":"EMILIN-1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15427","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-438","complexName":"EMILIN-2 complex","organismName":"Mus musculus; 10090","description":"Glycoprotein complex of the C1q/TNF superfamily found in the extracellular matrix (ECM) where it is an important component of the elastic fiber system. It is involved in cell adhesion, migration and proliferation, angiogenesis, blood pressure control and blood coagulation, apoptosis, platelet aggregation and possibly anti-microbial activities. Its function is strongly linked to its ability to bind integrins alpha4-beta1 (CPX-3118) and alpha9-beta1 (CPX-3123) via its gC1q domain. Also detected outside blood vessels in central nervous cell cells.","predictedComplex":false,"interactors":[{"ac":"EBI-11740304","identifier":"Q8K482","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K482/entry","name":"Emilin2","description":"EMILIN-2","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15427","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-439","complexName":"Beta-catenin destruction core complex, APC-AXIN2-GSK3B variant","organismName":"Homo sapiens; 9606","description":"Phosphorylates cytoplasmic beta-catenin (CTNNB1) by CSNK1A1 and glycogen synthase kinase 3 (GSK3) in the absence of WNT-signalling, thus positively controlling its continuous proteasome-mediated degradation. CSNK1A1 phosphorylates CTNNB1 on Ser-45 and primes successive phosphorylation of Thr-41, Ser-37, and Ser-33 by GSK3. Phosphorylation of CTNNB1 promotes its subsequent ubiquitination which targets the protein for degradation by the proteasome.  Without WNT, Axin is also phosphorylated by GSK3, and thereby kept in an active (‘open’) conformation for beta-catenin binding and degradation. Upon WNT stimulation, the  ternary WNT-FZ-LRP6 complex is formed and recruits the scaffold protein DVL and the beta-catenin destruction complex. As a result, GSK3 is inhibited, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activation of WNT responsive genes.","predictedComplex":false,"interactors":[{"ac":"EBI-1383726","identifier":"P48729","identifierLink":"https://www.uniprot.org/uniprotkb/P48729/entry","name":"CSNK1A1","description":"Casein kinase I isoform alpha","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11909","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373586","identifier":"P49841","identifierLink":"https://www.uniprot.org/uniprotkb/P49841/entry","name":"GSK3B","description":"Glycogen synthase kinase-3 beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4400025","identifier":"Q9Y2T1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2T1/entry","name":"AXIN2","description":"Axin-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727707","identifier":"P25054","identifierLink":"https://www.uniprot.org/uniprotkb/P25054/entry","name":"APC","description":"Adenomatous polyposis coli protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-440","complexName":"Beta-catenin destruction core complex, APC2-AXIN2-GSK3B variant","organismName":"Homo sapiens; 9606","description":"Phosphorylates cytoplasmic beta-catenin (CTNNB1) by CSNK1A1 and glycogen synthase kinase 3 (GSK3) in the absence of WNT-signalling, thus positively controlling its continuous proteasome-mediated degradation. CSNK1A1 phosphorylates CTNNB1 on Ser-45 and primes successive phosphorylation of Thr-41, Ser-37, and Ser-33 by GSK3. Phosphorylation of CTNNB1 promotes its subsequent ubiquitination which targets the protein for degradation by the proteasome.  Without WNT, Axin is also phosphorylated by GSK3, and thereby kept in an active (‘open’) conformation for beta-catenin binding and degradation. Upon WNT stimulation, the  ternary WNT-FZ-LRP6 complex is formed and recruits the scaffold protein DVL and the beta-catenin destruction complex. As a result, GSK3 is inhibited, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activation of WNT responsive genes.","predictedComplex":false,"interactors":[{"ac":"EBI-1053045","identifier":"O95996","identifierLink":"https://www.uniprot.org/uniprotkb/O95996/entry","name":"APC2","description":"Adenomatous polyposis coli protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1383726","identifier":"P48729","identifierLink":"https://www.uniprot.org/uniprotkb/P48729/entry","name":"CSNK1A1","description":"Casein kinase I isoform alpha","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11909","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373586","identifier":"P49841","identifierLink":"https://www.uniprot.org/uniprotkb/P49841/entry","name":"GSK3B","description":"Glycogen synthase kinase-3 beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4400025","identifier":"Q9Y2T1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2T1/entry","name":"AXIN2","description":"Axin-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-441","complexName":"Beta-catenin destruction core complex, APC-AXIN2-GSK3A variant","organismName":"Homo sapiens; 9606","description":"Phosphorylates cytoplasmic beta-catenin (CTNNB1) by CSNK1A1 and glycogen synthase kinase 3 (GSK3) in the absence of WNT-signalling, thus positively controlling its continuous proteasome-mediated degradation. CSNK1A1 phosphorylates CTNNB1 on Ser-45 and primes successive phosphorylation of Thr-41, Ser-37, and Ser-33 by GSK3. Phosphorylation of CTNNB1 promotes its subsequent ubiquitination which targets the protein for degradation by the proteasome.  Without Wnt, Axin is also phosphorylated by GSK3, and thereby kept in an active (‘open’) conformation for beta-catenin binding and degradation. Upon Wnt stimulation, the  ternary WNT-FZ-LRP6 complex is formed and recruits the scaffold protein DVL and the beta-catenin destruction complex. As a result, GSK3 is inhibited, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activation of Wnt responsive genes.\r\nGSK3A is normally excluded from the nucleus and appears to only accumulate there, and regulate CTNNB1 levels, following activation of calpain in response to calcium levels.","predictedComplex":false,"interactors":[{"ac":"EBI-1044067","identifier":"P49840","identifierLink":"https://www.uniprot.org/uniprotkb/P49840/entry","name":"GSK3A","description":"Glycogen synthase kinase-3 alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1383726","identifier":"P48729","identifierLink":"https://www.uniprot.org/uniprotkb/P48729/entry","name":"CSNK1A1","description":"Casein kinase I isoform alpha","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11909","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4400025","identifier":"Q9Y2T1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2T1/entry","name":"AXIN2","description":"Axin-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727707","identifier":"P25054","identifierLink":"https://www.uniprot.org/uniprotkb/P25054/entry","name":"APC","description":"Adenomatous polyposis coli protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-442","complexName":"Beta-catenin destruction core complex, APC2-AXIN1-GSK3A variant","organismName":"Homo sapiens; 9606","description":"Phosphorylates cytoplasmic beta-catenin (CTNNB1) by CSNK1A1 and glycogen synthase kinase 3 (GSK3) in the absence of WNT-signalling, thus positively controlling its continuous proteasome-mediated degradation. CSNK1A1 phosphorylates CTNNB1 on Ser-45 and primes successive phosphorylation of Thr-41, Ser-37, and Ser-33 by GSK3. Phosphorylation of CTNNB1 promotes its subsequent ubiquitination which targets the protein for degradation by the proteasome.  Without WNT, Axin is also phosphorylated by GSK3, and thereby kept in an active (‘open’) conformation for beta-catenin binding and degradation. Upon WNT stimulation, the  ternary WNT-FZ-LRP6 complex is formed and recruits the scaffold protein DVL and the beta-catenin destruction complex. As a result, GSK3 is inhibited, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activation of WNT responsive genes.\r\nGSK3A is normally excluded from the nucleus and appears to only accumulate there, and regulate CTNNB1 levels, following activation of calpain in response to calcium levels.","predictedComplex":false,"interactors":[{"ac":"EBI-1044067","identifier":"P49840","identifierLink":"https://www.uniprot.org/uniprotkb/P49840/entry","name":"GSK3A","description":"Glycogen synthase kinase-3 alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1053045","identifier":"O95996","identifierLink":"https://www.uniprot.org/uniprotkb/O95996/entry","name":"APC2","description":"Adenomatous polyposis coli protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1383726","identifier":"P48729","identifierLink":"https://www.uniprot.org/uniprotkb/P48729/entry","name":"CSNK1A1","description":"Casein kinase I isoform alpha","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11909","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-710484","identifier":"O15169","identifierLink":"https://www.uniprot.org/uniprotkb/O15169/entry","name":"AXIN1","description":"Axin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-443","complexName":"Beta-catenin destruction core complex, APC2-AXIN2-GSK3A variant","organismName":"Homo sapiens; 9606","description":"Phosphorylates cytoplasmic beta-catenin (CTNNB1) by CSNK1A1 and glycogen synthase kinase 3 (GSK3) in the absence of WNT-signalling, thus positively controlling its continuous proteasome-mediated degradation. CSNK1A1 phosphorylates CTNNB1 on Ser-45 and primes successive phosphorylation of Thr-41, Ser-37, and Ser-33 by GSK3. Phosphorylation of CTNNB1 promotes its subsequent ubiquitination which targets the protein for degradation by the proteasome.  Without WNT, Axin is also phosphorylated by GSK3, and thereby kept in an active (‘open’) conformation for beta-catenin binding and degradation. Upon WNT stimulation, the  ternary WNT-FZ-LRP6 complex is formed and recruits the scaffold protein DVL and the beta-catenin destruction complex. As a result, GSK3 is inhibited, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activation of WNT responsive genes.\r\nGSK3A is normally excluded from the nucleus and appears to only accumulate there, and regulate CTNNB1 levels, following activation of calpain in response to calcium levels.","predictedComplex":false,"interactors":[{"ac":"EBI-1044067","identifier":"P49840","identifierLink":"https://www.uniprot.org/uniprotkb/P49840/entry","name":"GSK3A","description":"Glycogen synthase kinase-3 alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1053045","identifier":"O95996","identifierLink":"https://www.uniprot.org/uniprotkb/O95996/entry","name":"APC2","description":"Adenomatous polyposis coli protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1383726","identifier":"P48729","identifierLink":"https://www.uniprot.org/uniprotkb/P48729/entry","name":"CSNK1A1","description":"Casein kinase I isoform alpha","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11909","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4400025","identifier":"Q9Y2T1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2T1/entry","name":"AXIN2","description":"Axin-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-444","complexName":"ACF chromatin remodeling complex","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex, that regulates the even spacing of nucleosomes along the chromatin thus promoting chromatin assembly and the repression of transcription. The Baz1a subunit can enhance and direct the process provided by the ATPase subunit,Smarca5, probably through targeting pericentromeric heterochromatin in late S phase. Moves end-positioned nucleosomes to a predominantly central position. The ATPase activity of the complex is regulated by the length of flanking DNA. Also involved in facilitating the DNA replication process.","predictedComplex":false,"interactors":[{"ac":"EBI-927547","identifier":"Q91ZW3","identifierLink":"https://www.uniprot.org/uniprotkb/Q91ZW3/entry","name":"Smarca5","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-927567","identifier":"O88379","identifierLink":"https://www.uniprot.org/uniprotkb/O88379/entry","name":"Baz1a","description":"Bromodomain adjacent to zinc finger domain protein 1A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46510","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-445","complexName":"Multimerin-1 complex","organismName":"Homo sapiens; 9606","description":"Glycoprotein complex of the C1q/TNF superfamily involved in cell adhesion of vascular endothelial cells and platelets via binding to integrins alphaIIb-beta3 (CPX-1799) and alphav-beta3 (CPX-1795). Binding to Factor V (P12259) and Factor Va (activated Factor V) inhibits thrombin generation. Sequestered in platelet alpha granules prior to secretion into the extracellular matrix (ECM).","predictedComplex":false,"interactors":[{"ac":"EBI-1641616","identifier":"Q13201","identifierLink":"https://www.uniprot.org/uniprotkb/Q13201/entry","name":"MMRN1","description":"Multimerin-1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15427","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-446","complexName":"CERF chromatin remodelling complex, SMARCA1 variant","organismName":"Homo sapiens; 9606","description":"Chromatin remodelling complex which plays a role in neural tube closure and reproduction. CERF complex facilitates the perturbation of chromatin structure in an ATP-dependent manner.","predictedComplex":false,"interactors":[{"ac":"EBI-11784677","identifier":"Q9BXF3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BXF3/entry","name":"CECR2","description":"Chromatin remodeling regulator CECR2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-65531027","identifier":"P28370-1","identifierLink":"https://www.uniprot.org/uniprotkb/P28370-1/entry","name":"SMARCA1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-447","complexName":"Multimerin-1 complex","organismName":"Mus musculus; 10090","description":"Glycoprotein complex of the C1q/TNF superfamily involved in cell adhesion of vascular endothelial cells and platelets via binding to integrins alphaIIb-beta3 (CPX-3116) and alphav-beta3 (CPX-3035). Binding to Factor V (O88783) and Factor Va (activated Factor V) inhibits thrombin generation. Sequestered in platelet alpha granules prior to secretion into the extracellular matrix (ECM).","predictedComplex":false,"interactors":[{"ac":"EBI-11785404","identifier":"B2RPV6","identifierLink":"https://www.uniprot.org/uniprotkb/B2RPV6/entry","name":"Mmrn1","description":"Multimerin-1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15427","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-448","complexName":"Beta-catenin destruction core complex, Apc2-Axin1-Gsk3b variant","organismName":"Mus musculus; 10090","description":"Phosphorylates cytoplasmic beta-catenin (Ctnnb1, Q02248) in the absence of WNT-signalling, thus positively controlling its continuous proteasome-mediated degradation. Csnk1a1 phosphorylates Ctnnb1 on Ser-45 and primes successive phosphorylation of Thr-41, Ser-37, and Ser-33 by GSK3. Phosphorylation of Ctnnb1 promotes its subsequent ubiquitination which targets the protein for degradation by the proteasome.  Without Wnt, Axin is also phosphorylated by GSK3, and thereby kept in an active, open conformation for beta-catenin binding and degradation. Upon Wnt stimulation, the  ternary Wnt-Fz-Lrp6 complex is formed and recruits the scaffold protein Dvl and the beta-catenin destruction complex. As a result, GSK3 is inhibited, Ctnnb1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the Tcf/Lef family, leading to activation of Wnt responsive genes.","predictedComplex":false,"interactors":[{"ac":"EBI-11785083","identifier":"Q9Z1K7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z1K7/entry","name":"Apc2","description":"Adenomatous polyposis coli protein 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2365912","identifier":"O35625","identifierLink":"https://www.uniprot.org/uniprotkb/O35625/entry","name":"Axin1","description":"Axin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-400793","identifier":"Q9WV60","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WV60/entry","name":"Gsk3b","description":"Glycogen synthase kinase-3 beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-771679","identifier":"Q8BK63","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BK63/entry","name":"Csnk1a1","description":"Casein kinase I isoform alpha","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11909","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-449","complexName":"Beta-catenin destruction core complex, Apc-Axin2-Gsk3b variant","organismName":"Mus musculus; 10090","description":"Phosphorylates cytoplasmic beta-catenin (Ctnnb1, Q02248) in the absence of WNT-signalling, thus positively controlling its continuous proteasome-mediated degradation. Csnk1a1 phosphorylates Ctnnb1 on Ser-45 and primes successive phosphorylation of Thr-41, Ser-37, and Ser-33 by GSK3. Phosphorylation of Ctnnb1 promotes its subsequent ubiquitination which targets the protein for degradation by the proteasome.  Without Wnt, Axin is also phosphorylated by GSK3, and thereby kept in an active, open conformation for beta-catenin binding and degradation. Upon Wnt stimulation, the  ternary Wnt-Fz-Lrp6 complex is formed and recruits the scaffold protein Dvl and the beta-catenin destruction complex. As a result, GSK3 is inhibited, Ctnnb1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the Tcf/Lef family, leading to activation of Wnt responsive genes.","predictedComplex":false,"interactors":[{"ac":"EBI-400793","identifier":"Q9WV60","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WV60/entry","name":"Gsk3b","description":"Glycogen synthase kinase-3 beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7690990","identifier":"O88566","identifierLink":"https://www.uniprot.org/uniprotkb/O88566/entry","name":"Axin2","description":"Axin-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-771679","identifier":"Q8BK63","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BK63/entry","name":"Csnk1a1","description":"Casein kinase I isoform alpha","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11909","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7848277","identifier":"Q61315","identifierLink":"https://www.uniprot.org/uniprotkb/Q61315/entry","name":"Apc","description":"Adenomatous polyposis coli protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-450","complexName":"Multimerin-2 complex","organismName":"Homo sapiens; 9606","description":"Glycoprotein complex of the C1q/TNF superfamily involved in cell adhesion of vascular endothelial cells via binding to VEGF-A (P15692, complex CPX-1977) and involved in epithelial tube formation. Impairs cell migration, organization of a functional vessel network, tumor growth and tumor angiogenesis and downregulates tyrosine kinase activity of VEGFR2 (P35968) by interfering with the VEGF-A/VEGFR2 interaction.","predictedComplex":false,"interactors":[{"ac":"EBI-2623273","identifier":"Q9H8L6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H8L6/entry","name":"MMRN2","description":"Multimerin-2","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15427","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-451","complexName":"Multimerin-2 complex","organismName":"Mus musculus; 10090","description":"Glycoprotein complex of the C1q/TNF superfamily involved in cell adhesion of vascular endothelial cells via binding to Vegf-A (Q00731, complex CPX-3160) and involved in epithelial tube formation. Impairs cell migration, organization of a functional vessel network, tumor growth and tumor angiogenesis and downregulates tyrosine kinase activity of VEGFR2 (P35918) by interfering with the VEGF-A/VEGFR2 interaction.","predictedComplex":false,"interactors":[{"ac":"EBI-11785492","identifier":"A6H6E2","identifierLink":"https://www.uniprot.org/uniprotkb/A6H6E2/entry","name":"Mmrn2","description":"Multimerin-2","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15427","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-452","complexName":"Beta-catenin destruction core complex, Apc2-Axin2-Gsk3b","organismName":"Mus musculus; 10090","description":"Phosphorylates cytoplasmic beta-catenin (Ctnnb1, Q02248) in the absence of WNT-signalling, thus positively controlling its continuous proteasome-mediated degradation. Csnk1a1 phosphorylates Ctnnb1 on Ser-45 and primes successive phosphorylation of Thr-41, Ser-37, and Ser-33 by GSK3. Phosphorylation of Ctnnb1 promotes its subsequent ubiquitination which targets the protein for degradation by the proteasome.  Without Wnt, Axin is also phosphorylated by GSK3, and thereby kept in an active, open conformation for beta-catenin binding and degradation. Upon Wnt stimulation, the  ternary Wnt-Fz-Lrp6 complex is formed and recruits the scaffold protein Dvl and the beta-catenin destruction complex. As a result, GSK3 is inhibited, Ctnnb1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the Tcf/Lef family, leading to activation of Wnt responsive genes.","predictedComplex":false,"interactors":[{"ac":"EBI-11785083","identifier":"Q9Z1K7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z1K7/entry","name":"Apc2","description":"Adenomatous polyposis coli protein 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-400793","identifier":"Q9WV60","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WV60/entry","name":"Gsk3b","description":"Glycogen synthase kinase-3 beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7690990","identifier":"O88566","identifierLink":"https://www.uniprot.org/uniprotkb/O88566/entry","name":"Axin2","description":"Axin-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-771679","identifier":"Q8BK63","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BK63/entry","name":"Csnk1a1","description":"Casein kinase I isoform alpha","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11909","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-453","complexName":"Beta-catenin destruction core complex, Apc-Axin1-Gsk3a variant","organismName":"Mus musculus; 10090","description":"Phosphorylates cytoplasmic beta-catenin (Ctnnb1, Q02248) in the absence of WNT-signalling, thus positively controlling its continuous proteasome-mediated degradation. Csnk1a1 phosphorylates Ctnnb1 on Ser-45 and primes successive phosphorylation of Thr-41, Ser-37, and Ser-33 by GSK3. Phosphorylation of Ctnnb1 promotes its subsequent ubiquitination which targets the protein for degradation by the proteasome.  Without Wnt, Axin is also phosphorylated by GSK3, and thereby kept in an active, open conformation for beta-catenin binding and degradation. Upon Wnt stimulation, the  ternary Wnt-Fz-Lrp6 complex is formed and recruits the scaffold protein Dvl and the beta-catenin destruction complex. As a result, GSK3 is inhibited, Ctnnb1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the Tcf/Lef family, leading to activation of Wnt responsive genes.\r\nGsk3a is normally excluded from the nucleus and appears to only accumulate there, and regulate Ctnnb1 levels, following activation of calpain in response to calcium levels.","predictedComplex":false,"interactors":[{"ac":"EBI-1203218","identifier":"Q2NL51","identifierLink":"https://www.uniprot.org/uniprotkb/Q2NL51/entry","name":"Gsk3a","description":"Glycogen synthase kinase-3 alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2365912","identifier":"O35625","identifierLink":"https://www.uniprot.org/uniprotkb/O35625/entry","name":"Axin1","description":"Axin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-771679","identifier":"Q8BK63","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BK63/entry","name":"Csnk1a1","description":"Casein kinase I isoform alpha","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11909","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7848277","identifier":"Q61315","identifierLink":"https://www.uniprot.org/uniprotkb/Q61315/entry","name":"Apc","description":"Adenomatous polyposis coli protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-454","complexName":"CERF chromatin remodelling complex, Smarca1 variant","organismName":"Mus musculus; 10090","description":"Chromatin remodelling complex which plays a role in neural tube closure and reproduction. CERF complex facilitates the perturbation of chromatin structure in an ATP-dependent manner.\r\n\r\nCerc2 Loss-of-function mutations results in lethal neural tube defect and is associated with suboptimal spermatogenesis in mice that reach adulthood.","predictedComplex":false,"interactors":[{"ac":"EBI-11786213","identifier":"Q6PGB8","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PGB8/entry","name":"Smarca1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11786531","identifier":"E9Q2Z1","identifierLink":"https://www.uniprot.org/uniprotkb/E9Q2Z1/entry","name":"Cecr2","description":"Chromatin remodeling regulator CECR2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR47092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-455","complexName":"RSF complex","organismName":"Homo sapiens; 9606","description":"A nucleosome remodeling complex that participates in chromatin assembly and facilitates DNA transcription. The RSF1 subunit functions as the histone chaperone through an association with the H3/H4 tetramer and is independent of the histone tails. The histone octamer (composed of H2A, H2B, H3 & H4) is required for the RSF complex to bind DNA. The SMARCA5 subunit provides the energy for the nucleosome spacing activity and is dependent on the histone tails.","predictedComplex":false,"interactors":[{"ac":"EBI-352588","identifier":"O60264","identifierLink":"https://www.uniprot.org/uniprotkb/O60264/entry","name":"SMARCA5","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-926768","identifier":"Q96T23","identifierLink":"https://www.uniprot.org/uniprotkb/Q96T23/entry","name":"RSF1","description":"Remodeling and spacing factor 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14296","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-456","complexName":"Beta-catenin destruction core complex, Apc2-Axin1-Gsk3a variant","organismName":"Mus musculus; 10090","description":"Phosphorylates cytoplasmic beta-catenin (Ctnnb1, Q02248) in the absence of WNT-signalling, thus positively controlling its continuous proteasome-mediated degradation. Csnk1a1 phosphorylates Ctnnb1 on Ser-45 and primes successive phosphorylation of Thr-41, Ser-37, and Ser-33 by GSK3. Phosphorylation of Ctnnb1 promotes its subsequent ubiquitination which targets the protein for degradation by the proteasome.  Without Wnt, Axin is also phosphorylated by GSK3, and thereby kept in an active, open conformation for beta-catenin binding and degradation. Upon Wnt stimulation, the  ternary Wnt-Fz-Lrp6 complex is formed and recruits the scaffold protein Dvl and the beta-catenin destruction complex. As a result, GSK3 is inhibited, Ctnnb1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the Tcf/Lef family, leading to activation of Wnt responsive genes.\r\nGsk3a is normally excluded from the nucleus and appears to only accumulate there, and regulate Ctnnb1 levels, following activation of calpain in response to calcium levels.","predictedComplex":false,"interactors":[{"ac":"EBI-11785083","identifier":"Q9Z1K7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z1K7/entry","name":"Apc2","description":"Adenomatous polyposis coli protein 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1203218","identifier":"Q2NL51","identifierLink":"https://www.uniprot.org/uniprotkb/Q2NL51/entry","name":"Gsk3a","description":"Glycogen synthase kinase-3 alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2365912","identifier":"O35625","identifierLink":"https://www.uniprot.org/uniprotkb/O35625/entry","name":"Axin1","description":"Axin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-771679","identifier":"Q8BK63","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BK63/entry","name":"Csnk1a1","description":"Casein kinase I isoform alpha","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11909","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-457","complexName":"Beta-catenin destruction core complex, Apc-Axin2-Gsk3a variant","organismName":"Mus musculus; 10090","description":"Phosphorylates cytoplasmic beta-catenin (Ctnnb1, Q02248) in the absence of WNT-signalling, thus positively controlling its continuous proteasome-mediated degradation. Csnk1a1 phosphorylates Ctnnb1 on Ser-45 and primes successive phosphorylation of Thr-41, Ser-37, and Ser-33 by GSK3. Phosphorylation of Ctnnb1 promotes its subsequent ubiquitination which targets the protein for degradation by the proteasome.  Without Wnt, Axin is also phosphorylated by GSK3, and thereby kept in an active, open conformation for beta-catenin binding and degradation. Upon Wnt stimulation, the  ternary Wnt-Fz-Lrp6 complex is formed and recruits the scaffold protein Dvl and the beta-catenin destruction complex. As a result, GSK3 is inhibited, Ctnnb1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the Tcf/Lef family, leading to activation of Wnt responsive genes.","predictedComplex":false,"interactors":[{"ac":"EBI-1203218","identifier":"Q2NL51","identifierLink":"https://www.uniprot.org/uniprotkb/Q2NL51/entry","name":"Gsk3a","description":"Glycogen synthase kinase-3 alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7690990","identifier":"O88566","identifierLink":"https://www.uniprot.org/uniprotkb/O88566/entry","name":"Axin2","description":"Axin-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-771679","identifier":"Q8BK63","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BK63/entry","name":"Csnk1a1","description":"Casein kinase I isoform alpha","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11909","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7848277","identifier":"Q61315","identifierLink":"https://www.uniprot.org/uniprotkb/Q61315/entry","name":"Apc","description":"Adenomatous polyposis coli protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-458","complexName":"Beta-catenin destruction core complex, Apc2-Axin2-Gsk3a variant","organismName":"Mus musculus; 10090","description":"Phosphorylates cytoplasmic beta-catenin (Ctnnb1, Q02248) in the absence of WNT-signalling, thus positively controlling its continuous proteasome-mediated degradation. Csnk1a1 phosphorylates Ctnnb1 on Ser-45 and primes successive phosphorylation of Thr-41, Ser-37, and Ser-33 by GSK3. Phosphorylation of Ctnnb1 promotes its subsequent ubiquitination which targets the protein for degradation by the proteasome.  Without Wnt, Axin is also phosphorylated by GSK3, and thereby kept in an active, open conformation for beta-catenin binding and degradation. Upon Wnt stimulation, the  ternary Wnt-Fz-Lrp6 complex is formed and recruits the scaffold protein Dvl and the beta-catenin destruction complex. As a result, GSK3 is inhibited, Ctnnb1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the Tcf/Lef family, leading to activation of Wnt responsive genes.\r\nGsk3a is normally excluded from the nucleus and appears to only accumulate there, and regulate Ctnnb1 levels, following activation of calpain in response to calcium levels.","predictedComplex":false,"interactors":[{"ac":"EBI-11785083","identifier":"Q9Z1K7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z1K7/entry","name":"Apc2","description":"Adenomatous polyposis coli protein 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1203218","identifier":"Q2NL51","identifierLink":"https://www.uniprot.org/uniprotkb/Q2NL51/entry","name":"Gsk3a","description":"Glycogen synthase kinase-3 alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7690990","identifier":"O88566","identifierLink":"https://www.uniprot.org/uniprotkb/O88566/entry","name":"Axin2","description":"Axin-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-771679","identifier":"Q8BK63","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BK63/entry","name":"Csnk1a1","description":"Casein kinase I isoform alpha","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11909","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-459","complexName":"Nuclear export complex FRAT1-GSK3B","organismName":"Homo sapiens; 9606","description":"Role in beta-catenin destruction complex disassembly. GSK3B-FRAT1 cannot bind to Axin and thus GSK3B is inhibited from participating in the Axin-dependent phosphorylation of CTNNB1. Initially forms a quaternary FRAT1-DVL-GSK3B-AXIN complex which dissociates, with GSK3B maintaining its association with FRAT1. GSK3B-FRAT1 then translocates from the nucleus to the cytoplasm. The binding of FRAT1 does not inhibit GSK3B from phosphorylating glycogen synthase.","predictedComplex":false,"interactors":[{"ac":"EBI-373586","identifier":"P49841","identifierLink":"https://www.uniprot.org/uniprotkb/P49841/entry","name":"GSK3B","description":"Glycogen synthase kinase-3 beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3934879","identifier":"Q92837","identifierLink":"https://www.uniprot.org/uniprotkb/Q92837/entry","name":"FRAT1","description":"Proto-oncogene FRAT1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR35154","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-460","complexName":"Platelet glycoprotein Ia* complex","organismName":"Homo sapiens; 9606","description":"Glycoprotein complex of the C1q/TNF superfamily involved in cell adhesion of vascular endothelial cells and platelets via binding to integrins alphaIIb-beta3 (CPX-1799) and alphav-beta3 (CPX-1795). Binding to Factor V (P12259) and Factor Va (activated Factor V) inhibits thrombin generation. Sequestered in platelet alpha granules prior to secretion into the extracellular matrix (ECM).","predictedComplex":false,"interactors":[{"ac":"EBI-11787214","identifier":"Q13201-PRO_0000367047","identifierLink":"https://www.uniprot.org/uniprotkb/Q13201-PRO_0000367047/entry","name":"MMRN1","description":"Platelet glycoprotein Ia*","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-461","complexName":"155 kDa platelet multimerin complex","organismName":"Homo sapiens; 9606","description":"Glycoprotein complex of the C1q/TNF superfamily involved in cell adhesion of vascular endothelial cells and platelets via binding to integrins alphaIIb-beta3 (CPX-1799) and alphav-beta3 (CPX-1795). Binding to Factor V (P12259) and Factor Va (activated Factor V) inhibits thrombin generation. Sequestered in platelet alpha granules prior to secretion into the extracellular matrix (ECM).","predictedComplex":false,"interactors":[{"ac":"EBI-11787271","identifier":"Q13201-PRO_0000367048","identifierLink":"https://www.uniprot.org/uniprotkb/Q13201-PRO_0000367048/entry","name":"MMRN1","description":"155 kDa platelet multimerin","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-462","complexName":"Nuclear export complex FRAT2-GSK3B","organismName":"Homo sapiens; 9606","description":"Role in beta-catenin destruction complex disassembly. GSK3B-FRAT2 cannot bind to Axin and thus GSK3B is inhibited from participating in the Axin-dependent phosphorylation of CTNNB1. Initially forms a quaternary FRAT2-DVL-GSK3B-AXIN complex which dissociates, with GSK3B maintaining its association with FRAT2. GSK3B-FRAT2 then translocates from the nucleus to the cytoplasm. The binding of FRAT2 does not inhibit GSK3B from phosphorylating glycogen synthase.","predictedComplex":false,"interactors":[{"ac":"EBI-373586","identifier":"P49841","identifierLink":"https://www.uniprot.org/uniprotkb/P49841/entry","name":"GSK3B","description":"Glycogen synthase kinase-3 beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6256130","identifier":"O75474","identifierLink":"https://www.uniprot.org/uniprotkb/O75474/entry","name":"FRAT2","description":"GSK-3-binding protein FRAT2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR35154","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-463","complexName":"RSF complex","organismName":"Mus musculus; 10090","description":"A nucleosome remodeling complex that participates in chromatin assembly and facilitates DNA transcription. The Rsf1 subunit functions as the histone chaperone through an association with the H3/H4 tetramer and is independent of the histone tails. The histone octamer (composed of H2A, H2B, H3 & H4) is required for the RSF complex to bind DNA. The Smarca5 subunit provides the energy for the nucleosome spacing activity and is dependent on the histone tails.","predictedComplex":false,"interactors":[{"ac":"EBI-11789393","identifier":"E9PWW9","identifierLink":"https://www.uniprot.org/uniprotkb/E9PWW9/entry","name":"Rsf1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14296","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-927547","identifier":"Q91ZW3","identifierLink":"https://www.uniprot.org/uniprotkb/Q91ZW3/entry","name":"Smarca5","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-464","complexName":"Nuclear export complex Frat3-Gsk3b","organismName":"Mus musculus; 10090","description":"Role in beta-catenin destruction complex disassembly. Gsk3b-Frat3 cannot bind to Axin and thus Gsk3b is inhibited from participating in the Axin-dependent phosphorylation of Ctnnb1. Initially forms a quaternary Frat3-Dvl-Gsk3b-AXIN complex which dissociates, with Gsk3b maintaining its association with Frat3. Gsk3b-Frat3 then translocates from the nucleus to the cytoplasm. The binding of Frat3 does not inhibit Gsk3b from phosphorylating glycogen synthase.","predictedComplex":false,"interactors":[{"ac":"EBI-11789470","identifier":"Q9WVA7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WVA7/entry","name":"Peg12","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR35154","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-400793","identifier":"Q9WV60","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WV60/entry","name":"Gsk3b","description":"Glycogen synthase kinase-3 beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-465","complexName":"DOM34-HBS1 ribosome dissociation complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Mediates dissociation of inactive 80S ribosomes associated in a non-translating, inactive pool, for example following stress-induced global shut-down of translation. Binds to the ribosomal A site. GTP hydrolysis, dissociation of HBS1 and accommodation of DOM34 in the ribosome, results in the binding of RLI1 (Q03195) followed by ATP-dependent subunit dissociation. Also plays a role in RNA quality control in No-Go decay, releasing ribosomes that are stalled at the 3'-end of mRNAs lacking a termination codon.","predictedComplex":false,"interactors":[{"ac":"EBI-6012","identifier":"P33309","identifierLink":"https://www.uniprot.org/uniprotkb/P33309/entry","name":"DOM34","description":"Protein DOM34","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10853","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8194","identifier":"P32769","identifierLink":"https://www.uniprot.org/uniprotkb/P32769/entry","name":"HBS1","description":"Elongation factor 1 alpha-like protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-989053","identifier":"CHEBI:15996","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15996","name":"gtp","description":"guanosine triphosphate - GTP","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-466","complexName":"Tenascin-C complex","organismName":"Homo sapiens; 9606","description":"A matricellular glycoprotein complex of the extracellular matrix found in the basement membrane of many cell types. Its expression is highly specific and restricted in space and time: it is expressed transiently in many developing organs and persists in the adult mainly in a few structures bearing high tensile stress, such as tendons, ligaments, and the smooth muscle walls of arteries. Transcriptionally regulated by a large number of transcription factors, growth factors and cytokines as well as mechanical stress and negatively regulated by microRNAs (e.g. miR-335). Involved in the regulation of many embryogenesis and organogenesis pathways such as cell adhesion, cell migration, cell growth, gene expression of PDGFRA/PDGFRB (P16234/P09619) (through activation via Wnt/beta-catenin signalling pathway), epithelial morphogenesis and neuromuscular junction development. Only widely expressed in adult tissues upon inflammation in response to injury and also appears to play a role in peripheral nervous system axon regeneration. May act as a pro-oncogene. Binds syndecans and a range of different integrins.","predictedComplex":false,"interactors":[{"ac":"EBI-9979894","identifier":"P24821","identifierLink":"https://www.uniprot.org/uniprotkb/P24821/entry","name":"TNC","description":"Tenascin","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46708","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-467","complexName":"eNoSc complex","organismName":"Homo sapiens; 9606","description":"A chromatin silencing complex that recruits histone-modifying enzymes and upregulates silencing of rDNA in response to glucose starvation. Upon glucose starvation, elevation of NAD+/NADP+ ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at Lys-9 (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. \r\n\r\nGlucose deprivation increases the affinity between SIRT1 and SUV39H1 and consequently strengthens the interaction between RRP8 and SIRT1.","predictedComplex":false,"interactors":[{"ac":"EBI-1802965","identifier":"Q96EB6","identifierLink":"https://www.uniprot.org/uniprotkb/Q96EB6/entry","name":"SIRT1","description":"NAD-dependent protein deacetylase sirtuin-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11085","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2008793","identifier":"O43159","identifierLink":"https://www.uniprot.org/uniprotkb/O43159/entry","name":"RRP8","description":"Ribosomal RNA-processing protein 8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12787","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-349968","identifier":"O43463","identifierLink":"https://www.uniprot.org/uniprotkb/O43463/entry","name":"SUV39H1","description":"Histone-lysine N-methyltransferase SUV39H1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46223","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-468","complexName":"eNoSc complex","organismName":"Mus musculus; 10090","description":"A chromatin silencing complex that recruits histone-modifying enzymes and upregulates silencing of rDNA in response to glucose starvation. Upon glucose starvation, elevation of NAD+/NADP+ ratio activates Sirt1, leading to histone H3 deacetylation followed by dimethylation of H3 at Lys-9 (H3K9me2) by Suv39h1 and the formation of silent chromatin in the rDNA locus. \r\n\r\nGlucose deprivation increases the affinity between Sirt1 and Suv39h1 and consequently  strengthens the interaction between Rrp8 and Sirt1.","predictedComplex":false,"interactors":[{"ac":"EBI-1802585","identifier":"Q923E4","identifierLink":"https://www.uniprot.org/uniprotkb/Q923E4/entry","name":"Sirt1","description":"NAD-dependent protein deacetylase sirtuin-1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11085","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302230","identifier":"O54864","identifierLink":"https://www.uniprot.org/uniprotkb/O54864/entry","name":"Suv39h1","description":"Histone-lysine N-methyltransferase SUV39H1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46223","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8387725","identifier":"Q9DB85","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DB85/entry","name":"Rrp8","description":"Ribosomal RNA-processing protein 8","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12787","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-469","complexName":"L3MBTL1 complex","organismName":"Homo sapiens; 9606","description":"L3MBTL1 complex functions as a transcriptional repressor, by compacting chromatin in a manner that is strictly dependent on histone methylation marks, specifically H4K20me1/2 and H1bK26me1/2. It also activates chromatin looping.","predictedComplex":false,"interactors":[{"ac":"EBI-1265089","identifier":"Q9Y468","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y468/entry","name":"L3MBTL1","description":"Lethal(3)malignant brain tumor-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12247","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-491274","identifier":"P06400","identifierLink":"https://www.uniprot.org/uniprotkb/P06400/entry","name":"RB1","description":"Retinoblastoma-associated protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-78176","identifier":"Q13185","identifierLink":"https://www.uniprot.org/uniprotkb/Q13185/entry","name":"CBX3","description":"Chromobox protein homolog 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22812","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-470","complexName":"L3MBTL1 complex","organismName":"Mus musculus; 10090","description":"L3MBTL1 complex functions as a transcriptional repressor, by compacting chromatin in a manner that is strictly dependent on histone methylation marks, specifically H4K20me1/2 and Hb1K26me1/2. It also activates chromatin looping.","predictedComplex":false,"interactors":[{"ac":"EBI-11792446","identifier":"A2A5N8","identifierLink":"https://www.uniprot.org/uniprotkb/A2A5N8/entry","name":"L3mbtl1","description":"Lethal(3)malignant brain tumor-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12247","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-78162","identifier":"P23198","identifierLink":"https://www.uniprot.org/uniprotkb/P23198/entry","name":"Cbx3","description":"Chromobox protein homolog 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22812","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-971782","identifier":"P13405","identifierLink":"https://www.uniprot.org/uniprotkb/P13405/entry","name":"Rb1","description":"Retinoblastoma-associated protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-471","complexName":"Tenascin-C complex","organismName":"Mus musculus; 10090","description":"A matricellular glycoprotein complex of the extracellular matrix found in the basement membrane of many cell types. Its expression is highly specific and restricted in space and time: it is expressed transiently in many developing organs and persists in the adult mainly in a few structures bearing high tensile stress, such as tendons, ligaments, and the smooth muscle walls of arteries. Transcriptionally regulated by a large number of transcription factors, growth factors and cytokines as well as mechanical stress and negatively regulated by microRNAs (e.g. miR-335). Involved in the regulation of many embryogenesis and organogenesis pathways such as cell adhesion, cell migration, cell growth, gene expression of Pdgfra and Pdgfrb (P26618/P05622) (through activation via Wnt/beta-catenin signalling pathway), epithelial morphogenesis and neuromuscular junction development. Only widely expressed in adult tissues upon inflammation in response to injury and also appears to play a role in peripheral nervous system axon regeneration. May act as a pro-oncogene. Binds syndecans and a range of different integrins.","predictedComplex":false,"interactors":[{"ac":"EBI-8315273","identifier":"Q80YX1","identifierLink":"https://www.uniprot.org/uniprotkb/Q80YX1/entry","name":"Tnc","description":"Tenascin","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46708","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-475","complexName":"Vitronectin-PAI-1 complex","organismName":"Homo sapiens; 9606","description":"Regulates the activity of the plasminogen activation system, an extracellular proteolytic cascade. Vitronectin binding extends the lifetime of active PAI-1, by slowing its transition to an inactive latent form, thus directly influencing angiogenesis and affecting cell adhesion and motility. Inhibits fibrinolysis, the breakdown of the fibrin clot which is the product of coagulation, transition to the inactive latent form.","predictedComplex":false,"interactors":[{"ac":"EBI-1036653","identifier":"P04004","identifierLink":"https://www.uniprot.org/uniprotkb/P04004/entry","name":"VTN","description":"Vitronectin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22917","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-953978","identifier":"P05121","identifierLink":"https://www.uniprot.org/uniprotkb/P05121/entry","name":"SERPINE1","description":"Plasminogen activator inhibitor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11461","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-476","complexName":"Nuclear exosome complex, DIS3-EXOSC10 variant","organismName":"Homo sapiens; 9606","description":"3' -5' exo- and endoribonuclease complex that is involved in RNA maturation and degradation which include the removal of unstable and aberrant transcripts and may also regulate the levels of specific transcripts in response to environmental factors. Restricted to processing linear and circular single-stranded RNAs only. RNAs with complex secondary structures, particularly at the 3' end of the molecule, may have to be unwound or pre-processed by co-factors prior to entering the complex. Although some RNAs may be targeted directly to the catalytic subunits, the majority of substrates enter the barrel-like structure of the exosome through a pore at the centre of the cap and are threaded through the central channel in a 3' to 5' orientation. The ribonuclease activity of the catalytic subunits facilitates the degradation process. \r\n\r\nA number of different exosome variants exist in the cell that are distinguished by the inclusion of their respective catalytic subunit(s): the main cytoplasmic exosome with DIS3L (CPX-592) or DIS3L and EXOSC10 (CPX-600),  the main nuclear exosome with DIS3 and EXOSC10 (this complex), the nucleolar exosome with EXOSC10 (CPX-591) and a rare variant found in both, the nucleus and cytosol, (CPX-593). \r\n\r\nThe nuclear RNA exosome is involved in a) proper maturation of most RNA species such as intron-removal from pre-mRNAs and tRNA precursors and rRNA, snRNA, snoRNA, lncRNA and enhancer RNA processing, especially the removal of their 3-prime ends, b) the elimination of RNA processing by-products and non-coding, cryptic transcripts, such as promoter-upstream transcripts (PROMPTs), enhancer RNAs (eRNAs), heterochromatin-forming repetitive elements (ribosomal DNA repeats and centromeres) and long non-coding RNAs, c) the elimination of mRNAs with processing defects and mRNAs that fail to undergo proper splicing or 3-prime end formation and d) gene expression either by mRNA processing or coordination of intron retention leading to regulation of decay of otherwise intact mRNAs. Nuclear exosome activity therefore limits or excludes export of target RNAs to the cytoplasm. Possibly involved in the degradation of mRNAs with defects in their co-transcriptional packaging into ribonucleoprotein particles (mRNPs), retention of aberrant transcripts on the chromatin, immunoglobulin (Ig) class switch recombination (CSR), Ig variable region somatic hypermutation (SHM) transcription termination or DNA damage repair processes. \r\n\r\nA small amount of this complex has also been found in the cytoplasm.","predictedComplex":false,"interactors":[{"ac":"EBI-2841747","identifier":"Q5RKV6","identifierLink":"https://www.uniprot.org/uniprotkb/Q5RKV6/entry","name":"EXOSC6","description":"Exosome complex component MTR3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301735","identifier":"Q13868","identifierLink":"https://www.uniprot.org/uniprotkb/Q13868/entry","name":"EXOSC2","description":"Exosome complex component RRP4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347966","identifier":"Q06265","identifierLink":"https://www.uniprot.org/uniprotkb/Q06265/entry","name":"EXOSC9","description":"Exosome complex component RRP45","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358236","identifier":"Q01780","identifierLink":"https://www.uniprot.org/uniprotkb/Q01780/entry","name":"EXOSC10","description":"Exosome complex component 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12124","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371823","identifier":"Q9NPD3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPD3/entry","name":"EXOSC4","description":"Exosome complex component RRP41","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371841","identifier":"Q15024","identifierLink":"https://www.uniprot.org/uniprotkb/Q15024/entry","name":"EXOSC7","description":"Exosome complex component RRP42","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371866","identifier":"Q9NQT5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NQT5/entry","name":"EXOSC3","description":"Exosome complex component RRP40","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371876","identifier":"Q9NQT4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NQT4/entry","name":"EXOSC5","description":"Exosome complex component RRP46","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371892","identifier":"Q9Y3B2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3B2/entry","name":"EXOSC1","description":"Exosome complex component CSL4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12686","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371922","identifier":"Q96B26","identifierLink":"https://www.uniprot.org/uniprotkb/Q96B26/entry","name":"EXOSC8","description":"Exosome complex component RRP43","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373539","identifier":"Q9Y2L1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2L1/entry","name":"DIS3","description":"Exosome complex exonuclease RRP44","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23355","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-477","complexName":"CRL4-DDB2 E3 ubiquitin ligase complex, CUL4A variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor CRBN. The complex recognises UV-induced cyclobutane pyrimidine dimers in chromatin and facilitates nucleotide excision repair. Ubiquitinates XPC (Q01831), histones and other chromatin-associated proteins located within approximately 100A around the DNA lesion. Ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair. Mutations in DDB2 can cause Xeroderma pigmentosum and other solar photosensitivity related diseases. Inactivated by the binding of the COP9 signalosome (CPX-1870/CPX-1871) which is overcome by substrate binding to the DDB2 subunit.","predictedComplex":false,"interactors":[{"ac":"EBI-1176171","identifier":"Q92466","identifierLink":"https://www.uniprot.org/uniprotkb/Q92466/entry","name":"DDB2","description":"DNA damage-binding protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15169","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456106","identifier":"Q13619","identifierLink":"https://www.uniprot.org/uniprotkb/Q13619/entry","name":"CUL4A","description":"Cullin-4A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-479","complexName":"Bloc-1 complex","organismName":"Caenorhabditis elegans; 6239","description":"Implicated in the formation and/or maturation of tubular vesicular intermediates between endosomes and lysosome-related organelles. Possible role in intracellular endosomal trafficking modulating SNARE localisation and activity. Involved in gut granule biogenesis.","predictedComplex":false,"interactors":[{"ac":"EBI-11838859","identifier":"Q95XD3","identifierLink":"https://www.uniprot.org/uniprotkb/Q95XD3/entry","name":"blos-2","description":"Biogenesis of lysosome-related organelles complex 1 subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR46479","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11838869","identifier":"O01822","identifierLink":"https://www.uniprot.org/uniprotkb/O01822/entry","name":"glo-2","description":"Biogenesis of lysosome-related organelles complex 1 subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-11838885","identifier":"Q18446","identifierLink":"https://www.uniprot.org/uniprotkb/Q18446/entry","name":"mutd-1","description":"Biogenesis of lysosome-related organelles complex 1 subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-11838896","identifier":"O44445","identifierLink":"https://www.uniprot.org/uniprotkb/O44445/entry","name":"snpn-1","description":"SNAPIN protein homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR31305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-322961","identifier":"Q9XWQ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XWQ1/entry","name":"dsbn-1","description":"Dysbindin protein homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-327378","identifier":"Q22756","identifierLink":"https://www.uniprot.org/uniprotkb/Q22756/entry","name":"blos-4","description":"Biogenesis of lysosome-related organelles complex 1 subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-328037","identifier":"Q22616","identifierLink":"https://www.uniprot.org/uniprotkb/Q22616/entry","name":"blos-1","description":"Biogenesis of lysosome-related organelles complex 1 subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-480","complexName":"AP-1 transcription factor complex FOS-JUN-NFATC2","organismName":"Homo sapiens; 9606","description":"Member of the AP-1 transcription factor family which assemble through the homo- or hetrodimerization of proteins containing a characteristic bZIP domain (basic region leucine zipper). Regulates DNA transcription and gene expression of many immuno-response genes.","predictedComplex":false,"interactors":[{"ac":"EBI-716258","identifier":"Q13469","identifierLink":"https://www.uniprot.org/uniprotkb/Q13469/entry","name":"NFATC2","description":"Nuclear factor of activated T-cells, cytoplasmic 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12533","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-852823","identifier":"P05412","identifierLink":"https://www.uniprot.org/uniprotkb/P05412/entry","name":"JUN","description":"Transcription factor Jun","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-852851","identifier":"P01100","identifierLink":"https://www.uniprot.org/uniprotkb/P01100/entry","name":"FOS","description":"Protein c-Fos","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-478","complexName":"ERCC1-XPF endonuclease complex","organismName":"Homo sapiens; 9606","description":"Structure-specific DNA endonuclease with a role in multiple DNA repair pathways. Participates in nucleotide excision repair mechanism by incising a DNA strand on the 5-prime side of the lesion. The complex is also involved in homologous recombination that assists in removing interstrand cross-links.","predictedComplex":false,"interactors":[{"ac":"EBI-12434851","identifier":"P07992-1","identifierLink":"https://www.uniprot.org/uniprotkb/P07992-1/entry","name":"ERCC1","description":"DNA excision repair protein ERCC-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2370770","identifier":"Q92889","identifierLink":"https://www.uniprot.org/uniprotkb/Q92889/entry","name":"ERCC4","description":"DNA repair endonuclease XPF","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10150","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-481","complexName":"MCL-1-BIM complex","organismName":"Homo sapiens; 9606","description":"An apoptotic regulatory complex where pro-apoptotic, BH3 domain-containing BCL2L11 can inhibit anti-apoptotic MCL1 and vice versa.","predictedComplex":false,"interactors":[{"ac":"EBI-526406","identifier":"O43521","identifierLink":"https://www.uniprot.org/uniprotkb/O43521/entry","name":"BCL2L11","description":"Bcl-2-like protein 11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7173045","identifier":"Q07820-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q07820-1/entry","name":"MCL1","description":"Induced myeloid leukemia cell differentiation protein Mcl-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-482","complexName":"SOSS1 complex","organismName":"Homo sapiens; 9606","description":"A double-stranded DNA break repair complex that senses single-stranded DNA (ssDNA) and promotes repair of DNA double-strand breaks (DSBs). The binding affinity for ssDNA becomes more significant the longer the ssDNA fragment is. Influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation (G2/M), homologous recombination-dependent repair of DSBs, ATM-dependent signaling pathways and maintenance of genomic stability. The SOSSA (INT3) subunit promotes nuclear localization of the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-2120336","identifier":"Q9BQ15","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BQ15/entry","name":"NABP2","description":"SOSS complex subunit B1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13356","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2680854","identifier":"Q68E01","identifierLink":"https://www.uniprot.org/uniprotkb/Q68E01/entry","name":"INTS3","description":"Integrator complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13587","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2881520","identifier":"Q9NRY2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NRY2/entry","name":"INIP","description":"SOSS complex subunit C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31526","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-483","complexName":"uPA-PAI-1 complex","organismName":"Homo sapiens; 9606","description":"Regulates the activity of the plasminogen activation system, an extracellular proteolytic cascade. Inhibited form of urokinase plasminogen activator uPA (PLAU), an enzyme responsible for the cleavage of plasminogen (P00747) to form plasmin. Formation of the complex plays a crucial role in fibrinolysis, cell adhesion and migration and tissue remodeling including tumor progression and metastasis.","predictedComplex":false,"interactors":[{"ac":"EBI-3905042","identifier":"P00749","identifierLink":"https://www.uniprot.org/uniprotkb/P00749/entry","name":"PLAU","description":"Urokinase-type plasminogen activator","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-953978","identifier":"P05121","identifierLink":"https://www.uniprot.org/uniprotkb/P05121/entry","name":"SERPINE1","description":"Plasminogen activator inhibitor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11461","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-484","complexName":"SLX4-TERF2 complex","organismName":"Homo sapiens; 9606","description":"Role in maintaining an average equilibrium telomere length thus preventing telomere overlengthening. TRF2 binds to telomeric DNA and functions as a measuring device to assess telomere length. Longer telomeres are bound by larger amount of TRF2, which subsequently recruits more SLX4 to telomeres. The double-layered SLX4-TRF2 platform then assembles a nuclease toolkit at telomeres for homologous-recombination-mediated telomere recombination, including telomere sister chromatid exchange and resolution of the t-loop formed by the 3-prime single-stranded overhang, base-pairing with the C-strand of the duplex region of telomeric DNAs.","predictedComplex":false,"interactors":[{"ac":"EBI-2370740","identifier":"Q8IY92","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IY92/entry","name":"SLX4","description":"Structure-specific endonuclease subunit SLX4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21541","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-706637","identifier":"Q15554","identifierLink":"https://www.uniprot.org/uniprotkb/Q15554/entry","name":"TERF2","description":"Telomeric repeat-binding factor 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46833","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-485","complexName":"UBC13-UEV1A ubiquitin-conjugating enzyme E2 complex","organismName":"Homo sapiens; 9606","description":"Implicated in the non-proteolytic regulation of signaling pathways by contributing to the addition of lysine 63-linked ubiquitin chains to proteins. Transfers the thioester-bound donor ubiquitin from UBE2N onto the UBE2V1 catalytically inactive E2 variant. The heterodimer, together with the RING ubiquitin ligase TRAF6, then catalyzes the formation of multiubiquitin chains linked by isopeptide bonds between Lys-63 and the C-terminus of the next monomer in the chain. This type of polyubiquitination does not lead to protein degradation by the proteasome but instead mediates activation of target genes by activating intracellular signaling cascades, in particular TRAF-dependent NF-kappa-B signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-1050671","identifier":"Q13404","identifierLink":"https://www.uniprot.org/uniprotkb/Q13404/entry","name":"UBE2V1","description":"Ubiquitin-conjugating enzyme E2 variant 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1052908","identifier":"P61088","identifierLink":"https://www.uniprot.org/uniprotkb/P61088/entry","name":"UBE2N","description":"Ubiquitin-conjugating enzyme E2 N","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-486","complexName":"bZIP transcription factor complex, FOS-JUN","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site. FOS-JUN is capable of binding DNA on its own or as part of larger, ternary complexes with more specific transcription factor activity.","predictedComplex":false,"interactors":[{"ac":"EBI-852823","identifier":"P05412","identifierLink":"https://www.uniprot.org/uniprotkb/P05412/entry","name":"JUN","description":"Transcription factor Jun","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-852851","identifier":"P01100","identifierLink":"https://www.uniprot.org/uniprotkb/P01100/entry","name":"FOS","description":"Protein c-Fos","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-999","complexName":"MET4-MET28-MET31 sulfur metabolism transcription factor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Transcription factor complex regulating sulfur metabolism. MET4 lacks DNA-binding ability and relies on interactions with MET31 and MET32 (Q03081), paralogous proteins that bind the same cis-regulatory element, to activate its targets. MET31 and MET32 are C2H2 zinc finger-containing proteins that act solely as adaptors for recruiting MET4 to promoters, binding to sites with a TGTGGC core. MET28 acts to stabilise the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-10757","identifier":"P32389","identifierLink":"https://www.uniprot.org/uniprotkb/P32389/entry","name":"MET4","description":"Transcriptional activator of sulfur metabolism MET4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11503","identifier":"P40573","identifierLink":"https://www.uniprot.org/uniprotkb/P40573/entry","name":"MET28","description":"Transcriptional activator of sulfur metabolism MET28","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11511","identifier":"Q03081","identifierLink":"https://www.uniprot.org/uniprotkb/Q03081/entry","name":"MET31","description":"Transcriptional regulator MET31","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1000","complexName":"Rde-10/Rde-11 complex","organismName":"Caenorhabditis elegans; 6239","description":"The complex interacts with primary siRNA bound target mRNA and is required for the small interfering RNA (siRNA) amplification which triggers RNA interference (RNAi)-induced mRNA degradation. Required in the endogenous and exogenous siRNA pathways for the biogenesis and accumulation of secondary siRNA intermediates, such as 22G-siRNAs derived from ergo-1 targets. These potentiate the silencing effect of primary siRNAs  at low dsRNA concentrations. The complex thus links the amplification of the RNAi response to the initial processing and utilization of the exogenous dsRNA trigger","predictedComplex":false,"interactors":[{"ac":"EBI-13638212","identifier":"Q9N3S2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9N3S2/entry","name":"rde-10","description":"RNA interference defective protein 10","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-13638222","identifier":"Q6BET5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6BET5/entry","name":"rde-11","description":"RNA interference defective protein 11","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]}]},{"complexAC":"CPX-1001","complexName":"Calcineurin-Calmodulin complex, gamma-R1 variant","organismName":"Homo sapiens; 9606","description":"A calcium-dependent, calmodulin-stimulated protein phosphatase complex that is activated by elevated cytoplasmic calcium ion concentrations. Important for many cellular activities such as homeostasis, angiogenesis, myogenesis, adipogenesis, osteogenesis, chondrocyte differentiation, cardiovascular system development, pancreatic beta-cell proliferation, hair follicle cell differentiation and remodeling, and activities of cells of the immune. Plays a pivotal role during nervous system development and in various functions of mature central and peripheral nervous system. Regulates the NFAT signaling cascade by binding to and dephosphorylating NFAT leading to nuclear translocation of this larger complex and increasing the DNA-binding affinity of the NFAT family of transcription factors. Calcineurin also promotes nuclear retention of NFAT by masking nuclear export signals (NES) and preventing NES-dependent nuclear export. Altered calcineurin-NFAT activation can mediate both neuroprotective and neurodegenerative signals and is linked to pathological features of neurodegenerative diseases such as amyotrophic lateral sclerosis, Huntingtons, Parkinsons, and Alzheimers diseases. \r\n\r\nModulates Ca2+-dependent inactivation (CDI) of voltage-gated L-type Ca2+ channels. CDI is initiated by Ca2+ binding to channel-associated calmodulin and subsequent activation of calcineurin, which is targeted to L channels by the A-kinase-anchoring protein AKAP5 (CPX-674). Channel activity is activated by phosphorylation of AKAP5-bound Protein Kinase A.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2827192","identifier":"P48454","identifierLink":"https://www.uniprot.org/uniprotkb/P48454/entry","name":"PPP3CC","description":"Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397435","identifier":"P62158","identifierLink":"https://www.uniprot.org/uniprotkb/P62158/entry","name":"calm_human","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-915984","identifier":"P63098","identifierLink":"https://www.uniprot.org/uniprotkb/P63098/entry","name":"PPP3R1","description":"Calcineurin subunit B type 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1002","complexName":"Calcineurin-Calmodulin complex, beta-R2 variant","organismName":"Homo sapiens; 9606","description":"A calcium-dependent, calmodulin-stimulated protein phosphatase complex that is activated by elevated cytoplasmic calcium ion concentrations. Important for many cellular activities such as homeostasis, angiogenesis, myogenesis, adipogenesis, osteogenesis, chondrocyte differentiation, cardiovascular system development, pancreatic beta-cell proliferation, hair follicle cell differentiation and remodeling, and activities of cells of the immune. Plays a pivotal role during nervous system development and in various functions of mature central and peripheral nervous system. Regulates the NFAT signaling cascade by binding to and dephosphorylating NFAT leading to nuclear translocation of this larger complex and increasing the DNA-binding affinity of the NFAT family of transcription factors. Calcineurin also promotes nuclear retention of NFAT by masking nuclear export signals (NES) and preventing NES-dependent nuclear export. Altered calcineurin-NFAT activation can mediate both neuroprotective and neurodegenerative signals and is linked to pathological features of neurodegenerative diseases such as amyotrophic lateral sclerosis, Huntingtons, Parkinsons, and Alzheimers diseases. \r\n\r\nModulates Ca2+-dependent inactivation (CDI) of voltage-gated L-type Ca2+ channels. CDI is initiated by Ca2+ binding to channel-associated calmodulin and subsequent activation of calcineurin, which is targeted to L channels by the A-kinase-anchoring protein AKAP5 (CPX-674). Channel activity is activated by phosphorylation of AKAP5-bound Protein Kinase A.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1759540","identifier":"P16298","identifierLink":"https://www.uniprot.org/uniprotkb/P16298/entry","name":"PPP3CB","description":"Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3906025","identifier":"Q96LZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96LZ3/entry","name":"PPP3R2","description":"Calcineurin subunit B type 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397435","identifier":"P62158","identifierLink":"https://www.uniprot.org/uniprotkb/P62158/entry","name":"calm_human","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1003","complexName":"Calcineurin-Calmodulin complex, alpha-R1 variant","organismName":"Homo sapiens; 9606","description":"A calcium-dependent, calmodulin-stimulated protein phosphatase complex that is activated by elevated cytoplasmic calcium ion concentrations. Important for many cellular activities such as homeostasis, angiogenesis, myogenesis, adipogenesis, osteogenesis, chondrocyte differentiation, cardiovascular system development, pancreatic beta-cell proliferation, hair follicle cell differentiation and remodeling, and activities of cells of the immune. Plays a pivotal role during nervous system development and in various functions of mature central and peripheral nervous system. Regulates the NFAT signaling cascade by binding to and dephosphorylating NFAT leading to nuclear translocation of this larger complex and increasing the DNA-binding affinity of the NFAT family of transcription factors. Calcineurin also promotes nuclear retention of NFAT by masking nuclear export signals (NES) and preventing NES-dependent nuclear export. Altered calcineurin-NFAT activation can mediate both neuroprotective and neurodegenerative signals and is linked to pathological features of neurodegenerative diseases such as amyotrophic lateral sclerosis, Huntingtons, Parkinsons, and Alzheimers diseases. \r\n\r\nModulates Ca2+-dependent inactivation (CDI) of voltage-gated L-type Ca2+ channels. CDI is initiated by Ca2+ binding to channel-associated calmodulin and subsequent activation of calcineurin, which is targeted to L channels by the A-kinase-anchoring protein AKAP5 (CPX-674). Channel activity is activated by phosphorylation of AKAP5-bound Protein Kinase A.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-352922","identifier":"Q08209","identifierLink":"https://www.uniprot.org/uniprotkb/Q08209/entry","name":"PPP3CA","description":"Protein phosphatase 3 catalytic subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397435","identifier":"P62158","identifierLink":"https://www.uniprot.org/uniprotkb/P62158/entry","name":"calm_human","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-915984","identifier":"P63098","identifierLink":"https://www.uniprot.org/uniprotkb/P63098/entry","name":"PPP3R1","description":"Calcineurin subunit B type 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1004","complexName":"PCAF-containing ATAC complex","organismName":"Homo sapiens; 9606","description":"Histone acetyl transferase complex that plays a role in regulation of transcription of a specific group of genes by increasing the decompaction of chromatin to facilitate the access of transcription factors to promoter regions. It preferentially acetylates  a single residue of Histone H3 (Lys-14) and only weakly acetylates Histone H4. Recruited to the promoters of the IE (immediate early) gene FOS (P01100), FOSL1 (P15407), EGR1 (P18146). The complex also regulates the activity of non-histone targets and orchestrates mitotic progression by regulating Cyclin A degradation through acetylation.Cyclin A/CDK2 kinase is essential for correct centrosome formation and inhibits SIRT2 (Q8IXJ6) function.","predictedComplex":false,"interactors":[{"ac":"EBI-2795509","identifier":"Q9ULM3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ULM3/entry","name":"YEATS2","description":"YEATS domain-containing protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23195","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2795524","identifier":"Q8IYH5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IYH5/entry","name":"ZZZ3","description":"ZZ-type zinc finger-containing protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22705","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-473249","identifier":"O75528","identifierLink":"https://www.uniprot.org/uniprotkb/O75528/entry","name":"TADA3","description":"Transcriptional adapter 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13556","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-477430","identifier":"Q92831","identifierLink":"https://www.uniprot.org/uniprotkb/Q92831/entry","name":"KAT2B","description":"Histone acetyltransferase KAT2B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45750","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-540834","identifier":"P61964","identifierLink":"https://www.uniprot.org/uniprotkb/P61964/entry","name":"WDR5","description":"WD repeat-containing protein 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-741953","identifier":"Q9NS73","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NS73/entry","name":"MBIP","description":"MAP3K12-binding inhibitory protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23404","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742268","identifier":"O75478","identifierLink":"https://www.uniprot.org/uniprotkb/O75478/entry","name":"TADA2A","description":"Transcriptional adapter 2-alpha","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12374","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743117","identifier":"Q96ES7","identifierLink":"https://www.uniprot.org/uniprotkb/Q96ES7/entry","name":"SGF29","description":"SAGA-associated factor 29","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21539","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-750300","identifier":"Q01658","identifierLink":"https://www.uniprot.org/uniprotkb/Q01658/entry","name":"DR1","description":"Protein Dr1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46138","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-750907","identifier":"Q9H8E8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H8E8/entry","name":"KAT14","description":"Cysteine-rich protein 2-binding protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20916","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1005","complexName":"Cascade complex","organismName":"Escherichia coli (strain K12); 83333","description":"CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). The system memorizes previous infections by integrating short sequences of invading genomes (spacers) into the CRISPR locus. The spacers, interspaced with repeats, are expressed as small guide CRISPR RNAs (crRNAs) that are employed by Cas proteins to target invaders sequence-specifically upon a reoccurring infection. Upon viral invasion, the Cascade complex binds double-stranded DNA exhibiting sequence complementary to the crRNA spacer sequence, while displacing the non-target strand to form an R-loop, and then recruits the nuclease Cas3/ygcB (P38036) for target degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-1125571","identifier":"P76632","identifierLink":"https://www.uniprot.org/uniprotkb/P76632/entry","name":"casB","description":"CRISPR system Cascade subunit CasB","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-1130217","identifier":"Q46897","identifierLink":"https://www.uniprot.org/uniprotkb/Q46897/entry","name":"casE","description":"CRISPR system Cascade subunit CasE","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-1130226","identifier":"Q46899","identifierLink":"https://www.uniprot.org/uniprotkb/Q46899/entry","name":"casC","description":"CRISPR system Cascade subunit CasC","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-1130234","identifier":"Q46901","identifierLink":"https://www.uniprot.org/uniprotkb/Q46901/entry","name":"casA","description":"CRISPR system Cascade subunit CasA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-13639846","identifier":"Q46898","identifierLink":"https://www.uniprot.org/uniprotkb/Q46898/entry","name":"casD","description":"CRISPR system Cascade subunit CasD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-13645746","identifier":"CHEBI:134528","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:134528","name":"crispr rna","description":"CRISPR RNA","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1006","complexName":"Calcineurin-Calmodulin-AKAP5 complex, beta-R1 variant","organismName":"Mus musculus; 10090","description":"Calcium-dependent, calmodulin-stimulated protein phosphatase calcineurin in complex with plasma-membrane anchor protein Akap5. Calcineurin is important for cardiac development and pathophysiology, for nervous-system development and for some of the plastic changes in neurons that are believed to underlie learning and memory. Akap5 recruits calcineurin to the vicinity of L-type Ca2+ channels for their activation by elevated Ca2+ entering the cell. Akap5 balances the opposing effects of calcineurin and protein kinase A (PKA) (P05132) on neuronal voltage-gated L-type Ca2+ channels and coordinates the activities of calcineurin, PKA and PKC on a number of other channels and receptors. Despite its atypical PxIxIT calcineurin-recognition motif that confers stronger binding affinity by calcineurin than other substrates it allows for effective disengagement of calcineurin to couple channel activation with downstream signaling events. The calcineurin-Akap5 complex has been shown to promote NFAT signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-397460","identifier":"P62204","identifierLink":"https://www.uniprot.org/uniprotkb/P62204/entry","name":"Calm1","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-642618","identifier":"P48453","identifierLink":"https://www.uniprot.org/uniprotkb/P48453/entry","name":"Ppp3cb","description":"Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6666164","identifier":"Q63810","identifierLink":"https://www.uniprot.org/uniprotkb/Q63810/entry","name":"Ppp3r1","description":"Calcineurin subunit B type 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7091108","identifier":"D3YVF0","identifierLink":"https://www.uniprot.org/uniprotkb/D3YVF0/entry","name":"Akap5","description":"A-kinase anchor protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15182","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1007","complexName":"Calcineurin-Calmodulin complex, gamma-R1 variant","organismName":"Mus musculus; 10090","description":"A calcium-dependent, calmodulin-stimulated protein phosphatase complex that is activated by elevated cytoplasmic calcium ion concentrations. Important for many cellular activities such as homeostasis, angiogenesis, myogenesis, adipogenesis, osteogenesis, chondrocyte differentiation, cardiovascular system development, pancreatic beta-cell proliferation, hair follicle cell differentiation and remodeling, and activities of cells of the immune. Plays a pivotal role during nervous system development and in various functions of mature central and peripheral nervous system. Regulates the NFAT signaling cascade by binding to and dephosphorylating NFAT leading to nuclear translocation of this larger complex and increasing the DNA-binding affinity of the NFAT family of transcription factors. Calcineurin also promotes nuclear retention of NFAT by masking nuclear export signals (NES) and preventing NES-dependent nuclear export. Altered calcineurin-NFAT activation can mediate both neuroprotective and neurodegenerative signals. \r\n\r\nModulates Ca2+-dependent inactivation (CDI) of voltage-gated L-type Ca2+ channels. CDI is initiated by Ca2+ binding to channel-associated calmodulin and subsequent activation of calcineurin, which is targeted to L channels by the A-kinase-anchoring protein AKAP5. Channel activity is activated by phosphorylation of AKAP5-bound Protein Kinase A.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-397460","identifier":"P62204","identifierLink":"https://www.uniprot.org/uniprotkb/P62204/entry","name":"Calm1","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-6271683","identifier":"P48455","identifierLink":"https://www.uniprot.org/uniprotkb/P48455/entry","name":"Ppp3cc","description":"Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6666164","identifier":"Q63810","identifierLink":"https://www.uniprot.org/uniprotkb/Q63810/entry","name":"Ppp3r1","description":"Calcineurin subunit B type 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1008","complexName":"Calcineurin-Calmodulin complex, beta-R2 variant","organismName":"Mus musculus; 10090","description":"A calcium-dependent, calmodulin-stimulated protein phosphatase complex that is activated by elevated cytoplasmic calcium ion concentrations. Important for many cellular activities such as homeostasis, angiogenesis, myogenesis, adipogenesis, osteogenesis, chondrocyte differentiation, cardiovascular system development, pancreatic beta-cell proliferation, hair follicle cell differentiation and remodeling, and activities of cells of the immune. Plays a pivotal role during nervous system development and in various functions of mature central and peripheral nervous system. Regulates the NFAT signaling cascade by binding to and dephosphorylating NFAT leading to nuclear translocation of this larger complex and increasing the DNA-binding affinity of the NFAT family of transcription factors. Calcineurin also promotes nuclear retention of NFAT by masking nuclear export signals (NES) and preventing NES-dependent nuclear export. Altered calcineurin-NFAT activation can mediate both neuroprotective and neurodegenerative signals. \r\n\r\nModulates Ca2+-dependent inactivation (CDI) of voltage-gated L-type Ca2+ channels. CDI is initiated by Ca2+ binding to channel-associated calmodulin and subsequent activation of calcineurin, which is targeted to L channels by the A-kinase-anchoring protein AKAP5. Channel activity is activated by phosphorylation of AKAP5-bound Protein Kinase A.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-13916676","identifier":"Q63811","identifierLink":"https://www.uniprot.org/uniprotkb/Q63811/entry","name":"Ppp3r2","description":"Calcineurin subunit B type 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397460","identifier":"P62204","identifierLink":"https://www.uniprot.org/uniprotkb/P62204/entry","name":"Calm1","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-642618","identifier":"P48453","identifierLink":"https://www.uniprot.org/uniprotkb/P48453/entry","name":"Ppp3cb","description":"Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1009","complexName":"Calcineurin-Calmodulin complex, beta-R1 variant","organismName":"Homo sapiens; 9606","description":"A calcium-dependent, calmodulin-stimulated protein phosphatase complex that is activated by elevated cytoplasmic calcium ion concentrations. Important for many cellular activities such as homeostasis, angiogenesis, myogenesis, adipogenesis, osteogenesis, chondrocyte differentiation, cardiovascular system development, pancreatic beta-cell proliferation, hair follicle cell differentiation and remodeling, and activities of cells of the immune. Plays a pivotal role during nervous system development and in various functions of mature central and peripheral nervous system. Regulates the NFAT signaling cascade by binding to and dephosphorylating NFAT leading to nuclear translocation of this larger complex and increasing the DNA-binding affinity of the NFAT family of transcription factors. Calcineurin also promotes nuclear retention of NFAT by masking nuclear export signals (NES) and preventing NES-dependent nuclear export. Altered calcineurin-NFAT activation can mediate both neuroprotective and neurodegenerative signals and is linked to pathological features of neurodegenerative diseases such as amyotrophic lateral sclerosis, Huntingtons, Parkinsons, and Alzheimers diseases. \r\n\r\nModulates Ca2+-dependent inactivation (CDI) of voltage-gated L-type Ca2+ channels. CDI is initiated by Ca2+ binding to channel-associated calmodulin and subsequent activation of calcineurin, which is targeted to L channels by the A-kinase-anchoring protein AKAP5 (CPX-674). Channel activity is activated by phosphorylation of AKAP5-bound Protein Kinase A.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1759540","identifier":"P16298","identifierLink":"https://www.uniprot.org/uniprotkb/P16298/entry","name":"PPP3CB","description":"Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397435","identifier":"P62158","identifierLink":"https://www.uniprot.org/uniprotkb/P62158/entry","name":"calm_human","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-915984","identifier":"P63098","identifierLink":"https://www.uniprot.org/uniprotkb/P63098/entry","name":"PPP3R1","description":"Calcineurin subunit B type 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1010","complexName":"Calcineurin-Calmodulin complex, alpha-R1 variant","organismName":"Mus musculus; 10090","description":"A calcium-dependent, calmodulin-stimulated protein phosphatase complex that is activated by elevated cytoplasmic calcium ion concentrations. Important for many cellular activities such as homeostasis, angiogenesis, myogenesis, adipogenesis, osteogenesis, chondrocyte differentiation, cardiovascular system development, pancreatic beta-cell proliferation, hair follicle cell differentiation and remodeling, and activities of cells of the immune. Plays a pivotal role during nervous system development and in various functions of mature central and peripheral nervous system. Regulates the NFAT signaling cascade by binding to and dephosphorylating NFAT leading to nuclear translocation of this larger complex and increasing the DNA-binding affinity of the NFAT family of transcription factors. Calcineurin also promotes nuclear retention of NFAT by masking nuclear export signals (NES) and preventing NES-dependent nuclear export. Altered calcineurin-NFAT activation can mediate both neuroprotective and neurodegenerative signals. \r\n\r\nModulates Ca2+-dependent inactivation (CDI) of voltage-gated L-type Ca2+ channels. CDI is initiated by Ca2+ binding to channel-associated calmodulin and subsequent activation of calcineurin, which is targeted to L channels by the A-kinase-anchoring protein AKAP5. Channel activity is activated by phosphorylation of AKAP5-bound Protein Kinase A.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-397208","identifier":"P63328","identifierLink":"https://www.uniprot.org/uniprotkb/P63328/entry","name":"Ppp3ca","description":"Protein phosphatase 3 catalytic subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397460","identifier":"P62204","identifierLink":"https://www.uniprot.org/uniprotkb/P62204/entry","name":"Calm1","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-6666164","identifier":"Q63810","identifierLink":"https://www.uniprot.org/uniprotkb/Q63810/entry","name":"Ppp3r1","description":"Calcineurin subunit B type 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1011","complexName":"Calcineurin-Calmodulin complex, beta-R1 variant","organismName":"Mus musculus; 10090","description":"A calcium-dependent, calmodulin-stimulated protein phosphatase complex that is activated by elevated cytoplasmic calcium ion concentrations. Important for many cellular activities such as homeostasis, angiogenesis, myogenesis, adipogenesis, osteogenesis, chondrocyte differentiation, cardiovascular system development, pancreatic beta-cell proliferation, hair follicle cell differentiation and remodeling, and activities of cells of the immune. Plays a pivotal role during nervous system development and in various functions of mature central and peripheral nervous system. Regulates the NFAT signaling cascade by binding to and dephosphorylating NFAT leading to nuclear translocation of this larger complex and increasing the DNA-binding affinity of the NFAT family of transcription factors. Calcineurin also promotes nuclear retention of NFAT by masking nuclear export signals (NES) and preventing NES-dependent nuclear export. Altered calcineurin-NFAT activation can mediate both neuroprotective and neurodegenerative signals. \r\n\r\nModulates Ca2+-dependent inactivation (CDI) of voltage-gated L-type Ca2+ channels. CDI is initiated by Ca2+ binding to channel-associated calmodulin and subsequent activation of calcineurin, which is targeted to L channels by the A-kinase-anchoring protein AKAP5. Channel activity is activated by phosphorylation of AKAP5-bound Protein Kinase A.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-397460","identifier":"P62204","identifierLink":"https://www.uniprot.org/uniprotkb/P62204/entry","name":"Calm1","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-642618","identifier":"P48453","identifierLink":"https://www.uniprot.org/uniprotkb/P48453/entry","name":"Ppp3cb","description":"Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6666164","identifier":"Q63810","identifierLink":"https://www.uniprot.org/uniprotkb/Q63810/entry","name":"Ppp3r1","description":"Calcineurin subunit B type 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1012","complexName":"Tenascin-W complex","organismName":"Homo sapiens; 9606","description":"A matricellular glycoprotein complex of the extracellular matrix found in a range of tissues, predominantly neuronic and bone tissues. Expression is highly controlled and more prominent in developing embryos than adult tissues. Involved in neurite outgrowth, cell adhesion and cell migration. Appears to be a marker for transformed cells in adult tumors, especially the stroma of most solid tumors and blood vessels of gliomas where it displays pro-angiogenic activity.","predictedComplex":false,"interactors":[{"ac":"EBI-13640827","identifier":"Q9UQP3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UQP3/entry","name":"TNN","description":"Tenascin-N","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19143","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1013","complexName":"Tenascin-W complex","organismName":"Mus musculus; 10090","description":"A matricellular glycoprotein complex of the extracellular matrix found in a range of tissues, predominantly neuronic and bone tissues. Expression is highly controlled and more prominent in developing embryos than adult tissues. Involved in neurite outgrowth, cell adhesion and cell migration. Appears to be a marker for transformed cells in adult tumors, esp the stroma of most solid tumors and blood vessels of gliomas where it displays pro-angiogenic activity.","predictedComplex":false,"interactors":[{"ac":"EBI-13641178","identifier":"Q80Z71","identifierLink":"https://www.uniprot.org/uniprotkb/Q80Z71/entry","name":"Tnn","description":"Tenascin-N","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR19143","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1014","complexName":"Tenascin-X complex","organismName":"Homo sapiens; 9606","description":"A matricellular glycoprotein complex of the extracellular matrix (ECM) constitutively expressed in collagen-rich connective tissues and peripheral nerves. Present in particularly highly levels in developing heart, skeletal muscles, tendons, ligaments and limbs. Plays an important role in ECM architecture, tissue integrity and in the biomechanical properties of connective tissues. Binds to and bridges collagen fibrils and regulates collagen deposition. Binds heparin but, unlike other members of the Tenascin family, does not bind fibronectin. May also interact with heparin-sulfate proteoglycan receptors. Involved in the regulation of many cellular processes such as cell adhesion, cell migration, cell fate determination or cell differentiation, epithelial cell plasticity (e.g. epithelial to mesenchymal transition or vice versa), cell proliferation and the vascular endothelial growth factor (VEGF) signaling pathway. Regulates transforming growth factor beta activation via cell adhesion by binding of the FBG-like domain (Fibrinogen-like globular domain, IPR002181) of Tenascin-X to alpha11beta1 integrin (CPX-1818). May act as a tumour suppressor. \r\n\r\nAn alternative promoter and transcription start site is activated by hypoxia in the adrenal gland resulting in a transcript encoding a truncated short TNXB protein with cytoplasmic localization.","predictedComplex":false,"interactors":[{"ac":"EBI-2821024","identifier":"P22105","identifierLink":"https://www.uniprot.org/uniprotkb/P22105/entry","name":"TNXB","description":"Tenascin-X","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46708","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1015","complexName":"MET4-MET28-MET32 sulfur metabolism transcription factor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Transcription factor complex regulating sulfur metabolism. MET4 lacks DNA-binding ability and relies on interactions with MET31 (Q03081) and MET32, paralogous proteins that bind the same cis-regulatory element, to activate its targets. MET31 and MET32 are C2H2 zinc finger-containing proteins that act solely as adaptors for recruiting MET4 to promoters, binding to sites with a TGTGGC core. MET28 acts to stabilise the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-10757","identifier":"P32389","identifierLink":"https://www.uniprot.org/uniprotkb/P32389/entry","name":"MET4","description":"Transcriptional activator of sulfur metabolism MET4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11503","identifier":"P40573","identifierLink":"https://www.uniprot.org/uniprotkb/P40573/entry","name":"MET28","description":"Transcriptional activator of sulfur metabolism MET28","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11519","identifier":"Q12041","identifierLink":"https://www.uniprot.org/uniprotkb/Q12041/entry","name":"MET32","description":"Transcriptional regulator MET32","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1016","complexName":"CBF1-MET4-MET28 sulfur metabolism transcription factor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Transcription factor complex regulating sulfur metabolism. MET4 lacks DNA-binding ability and relies on its interaction with CBF1 to activate its targets. CBF1 is a basic helix–loop–helix factor protein that that homodimerizes to bind a  cis-regulatory element CACGTGA motif and then recruits the transactivator MET4 to promoters. MET28 acts to stabilise the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-10757","identifier":"P32389","identifierLink":"https://www.uniprot.org/uniprotkb/P32389/entry","name":"MET4","description":"Transcriptional activator of sulfur metabolism MET4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11503","identifier":"P40573","identifierLink":"https://www.uniprot.org/uniprotkb/P40573/entry","name":"MET28","description":"Transcriptional activator of sulfur metabolism MET28","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4096","identifier":"P17106","identifierLink":"https://www.uniprot.org/uniprotkb/P17106/entry","name":"CBF1","description":"Centromere-binding protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47787","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1017","complexName":"Phagocyte NADPH oxidase complex, RAC1 variant","organismName":"Homo sapiens; 9606","description":"Plays a crucial role in host defense against microbial infections by generating reactive oxygen species. Transfers electrons across the wall of the phagocytic vacuole, forming superoxide in the lumen and promoting microbial killing through the generation of reactive oxygen species and through the activity of myeloperoxidase.","predictedComplex":false,"interactors":[{"ac":"EBI-1036870","identifier":"Q15080","identifierLink":"https://www.uniprot.org/uniprotkb/Q15080/entry","name":"NCF4","description":"Neutrophil cytosol factor 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15706","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25820308","identifier":"CHEBI:37565","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:37565","name":"gtp(4-)","description":"GTP(4-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-395044","identifier":"P14598","identifierLink":"https://www.uniprot.org/uniprotkb/P14598/entry","name":"NCF1","description":"Neutrophil cytosol factor 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15706","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-413628","identifier":"P63000","identifierLink":"https://www.uniprot.org/uniprotkb/P63000/entry","name":"RAC1","description":"Ras-related C3 botulinum toxin substrate 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24072","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-489611","identifier":"P19878","identifierLink":"https://www.uniprot.org/uniprotkb/P19878/entry","name":"NCF2","description":"Neutrophil cytosol factor 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15175","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6253630","identifier":"P04839","identifierLink":"https://www.uniprot.org/uniprotkb/P04839/entry","name":"CYBB","description":"NADPH oxidase 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11972","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-986058","identifier":"P13498","identifierLink":"https://www.uniprot.org/uniprotkb/P13498/entry","name":"CYBA","description":"Cytochrome b-245 light chain","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15168","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1018","complexName":"DRS2-CDC50 P4-ATPase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A membrane pump which actively translocates, or flips, phospholipids across cell membranes from the exoplasmic to the cytoplasmic leaflet of the lipid bilayer. This generates and maintains membrane lipid asymmetry, a property essential for a wide variety of cellular processes such as vesicle budding and intracellular vesicle trafficking. Transport is accomplished by cyclic changes between two main enzyme conformations, during which the DRS2 ATPase is phosphorylated by ATP at a conserved aspartate residue (Asp-560) and subsequently dephosphorylated. These processes are coupled to vectorial transport and counter-transport by a controlled opening and closing of cytoplasmic and exoplasmic pathways, which give access to the ion-binding sites that are buried inside the membrane-spanning region of the pump","predictedComplex":false,"interactors":[{"ac":"EBI-22014","identifier":"P25656","identifierLink":"https://www.uniprot.org/uniprotkb/P25656/entry","name":"CDC50","description":"Phospholipid-transporting ATPase accessory subunit CDC50","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10926","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3106","identifier":"P39524","identifierLink":"https://www.uniprot.org/uniprotkb/P39524/entry","name":"DRS2","description":"Phospholipid-transporting ATPase DRS2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1019","complexName":"Tenascin-R complex","organismName":"Homo sapiens; 9606","description":"A matricellular glycoprotein complex of the extracellular matrix (ECM), and in particularly of the perineuronal net, where it assembles complexes of ECM proteins, glycosaminoglycans and proteoglycans. Almost exclusively expressed by and located on oligodendrocyte and myelin in the central nervous system. Also appears transiently on Schwann cells during peripheral nerve development and at differentiated nodes of Ranvier. Not expressed by astrocytes or fibroblasts but may regulate their adhesion properties. Expression is low in embryos and increases with progression to adulthood but decreases with individual cell differentiation. Regulated by various growth factors and lectins. \r\n\r\nRegulates cell adhesion, migration and differentiation and neurite outgrowth through domain-specific interactions depending on cell type and developmental context. Positively regulates cell adhesion and differentiation by binding surface sulfatides on O4+ oligodendrocytes. Negatively regulates fibronectin- and integrin-mediated neurite outgrowth and cell adhesion by interacting with contactin-1 (CNTN1/F3, Q12860) or fibronectin FN1 (P02751) itself or by binding cell-surface chondroitin sulfate glycosaminoglycans or gangliosides of oligodendrocyte or their precursors. Oligomerisation negatively affects its inhibitory role on cell adhesion and neural outgrowth. Regulates cell plasticity by regulating secretion of growth factor and cytokines. Induces the generation of GABAergic neurons. Involved in synapse formation.","predictedComplex":false,"interactors":[{"ac":"EBI-3956837","identifier":"Q92752","identifierLink":"https://www.uniprot.org/uniprotkb/Q92752/entry","name":"TNR","description":"Tenascin-R","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19143","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1020","complexName":"BLI-3/DOXA-1/TSP-15 dual oxidase complex","organismName":"Caenorhabditis elegans; 6239","description":"Required for the biogenesis of the reactive oxygen species H2O2. The complex plays a role in cuticle biogenesis and the production of ROS is probably used by the peroxidase mlt-7 for the formation of tyrosine cross-links in cuticle collagens and therefore the stabilisation of the cuticular extracellular matrix.","predictedComplex":false,"interactors":[{"ac":"EBI-13643206","identifier":"O61213","identifierLink":"https://www.uniprot.org/uniprotkb/O61213/entry","name":"bli-3","description":"Dual oxidase 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11972","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13643241","identifier":"P34298","identifierLink":"https://www.uniprot.org/uniprotkb/P34298/entry","name":"doxa-1","description":"Dual oxidase maturation factor 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR31158","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13643253","identifier":"Q9XVM9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XVM9/entry","name":"tsp-15","description":"Tetraspanin-15","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR19282","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1021","complexName":"DNF1-LEM3 P4-ATPase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A membrane pump which actively translocates, or flips, phospholipids across cell membranes from the exoplasmic to the cytoplasmic leaflet of the lipid bilayer. This generates and maintains membrane lipid asymmetry, a property essential for a wide variety of cellular processes such as vesicle budding and intracellular vesicle trafficking. Transport is accomplished by cyclic changes between two main enzyme conformations, during which the DNF1 ATPase is phosphorylated by ATP at a conserved aspartate residue (Asp-667) and subsequently dephosphorylated. These processes are coupled to vectorial transport and counter-transport by a controlled opening and closing of cytoplasmic and exoplasmic pathways, which give access to the ion-binding sites that are buried inside the membrane-spanning region of the pump. Also involved in transport of the tryptophan permease TAT2 to the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-28396","identifier":"P42838","identifierLink":"https://www.uniprot.org/uniprotkb/P42838/entry","name":"LEM3","description":"Phospholipid-transporting ATPase accessory subunit LEM3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10926","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3121","identifier":"P32660","identifierLink":"https://www.uniprot.org/uniprotkb/P32660/entry","name":"DNF1","description":"Phospholipid-transporting ATPase DNF1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1022","complexName":"DNF2-LEM3 P4-ATPase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A membrane pump which actively translocates, or flips, phospholipids across cell membranes from the exoplasmic to the cytoplasmic leaflet of the lipid bilayer. This generates and maintains membrane lipid asymmetry, a property essential for a wide variety of cellular processes such as vesicle budding and intracellular vesicle trafficking. Transport is accomplished by cyclic changes between two main enzyme conformations, during which the DNF2 ATPase is phosphorylated by ATP at a conserved aspartate residue (Asp-712) and subsequently dephosphorylated. These processes are coupled to vectorial transport and counter-transport by a controlled opening and closing of cytoplasmic and exoplasmic pathways, which give access to the ion-binding sites that are buried inside the membrane-spanning region of the pump. Also involved in transport of the tryptophan permease TAT2 to the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-28396","identifier":"P42838","identifierLink":"https://www.uniprot.org/uniprotkb/P42838/entry","name":"LEM3","description":"Phospholipid-transporting ATPase accessory subunit LEM3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10926","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3114","identifier":"Q12675","identifierLink":"https://www.uniprot.org/uniprotkb/Q12675/entry","name":"DNF2","description":"Phospholipid-transporting ATPase DNF2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1023","complexName":"Methylosome","organismName":"Mus musculus; 10090","description":"The methylomose is a large protein complex (20S) that possesses arginine methyltransferase activity and modifies specific arginines to dimethylarginines in the arginine- and glycine-rich domains of several spliceosomal Sm proteins. This modification targets  these proteins to the survival of motor neurons (SMN) complex for assembly into small nuclear ribonucleoprotein (snRNP) core particles. Binding to Chtop(Q9CY57) recruits the methylosome complex to selective sites on the chromosome, where it methylates Histone H4 Arg-3 and activates the transcription of cancer-related genes.","predictedComplex":false,"interactors":[{"ac":"EBI-13644126","identifier":"Q61189","identifierLink":"https://www.uniprot.org/uniprotkb/Q61189/entry","name":"Clns1a","description":"Methylosome subunit pICln","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21399","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2527009","identifier":"Q8CIG8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CIG8/entry","name":"Prmt5","description":"Protein arginine N-methyltransferase 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10738","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2940098","identifier":"Q99J09","identifierLink":"https://www.uniprot.org/uniprotkb/Q99J09/entry","name":"Wdr77","description":"Methylosome protein WDR77","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46853","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1024","complexName":"PCAF histone acetylase complex","organismName":"Mus musculus; 10090","description":"A histone acetyl transferase complex that plays a role in regulation of transcription of a specific group of genes by increasing the decompaction of chromatin to facilitate the access of transcription factors to promoter regions. It preferentially acetylates  a single residue of Histone H3 (Lys-14) and is only able to weakly acetylate a single residue of Histone H4 (Lys-8) within nucleosomal substrates. The complex may also acetylate non-histone proteins, such as transcription factors.\r\n.","predictedComplex":false,"interactors":[{"ac":"EBI-12667195","identifier":"B0QZW4","identifierLink":"https://www.uniprot.org/uniprotkb/B0QZW4/entry","name":"Supt3","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-2325611","identifier":"Q9JHD1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JHD1/entry","name":"Kat2b","description":"Histone acetyltransferase KAT2B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45750","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942477","identifier":"Q80YV3","identifierLink":"https://www.uniprot.org/uniprotkb/Q80YV3/entry","name":"Trrap","description":"Transformation/transcription domain-associated protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2943161","identifier":"Q91WQ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q91WQ5/entry","name":"Taf5l","description":"TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR19879","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2943181","identifier":"Q8R2K4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R2K4/entry","name":"Taf6l","description":"TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10221","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2943209","identifier":"Q8R0L9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R0L9/entry","name":"Tada3","description":"Transcriptional adapter 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13556","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2943311","identifier":"Q8VI33","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VI33/entry","name":"Taf9","description":"Transcription initiation factor TFIID subunit 9","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR48068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5744209","identifier":"Q8K0H5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K0H5/entry","name":"Taf10","description":"Transcription initiation factor TFIID subunit 10","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21242","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7990347","identifier":"Q8CHV6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CHV6/entry","name":"Tada2a","description":"Transcriptional adapter 2-alpha","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12374","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7990784","identifier":"Q8VE65","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VE65/entry","name":"Taf12","description":"Transcription initiation factor TFIID subunit 12","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1025","complexName":"GCN5-containing ATAC complex","organismName":"Mus musculus; 10090","description":"A histone acetyl transferase complex that plays a role in regulation of transcription of a specific group of genes by increasing the decompaction of chromatin to facilitate the access of transcription factors to promoter regions. It preferentially acetylates  a single residue of Histone H3 (Lys-14) and only weakly acetylates Histone H4. Recruited to the promoters of the IE (immediate early) gene Fos (P01101), Fosl1 (P48755), Egr1 (P08046). The complex also regulates the activity of non-histone targets and orchestrates mitotic progression by regulating Cyclin A degradation through acetylation.Cyclin A/Cdk2 kinase is essential for correct centrosome formation and inhibits Sirt2 (Q8VDQ8) function.","predictedComplex":false,"interactors":[{"ac":"EBI-1247084","identifier":"P61965","identifierLink":"https://www.uniprot.org/uniprotkb/P61965/entry","name":"Wdr5","description":"WD repeat-containing protein 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2943116","identifier":"Q9JHD2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JHD2/entry","name":"Kat2a","description":"Histone acetyltransferase KAT2A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45750","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2943209","identifier":"Q8R0L9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R0L9/entry","name":"Tada3","description":"Transcriptional adapter 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13556","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5737882","identifier":"Q6KAQ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q6KAQ7/entry","name":"Zzz3","description":"ZZ-type zinc finger-containing protein 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22705","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5738806","identifier":"Q3TUF7","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TUF7/entry","name":"Yeats2","description":"YEATS domain-containing protein 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23195","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-688604","identifier":"Q99LQ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q99LQ1/entry","name":"Mbip","description":"MAP3K12-binding inhibitory protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23404","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7990274","identifier":"Q9DA08","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DA08/entry","name":"Sgf29","description":"SAGA-associated factor 29","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21539","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7990301","identifier":"Q91WV0","identifierLink":"https://www.uniprot.org/uniprotkb/Q91WV0/entry","name":"Dr1","description":"Protein Dr1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46138","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7990326","identifier":"Q8CID0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CID0/entry","name":"Kat14","description":"Cysteine-rich protein 2-binding protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR20916","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7990347","identifier":"Q8CHV6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CHV6/entry","name":"Tada2a","description":"Transcriptional adapter 2-alpha","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12374","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1026","complexName":"DNF3-CRF1 P4-ATPase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A membrane pump which actively translocates, or flips, phospholipids across cell membranes from the exoplasmic to the cytoplasmic leaflet of the lipid bilayer. This generates and maintains membrane lipid asymmetry, a property essential for a wide variety of cellular processes such as vesicle budding and intracellular vesicle trafficking. Transport is accomplished by cyclic changes between two main enzyme conformations, during which the DNF3 ATPase is phosphorylated by ATP at a conserved aspartate residue (Asp-566) and subsequently dephosphorylated. These processes are coupled to vectorial transport and counter-transport by a controlled opening and closing of cytoplasmic and exoplasmic pathways, which give access to the ion-binding sites that are buried inside the membrane-spanning region of the pump.","predictedComplex":false,"interactors":[{"ac":"EBI-28524","identifier":"P53740","identifierLink":"https://www.uniprot.org/uniprotkb/P53740/entry","name":"yn8s","description":"Phospholipid-transporting ATPase accessory subunit CRF1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10926","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3142","identifier":"Q12674","identifierLink":"https://www.uniprot.org/uniprotkb/Q12674/entry","name":"DNF3","description":"Probable phospholipid-transporting ATPase DNF3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1027","complexName":"Importin complex, KPNA2 variant","organismName":"Homo sapiens; 9606","description":"A nuclear import complex that functions as a nuclear import receptor for proteins containing a nuclear localisation signal (NLS). Subunit KPNA2 specifically and directly binds to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1. KPNB1 binds to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, RAN-dependent mechanism. At the nucleoplasmic side of the NPC, RAN-GTP (P62826) binds to KPNB1, the three components separate and KPNA2 and KPNB1 are re-exported from the nucleus to the cytoplasm where GTP is hydrolysed. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of RAN between the cytoplasm and nucleus.","predictedComplex":false,"interactors":[{"ac":"EBI-286758","identifier":"Q14974","identifierLink":"https://www.uniprot.org/uniprotkb/Q14974/entry","name":"KPNB1","description":"Importin subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-349938","identifier":"P52292","identifierLink":"https://www.uniprot.org/uniprotkb/P52292/entry","name":"KPNA2","description":"Importin subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23316","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1029","complexName":"PCAF-containing ATAC complex","organismName":"Mus musculus; 10090","description":"A histone acetyl transferase complex that plays a role in regulation of transcription of a specific group of genes by increasing the decompaction of chromatin to facilitate the access of transcription factors to promoter regions. It preferentially acetylates  a single residue of Histone H3 (Lys-14) and only weakly acetylates Histone H4. Recruited to the promoters of the IE (immediate early) gene Fos (P01101), Fosl1 (P48755), Egr1 (P08046). The complex also regulates the activity of non-histone targets and orchestrates mitotic progression by regulating Cyclin A degradation through acetylation.Cyclin A/Cdk2 kinase is essential for correct centrosome formation and inhibits Sirt2 (Q8VDQ8) function.","predictedComplex":false,"interactors":[{"ac":"EBI-1247084","identifier":"P61965","identifierLink":"https://www.uniprot.org/uniprotkb/P61965/entry","name":"Wdr5","description":"WD repeat-containing protein 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2325611","identifier":"Q9JHD1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JHD1/entry","name":"Kat2b","description":"Histone acetyltransferase KAT2B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45750","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2943209","identifier":"Q8R0L9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R0L9/entry","name":"Tada3","description":"Transcriptional adapter 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13556","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5737882","identifier":"Q6KAQ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q6KAQ7/entry","name":"Zzz3","description":"ZZ-type zinc finger-containing protein 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22705","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5738806","identifier":"Q3TUF7","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TUF7/entry","name":"Yeats2","description":"YEATS domain-containing protein 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23195","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-688604","identifier":"Q99LQ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q99LQ1/entry","name":"Mbip","description":"MAP3K12-binding inhibitory protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23404","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7990274","identifier":"Q9DA08","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DA08/entry","name":"Sgf29","description":"SAGA-associated factor 29","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21539","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7990301","identifier":"Q91WV0","identifierLink":"https://www.uniprot.org/uniprotkb/Q91WV0/entry","name":"Dr1","description":"Protein Dr1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46138","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7990326","identifier":"Q8CID0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CID0/entry","name":"Kat14","description":"Cysteine-rich protein 2-binding protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR20916","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7990347","identifier":"Q8CHV6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CHV6/entry","name":"Tada2a","description":"Transcriptional adapter 2-alpha","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12374","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1030","complexName":"BAF chromatin remodeling complex","organismName":"Caenorhabditis elegans; 6239","description":"An ATP-dependent chromatin remodeling complex that is part of the SWI/SNF chromatin remodeling complex superfamily and is involved in remodeling chromatin structure by destabilizing the histone-DNA interaction. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). The complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis.\r\n\r\nThe complex is involved in a variety of developmental processes including embryonic cell divisions, larval asymmetric cell divisions, generation of neuroblasts and neurons, muscle differentiation, somatic gonadogenesis, vulval induction, and timing of larval development.\r\n\r\nPlays a role in the terminal differentiation of neurons. Specifically, the ham-3 subunit is involved in HSN motor neuron positioning, axon guidance and serotonin synthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-13645508","identifier":"G5EF53","identifierLink":"https://www.uniprot.org/uniprotkb/G5EF53/entry","name":"swsn-4","description":"SWI/SNF chromatin remodeling complex core catalytic subunit swsn-4","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13645532","identifier":"Q9N4N4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9N4N4/entry","name":"swsn-6","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13645548","identifier":"J7SA49","identifierLink":"https://www.uniprot.org/uniprotkb/J7SA49/entry","name":"let-526","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16630598","identifier":"Q2A950","identifierLink":"https://www.uniprot.org/uniprotkb/Q2A950/entry","name":"phf-10","description":"PHD finger protein 10","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-315606","identifier":"Q17581","identifierLink":"https://www.uniprot.org/uniprotkb/Q17581/entry","name":"swsn-9","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR22881","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-360213","identifier":"Q21831","identifierLink":"https://www.uniprot.org/uniprotkb/Q21831/entry","name":"snfc-5","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6733661","identifier":"H8ESF3","identifierLink":"https://www.uniprot.org/uniprotkb/H8ESF3/entry","name":"swsn-1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6734414","identifier":"O02101","identifierLink":"https://www.uniprot.org/uniprotkb/O02101/entry","name":"swsn-2.2","description":"SWI/SNF chromatin-remodeling accessory subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6742050","identifier":"Q09646","identifierLink":"https://www.uniprot.org/uniprotkb/Q09646/entry","name":"ham-3","description":"SWI/SNF chromatin-remodeling accessory subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6755632","identifier":"Q9BL39","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BL39/entry","name":"swsn-3","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1031","complexName":"PBAF chromatin remodeling complex","organismName":"Caenorhabditis elegans; 6239","description":"An ATP-dependent chromatin remodeling complex that is part of the SWI/SNF chromatin remodeling complex superfamily and is involved in remodeling chromatin structure by destabilizing the histone-DNA interaction. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). The complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis.\r\n\r\nThe complex is involved in a variety of developmental processes including embryonic cell divisions, larval asymmetric cell divisions, generation of neuroblasts and neurons, muscle differentiation, somatic gonadogenesis, vulval induction, and timing of larval development.\r\n\r\nThe complex mediates the response to stress resistance. Subunits pbrm-1 and swsn-7 are recruited to ethanol and stress response elements (ESRE) within the promoters of stress-inducible genes to positively regulate the expression, in response to heat stress and hypoxia.\r\n\r\nPlays a role in the terminal differentiation of neurons. Specifically, the ham-3 subunit is involved in HSN motor neuron positioning, axon guidance and serotonin synthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-13645508","identifier":"G5EF53","identifierLink":"https://www.uniprot.org/uniprotkb/G5EF53/entry","name":"swsn-4","description":"SWI/SNF chromatin remodeling complex core catalytic subunit swsn-4","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13645532","identifier":"Q9N4N4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9N4N4/entry","name":"swsn-6","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13645585","identifier":"Q09441","identifierLink":"https://www.uniprot.org/uniprotkb/Q09441/entry","name":"swsn-7","description":"SWI/SNF chromatin remodeling complex subunit swsn-7","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR22970","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13645601","identifier":"G5EEY5","identifierLink":"https://www.uniprot.org/uniprotkb/G5EEY5/entry","name":"pbrm-1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR16062","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16630598","identifier":"Q2A950","identifierLink":"https://www.uniprot.org/uniprotkb/Q2A950/entry","name":"phf-10","description":"PHD finger protein 10","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-315606","identifier":"Q17581","identifierLink":"https://www.uniprot.org/uniprotkb/Q17581/entry","name":"swsn-9","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR22881","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-316362","identifier":"Q09477","identifierLink":"https://www.uniprot.org/uniprotkb/Q09477/entry","name":"dpff-1","description":"Zinc finger protein dpff-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-360213","identifier":"Q21831","identifierLink":"https://www.uniprot.org/uniprotkb/Q21831/entry","name":"snfc-5","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6733661","identifier":"H8ESF3","identifierLink":"https://www.uniprot.org/uniprotkb/H8ESF3/entry","name":"swsn-1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6734414","identifier":"O02101","identifierLink":"https://www.uniprot.org/uniprotkb/O02101/entry","name":"swsn-2.2","description":"SWI/SNF chromatin-remodeling accessory subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6742050","identifier":"Q09646","identifierLink":"https://www.uniprot.org/uniprotkb/Q09646/entry","name":"ham-3","description":"SWI/SNF chromatin-remodeling accessory subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6755632","identifier":"Q9BL39","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BL39/entry","name":"swsn-3","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1032","complexName":"Importin complex, Snurportin variant","organismName":"Homo sapiens; 9606","description":"A nuclear import complex that functions as a nuclear import receptor and specifically imports m3G-capped U snRNAs. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1. KPNB1 binds to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran-GTP (P62826) binds to KPNB1, the three components separate and SNUPN and KPNB1 are re-exported from the nucleus to the cytoplasm where GTP is hydrolysed. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.","predictedComplex":false,"interactors":[{"ac":"EBI-286758","identifier":"Q14974","identifierLink":"https://www.uniprot.org/uniprotkb/Q14974/entry","name":"KPNB1","description":"Importin subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714033","identifier":"O95149","identifierLink":"https://www.uniprot.org/uniprotkb/O95149/entry","name":"SNUPN","description":"Snurportin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13403","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1033","complexName":"Tenascin-R complex","organismName":"Mus musculus; 10090","description":"A matricellular glycoprotein complex of the extracellular matrix (ECM), and in particularly of the perineuronal net, where it assembles complexes of ECM proteins, glycosaminoglycans and proteoglycans. Almost exclusively expressed by and located on oligodendrocyte and myelin in the central nervous system. Also appears transiently on Schwann cells during peripheral nerve development and at differentiated nodes of Ranvier. Not expressed by astrocytes or fibroblasts but may regulate their adhesion properties. Expression is low in embryos and increases with progression to adulthood but decreases with individual cell differentiation. Regulated by various growth factors and lectins. \r\n\r\nRegulates cell adhesion, migration and differentiation and neurite outgrowth through domain-specific interactions depending on cell type and developmental context: Positively regulates cell adhesion and differentiation by binding surface sulfatides on O4+ oligodendrocytes. Negatively regulates fibronectin- and integrin-mediated neurite outgrowth and cell adhesion by interacting with contactin-1 (CNTN1/F3, P12960) or fibronectin FN1 (P11276) itself or by binding cell-surface chondroitin sulfate glycosaminoglycans or gangliosides of oligodendrocyte or their precursors. Oligomerisation negatively affects its inhibitory role on cell adhesion and neural outgrowth. Regulates cell plasticity by regulating secretion of growth factor and cytokines. Induces the generation of GABAergic neurons. Involved in synapse formation.","predictedComplex":false,"interactors":[{"ac":"EBI-774167","identifier":"Q8BYI9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BYI9/entry","name":"Tnr","description":"Tenascin-R","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR19143","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1034","complexName":"Tenascin-X complex","organismName":"Mus musculus; 10090","description":"A matricellular glycoprotein complex of the extracellular matrix (ECM) constitutively expressed in collagen-rich connective tissues and peripheral nerves. Present in particularly highly levels in developing heart, skeletal muscles, tendons, ligaments and limbs. Plays an important role in ECM architecture, tissue integrity and in the biomechanical properties of connective tissues. Binds to and bridges collagen fibrils and regulates collagen deposition. Binds heparin but, unlike other members of the Tenascin family, does not bind fibronectin. May also interact with heparin-sulfate proteoglycan receptors. May also interact with heparin-sulfate proteoglycan receptors. Involved in the regulation of many cellular processes such as cell adhesion, cell migration, cell fate determination or cell differentiation, epithelial cell plasticity (e.g. epithelial to mesenchymal transition or vice versa), cell proliferation and the vascular endothelial growth factor (VEGF) signaling pathway. Regulates transforming growth factor beta activation via cell adhesion by binding of the FBG-like domain (Fibrinogen-like globular domain, IPR002181) of Tenascin-X to alpha11beta1 integrin (CPX-3125). May act as a tumour suppressor. \r\n\r\nAn alternative promoter and transcription start site is activated by hypoxia in the adrenal gland resulting in a transcript encoding a truncated short TNXB protein with cytoplasmic localization.","predictedComplex":false,"interactors":[{"ac":"EBI-13646135","identifier":"O54796","identifierLink":"https://www.uniprot.org/uniprotkb/O54796/entry","name":"Tnx","description":null,"stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-1035","complexName":"Tenascin-X complex","organismName":"Bos taurus; 9913","description":"A matricellular glycoprotein complex of the extracellular matrix (ECM) constitutively expressed in collagen-rich connective tissues and peripheral nerves. Present in particularly highly levels in developing heart, skeletal muscles, tendons, ligaments and limbs. Plays an important role in ECM architecture, tissue integrity and in the biomechanical properties of connective tissues. Binds to and bridges collagen fibrils and regulates collagen deposition. Binds heparin but, unlike other members of the Tenascin family, does not bind fibronectin.  May also interact with heparin-sulfate proteoglycan receptors. Involved in the regulation of many cellular processes such as cell adhesion, cell migration, cell fate determination or cell differentiation, epithelial cell plasticity (e.g. epithelial to mesenchymal transition or vice versa), cell proliferation and the vascular endothelial growth factor (VEGF) signaling pathway. Regulates transforming growth factor beta activation via cell adhesion by binding of the FBG-like domain (Fibrinogen-like globular domain, IPR002181) of Tenascin-X to alpha11beta1 integrin (CPX-3125). May act as a tumour suppressor. \r\n\r\nAn alternative promoter and transcription start site is activated by hypoxia in the adrenal gland resulting in a transcript encoding a truncated short TNXB protein with cytoplasmic localization.","predictedComplex":false,"interactors":[{"ac":"EBI-13646261","identifier":"O18977","identifierLink":"https://www.uniprot.org/uniprotkb/O18977/entry","name":"TN-X","description":null,"stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[]}]},{"complexAC":"CPX-1042","complexName":"GAL3-GAL80 transcription regulation complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Acts to relieve the repression of the GAL4  positive regulator of gene expression. The GAL network is a small set of genes that regulates galactose import and metabolism. The transcriptional activator GAL4 activates a set of enzymatic and regulatory genes by binding to their promoter regions. When galactose is the sole carbon source, the galactose-metabolizing enzymes are expressed at 1000 times their level in glucose. \r\n\r\nIn the absence of galactose, GAL4 activity is repressed by forming a complex with the transcriptional repressor GAL80 (CPX-1044). In the presence of galactose and ATP, the GAL3-GAL80 complex forms, removing GAL80 from the GAL4-activation domain, which is then able to recruit the transcriptional machinery. It is also possible a tripartite complex forms (GAL4-GAL80-GAL3), which counterbalances the effect of GAL80 on GAL4 and allows GAL4 to interact with  promoters. GAL3 primarily binds with ATP and galactose in the cytoplasm,  then moves into the nucleus to interact with GAL80. A paralogous complex, GAL1-GAL80 (CPX-1043) can also form but appears to have lower activity as a transcriptional inducer of GAL genes. It is possible that GAL3-GAL80 may be involved solely in the short-term response to galactose and GAL1-GAL80 is required for continued expression of the GAL genes.","predictedComplex":false,"interactors":[{"ac":"EBI-13916437","identifier":"CHEBI:28061","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:28061","name":"alpha-d-galactose","description":"alpha-D-galactose","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-13916452","identifier":"CHEBI:30617","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30617","name":"mgatp(2-)","description":"MgATP(2-)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2061197","identifier":"P04387","identifierLink":"https://www.uniprot.org/uniprotkb/P04387/entry","name":"GAL80","description":"Galactose/lactose metabolism regulatory protein GAL80","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43708","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7282","identifier":"P13045","identifierLink":"https://www.uniprot.org/uniprotkb/P13045/entry","name":"GAL3","description":"Protein GAL3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10457","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1043","complexName":"GAL1-GAL80 transcription regulation complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Acts to relieve the repression of the GAL4  positive regulator of gene expression. The GAL network is a small set of genes that regulates galactose import and metabolism. The transcriptional activator GAL4 activates a set of enzymatic and regulatory genes by binding to their promoter regions. When galactose is the sole carbon source, the galactose-metabolizing enzymes are expressed at 1000 times their level in glucose. \r\n\r\nIn the absence of galactose, GAL4 activity is repressed by forming a complex with the transcriptional repressor GAL80 (CPX-1044). In the presence of galactose and ATP, the GAL1-GAL80 complex forms, removing GAL80 from the GAL4-activation domain, which is then able to recruit the transcriptional machinery. It is also possible a tripartite complex forms (GAL4-GAL80-GAL1), which counterbalances the effect of GAL80 on GAL4 and allows GAL4 to interact with  promoters. GAL1 primarily binds with ATP and galactose in the cytoplasm,  then moves into the nucleus to interact with GAL80. A paralogous complex, GAL3-GAL80 (CPX-1042) can also form and appears to have significantly higher activity as a transcriptional inducer of GAL genes. The importance of GAL1-GAL80 is unclear as it appears that GAL1 is not sufficiently expressed in the absence of galactose to serve as an inducer but other evidence suggests the complex may be required for the continued expression of the GAL genes.","predictedComplex":false,"interactors":[{"ac":"EBI-13916437","identifier":"CHEBI:28061","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:28061","name":"alpha-d-galactose","description":"alpha-D-galactose","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-13916452","identifier":"CHEBI:30617","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30617","name":"mgatp(2-)","description":"MgATP(2-)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2061197","identifier":"P04387","identifierLink":"https://www.uniprot.org/uniprotkb/P04387/entry","name":"GAL80","description":"Galactose/lactose metabolism regulatory protein GAL80","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43708","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7272","identifier":"P04385","identifierLink":"https://www.uniprot.org/uniprotkb/P04385/entry","name":"GAL1","description":"Galactokinase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10457","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1044","complexName":"GAL4-GAL80 transcription repressor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Acts to repress the GAL4  positive regulator of gene expression. The GAL network is a small set of genes that regulates galactose import and metabolism. The transcriptional activator GAL4 activates a set of enzymatic and regulatory genes by binding to their promoter regions. When galactose is the sole carbon source, the galactose-metabolizing enzymes are expressed at 1000 times their level in glucose. In the absence of galactose, GAL4 activity is repressed by forming a complex with the transcriptional repressor GAL80. \r\n\r\nIn the presence of galactose and ATP, the GAL3-GAL80 complex (CPX-1042) forms, removing GAL80 from the GAL4-activation domain, which is then able to recruit the transcriptional machinery. It is also possible a tripartite complex forms (GAL4-GAL80-GAL3), which counterbalances the effect of GAL80 on GAL4 and allows GAL4 to interact with  promoters. GAL3 primarily binds with ATP and galactose in the cytoplasm,  then moves into the nucleus to interact with GAL80. A paralogous complex, GAL1-GAL80 (CPX-1043) can also form but appears to have lower activity as a transcriptional inducer of GAL genes. It is possible that GAL3-GAL80 may be involved solely in the short-term response to galactose and GAL1-GAL80 is required for continued expression of the GAL genes.","predictedComplex":false,"interactors":[{"ac":"EBI-2061197","identifier":"P04387","identifierLink":"https://www.uniprot.org/uniprotkb/P04387/entry","name":"GAL80","description":"Galactose/lactose metabolism regulatory protein GAL80","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43708","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4399035","identifier":"CHEBI:15846","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15846","name":"nad+","description":"nicotinamide adenine dinucleotide - oxidised form","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-4407660","identifier":"P04386","identifierLink":"https://www.uniprot.org/uniprotkb/P04386/entry","name":"GAL4","description":"Regulatory protein GAL4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47424","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1045","complexName":"ERV41-ERV46 retrograde receptor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Transporter complex that recognises, binds and returns endoplasmic reticulum (ER) resident proteins that have trafficked to Golgi compartments. Targets proteins lacking the HDEL motif recognised by COPI-coated vesicles. Transported back to the Golgi by COPII (CPX-2523) for the next round of retrograde transport.","predictedComplex":false,"interactors":[{"ac":"EBI-20659","identifier":"P39727","identifierLink":"https://www.uniprot.org/uniprotkb/P39727/entry","name":"ERV46","description":"ER-derived vesicles protein ERV46","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10984","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27850","identifier":"Q04651","identifierLink":"https://www.uniprot.org/uniprotkb/Q04651/entry","name":"ERV41","description":"ER-derived vesicles protein ERV41","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10984","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1047","complexName":"BUD23-TRM112 methyltransferase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"S-adenosylmethionine-dependent methyltransferase which plays a role in the synthesis of the small ribosomal subunit by catalyzing the N7-methylation of guanosine-1575 of 18S rRNA at the 20S pre-rRNA stage. The complex interacts with the box C/D snoRNA U3-associated DEAH RNA helicase DHR1, which appears to play a role in central pseudoknot formation, so may also contribute to controlling the folding of small subunit rRNA. May play a role in 40S ribosome maturation.","predictedComplex":false,"interactors":[{"ac":"EBI-21924","identifier":"P25627","identifierLink":"https://www.uniprot.org/uniprotkb/P25627/entry","name":"BUD23","description":"18S rRNA (guanine(1575)-N(7))-methyltransferase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12734","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28520","identifier":"P53738","identifierLink":"https://www.uniprot.org/uniprotkb/P53738/entry","name":"TRM112","description":"Multifunctional methyltransferase subunit TRM112","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12773","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1048","complexName":"Calcineurin-Calmodulin complex, alpha-R2 variant","organismName":"Homo sapiens; 9606","description":"A calcium-dependent, calmodulin-stimulated protein phosphatase complex that is activated by elevated cytoplasmic calcium ion concentrations. Important for many cellular activities such as homeostasis, angiogenesis, myogenesis, adipogenesis, osteogenesis, chondrocyte differentiation, cardiovascular system development, pancreatic beta-cell proliferation, hair follicle cell differentiation and remodeling, and activities of cells of the immune. Plays a pivotal role during nervous system development and in various functions of mature central and peripheral nervous system. Regulates the NFAT signaling cascade by binding to and dephosphorylating NFAT leading to nuclear translocation of this larger complex and increasing the DNA-binding affinity of the NFAT family of transcription factors. Calcineurin also promotes nuclear retention of NFAT by masking nuclear export signals (NES) and preventing NES-dependent nuclear export. Altered calcineurin-NFAT activation can mediate both neuroprotective and neurodegenerative signals and is linked to pathological features of neurodegenerative diseases such as amyotrophic lateral sclerosis, Huntingtons, Parkinsons, and Alzheimers diseases. \r\n\r\nModulates Ca2+-dependent inactivation (CDI) of voltage-gated L-type Ca2+ channels. CDI is initiated by Ca2+ binding to channel-associated calmodulin and subsequent activation of calcineurin, which is targeted to L channels by the A-kinase-anchoring protein AKAP5 (CPX-674). Channel activity is activated by phosphorylation of AKAP5-bound Protein Kinase A.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-352922","identifier":"Q08209","identifierLink":"https://www.uniprot.org/uniprotkb/Q08209/entry","name":"PPP3CA","description":"Protein phosphatase 3 catalytic subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3906025","identifier":"Q96LZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96LZ3/entry","name":"PPP3R2","description":"Calcineurin subunit B type 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397435","identifier":"P62158","identifierLink":"https://www.uniprot.org/uniprotkb/P62158/entry","name":"calm_human","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1049","complexName":"Calcineurin-Calmodulin complex, alpha-R2 variant","organismName":"Mus musculus; 10090","description":"A calcium-dependent, calmodulin-stimulated protein phosphatase complex that is activated by elevated cytoplasmic calcium ion concentrations. Important for many cellular activities such as homeostasis, angiogenesis, myogenesis, adipogenesis, osteogenesis, chondrocyte differentiation, cardiovascular system development, pancreatic beta-cell proliferation, hair follicle cell differentiation and remodeling, and activities of cells of the immune. Plays a pivotal role during nervous system development and in various functions of mature central and peripheral nervous system. Regulates the NFAT signaling cascade by binding to and dephosphorylating NFAT leading to nuclear translocation of this larger complex and increasing the DNA-binding affinity of the NFAT family of transcription factors. Calcineurin also promotes nuclear retention of NFAT by masking nuclear export signals (NES) and preventing NES-dependent nuclear export. Altered calcineurin-NFAT activation can mediate both neuroprotective and neurodegenerative signals. \r\n\r\nModulates Ca2+-dependent inactivation (CDI) of voltage-gated L-type Ca2+ channels. CDI is initiated by Ca2+ binding to channel-associated calmodulin and subsequent activation of calcineurin, which is targeted to L channels by the A-kinase-anchoring protein AKAP5. Channel activity is activated by phosphorylation of AKAP5-bound Protein Kinase A.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-13916676","identifier":"Q63811","identifierLink":"https://www.uniprot.org/uniprotkb/Q63811/entry","name":"Ppp3r2","description":"Calcineurin subunit B type 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397208","identifier":"P63328","identifierLink":"https://www.uniprot.org/uniprotkb/P63328/entry","name":"Ppp3ca","description":"Protein phosphatase 3 catalytic subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397460","identifier":"P62204","identifierLink":"https://www.uniprot.org/uniprotkb/P62204/entry","name":"Calm1","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1050","complexName":"Calcineurin-Calmodulin complex, gamma-R2 variant","organismName":"Homo sapiens; 9606","description":"A calcium-dependent, calmodulin-stimulated protein phosphatase complex that is activated by elevated cytoplasmic calcium ion concentrations. Important for many cellular activities such as homeostasis, angiogenesis, myogenesis, adipogenesis, osteogenesis, chondrocyte differentiation, cardiovascular system development, pancreatic beta-cell proliferation, hair follicle cell differentiation and remodeling, and activities of cells of the immune. Plays a pivotal role during nervous system development and in various functions of mature central and peripheral nervous system. Regulates the NFAT signaling cascade by binding to and dephosphorylating NFAT leading to nuclear translocation of this larger complex and increasing the DNA-binding affinity of the NFAT family of transcription factors. Calcineurin also promotes nuclear retention of NFAT by masking nuclear export signals (NES) and preventing NES-dependent nuclear export. Altered calcineurin-NFAT activation can mediate both neuroprotective and neurodegenerative signals and is linked to pathological features of neurodegenerative diseases such as amyotrophic lateral sclerosis, Huntingtons, Parkinsons, and Alzheimers diseases. \r\n\r\nModulates Ca2+-dependent inactivation (CDI) of voltage-gated L-type Ca2+ channels. CDI is initiated by Ca2+ binding to channel-associated calmodulin and subsequent activation of calcineurin, which is targeted to L channels by the A-kinase-anchoring protein AKAP5 (CPX-674). Channel activity is activated by phosphorylation of AKAP5-bound Protein Kinase A.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2827192","identifier":"P48454","identifierLink":"https://www.uniprot.org/uniprotkb/P48454/entry","name":"PPP3CC","description":"Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3906025","identifier":"Q96LZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96LZ3/entry","name":"PPP3R2","description":"Calcineurin subunit B type 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397435","identifier":"P62158","identifierLink":"https://www.uniprot.org/uniprotkb/P62158/entry","name":"calm_human","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1051","complexName":"Calcineurin-Calmodulin complex, gamma-R2 variant","organismName":"Mus musculus; 10090","description":"A calcium-dependent, calmodulin-stimulated protein phosphatase complex that is activated by elevated cytoplasmic calcium ion concentrations. Important for many cellular activities such as homeostasis, angiogenesis, myogenesis, adipogenesis, osteogenesis, chondrocyte differentiation, cardiovascular system development, pancreatic beta-cell proliferation, hair follicle cell differentiation and remodeling, and activities of cells of the immune. Plays a pivotal role during nervous system development and in various functions of mature central and peripheral nervous system. Regulates the NFAT signaling cascade by binding to and dephosphorylating NFAT leading to nuclear translocation of this larger complex and increasing the DNA-binding affinity of the NFAT family of transcription factors. Calcineurin also promotes nuclear retention of NFAT by masking nuclear export signals (NES) and preventing NES-dependent nuclear export. Altered calcineurin-NFAT activation can mediate both neuroprotective and neurodegenerative signals. \r\n\r\nModulates Ca2+-dependent inactivation (CDI) of voltage-gated L-type Ca2+ channels. CDI is initiated by Ca2+ binding to channel-associated calmodulin and subsequent activation of calcineurin, which is targeted to L channels by the A-kinase-anchoring protein AKAP5. Channel activity is activated by phosphorylation of AKAP5-bound Protein Kinase A.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-13916676","identifier":"Q63811","identifierLink":"https://www.uniprot.org/uniprotkb/Q63811/entry","name":"Ppp3r2","description":"Calcineurin subunit B type 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397460","identifier":"P62204","identifierLink":"https://www.uniprot.org/uniprotkb/P62204/entry","name":"Calm1","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-6271683","identifier":"P48455","identifierLink":"https://www.uniprot.org/uniprotkb/P48455/entry","name":"Ppp3cc","description":"Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1052","complexName":"TRM9-TRM112 methyltransferase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"S-adenosylmethionine-dependent methyltransferase involved in the formation of mcm5(s2)U (5-methoxycarbonylmethyl(2-thio)uridine) modifications at position 34 from the anticodon loop of some tRNAs. This modification is present at the wobble position of tRNAArg(UCU), tRNAGly(UCC), tRNALys(UUU), tRNAGln(UUG) and tRNAGlu(UUC). Modifications in the anticodon loop of tRNAs are known to influence the translation rate and fidelity of decoding.","predictedComplex":false,"interactors":[{"ac":"EBI-27735","identifier":"P49957","identifierLink":"https://www.uniprot.org/uniprotkb/P49957/entry","name":"TRM9","description":"tRNA (carboxymethyluridine(34)-5-O)-methyltransferase","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13069","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28520","identifier":"P53738","identifierLink":"https://www.uniprot.org/uniprotkb/P53738/entry","name":"TRM112","description":"Multifunctional methyltransferase subunit TRM112","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12773","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1053","complexName":"Cleavage and polyadenylation specificity factor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Endonuclease complex required for mRNA 3' end processing to form a defined 3' end of the transcribed RNA. The complex cleaves pre-mRNAs, adds a polyadenylate tail, and triggers transcription termination. The 3' end of mature mRNAs is generated by a site-specific endonucleolytic cleavage of an internal phosphodiester bond of the primary transcript by YSH1. The upstream cleavage product generated is then polyadenylated by PAP1 to form a 50-90 adenosine tail at its 3-prime hydroxyl end, which is required for nuclear export, translation, and stability of mRNA. The downstream cleavage product is rapidly degraded. Cleavage and polyadenylation cycles are regulated by phosphorylation/dephosphorylation. Phosphorylation of CPF is inhibitory to polyadenylation therefore dephosphorylation of CPF by GLC7 is required to switch the processing complex to one competent for poly(A) addition.","predictedComplex":false,"interactors":[{"ac":"EBI-12917","identifier":"P29468","identifierLink":"https://www.uniprot.org/uniprotkb/P29468/entry","name":"PAP1","description":"Poly(A) polymerase","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10682","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13715","identifier":"P32598","identifierLink":"https://www.uniprot.org/uniprotkb/P32598/entry","name":"GLC7","description":"Serine/threonine-protein phosphatase PP1-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11668","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14145","identifier":"Q01329","identifierLink":"https://www.uniprot.org/uniprotkb/Q01329/entry","name":"PTA1","description":"Pre-tRNA-processing protein PTA1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15245","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14915","identifier":"P42073","identifierLink":"https://www.uniprot.org/uniprotkb/P42073/entry","name":"REF2","description":"RNA end formation protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-18134","identifier":"P53538","identifierLink":"https://www.uniprot.org/uniprotkb/P53538/entry","name":"SSU72","description":"RNA polymerase II subunit A C-terminal domain phosphatase SSU72","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR20383","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23382","identifier":"P39927","identifierLink":"https://www.uniprot.org/uniprotkb/P39927/entry","name":"PTI1","description":"Protein PTI1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45735","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26608","identifier":"P36104","identifierLink":"https://www.uniprot.org/uniprotkb/P36104/entry","name":"SWD2","description":"COMPASS component SWD2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19861","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26710","identifier":"P35728","identifierLink":"https://www.uniprot.org/uniprotkb/P35728/entry","name":"MPE1","description":"Protein MPE1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15439","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28378","identifier":"P42841","identifierLink":"https://www.uniprot.org/uniprotkb/P42841/entry","name":"PFS2","description":"Polyadenylation factor subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22836","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31412","identifier":"Q12102","identifierLink":"https://www.uniprot.org/uniprotkb/Q12102/entry","name":"CFT2","description":"Cleavage factor two protein 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45922","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32872","identifier":"Q06632","identifierLink":"https://www.uniprot.org/uniprotkb/Q06632/entry","name":"CFT1","description":"Protein CFT1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-33763","identifier":"Q08553","identifierLink":"https://www.uniprot.org/uniprotkb/Q08553/entry","name":"SYC1","description":"Protein SYC1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-38049","identifier":"Q06102","identifierLink":"https://www.uniprot.org/uniprotkb/Q06102/entry","name":"YTH1","description":"mRNA 3'-end-processing protein YTH1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-38345","identifier":"Q06224","identifierLink":"https://www.uniprot.org/uniprotkb/Q06224/entry","name":"YSH1","description":"Endoribonuclease YSH1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11203","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6940","identifier":"P45976","identifierLink":"https://www.uniprot.org/uniprotkb/P45976/entry","name":"FIP1","description":"Pre-mRNA polyadenylation factor FIP1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1054","complexName":"Importin complex, KPNA2 variant","organismName":"Mus musculus; 10090","description":"A nuclear import complex that functions as a nuclear import receptor for proteins containing a nuclear localisation signal (NLS). Subunit Kpna2 specifically and directly binds to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by Kpnb1. Kpnb1 binds to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran-GTP (P62827) binds to Kpnb1, the three components separate and Kpna2 and Kpnb1 are re-exported from the nucleus to the cytoplasm where GTP is hydrolysed. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.","predictedComplex":false,"interactors":[{"ac":"EBI-3043908","identifier":"P52293","identifierLink":"https://www.uniprot.org/uniprotkb/P52293/entry","name":"Kpna2","description":"Importin subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23316","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-540580","identifier":"P70168","identifierLink":"https://www.uniprot.org/uniprotkb/P70168/entry","name":"Kpnb1","description":"Importin subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1055","complexName":"Importin complex, KPNA1 variant","organismName":"Homo sapiens; 9606","description":"A nuclear import complex that functions as a nuclear import receptor for proteins containing a nuclear localisation signal (NLS). Subunit KPNA1 specifically and directly binds to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1. KPNB1 binds to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, RAN-dependent mechanism. At the nucleoplasmic side of the NPC, RAN-GTP (P62826) binds to KPNB1, the three components separate and KPNA1 and KPNB1 are re-exported from the nucleus to the cytoplasm where GTP is hydrolysed. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of RAN between the cytoplasm and nucleus.","predictedComplex":false,"interactors":[{"ac":"EBI-286758","identifier":"Q14974","identifierLink":"https://www.uniprot.org/uniprotkb/Q14974/entry","name":"KPNB1","description":"Importin subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358383","identifier":"P52294","identifierLink":"https://www.uniprot.org/uniprotkb/P52294/entry","name":"KPNA1","description":"Importin subunit alpha-5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23316","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1056","complexName":"Importin complex, KPNA1 variant","organismName":"Mus musculus; 10090","description":"A nuclear import complex that functions as a nuclear import receptor for proteins containing a nuclear localisation signal (NLS). Subunit Kpna1 specifically and directly binds to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by Kpnb1. Kpnb1 binds to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran-GTP (P62827) binds to Kpnb1, the three components separate and Kpna1 and Kpnb1 are re-exported from the nucleus to the cytoplasm where GTP is hydrolysed. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.","predictedComplex":false,"interactors":[{"ac":"EBI-540580","identifier":"P70168","identifierLink":"https://www.uniprot.org/uniprotkb/P70168/entry","name":"Kpnb1","description":"Importin subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8573008","identifier":"Q60960","identifierLink":"https://www.uniprot.org/uniprotkb/Q60960/entry","name":"Kpna1","description":"Importin subunit alpha-5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23316","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1057","complexName":"Importin complex, KPNA3 variant","organismName":"Homo sapiens; 9606","description":"A nuclear import complex that functions as a nuclear import receptor for proteins containing a nuclear localisation signal (NLS). Subunit KPNA3 specifically and directly binds to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1. KPNB1 binds to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, RAN-dependent mechanism. At the nucleoplasmic side of the NPC, RAN-GTP (P62826) binds to KPNB1, the three components separate and KPNA3 and KPNB1 are re-exported from the nucleus to the cytoplasm where GTP is hydrolysed. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of RAN between the cytoplasm and nucleus.","predictedComplex":false,"interactors":[{"ac":"EBI-286758","identifier":"Q14974","identifierLink":"https://www.uniprot.org/uniprotkb/Q14974/entry","name":"KPNB1","description":"Importin subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358297","identifier":"O00505","identifierLink":"https://www.uniprot.org/uniprotkb/O00505/entry","name":"KPNA3","description":"Importin subunit alpha-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23316","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1058","complexName":"Importin complex, KPNA3 variant","organismName":"Mus musculus; 10090","description":"A nuclear import complex that functions as a nuclear import receptor for proteins containing a nuclear localisation signal (NLS). Subunit Kpna3 specifically and directly binds to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by Kpnb1. Kpnb1 binds to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran-GTP (P62827) binds to Kpnb1, the three components separate and Kpna3 and Kpnb1 are re-exported from the nucleus to the cytoplasm where GTP is hydrolysed. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.","predictedComplex":false,"interactors":[{"ac":"EBI-3043911","identifier":"O35344","identifierLink":"https://www.uniprot.org/uniprotkb/O35344/entry","name":"Kpna3","description":"Importin subunit alpha-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23316","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-540580","identifier":"P70168","identifierLink":"https://www.uniprot.org/uniprotkb/P70168/entry","name":"Kpnb1","description":"Importin subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1059","complexName":"Sorf-1-Sorf-2 complex","organismName":"Caenorhabditis elegans; 6239","description":"Endosomal trafficking complex. The complex acts in conjunction with rab switching proteins to negatively regulate the levels of phosphatidylinositol 3-phosphate (PtdIns3P) to allow for the conversion of early endosomes into late endosomes. In addition, the complex recruits bec-1 to suppress phosphatidylinositol 3-kinase (PI3K) activity in order to negatively regulate endosomal PtdIns3P.","predictedComplex":false,"interactors":[{"ac":"EBI-13941886","identifier":"Q23533","identifierLink":"https://www.uniprot.org/uniprotkb/Q23533/entry","name":"sorf-1","description":"Suppressor of organelle fusion 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-13941960","identifier":"Q10122","identifierLink":"https://www.uniprot.org/uniprotkb/Q10122/entry","name":"sorf-2","description":"Suppressor of organelle fusion 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR46866","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1060","complexName":"Importin complex, KPNA4 variant","organismName":"Homo sapiens; 9606","description":"A nuclear import complex that functions as a nuclear import receptor for proteins containing a nuclear localisation signal (NLS). Subunit KPNA4 specifically and directly binds to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1. KPNB1 binds to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, RAN-dependent mechanism. At the nucleoplasmic side of the NPC, RAN-GTP (P62826) binds to KPNB1, the three components separate and KPNA4 and KPNB1 are re-exported from the nucleus to the cytoplasm where GTP is hydrolysed. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of RAN between the cytoplasm and nucleus.","predictedComplex":false,"interactors":[{"ac":"EBI-286758","identifier":"Q14974","identifierLink":"https://www.uniprot.org/uniprotkb/Q14974/entry","name":"KPNB1","description":"Importin subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-396343","identifier":"O00629","identifierLink":"https://www.uniprot.org/uniprotkb/O00629/entry","name":"KPNA4","description":"Importin subunit alpha-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23316","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1061","complexName":"Importin complex, KPNA4 variant","organismName":"Mus musculus; 10090","description":"A nuclear import complex that functions as a nuclear import receptor for proteins containing a nuclear localisation signal (NLS). Subunit Kpna4 specifically and directly binds to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by Kpnb1. Kpnb1 binds to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran-GTP (P62827) binds to Kpnb1, the three components separate and Kpna4 and Kpnb1 are re-exported from the nucleus to the cytoplasm where GTP is hydrolysed. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.","predictedComplex":false,"interactors":[{"ac":"EBI-540580","identifier":"P70168","identifierLink":"https://www.uniprot.org/uniprotkb/P70168/entry","name":"Kpnb1","description":"Importin subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8372758","identifier":"O35343","identifierLink":"https://www.uniprot.org/uniprotkb/O35343/entry","name":"Kpna4","description":"Importin subunit alpha-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23316","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1062","complexName":"Amyloid-beta protein 40/42 complex","organismName":"Homo sapiens; 9606","description":"Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. May have a role in depressing synaptic activity thus preventing excitotoxicity. Influences synaptic plasticity through various receptors, including NMDAR, mGluR and alpha7 nicotinic acetylcholine receptors (CPX-236). Mediates dendritic spine loss leading to decreased synapse density, inhibition of long-term potentiation (LTP), enhancement of long-term depression (LTD), excessive calcium influx and mitochondrial impairment. May affect metal ion homeostasis by chelating synaptic copper, zinc or iron ions. Mostly found in the extracellular space with a small proportion occurring as membrane-bound species. Dimers and oligomers (CPX-1120) of soluble amyloid-beta peptides are the main pathogenic species linked to Alzheimer's disease. Insoluble fibrils and plaques form during the latter stages of the disease. Chaperones, such as alphaB-crystallins or clusterin (P10909), bind to misfolded oligomeric species and form long-lived complexes, thereby preventing both their further growth into fibrils and their dissociation into synaptotoxic dimers. \r\n\r\nAmyloid-beta peptide may act as transcription factor for its own precursor protein APP and its cleavage enzyme BACE1 (P56817) initiating a positive feedback mechanism that ultimately leads to amyloidogenesis and Alzheimer's disease.","predictedComplex":false,"interactors":[{"ac":"EBI-2431589","identifier":"P05067-PRO_0000000093","identifierLink":"https://www.uniprot.org/uniprotkb/P05067-PRO_0000000093/entry","name":"APP","description":"Amyloid-beta protein 40","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-821758","identifier":"P05067-PRO_0000000092","identifierLink":"https://www.uniprot.org/uniprotkb/P05067-PRO_0000000092/entry","name":"APP","description":"Amyloid-beta protein 42","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-1063","complexName":"Importin complex, KPNA5 variant","organismName":"Homo sapiens; 9606","description":"A nuclear import complex that functions as a nuclear import receptor for proteins containing a nuclear localisation signal (NLS). Subunit KPNA5 specifically and directly binds to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1. KPNB1 binds to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, RAN-dependent mechanism. At the nucleoplasmic side of the NPC, RAN-GTP (P62826) binds to KPNB1, the three components separate and KPNA5 and KPNB1 are re-exported from the nucleus to the cytoplasm where GTP is hydrolysed. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of RAN between the cytoplasm and nucleus.","predictedComplex":false,"interactors":[{"ac":"EBI-286758","identifier":"Q14974","identifierLink":"https://www.uniprot.org/uniprotkb/Q14974/entry","name":"KPNB1","description":"Importin subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-540602","identifier":"O15131","identifierLink":"https://www.uniprot.org/uniprotkb/O15131/entry","name":"KPNA5","description":"Importin subunit alpha-6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23316","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1064","complexName":"Importin complex, KPNA6 variant","organismName":"Homo sapiens; 9606","description":"A nuclear import complex that functions as a nuclear import receptor for proteins containing a nuclear localisation signal (NLS). Subunit KPNA6 specifically and directly binds to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1. KPNB1 binds to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, RAN-dependent mechanism. At the nucleoplasmic side of the NPC, RAN-GTP (P62826) binds to KPNB1, the three components separate and KPNA6 and KPNB1 are re-exported from the nucleus to the cytoplasm where GTP is hydrolysed. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of RAN between the cytoplasm and nucleus.","predictedComplex":false,"interactors":[{"ac":"EBI-286758","identifier":"Q14974","identifierLink":"https://www.uniprot.org/uniprotkb/Q14974/entry","name":"KPNB1","description":"Importin subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359923","identifier":"O60684","identifierLink":"https://www.uniprot.org/uniprotkb/O60684/entry","name":"KPNA6","description":"Importin subunit alpha-7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23316","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1065","complexName":"Importin complex, KPNA6 variant","organismName":"Mus musculus; 10090","description":"A nuclear import complex that functions as a nuclear import receptor for proteins containing a nuclear localisation signal (NLS). Subunit Kpna6 specifically and directly binds to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by Kpnb1. Kpnb1 binds to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran-GTP (P62827) binds to Kpnb1, the three components separate and Kpna6 and Kpnb1 are re-exported from the nucleus to the cytoplasm where GTP is hydrolysed. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.","predictedComplex":false,"interactors":[{"ac":"EBI-11298230","identifier":"O35345","identifierLink":"https://www.uniprot.org/uniprotkb/O35345/entry","name":"Kpna6","description":"Importin subunit alpha-7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23316","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-540580","identifier":"P70168","identifierLink":"https://www.uniprot.org/uniprotkb/P70168/entry","name":"Kpnb1","description":"Importin subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1066","complexName":"Importin complex, KPNA7 variant","organismName":"Homo sapiens; 9606","description":"A nuclear import complex that functions as a nuclear import receptor for proteins containing a nuclear localisation signal (NLS). Subunit KPNA7 specifically and directly binds to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1. KPNB1 binds to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, RAN-dependent mechanism. At the nucleoplasmic side of the NPC, RAN-GTP (P62826) binds to KPNB1, the three components separate and KPNA7 and KPNB1 are re-exported from the nucleus to the cytoplasm where GTP is hydrolysed. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of RAN between the cytoplasm and nucleus.","predictedComplex":false,"interactors":[{"ac":"EBI-13942676","identifier":"A9QM74","identifierLink":"https://www.uniprot.org/uniprotkb/A9QM74/entry","name":"KPNA7","description":"Importin subunit alpha-8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23316","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-286758","identifier":"Q14974","identifierLink":"https://www.uniprot.org/uniprotkb/Q14974/entry","name":"KPNB1","description":"Importin subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1067","complexName":"Importin complex, KPNA7 variant","organismName":"Mus musculus; 10090","description":"A nuclear import complex that functions as a nuclear import receptor for proteins containing a nuclear localisation signal (NLS). Subunit Kpna7 specifically and directly binds to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by Kpnb1. Kpnb1 binds to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran-GTP (P62827) binds to Kpnb1, the three components separate and Kpna7 and Kpnb1 are re-exported from the nucleus to the cytoplasm where GTP is hydrolysed. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.","predictedComplex":false,"interactors":[{"ac":"EBI-13943188","identifier":"C0LLJ0","identifierLink":"https://www.uniprot.org/uniprotkb/C0LLJ0/entry","name":"Kpna7","description":"Importin subunit alpha-8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23316","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-540580","identifier":"P70168","identifierLink":"https://www.uniprot.org/uniprotkb/P70168/entry","name":"Kpnb1","description":"Importin subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1068","complexName":"Importin complex, KAP60-KAP95","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A nuclear import complex that functions as a nuclear import receptor for proteins containing a nuclear localisation signal (NLS). Subunit SRP1 specifically and directly binds to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KAP95. KAP95 binds to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, GSP1-dependent mechanism. At the nucleoplasmic side of the NPC, GSP1-GTP (P32835) binds to KAP95, the three components separate and SRP1 and KAP95 are re-exported from the nucleus to the cytoplasm where GTP is hydrolysed. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of GSP1 between the cytoplasm and nucleus.","predictedComplex":false,"interactors":[{"ac":"EBI-1797","identifier":"Q02821","identifierLink":"https://www.uniprot.org/uniprotkb/Q02821/entry","name":"SRP1","description":"Importin subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23316","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9145","identifier":"Q06142","identifierLink":"https://www.uniprot.org/uniprotkb/Q06142/entry","name":"KAP95","description":"Importin subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1069","complexName":"Amyloid-beta protein 40 complex","organismName":"Homo sapiens; 9606","description":"Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. May have a role in depressing synaptic activity thus preventing excitotoxicity. Influences synaptic plasticity through various receptors, including NMDAR, mGluR and alpha7 nicotinic acetylcholine receptors (CPX-236). Mediates dendritic spine loss leading to decreased synapse density, inhibition of long-term potentiation (LTP), enhancement of long-term depression (LTD), excessive calcium influx and mitochondrial impairment. May affect metal ion homeostasis by celating synaptic copper, zinc or iron ions. Mostly found in the extracellular space with a small proportion occurring as membrane-bound species. Dimers and oligomers of soluble amyloid-beta peptides are the main pathogenic species linked to Alzheimer's disease. Insoluble fibrils and plaques form during the latter stages of the disease. Chaperones, such as alphaB-crystallins or clusterin (P10909), bind to misfolded oligomeric species and form long-lived complexes, thereby preventing both their further growth into fibrils and their dissociation into synaptotoxic dimers. \r\n\r\nAmyloid-beta peptide may act as transcription factor for its own precursor protein APP and its cleavage enzyme BACE1 (P56817) initiating a positive feedback mechanism that ultimately leads to amyloidogenesis and Alzheimer's disease.","predictedComplex":false,"interactors":[{"ac":"EBI-2431589","identifier":"P05067-PRO_0000000093","identifierLink":"https://www.uniprot.org/uniprotkb/P05067-PRO_0000000093/entry","name":"APP","description":"Amyloid-beta protein 40","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-1070","complexName":"Amyloid-beta protein 42 complex","organismName":"Homo sapiens; 9606","description":"Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. May have a role in depressing synaptic activity thus preventing excitotoxicity. Influences synaptic plasticity through various receptors, including NMDAR, mGluR and alpha7 nicotinic acetylcholine receptors (CPX-236). Mediates dendritic spine loss leading to decreased synapse density, inhibition of long-term potentiation (LTP), enhancement of long-term depression (LTD), excessive calcium influx and mitochondrial impairment. May affect metal ion homeostasis by celating synaptic copper, zinc or iron ions. Oligomers of protein 42 only may have positive neurogenetic effects by activating synaptic protein kinases. Mostly found in the extracellular space with a small proportion occurring as membrane-bound species. Dimers and oligomers of soluble amyloid-beta peptides are the main pathogenic species linked to Alzheimer's disease. Insoluble fibrils and plaques form during the latter stages of the disease. Chaperones, such as alphaB-crystallins or clusterin (P10909), bind to misfolded oligomeric species and form long-lived complexes, thereby preventing both their further growth into fibrils and their dissociation into synaptotoxic dimers. \r\n\r\nAmyloid-beta peptide may act as transcription factor for its own precursor protein APP and its cleavage enzyme BACE1 (P56817) initiating a positive feedback mechanism that ultimately leads to amyloidogenesis and Alzheimer's disease.","predictedComplex":false,"interactors":[{"ac":"EBI-821758","identifier":"P05067-PRO_0000000092","identifierLink":"https://www.uniprot.org/uniprotkb/P05067-PRO_0000000092/entry","name":"APP","description":"Amyloid-beta protein 42","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-1071","complexName":"RecQ helicase-Topo III complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for both the early and late steps of DNA double-strand break (DSB) via dissolution of double Holliday junctions. Early in the repair of a two-ended DSB, the complex contributes to DSB end resection by facilitating the formation of a single-strand 3' overhang on which the homologous recombination (HR) factor Rad51 (P25454) filament assembles. The complex has also been implicated in the unwinding of strand invasion after extension of the invading 3' end by DNA synthesis to promote DSB repair by synthesis-dependent strand annealing, as well as reversal of strand invasion prior to 3' end extension. Through these functions, the complex promotes non-crossover outcomes of HR and regulates HR levels.","predictedComplex":false,"interactors":[{"ac":"EBI-17059","identifier":"P35187","identifierLink":"https://www.uniprot.org/uniprotkb/P35187/entry","name":"SGS1","description":"ATP-dependent helicase SGS1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13710","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19365","identifier":"P13099","identifierLink":"https://www.uniprot.org/uniprotkb/P13099/entry","name":"TOP3","description":"DNA topoisomerase 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11390","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-38690","identifier":"Q02685","identifierLink":"https://www.uniprot.org/uniprotkb/Q02685/entry","name":"RMI1","description":"RecQ-mediated genome instability protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1074","complexName":"SF1-U2AF65 splicing factor complex","organismName":"Homo sapiens; 9606","description":"Spliceosome complexes that recognizes consensus sequences at the 3-prime splice sites of pre-mRNAs. Once bound to the pre-mRNA, U2AF2 recruits the U2 small nuclear ribonucleoprotein particle (snRNP) to the assembling spliceosome. Phosphorylation of SF1 by UHMK1 (Q8TAS1) enhances SF1-U2AF2 interactions and promotes assembly of the ternary complex of SF1, U2AF2, and the 3-prime splice site.","predictedComplex":false,"interactors":[{"ac":"EBI-742339","identifier":"P26368","identifierLink":"https://www.uniprot.org/uniprotkb/P26368/entry","name":"U2AF2","description":"Splicing factor U2AF 65 kDa subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744603","identifier":"Q15637","identifierLink":"https://www.uniprot.org/uniprotkb/Q15637/entry","name":"SF1","description":"Splicing factor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11208","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1075","complexName":"Ribonucleoside-diphosphate reductase 1 complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the reduction of ribonucleotides to the corresponding deoxyribonucleotides, an essential step in the de novo synthesis of monomeric precursors for DNA replication and repair. The binding of effector dATP alters the active site to select for pyrimidines over purines, whereas effectors dGTP and TTP select for substrates ADP and GDP, respectively.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-370018","identifier":"P00452","identifierLink":"https://www.uniprot.org/uniprotkb/P00452/entry","name":"nrdA","description":"Ribonucleoside-diphosphate reductase 1 subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11573","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-555196","identifier":"P69924","identifierLink":"https://www.uniprot.org/uniprotkb/P69924/entry","name":"nrdB","description":"Ribonucleoside-diphosphate reductase 1 subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR23409","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1076","complexName":"mCRD-poly(A)-bridging complex","organismName":"Homo sapiens; 9606","description":"mRNA-bridging complex that forms between the 3-prime poly(A) tail and the major coding-region determinant of instability (mCRD) domain. Protects mRNA containing an mCRD domain prior to translation by stabilizing the poly(A) tail/PABP complex, thus blocking poly(A) nuclease access to the poly(A) tail. During translation, ribosomal movement up to or across the mCRD displaces or reorganizes the bridging complex, thereby allowing formation of metastable structures which expose the poly(A) tail to nuclease attack.\r\nThe complex is disrupted by competitive binding of PAIP2 (Q9BPZ3) to PABPC1, thus displacing PAIP1 from PABPC1 and PABPC1 from the poly(A) tail leading to premature deadenylation and mRNA decay.","predictedComplex":false,"interactors":[{"ac":"EBI-1024357","identifier":"O60506","identifierLink":"https://www.uniprot.org/uniprotkb/O60506/entry","name":"SYNCRIP","description":"Heterogeneous nuclear ribonucleoprotein Q","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21245","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-299674","identifier":"Q14103","identifierLink":"https://www.uniprot.org/uniprotkb/Q14103/entry","name":"HNRNPD","description":"Heterogeneous nuclear ribonucleoprotein D0","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48033","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-719186","identifier":"O75534","identifierLink":"https://www.uniprot.org/uniprotkb/O75534/entry","name":"CSDE1","description":"Cold shock domain-containing protein E1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12913","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-81519","identifier":"Q9H074","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H074/entry","name":"PAIP1","description":"Polyadenylate-binding protein-interacting protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23254","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-81531","identifier":"P11940","identifierLink":"https://www.uniprot.org/uniprotkb/P11940/entry","name":"PABPC1","description":"Polyadenylate-binding protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24012","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1077","complexName":"Chemotaxis phosphorelay complex CheA-CheY","organismName":"Escherichia coli (strain K12); 83333","description":"Plays a role in chemotaxis, the movement toward or away from chemicals. The complex is formed to activate cheY protein that then induces the change of the flagellar rotors from counterclocwise to clockwise rotation. cheA interacts with transmembrane chemoreceptors to generate stimulus signals via autophosphorylion of cheA which then serves as a phosphodonor for cheY. The P-cheY generated by this interaction binds to fliM (P06974), the switch component of the flagellar motor.","predictedComplex":false,"interactors":[{"ac":"EBI-1026773","identifier":"P07363","identifierLink":"https://www.uniprot.org/uniprotkb/P07363/entry","name":"cheA","description":"Chemotaxis protein CheA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43395","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-546693","identifier":"P0AE67","identifierLink":"https://www.uniprot.org/uniprotkb/P0AE67/entry","name":"cheY","description":"Chemotaxis protein CheY","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43228","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1078","complexName":"mCRD-poly(A)-bridging complex","organismName":"Mus musculus; 10090","description":"mRNA-bridging complex that forms between the 3-prime poly(A) tail and the major coding-region determinant of instability (mCRD) domain. Protects mRNA containing an mCRD domain prior to translation by stabilizing the poly(A) tail/PABP complex, thus blocking poly(A) nuclease access to the poly(A) tail. During translation, ribosomal movement up to or across the mCRD displaces or reorganizes the bridging complex, thereby allowing formation of metastable structures which expose the poly(A) tail to nuclease attack.\r\n\r\nThe complex is disrupted by competitive binding of Paip2 (Q9D6V8) to Pabpc1, thus displacing Paip1 from Pabpc1 and Pabpc1 from the poly(A) tail leading to premature deadenylation and mRNA decay.","predictedComplex":false,"interactors":[{"ac":"EBI-2735641","identifier":"Q7TMK9","identifierLink":"https://www.uniprot.org/uniprotkb/Q7TMK9/entry","name":"Syncrip","description":"Heterogeneous nuclear ribonucleoprotein Q","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21245","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-299932","identifier":"Q60668","identifierLink":"https://www.uniprot.org/uniprotkb/Q60668/entry","name":"Hnrnpd","description":"Heterogeneous nuclear ribonucleoprotein D0","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR48033","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-644652","identifier":"Q8VE62","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VE62/entry","name":"Paip1","description":"Polyadenylate-binding protein-interacting protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23254","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-773902","identifier":"P29341","identifierLink":"https://www.uniprot.org/uniprotkb/P29341/entry","name":"Pabpc1","description":"Polyadenylate-binding protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24012","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8318466","identifier":"Q91W50","identifierLink":"https://www.uniprot.org/uniprotkb/Q91W50/entry","name":"Csde1","description":"Cold shock domain-containing protein E1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12913","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1079","complexName":"DinJ-YafQ toxin-antitoxin complex","organismName":"Escherichia coli (strain K12); 83333","description":"Type II toxin-antitoxin (TA) system formed by the toxin (yafQ), and the antitoxin (dinJ). TA systems act as effectors of dormancy and persistence, with the toxin causing growth arrest by interfering with a vital cellular process, such as  transcription, translation or DNA replication,  and the cognate antitoxin neutralizing the toxin activity during normal growth conditions. The toxin yafQ degrades mRNA at adenosine-rich codons, most likely while it is bound to the ribosome. The binding of dinJ occludes the active site of yafQ. Under conditions of stress the antitoxins are selectively degraded by cellular proteases such as Lon (P0A9M0) and ClpXP (CPX-3176), leaving the toxins to exert their effectsl which result in growth arrest and cell dormancy. Both the antitoxin and, in most cases, the TA complex bind the TA promoter to repress transcription, with TA complexes repressing transcription more efficiently than the antitoxins alone by increasing the co-operativity of antitoxin binding to operators.The toxin yafQ degrades mRNA at adenosine-rich codons, most likely while it is bound to the ribosome.","predictedComplex":false,"interactors":[{"ac":"EBI-552648","identifier":"Q47149","identifierLink":"https://www.uniprot.org/uniprotkb/Q47149/entry","name":"yafQ","description":"mRNA interferase toxin YafQ","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR40588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6406953","identifier":"Q47150","identifierLink":"https://www.uniprot.org/uniprotkb/Q47150/entry","name":"dinJ","description":"Antitoxin DinJ","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR38781","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1080","complexName":"CRD-mediated mRNA stability complex","organismName":"Homo sapiens; 9606","description":"mRNA-binding complex that binds to the coding-region determinant of instability (CRD). Stabilizes mRNA (e.g. MYC mRNA) by inhibiting poly(A) tail deadenylation and premature mRNA decay by polysome-associated endonucleases. Active mainly during embryogenesis and tumorigenesis.","predictedComplex":false,"interactors":[{"ac":"EBI-1024357","identifier":"O60506","identifierLink":"https://www.uniprot.org/uniprotkb/O60506/entry","name":"SYNCRIP","description":"Heterogeneous nuclear ribonucleoprotein Q","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21245","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1053892","identifier":"Q9NZI8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZI8/entry","name":"IGF2BP1","description":"Insulin-like growth factor 2 mRNA-binding protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10288","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14022093","identifier":"CHEBI:33699","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:33699","name":"messenger rna","description":"messenger RNA","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-351126","identifier":"Q00839","identifierLink":"https://www.uniprot.org/uniprotkb/Q00839/entry","name":"HNRNPU","description":"Heterogeneous nuclear ribonucleoprotein U","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12381","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352022","identifier":"Q08211","identifierLink":"https://www.uniprot.org/uniprotkb/Q08211/entry","name":"DHX9","description":"ATP-dependent RNA helicase A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18934","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-354065","identifier":"P67809","identifierLink":"https://www.uniprot.org/uniprotkb/P67809/entry","name":"YBX1","description":"Y-box-binding protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11544","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1081","complexName":"RelBE toxin-antitoxin complex","organismName":"Escherichia coli (strain K12); 83333","description":"Type II toxin-antitoxin (TA) system formed by the toxin (relE), and the antitoxin (relB). TA systems act as effectors of dormancy and persistence, with the toxin causing growth arrest by interfering with a vital cellular process, such as  transcription, translation or DNA replication,  and the cognate antitoxin neutralizing the toxin activity during normal growth conditions. Free relE toxin is capable of cleaving mRNA during translation at the ribosomal A site, thus inhibiting translation during amino acid starvation (the stringent response). The antitoxin, relB, both binds and inhibits relE by inducing conformational changes in the relE active site. Under conditions of stress the antitoxins are selectively degraded by cellular proteases such as Lon (P0A9M0) and ClpXP (CPX-3176), leaving the toxins to exert their effectsl which result in growth arrest and cell dormancy. Both the antitoxin and, in most cases, the TA complex bind the TA promoter to repress transcription, with TA complexes repressing transcription more efficiently than the antitoxins alone by increasing the co-operativity of antitoxin binding to operators.","predictedComplex":false,"interactors":[{"ac":"EBI-1124503","identifier":"P0C079","identifierLink":"https://www.uniprot.org/uniprotkb/P0C079/entry","name":"relB","description":"Antitoxin RelB","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR38781","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549378","identifier":"P0C077","identifierLink":"https://www.uniprot.org/uniprotkb/P0C077/entry","name":"relE","description":"mRNA interferase toxin RelE","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR35601","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1082","complexName":"Flagellar Motor Switch Complex, CW variant","organismName":"Escherichia coli (strain K12); 83333","description":"Plays a role in chemotaxis, the movement toward or away from chemicals. The flagellar motor of bacteria is a rotary device energized by the membrane ion gradient and the complex is required for the rotation and directional switching of the flagellum and also functions in flagellar assembly. Motor torque is produced at the top of the switch complex, where the fliG C-terminal domain bears several conserved charged residues that interact with charged groups of the stator protein motA (P09348). The conformation of this complex is such that the flagellum rotates in a clockwise (CW) direction, induced by binding of cheY-P to the lower part of the C-ring.","predictedComplex":false,"interactors":[{"ac":"EBI-1126524","identifier":"P0ABZ1","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABZ1/entry","name":"fliG","description":"Flagellar motor switch protein FliG","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30534","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2011987","identifier":"P15070","identifierLink":"https://www.uniprot.org/uniprotkb/P15070/entry","name":"fliN","description":"Flagellar motor switch protein FliN","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43484","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-546693","identifier":"P0AE67","identifierLink":"https://www.uniprot.org/uniprotkb/P0AE67/entry","name":"cheY","description":"Chemotaxis protein CheY","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43228","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-560439","identifier":"P06974","identifierLink":"https://www.uniprot.org/uniprotkb/P06974/entry","name":"fliM","description":"Flagellar motor switch protein FliM","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30034","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1083","complexName":"Cobalamin outer membrane transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"A member of the TonB-dependent transporter family (TBDTs) which binds and then transports cobalamine (vitamin B12) across the outer membrane. TBDTs are energy-dependent gated channels that usually transport large metal complexes which cannot fit through porins, and are too scarce to enter by mass-action-driven transport. Energy-dependent uptake through TBDTs requires interaction with tonB in complex with exbB and exbD in the inner membrane, ExbBD. tonB undergoes rapid energized movement driven by ExbBD which harvest the electrochemical force from the electrochemical proton gradient created by the proton gradient across the inner membrane and convert it into rotational motion. Hence, tonB may pull or twist the N-termini of TBDTs to promote transport of substrates into the periplasm. ATP-binding-cassette (ABC) transporters subsequently move the cyanocobalamine through the periplasm and inner membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-1037258","identifier":"P06129","identifierLink":"https://www.uniprot.org/uniprotkb/P06129/entry","name":"btuB","description":"Vitamin B12 transporter BtuB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30069","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6399986","identifier":"P0ABU7","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABU7/entry","name":"exbB","description":"Biopolymer transport protein ExbB","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6399993","identifier":"P02929","identifierLink":"https://www.uniprot.org/uniprotkb/P02929/entry","name":"tonB","description":"Protein TonB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33446","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6417016","identifier":"P0ABV2","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABV2/entry","name":"exbD","description":"Biopolymer transport protein ExbD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1084","complexName":"MqsRA toxin-antitoxin complex","organismName":"Escherichia coli (strain K12); 83333","description":"Type II toxin-antitoxin (TA) module consisting of MqsR toxins bound to MqsA antitoxin dimer. TA systems act as effectors of dormancy and persistence and are composed of a toxin, which causes growth arrest by interfering with a vital cellular process, and a cognate antitoxin, which neutralizes the toxin activity during normal growth conditions.  Under conditions of stress the antitoxins are selectively degraded, leaving the toxins to exert their toxic effects, leading to growth arrest and dormancy. Type II TA complexes are small protein-protein pairs; under growth conditions, the toxin is bound to the antitoxin, which inhibits its activity. Unlike other type II toxins, mqsR does not enhance the binding of mqsA to the mqsRA promoter. Instead, MqsR disrupts the MqsA-DNA interaction. Under stress conditions, cellular proteases such as Lon (P0A9M0) and ClpXP (CPX-3176) are activated that preferentially cleave the antitoxins, freeing the toxins to inhibit growth by inhibiting translation or replication, enabling cells to enter a metabolically dormant state until the stress is removed. MqsR toxin is the most up-regulated gene in the persister phenotype of cells. When active, MqsA binds its promoter with extremely tight affinity, however this is destabilized by TA complex formation as the binding sites of MqsR and DNA on MqsA overlap and their binding is mutually exclusive. Plays a role in biofilm formation.","predictedComplex":false,"interactors":[{"ac":"EBI-1120353","identifier":"Q46864","identifierLink":"https://www.uniprot.org/uniprotkb/Q46864/entry","name":"mqsA","description":"Antitoxin MqsA","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR36511","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1131259","identifier":"Q46865","identifierLink":"https://www.uniprot.org/uniprotkb/Q46865/entry","name":"mqsR","description":"mRNA interferase toxin MqsR","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]}]},{"complexAC":"CPX-1085","complexName":"Flagellar Motor Switch Complex, CCW variant","organismName":"Escherichia coli (strain K12); 83333","description":"Plays a role in chemotaxis, the movement toward or away from chemicals. The flagellar motor of bacteria is a rotary device energized by the membrane ion gradient and the complex is required for the rotation and directional switching of the flagellum and also functions in flagellar assembly. Motor torque is produced at the top of the switch complex, where the fliG C-terminal domain bears several conserved charged residues that interact with charged groups of the stator protein motA (P09348). The conformation of this complex is such that the flagellum rotates in a counter-clockwise (CCW) direction.","predictedComplex":false,"interactors":[{"ac":"EBI-1126524","identifier":"P0ABZ1","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABZ1/entry","name":"fliG","description":"Flagellar motor switch protein FliG","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30534","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2011987","identifier":"P15070","identifierLink":"https://www.uniprot.org/uniprotkb/P15070/entry","name":"fliN","description":"Flagellar motor switch protein FliN","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43484","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-560439","identifier":"P06974","identifierLink":"https://www.uniprot.org/uniprotkb/P06974/entry","name":"fliM","description":"Flagellar motor switch protein FliM","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30034","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1086","complexName":"MazEF toxin-antitoxin complex","organismName":"Escherichia coli (strain K12); 83333","description":"Type II toxin-antitoxin (TA) system formed by the toxin (maxF), and the antitoxin (mazE). TA systems act as effectors of dormancy and persistence, with the toxin causing growth arrest by interfering with a vital cellular process, such as  transcription, translation or DNA replication,  and the cognate antitoxin neutralizing the toxin activity during normal growth conditions. Presence of free mazF toxin induces programmed cell death by cleavage of RNA specifically at ACA sequences to block protein synthesis. Under conditions of stress the antitoxins are selectively degraded by cellular proteases such as Lon (P0A9M0) and ClpXP (CPX-3176), leaving the toxins to exert their effectsl which result in growth arrest and cell dormancy. Both the antitoxin and, in most cases, the TA complex bind the TA promoter to repress transcription, with TA complexes repressing transcription more efficiently than the antitoxins alone by increasing the co-operativity of antitoxin binding to operators. Plays a role in biofilm formation.","predictedComplex":false,"interactors":[{"ac":"EBI-1036253","identifier":"P0AE70","identifierLink":"https://www.uniprot.org/uniprotkb/P0AE70/entry","name":"mazF","description":"Endoribonuclease toxin MazF","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33988","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1130282","identifier":"P0AE72","identifierLink":"https://www.uniprot.org/uniprotkb/P0AE72/entry","name":"mazE","description":"Antitoxin MazE","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR40516","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1087","complexName":"YoeB-YefM toxin-antitoxin complex","organismName":"Escherichia coli (strain K12); 83333","description":"Type II toxin-antitoxin (TA) system formed by the toxin (yoeB), and the antitoxin (yefM). TA systems act as effectors of dormancy and persistence, with the toxin causing growth arrest by interfering with a vital cellular process, such as  transcription, translation or DNA replication,  and the cognate antitoxin neutralizing the toxin activity during normal growth conditions. yoeB has translation-dependent mRNA degradation activity and preferentially cleaves at 3-prime ends of purine-rich ribonucleotides. Under conditions of stress the antitoxins are selectively degraded by cellular proteases such as Lon (P0A9M0) and ClpXP (CPX-3176), leaving the toxins to exert their effectsl which result in growth arrest and cell dormancy. Both the antitoxin and, in most cases, the TA complex bind the TA promoter to repress transcription, with TA complexes repressing transcription more efficiently than the antitoxins alone by increasing the co-operativity of antitoxin binding to operators.","predictedComplex":false,"interactors":[{"ac":"EBI-8755628","identifier":"P69346","identifierLink":"https://www.uniprot.org/uniprotkb/P69346/entry","name":"yefM","description":"Antitoxin YefM","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33713","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8755644","identifier":"P69348","identifierLink":"https://www.uniprot.org/uniprotkb/P69348/entry","name":"yoeB","description":"Toxin YoeB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR38039","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1088","complexName":"Chemotaxis phosphorelay complex CheY-CheZ","organismName":"Escherichia coli (strain K12); 83333","description":"Plays a role in chemotaxis, the movement toward or away from chemicals. The flagellar motor of bacteria is a rotary device energized by the membrane ion gradient and the complex is required for the rotation and directional switching of the flagellum and also functions in flagellar assembly. Motor torque is produced at the top of the switch complex, where the fliG C-terminal domain bears several conserved charged residues that interact with charged groups of the stator protein motA (P09348). The directionality of the rotation is determined by binding of cheY-P to the lower part of the C-ring which switches the directionality from counter-clockwise to clockwise. The cheY-cheZ complex enhances the dephosphorylation rate of P-cheY. This dephosphorylation reduces the binding of cheY to the switch and ensures rapid locomotor responses to changes in the supply of signaling phosphoryl groups to cheY, thus enabling a continuous response to environmental changes.","predictedComplex":false,"interactors":[{"ac":"EBI-546693","identifier":"P0AE67","identifierLink":"https://www.uniprot.org/uniprotkb/P0AE67/entry","name":"cheY","description":"Chemotaxis protein CheY","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43228","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-546726","identifier":"P0A9H9","identifierLink":"https://www.uniprot.org/uniprotkb/P0A9H9/entry","name":"cheZ","description":"Protein phosphatase CheZ","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43693","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1089","complexName":"CRD-mediated mRNA stability complex","organismName":"Mus musculus; 10090","description":"mRNA-binding complex that binds to the coding-region determinant of instability (CRD). Stabilizes mRNA (e.g. Myc mRNA) by inhibiting poly(A) tail deadenylation and premature mRNA decay by polysome-associated endonucleases. Active mainly during embryogenesis and tumorigenesis.","predictedComplex":false,"interactors":[{"ac":"EBI-14022093","identifier":"CHEBI:33699","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:33699","name":"messenger rna","description":"messenger RNA","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2657677","identifier":"O70133","identifierLink":"https://www.uniprot.org/uniprotkb/O70133/entry","name":"Dhx9","description":"ATP-dependent RNA helicase A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18934","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2735641","identifier":"Q7TMK9","identifierLink":"https://www.uniprot.org/uniprotkb/Q7TMK9/entry","name":"Syncrip","description":"Heterogeneous nuclear ribonucleoprotein Q","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21245","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-529674","identifier":"Q8VEK3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VEK3/entry","name":"Hnrnpu","description":"Heterogeneous nuclear ribonucleoprotein U","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12381","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-529779","identifier":"P62960","identifierLink":"https://www.uniprot.org/uniprotkb/P62960/entry","name":"Ybx1","description":"Y-box-binding protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11544","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8419818","identifier":"O88477","identifierLink":"https://www.uniprot.org/uniprotkb/O88477/entry","name":"Igf2bp1","description":"Insulin-like growth factor 2 mRNA-binding protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10288","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1090","complexName":"MukBEF condensin complex","organismName":"Escherichia coli (strain K12); 83333","description":"Key mediator of chromosome condensation, ensuring chromosomes are efficiently separated during replication and are faithfully segregated into daughter cells. A direct interaction between ParC of Topoisomerase IV (CPX-1104) and MukB leads to a fraction of TopoIV molecules being bound to MukBEF clusters Involved in chromosome condensation and segregation. MukB can stimulate the ability of topoisomerase IV to relax negatively supercoiled DNA.","predictedComplex":false,"interactors":[{"ac":"EBI-542943","identifier":"P22523","identifierLink":"https://www.uniprot.org/uniprotkb/P22523/entry","name":"mukB","description":"Chromosome partition protein MukB","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42963","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-554672","identifier":"P22524","identifierLink":"https://www.uniprot.org/uniprotkb/P22524/entry","name":"mukE","description":"Chromosome partition protein MukE","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-554679","identifier":"P60293","identifierLink":"https://www.uniprot.org/uniprotkb/P60293/entry","name":"mukF","description":"Chromosome partition protein MukF","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]}]},{"complexAC":"CPX-1092","complexName":"Succinyl-CoA synthetase","organismName":"Escherichia coli (strain K12); 83333","description":"Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. It catalyzes the reversible interchange of purine nucleoside diphosphate, succinyl-CoA and phosphate with purine nucleoside triphosphate, succinate, and CoA via a phosphorylated histidine intermediate.","predictedComplex":false,"interactors":[{"ac":"EBI-369078","identifier":"P0AGE9","identifierLink":"https://www.uniprot.org/uniprotkb/P0AGE9/entry","name":"sucD","description":"Succinate--CoA ligase [ADP-forming] subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-369117","identifier":"P0A836","identifierLink":"https://www.uniprot.org/uniprotkb/P0A836/entry","name":"sucC","description":"Succinate--CoA ligase [ADP-forming] subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11815","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1093","complexName":"LptDE outer membrane translocon complex","organismName":"Escherichia coli (strain K12); 83333","description":"Required for the assembly of the dense outer membrane coating of lipopolysaccharides( LPS) required by Gram-negative bacteria to protect themselves from chemical stressors. Part of a seven-subunit assembly  that spans the cellular envelope. Inserts LPS laterally into the outer leaflet of the outer membrane where it is dispersed across the extracellular surface.A lateral gate in the beta-barrel of LptD allows LPS to proceed to the outer leaflet of the outer membrane. The specific disulfide bond configuration of the lptDE heterodimer restricts the size of the lateral gate on the periplasmic side, and may prevent incorrect insertion of LPS into the inner leaflet of the outer membrane. lptE is embedded into the lptD lumen, thus potentially preserving membrane impermeability.","predictedComplex":false,"interactors":[{"ac":"EBI-1119442","identifier":"P0ADC1","identifierLink":"https://www.uniprot.org/uniprotkb/P0ADC1/entry","name":"lptE","description":"LPS-assembly lipoprotein LptE","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR38098","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549369","identifier":"P31554","identifierLink":"https://www.uniprot.org/uniprotkb/P31554/entry","name":"lptD","description":"LPS-assembly protein LptD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30189","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1094","complexName":"YgjD-YeaZ-YjeE complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyses the transfer of the threonylcarbamoyl-moiety of threonylcarbamoyladenylate onto A37 of substrate tRNA in the cytoplasm, or more probably in E.coli, the formation of 'cyclic t6A' (ct6A), which is a cyclized active ester with an oxazolone ring. The N6-threonylcarbamoyladenosine (t6A) modification is present at position 37 of tRNAs that recognize ANN-codons, with N being any nucleotide, enhancing the codon-anti-codon interaction and is required for recognition of the AUG start codon. The modification is thus important for maintaining translational fidelity. A stable YgjD-YeaZ heterodimer first forms, which has an atypical ADP-binding site at the YgjD-YeaZ interface that may also be the binding site for YjeE as the ternary complex only forms in the presence of ATP. An additional YrdC protein is necessary for T6a activity.","predictedComplex":false,"interactors":[{"ac":"EBI-1108845","identifier":"CHEBI:15422","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15422","name":"atp","description":"ATP","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2929936","identifier":"CHEBI:29033","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29033","name":"iron2plus","description":"iron(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-560669","identifier":"P76256","identifierLink":"https://www.uniprot.org/uniprotkb/P76256/entry","name":"tsaB","description":"tRNA threonylcarbamoyladenosine biosynthesis protein TsaB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11735","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-561268","identifier":"P0AF67","identifierLink":"https://www.uniprot.org/uniprotkb/P0AF67/entry","name":"tsaE","description":"tRNA threonylcarbamoyladenosine biosynthesis protein TsaE","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33540","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-561994","identifier":"P05852","identifierLink":"https://www.uniprot.org/uniprotkb/P05852/entry","name":"tsaD","description":"tRNA N6-adenosine threonylcarbamoyltransferase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11735","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1095","complexName":"Holo-translocon SecYEG-SecDF-YajC-YidC complex","organismName":"Escherichia coli (strain K12); 83333","description":"Functions in both protein secretion to the trans side of the plasma membrane and insertion of membrane proteins into the lipid bilayer. The HTL complex is more proficient in cotranslational membrane protein insertion compared with SecYEG (CPX-1096) alone and the post-translational secretion of a beta-barreled outer-membrane protein driven by secA and ATP becomes much more dependent on the proton-motive force than is the case for SecYEG. The yidC periplasmic and secD periplasmic region P1-head domains are positioned to interact with translocation substrates preventing backsliding of the polypeptide through the translocation channel.","predictedComplex":false,"interactors":[{"ac":"EBI-1130723","identifier":"P0ADZ7","identifierLink":"https://www.uniprot.org/uniprotkb/P0ADZ7/entry","name":"yajC","description":"Sec translocon accessory complex subunit YajC","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33909","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13950946","identifier":"P0AG93","identifierLink":"https://www.uniprot.org/uniprotkb/P0AG93/entry","name":"secF","description":"Protein translocase subunit SecF","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30081","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-555724","identifier":"P0AG90","identifierLink":"https://www.uniprot.org/uniprotkb/P0AG90/entry","name":"secD","description":"Protein translocase subunit SecD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30081","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6400779","identifier":"P25714","identifierLink":"https://www.uniprot.org/uniprotkb/P25714/entry","name":"yidC","description":"Membrane protein insertase YidC","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR12428","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6404248","identifier":"P0AG99","identifierLink":"https://www.uniprot.org/uniprotkb/P0AG99/entry","name":"secG","description":"Protein-export membrane protein SecG","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34182","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6404267","identifier":"P0AG96","identifierLink":"https://www.uniprot.org/uniprotkb/P0AG96/entry","name":"secE","description":"Protein translocase subunit SecE","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33910","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-761422","identifier":"P0AGA2","identifierLink":"https://www.uniprot.org/uniprotkb/P0AGA2/entry","name":"secY","description":"Protein translocase subunit SecY","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10906","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1096","complexName":"Protein-conducting channel SecYEG complex","organismName":"Escherichia coli (strain K12); 83333","description":"Functions in both protein secretion to the trans side of the plasma membrane and insertion of membrane proteins into the lipid bilayer. Associates with the motor ATPase SecA, which drives post-translational translocation of pre-proteins across the membrane.Membrane proteins are targeted to the membrane co-translationally by the signal recognition particle (SRP) associating with its receptor at the cytosolic surface. The ribosome nascent chain complex is then passed onto the dimeric SecYEG complex and the nascent membrane protein is threaded through the protein channel and into the bilayer via a lateral gate. Also forms a holo-translocon super-complex comprising of the SecYEG core complex, the accessory sub-complex SecDF-YajC and YidC.","predictedComplex":false,"interactors":[{"ac":"EBI-6404248","identifier":"P0AG99","identifierLink":"https://www.uniprot.org/uniprotkb/P0AG99/entry","name":"secG","description":"Protein-export membrane protein SecG","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34182","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6404267","identifier":"P0AG96","identifierLink":"https://www.uniprot.org/uniprotkb/P0AG96/entry","name":"secE","description":"Protein translocase subunit SecE","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33910","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-761422","identifier":"P0AGA2","identifierLink":"https://www.uniprot.org/uniprotkb/P0AGA2/entry","name":"secY","description":"Protein translocase subunit SecY","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10906","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1097","complexName":"C-to-U editosome complex","organismName":"Homo sapiens; 9606","description":"mRNA editing complex that deaminates a CAA (Gln) to an UAA (Stop) codon in the ApoB mRNA in the luminal gastrointestinal tract and liver in healthy individuals, resulting in the generation of a truncated ApoB48 protein (P04114-PRO_0000020751) which mediates the absorption of dietary lipid from the intestine. The complex recognizes, and binds to, an 11-nucleotide mooring sequence downstream of the editing site and, in addition to C to U editing, also protects the edited ApoB mRNA from nonsense-mediated decay. APOBEC1 mediates nucleocytoplasmic shuttling via its respective nuclear localisation and export signals. The editosome binds its target mRNA in the nucleus and retains its edited form during nuclear export, transporting the ApoB48 RNA to the cytoplasm for translation. In neurofibromatosis type I patients the complex deaminates a CGA (Arg) to an UGA (Stop) in the NF1 mRNA. May play a role in the epigenetic regulation of gene expression via APOBEC1's oxidative demetylation activity of 5-hydroxymethylcytosines (5hmCs). \r\n\r\nThe holocomplex contains at a minimum APOBEC1, A1CF and SYNCRIP. HNRNPAB may form a separate complex with APOBEC1. High concentrations of SYNCRIP preferentially bind to A1CF causing abrogation of mRNA editing.","predictedComplex":false,"interactors":[{"ac":"EBI-1024377","identifier":"O60506-1","identifierLink":"https://www.uniprot.org/uniprotkb/O60506-1/entry","name":"SYNCRIP","description":"Heterogeneous nuclear ribonucleoprotein Q","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-1044873","identifier":"Q99729","identifierLink":"https://www.uniprot.org/uniprotkb/Q99729/entry","name":"HNRNPAB","description":"Heterogeneous nuclear ribonucleoprotein A/B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48033","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12819523","identifier":"P41238","identifierLink":"https://www.uniprot.org/uniprotkb/P41238/entry","name":"APOBEC1","description":"C->U-editing enzyme APOBEC-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13857","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2809489","identifier":"Q9NQ94","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NQ94/entry","name":"A1CF","description":"APOBEC1 complementation factor","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21245","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1098","complexName":"C-to-U editosome complex","organismName":"Mus musculus; 10090","description":"mRNA editing complex that deaminates a CAA (Gln) to an UAA (Stop) codon in the ApoB mRNA in the luminal gastrointestinal tract and liver in healthy individuals, resulting in the generation of a truncated ApoB48 protein (E9Q414-PRO_0000420970) which mediates the absorption of dietary lipid from the intestine. The complex recognizes, and binds to, an 11-nucleotide mooring sequence downstream of the editing site and, in addition to C to U editing, also protects the edited ApoB mRNA from nonsense-mediated decay. APOBEC1 mediates nucleocytoplasmic shuttling via its respective nuclear localisation and export signals. The editosome binds its target mRNA in the nucleus and retains its edited form during nuclear export, transporting the ApoB48 RNA to the cytoplasm for translation. May play a role in the epigenetic regulation of gene expression via Apobec1's oxidative demetylation activity of 5-hydroxymethylcytosines (5hmCs). \r\n\r\nThe holocomplex contains at a minimum APOBEC1, A1CF and SYNCRIP. HNRNPAB may form a separate complex with APOBEC1. High concentrations of SYNCRIP preferentially bind to A1CF causing abrogation of mRNA editing.","predictedComplex":false,"interactors":[{"ac":"EBI-13952449","identifier":"P51908","identifierLink":"https://www.uniprot.org/uniprotkb/P51908/entry","name":"Apobec1","description":"C->U-editing enzyme APOBEC-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13857","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13952502","identifier":"Q7TMK9-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q7TMK9-1/entry","name":"Syncrip","description":"Heterogeneous nuclear ribonucleoprotein Q","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-13952511","identifier":"Q5YD48","identifierLink":"https://www.uniprot.org/uniprotkb/Q5YD48/entry","name":"A1cf","description":"APOBEC1 complementation factor","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21245","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-299641","identifier":"Q99020","identifierLink":"https://www.uniprot.org/uniprotkb/Q99020/entry","name":"Hnrnpab","description":"Heterogeneous nuclear ribonucleoprotein A/B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR48033","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1099","complexName":"B-WICH chromatin remodelling complex","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex that exposes DNA by sliding away histone octamers. Positively regulates histone H3 acetylation, in particular H3K9, by recruiting several histone acetyltransferases (HATs), such as KAT2B (PCAF, Q92831), p300 (Q09472), and KAT2A (GCN5, Q92830). Binds to both ribosomal DNA promoters and coding regions. Facilitates RNA polymerase I and III transcription by preventing compaction of chromatin at rDNA loci allowing HATs to assemble. An open chromatin structure is a prerequisite for the binding of the RNA polymerase machinery and also the regulatory factor MYC (P01106), which activates both RNA pol I genes and RNA pol III genes. May also activate RNA polymerase II gene transcription. The different subunits of the complex potentially have specific roles that lead to the stepwise modification of chromatin, and may not all associate simultaneously with the BAZ1B-SMARCA5 core. The B-WICH assembly may thus represent a number of smaller complexes. At the start of the cell division process, when Pol I transcription is arrested, B-WICH is in a disassembled state due to the phosphorylation of BAZ1B. The complex assembles on the active gene during early G1 phase. Polymeric actin interacts with Pol I, an interaction that is required for transcription. One speculative model is that NM1 (O00159-3) interacts with actin and the rDNA via its C-terminus, generating local force that pulls the polymerase along the active gene. Once dissociated from actin, NM1 interacts with SMARCA5 in a BAZ1B-dependent manner, a mechanism that stabilizes the complex on the rDNA. Additional components then assemble into the B-WICH complex(es) mediated by specific RNA species. \r\n\r\nParticularly important during embryonic and neonatal development, especially for craniofacial features.","predictedComplex":false,"interactors":[{"ac":"EBI-10965365","identifier":"O00159-3","identifierLink":"https://www.uniprot.org/uniprotkb/O00159-3/entry","name":"MYO1C","description":"Unconventional myosin-Ic","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-295284","identifier":"Q03468","identifierLink":"https://www.uniprot.org/uniprotkb/Q03468/entry","name":"ERCC6","description":"DNA excision repair protein ERCC-6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45629","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301977","identifier":"P35659","identifierLink":"https://www.uniprot.org/uniprotkb/P35659/entry","name":"DEK","description":"Protein DEK","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13468","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352588","identifier":"O60264","identifierLink":"https://www.uniprot.org/uniprotkb/O60264/entry","name":"SMARCA5","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357942","identifier":"Q9NR30","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NR30/entry","name":"DDX21","description":"Nucleolar RNA helicase 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47958","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-676973","identifier":"Q9BQG0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BQG0/entry","name":"MYBBP1A","description":"Myb-binding protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13213","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-876542","identifier":"O75533","identifierLink":"https://www.uniprot.org/uniprotkb/O75533/entry","name":"SF3B1","description":"Splicing factor 3B subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-927482","identifier":"Q9UIG0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UIG0/entry","name":"BAZ1B","description":"Tyrosine-protein kinase BAZ1B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9494077","identifier":"CHEBI:18111","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18111","name":"ribosomal rna","description":"ribosomal RNA","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1100","complexName":"DRM complex","organismName":"Caenorhabditis elegans; 6239","description":"Transcription factor complex with a role in in germline X-chromosome regulation. Appears to repress transcription of germline-expressed genes and promote expression of somatic and X-linked genes. The complex represses transcription  in vulval precursor cells to negatively regulate vulval development. This is most probably via antagonism of the Ras-signalling pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-13952825","identifier":"P30630","identifierLink":"https://www.uniprot.org/uniprotkb/P30630/entry","name":"lin-9","description":"Protein lin-9","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR21689","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2913777","identifier":"Q10120","identifierLink":"https://www.uniprot.org/uniprotkb/Q10120/entry","name":"lin-52","description":"Protein lin-52","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR31489","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-321470","identifier":"G5EDT1","identifierLink":"https://www.uniprot.org/uniprotkb/G5EDT1/entry","name":"lin-35","description":"Retinoblastoma-like protein homolog lin-35","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-324314","identifier":"P90916","identifierLink":"https://www.uniprot.org/uniprotkb/P90916/entry","name":"lin-53","description":"Probable histone-binding protein lin-53","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-324325","identifier":"Q23482","identifierLink":"https://www.uniprot.org/uniprotkb/Q23482/entry","name":"lin-37","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR31336","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-324825","identifier":"Q22703","identifierLink":"https://www.uniprot.org/uniprotkb/Q22703/entry","name":"dpl-1","description":"Transcription factor dpl-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12548","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-331564","identifier":"G5EF11","identifierLink":"https://www.uniprot.org/uniprotkb/G5EF11/entry","name":"efl-1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12081","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6762766","identifier":"Q95QD7","identifierLink":"https://www.uniprot.org/uniprotkb/Q95QD7/entry","name":"lin-54","description":"Protein lin-54","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12446","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1104","complexName":"Topoisomerase IV","organismName":"Escherichia coli (strain K12); 83333","description":"Type II DNA topoisomerase responsible for relaxing supercoiled DNA by introducing a double-stranded break in DNA and passing a second duplex segment of DNA through the break before resealing it. Acts on topologically different substrates including (+) and negative (−) supercoiled DNA and knotted and catenated DNA. Decatenates newly replicated DNA, removing the majority of links behind the replication forks.","predictedComplex":false,"interactors":[{"ac":"EBI-547277","identifier":"P20083","identifierLink":"https://www.uniprot.org/uniprotkb/P20083/entry","name":"parE","description":"DNA topoisomerase 4 subunit B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR45866","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-878544","identifier":"P0AFI2","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFI2/entry","name":"parC","description":"DNA topoisomerase 4 subunit A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43493","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1105","complexName":"Amyloid-beta protein 40/42 complex","organismName":"Mus musculus; 10090","description":"Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. May have a role in depressing synaptic activity thus preventing excitotoxicity. Influences synaptic plasticity through various receptors, including NMDAR, mGluR and alpha7 nicotinic acetylcholine receptors (CPX-234). Mediates dendritic spine loss leading to decreased synapse density, inhibition of long-term potentiation (LTP), enhancement of long-term depression (LTD), excessive calcium influx and mitochondrial impairment. May affect metal ion homeostasis by celating synaptic copper, zinc or iron ions. Mostly found in the extracellular space with a small proportion occurring as membrane-bound species. Dimers and oligomers (CPX-1121) of soluble amyloid-beta peptides are the main pathogenic species linked to Alzheimer's disease. Insoluble fibrils and plaques form during the latter stages of the disease. Chaperones, such as alphaB-crystallins or clusterin (Q06890), bind to misfolded oligomeric species and form long-lived complexes, thereby preventing both their further growth into fibrils and their dissociation into synaptotoxic dimers. \r\n\r\nAmyloid-beta peptide may act as transcription factor for its own precursor protein App and its cleavage enzyme BACE1 (P56818) initiating a positive feedback mechanism that ultimately leads to amyloidogenesis and Alzheimer's disease.","predictedComplex":false,"interactors":[{"ac":"EBI-14022231","identifier":"P12023-PRO_0000000118","identifierLink":"https://www.uniprot.org/uniprotkb/P12023-PRO_0000000118/entry","name":"App","description":"Amyloid-beta protein 42","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-14022236","identifier":"P12023-PRO_0000000119","identifierLink":"https://www.uniprot.org/uniprotkb/P12023-PRO_0000000119/entry","name":"App","description":"Amyloid-beta protein 40","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-1106","complexName":"Amyloid-beta protein 40 complex","organismName":"Mus musculus; 10090","description":"Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. May have a role in depressing synaptic activity thus preventing excitotoxicity. Influences synaptic plasticity through various receptors, including NMDAR, mGluR and alpha7 nicotinic acetylcholine receptors (CPX-234). Mediates dendritic spine loss leading to decreased synapse density, inhibition of long-term potentiation (LTP), enhancement of long-term depression (LTD), excessive calcium influx and mitochondrial impairment. May affect metal ion homeostasis by celating synaptic copper, zinc or iron ions. Mostly found in the extracellular space with a small proportion occurring as membrane-bound species. Dimers and oligomers (CPX-1181) of soluble amyloid-beta peptides are the main pathogenic species linked to Alzheimer's disease. Insoluble fibrils and plaques form during the latter stages of the disease. Chaperones, such as alphaB-crystallins or clusterin (Q06890), bind to misfolded oligomeric species and form long-lived complexes, thereby preventing both their further growth into fibrils and their dissociation into synaptotoxic dimers. \r\n\r\nAmyloid-beta peptide may act as transcription factor for its own precursor protein App and its cleavage enzyme BACE1 (P56818) initiating a positive feedback mechanism that ultimately leads to amyloidogenesis and Alzheimer's disease.","predictedComplex":false,"interactors":[{"ac":"EBI-14022236","identifier":"P12023-PRO_0000000119","identifierLink":"https://www.uniprot.org/uniprotkb/P12023-PRO_0000000119/entry","name":"App","description":"Amyloid-beta protein 40","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-1107","complexName":"Amyloid-beta protein 42 complex","organismName":"Mus musculus; 10090","description":"Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. May have a role in depressing synaptic activity thus preventing excitotoxicity. Influences synaptic plasticity through various receptors, including NMDAR, mGluR and alpha7 nicotinic acetylcholine receptors (CPX-234). Mediates dendritic spine loss leading to decreased synapse density, inhibition of long-term potentiation (LTP), enhancement of long-term depression (LTD), excessive calcium influx and mitochondrial impairment. May affect metal ion homeostasis by celating synaptic copper, zinc or iron ions. Oligomers of protein 42 only may have positive neurogenetic effects by activating synaptic protein kinases. Mostly found in the extracellular space with a small proportion occurring as membrane-bound species. Dimers and oligomers (CPX-1139) of soluble amyloid-beta peptides are the main pathogenic species linked to Alzheimer's disease. Insoluble fibrils and plaques form during the latter stages of the disease. Chaperones, such as alphaB-crystallins or clusterin (Q06890), bind to misfolded oligomeric species and form long-lived complexes, thereby preventing both their further growth into fibrils and their dissociation into synaptotoxic dimers. \r\n\r\nAmyloid-beta peptide may act as transcription factor for its own precursor protein App and its cleavage enzyme BACE1 (P56818) initiating a positive feedback mechanism that ultimately leads to amyloidogenesis and Alzheimer's disease.","predictedComplex":false,"interactors":[{"ac":"EBI-14022231","identifier":"P12023-PRO_0000000118","identifierLink":"https://www.uniprot.org/uniprotkb/P12023-PRO_0000000118/entry","name":"App","description":"Amyloid-beta protein 42","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-1108","complexName":"Amyloid-beta protein 40/42 complex","organismName":"Rattus norvegicus; 10116","description":"Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. May have a role in depressing synaptic activity thus preventing excitotoxicity. Influences synaptic plasticity through various receptors, including NMDAR, mGluR and alpha7 nicotinic acetylcholine receptors (CPX-233). Mediates dendritic spine loss leading to decreased synapse density, inhibition of long-term potentiation (LTP), enhancement of long-term depression (LTD), excessive calcium influx and mitochondrial impairment. May affect metal ion homeostasis by celating synaptic copper, zinc or iron ions. Mostly found in the extracellular space with a small proportion occurring as membrane-bound species. Dimers and oligomers of soluble amyloid-beta peptides are the main pathogenic species linked to Alzheimer's disease. Insoluble fibrils and plaques form during the latter stages of the disease. Chaperones, such as alphaB-crystallins or clusterin (P05371), bind to misfolded oligomeric species and form long-lived complexes, thereby preventing both their further growth into fibrils and their dissociation into synaptotoxic dimers. \r\n\r\nAmyloid-beta peptide may act as transcription factor for its own precursor protein App and its cleavage enzyme BACE1 (P56819) initiating a positive feedback mechanism that ultimately leads to amyloidogenesis and Alzheimer's disease.","predictedComplex":false,"interactors":[{"ac":"EBI-14022881","identifier":"P08592-PRO_0000000163","identifierLink":"https://www.uniprot.org/uniprotkb/P08592-PRO_0000000163/entry","name":"App","description":"Amyloid-beta protein 42","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-14022886","identifier":"P08592-PRO_0000000164","identifierLink":"https://www.uniprot.org/uniprotkb/P08592-PRO_0000000164/entry","name":"App","description":"Amyloid-beta protein 40","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-1109","complexName":"Amyloid-beta protein 40 complex","organismName":"Rattus norvegicus; 10116","description":"Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. May have a role in depressing synaptic activity thus preventing excitotoxicity. Influences synaptic plasticity through various receptors, including NMDAR, mGluR and alpha7 nicotinic acetylcholine receptors (CPX-233). Mediates dendritic spine loss leading to decreased synapse density, inhibition of long-term potentiation (LTP), enhancement of long-term depression (LTD), excessive calcium influx and mitochondrial impairment. May affect metal ion homeostasis by celating synaptic copper, zinc or iron ions. Mostly found in the extracellular space with a small proportion occurring as membrane-bound species. Dimers and oligomers (CPX-1182) of soluble amyloid-beta peptides are the main pathogenic species linked to Alzheimer's disease. Insoluble fibrils and plaques form during the latter stages of the disease. Chaperones, such as alphaB-crystallins or clusterin (P05371), bind to misfolded oligomeric species and form long-lived complexes, thereby preventing both their further growth into fibrils and their dissociation into synaptotoxic dimers. \r\n\r\nAmyloid-beta peptide may act as transcription factor for its own precursor protein App and its cleavage enzyme BACE1 (P56819) initiating a positive feedback mechanism that ultimately leads to amyloidogenesis and Alzheimer's disease.","predictedComplex":false,"interactors":[{"ac":"EBI-14022886","identifier":"P08592-PRO_0000000164","identifierLink":"https://www.uniprot.org/uniprotkb/P08592-PRO_0000000164/entry","name":"App","description":"Amyloid-beta protein 40","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-1110","complexName":"Amyloid-beta protein 42 complex","organismName":"Rattus norvegicus; 10116","description":"Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. May have a role in depressing synaptic activity thus preventing excitotoxicity. Influences synaptic plasticity through various receptors, including NMDAR, mGluR and alpha7 nicotinic acetylcholine receptors (CPX-233). Mediates dendritic spine loss leading to decreased synapse density, inhibition of long-term potentiation (LTP), enhancement of long-term depression (LTD), excessive calcium influx and mitochondrial impairment. May affect metal ion homeostasis by celating synaptic copper, zinc or iron ions. Oligomers of protein 42 only may have positive neurogenetic effects by activating synaptic protein kinases. Mostly found in the extracellular space with a small proportion occurring as membrane-bound species. Dimers and oligomers of soluble amyloid-beta peptides are the main pathogenic species linked to Alzheimer's disease. Insoluble fibrils and plaques form during the latter stages of the disease. Chaperones, such as alphaB-crystallins or clusterin (P05371), bind to misfolded oligomeric species and form long-lived complexes, thereby preventing both their further growth into fibrils and their dissociation into synaptotoxic dimers. \r\n\r\nAmyloid-beta peptide may act as transcription factor for its own precursor protein App and its cleavage enzyme BACE1 (P56819) initiating a positive feedback mechanism that ultimately leads to amyloidogenesis and Alzheimer's disease.","predictedComplex":false,"interactors":[{"ac":"EBI-14022881","identifier":"P08592-PRO_0000000163","identifierLink":"https://www.uniprot.org/uniprotkb/P08592-PRO_0000000163/entry","name":"App","description":"Amyloid-beta protein 42","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-1111","complexName":"Importin complex, Snurportin variant","organismName":"Mus musculus; 10090","description":"A nuclear import complex that functions as a nuclear import receptor and specifically imports m3G-capped U snRNAs. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by Kpnb1. Kpnb1 binds to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran-GTP (P62827) binds to Kpnb1, the three components separate and Snupn and Kpnb1 are re-exported from the nucleus to the cytoplasm where GTP is hydrolysed. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.","predictedComplex":false,"interactors":[{"ac":"EBI-14029989","identifier":"Q80W37","identifierLink":"https://www.uniprot.org/uniprotkb/Q80W37/entry","name":"Snupn","description":"Snurportin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13403","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-540580","identifier":"P70168","identifierLink":"https://www.uniprot.org/uniprotkb/P70168/entry","name":"Kpnb1","description":"Importin subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1112","complexName":"Calcineurin-Calmodulin-AKAP5 complex, gamma-R1 variant","organismName":"Homo sapiens; 9606","description":"Calcium-dependent, calmodulin-stimulated protein phosphatase calcineurin in complex with plasma-membrane anchor protein AKAP5. Calcineurin is important for cardiac development and pathophysiology, for nervous-system development and for some of the plastic changes in neurons that are believed to underlie learning and memory. AKAP5 recruits calcineurin to the vicinity of L-type Ca2+ channels for their activation by elevated Ca2+ entering the cell. AKAP5 balances the opposing effects of calcineurin and protein kinase A (PKA) (P17612) on neuronal voltage-gated L-type Ca2+ channels and coordinates the activities of calcineurin, PKA and PKC on a number of other channels and receptors. Despite its atypical PxIxIT calcineurin-recognition motif that confers stronger binding affinity by calcineurin than other substrates it allows for effective disengagement of calcineurin to couple channel activation with downstream signaling events. The calcineurin-AKAP5 complex has been shown to promote NFAT signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2827192","identifier":"P48454","identifierLink":"https://www.uniprot.org/uniprotkb/P48454/entry","name":"PPP3CC","description":"Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397435","identifier":"P62158","identifierLink":"https://www.uniprot.org/uniprotkb/P62158/entry","name":"calm_human","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-703640","identifier":"P24588","identifierLink":"https://www.uniprot.org/uniprotkb/P24588/entry","name":"AKAP5","description":"A-kinase anchor protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15182","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-915984","identifier":"P63098","identifierLink":"https://www.uniprot.org/uniprotkb/P63098/entry","name":"PPP3R1","description":"Calcineurin subunit B type 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3197","complexName":"Voltage-gated potassium channel complex variant 2","organismName":"Mus musculus; 10090","description":"Mediates the repolarizing IKr current in the cardiac action potential, conducting potassium (K+) ions out of the muscle cells of the cardiac myocyte. This current is critical in correctly timing the return to the resting state (repolarization) of the cell membrane during the cardiac action potential. In the nervous system, the complex is mainly involved in regulating spike-frequency adaptation and controlling resting potential, and abnormal expression is associated with the onset of schizophrenia. The complex also participates in cell proliferation and differentiation, regulating apoptosis, and is involved in regulating the secretory activity of pancreatic beta cells and chromaffin cells, as well as in regulating the contractility of smooth-muscle cells in the portal vein, the jejunum, and the epididymal duct, possibly by regulating the excitability of these cells.","predictedComplex":false,"interactors":[{"ac":"EBI-9688270","identifier":"O35219","identifierLink":"https://www.uniprot.org/uniprotkb/O35219/entry","name":"Kcnh2","description":"Voltage-gated inwardly rectifying potassium channel KCNH2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10217","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9688343","identifier":"Q9D808","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D808/entry","name":"Kcne2","description":"Potassium voltage-gated channel subfamily E member 2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15282","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3198","complexName":"Voltage-gated potassium channel complex variant 1","organismName":"Mus musculus; 10090","description":"Mediates the repolarizing IKr current in the cardiac action potential, conducting potassium (K+) ions out of the muscle cells of the cardiac myocyte. This current is critical in correctly timing the return to the resting state (repolarization) of the cell membrane during the cardiac action potential. In the nervous system, the complex is mainly involved in regulating spike-frequency adaptation and controlling resting potential, and abnormal expression is associated with the onset of schizophrenia. The complex also participates in cell proliferation and differentiation, regulating apoptosis, and is involved in regulating the secretory activity of pancreatic beta cells and chromaffin cells, as well as in regulating the contractility of smooth-muscle cells in the portal vein, the jejunum, and the epididymal duct, possibly by regulating the excitability of these cells.","predictedComplex":false,"interactors":[{"ac":"EBI-9688270","identifier":"O35219","identifierLink":"https://www.uniprot.org/uniprotkb/O35219/entry","name":"Kcnh2","description":"Voltage-gated inwardly rectifying potassium channel KCNH2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10217","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9688385","identifier":"P23299","identifierLink":"https://www.uniprot.org/uniprotkb/P23299/entry","name":"Kcne1","description":"Potassium voltage-gated channel subfamily E member 1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15282","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3074","complexName":"Doa10 E3 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Transmembrane E3 ubiquitin ligase complex involved in the endoplasmic reticulum-associated degradation (ERAD) pathway, directing misfolded proteins to proteasomal degradation. Required for ERAD-C subpathway which degrades proteins with misfolded cytoplasmic domains. The Doa10 core complex acts together with the E2 ubiquitin conjugating enzymes Ubc6 (P33296) and Cue1-Ubc7 (CPX-2948) and also the Cdc48p-Npl4p-Ufd1p AAA ATPase complex (CPX-2946).","predictedComplex":false,"interactors":[{"ac":"EBI-18208","identifier":"P40318","identifierLink":"https://www.uniprot.org/uniprotkb/P40318/entry","name":"SSM4","description":"ERAD-associated E3 ubiquitin-protein ligase DOA10","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13145","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27730","identifier":"Q04228","identifierLink":"https://www.uniprot.org/uniprotkb/Q04228/entry","name":"UBX2","description":"UBX domain-containing protein 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23322","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3079","complexName":"USF1-USF2 upstream stimulatory factor complex","organismName":"Homo sapiens; 9606","description":"Ubiquitous upstream stimulatory factor transcription factor that binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters.","predictedComplex":false,"interactors":[{"ac":"EBI-1054489","identifier":"P22415","identifierLink":"https://www.uniprot.org/uniprotkb/P22415/entry","name":"USF1","description":"Upstream stimulatory factor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1055994","identifier":"Q15853","identifierLink":"https://www.uniprot.org/uniprotkb/Q15853/entry","name":"USF2","description":"Upstream stimulatory factor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3082","complexName":"USF1 upstream stimulatory factor complex","organismName":"Homo sapiens; 9606","description":"Ubiquitous upstream stimulatory factor transcription factor that binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters.","predictedComplex":false,"interactors":[{"ac":"EBI-1054489","identifier":"P22415","identifierLink":"https://www.uniprot.org/uniprotkb/P22415/entry","name":"USF1","description":"Upstream stimulatory factor 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3083","complexName":"USF2 upstream stimulatory factor complex","organismName":"Homo sapiens; 9606","description":"Ubiquitous upstream stimulatory factor transcription factor that binds to a symmetrical DNA sequence (E-box) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters.","predictedComplex":false,"interactors":[{"ac":"EBI-1055994","identifier":"Q15853","identifierLink":"https://www.uniprot.org/uniprotkb/Q15853/entry","name":"USF2","description":"Upstream stimulatory factor 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3084","complexName":"USF2 upstream stimulatory factor complex","organismName":"Mus musculus; 10090","description":"Ubiquitous upstream stimulatory factor transcription factor that binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters.","predictedComplex":false,"interactors":[{"ac":"EBI-647583","identifier":"Q64705","identifierLink":"https://www.uniprot.org/uniprotkb/Q64705/entry","name":"Usf2","description":"Upstream stimulatory factor 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3085","complexName":"USF1 upstream stimulatory factor complex","organismName":"Mus musculus; 10090","description":"Ubiquitous upstream stimulatory factor transcription factor that binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters.","predictedComplex":false,"interactors":[{"ac":"EBI-2325635","identifier":"Q61069","identifierLink":"https://www.uniprot.org/uniprotkb/Q61069/entry","name":"Usf1","description":"Upstream stimulatory factor 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3086","complexName":"USF1-USF2 upstream stimulatory factor complex","organismName":"Mus musculus; 10090","description":"Ubiquitous upstream stimulatory factor transcription factor that binds to a symmetrical DNA sequence (E-boxes) (5'-CACGTG-3') that is found in a variety of viral and cellular promoters.","predictedComplex":false,"interactors":[{"ac":"EBI-2325635","identifier":"Q61069","identifierLink":"https://www.uniprot.org/uniprotkb/Q61069/entry","name":"Usf1","description":"Upstream stimulatory factor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-647583","identifier":"Q64705","identifierLink":"https://www.uniprot.org/uniprotkb/Q64705/entry","name":"Usf2","description":"Upstream stimulatory factor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3080","complexName":"Microprocessor complex","organismName":"Homo sapiens; 9606","description":"Responsible for the processing of the primary transcripts during the generation of microRNAs, cleaving  the primary transcript (pri-miRNA) at the stem of a hairpin structure to form the mature approximately 22 nucleotide miRNA. May also play a role in the destabilization of mRNAs and other RNA types. DGCR8 may play a major role in substrate recognition by directly anchoring at the ssRNA-dsRNA junction. DGCR8 also interacts with the stem of a pproximately33 bp and the terminal loop for full activity although the terminal loop structure is not critical for DGCR8 binding and cleavage reaction. Binding of DGCR8 to the RNA positions the processing center of DROSHA approximately 11 bp from the junction, DROSHA then catalyses the substrate, with its two RNase III domains forming an intramolecular dimer where the domain 1 cuts the 3' strand while the domain 2 cleaves the 5-prime strand of pri-miRNAs, independently of each other. The Microprocessor recognizes and cleaves hairpin structures at the 5-prime UTR and the coding region of Dgcr8 mRNA. This self-regulation by the negative feedback loop contributes to the homeostatic control of miRNA generation.","predictedComplex":false,"interactors":[{"ac":"EBI-528367","identifier":"Q9NRR4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NRR4/entry","name":"DROSHA","description":"Ribonuclease 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11207","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-528411","identifier":"Q8WYQ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WYQ5/entry","name":"DGCR8","description":"Microprocessor complex subunit DGCR8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13482","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3081","complexName":"Microprocessor complex","organismName":"Mus musculus; 10090","description":"Responsible for the processing of the primary transcripts during the generation of microRNAs, cleaving  the primary transcript (pri-miRNA) at the stem of a hairpin structure to form the mature approximately 22 nucleotide miRNA. May also play a role in the destabilization of mRNAs and other RNA types. DGCR8 may play a major role in substrate recognition by directly anchoring at the ssRNA-dsRNA junction. DGCR8 also interacts with the stem of approximately 33 bp and the terminal loop for full activity although the terminal loop structure is not critical for DGCR8 binding and cleavage reaction. Binding of DGCR8 to the RNA positions the processing center of DROSHA approximately 11 bp from the junction, DROSHA then catalyses the substrate, with its two RNase III domains forming an intramolecular dimer where the domain 1 cuts the 3-prime strand while the domain 2 cleaves the 5-prime strand of pri-miRNAs, independently of each other. The Microprocessor recognizes and cleaves hairpin structures at the 5-prime UTR and the coding region of Dgcr8 mRNA. This self-regulation by the negative feedback loop contributes to the homeostatic control of miRNA generation.","predictedComplex":false,"interactors":[{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9518948","identifier":"Q9EQM6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9EQM6/entry","name":"Dgcr8","description":"Microprocessor complex subunit DGCR8","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13482","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9518967","identifier":"Q5HZJ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q5HZJ0/entry","name":"Drosha","description":"Ribonuclease 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11207","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3088","complexName":"PAS complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Role in the synthesis and turnover of the low abundance, signaling lipid phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2; CHEBI:16851). PtIns(3,2)P2 has been implicated in processes such as vacuole morphology, homeostasis, membrane scission, acidification and transport vesicle formation.","predictedComplex":false,"interactors":[{"ac":"EBI-22968","identifier":"P43601","identifierLink":"https://www.uniprot.org/uniprotkb/P43601/entry","name":"ATG18","description":"Autophagy-related protein 18","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11227","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27189","identifier":"Q06708","identifierLink":"https://www.uniprot.org/uniprotkb/Q06708/entry","name":"VAC14","description":"Vacuole morphology and inheritance protein 14","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR16023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28407","identifier":"P42837","identifierLink":"https://www.uniprot.org/uniprotkb/P42837/entry","name":"FIG4","description":"Polyphosphoinositide phosphatase","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45738","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28714","identifier":"P53950","identifierLink":"https://www.uniprot.org/uniprotkb/P53950/entry","name":"VAC7","description":"Vacuolar segregation protein 7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28258","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6754","identifier":"P34756","identifierLink":"https://www.uniprot.org/uniprotkb/P34756/entry","name":"FAB1","description":"1-phosphatidylinositol 3-phosphate 5-kinase FAB1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45748","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3089","complexName":"EFF-1 complex","organismName":"Caenorhabditis elegans; 6239","description":"Cell-cell fusion complex. EFF-1 prefusion monomers cluster at the surface of adjacent cells. Parallel EFF-1 interactions occur across cells and a third monomer, which can come from either cell, adds on to make an intermediate, extended trimer. The EFF-1 trimer then serves as a scaffold for zippering up the extracellular domains, bringing the transmembrane segments into close proximity such that they can continue zippering two membranes into one.","predictedComplex":false,"interactors":[{"ac":"EBI-9526485","identifier":"G5ECA1","identifierLink":"https://www.uniprot.org/uniprotkb/G5ECA1/entry","name":"eff-1","description":null,"stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR37415","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3092","complexName":"Ryanodine 1 complex","organismName":"Mus musculus; 10090","description":"A large homotetrameric intracellular calcium channel predominantly of the skeletal muscle that is crucial for excitation-contraction (E-C) coupling. Following the depolarization of the transverse tubule (T-tubule) membrane, RyR1 opening releases Ca2+ stored in the sarcoplasmic reticulum (SR) into the myoplasm. This increase of cytoplasmic Ca2+ triggers the interaction of actin and myosin that causes contraction of the muscle fibers. Implicated in skeletal muscle development, ossification, dermatogenesis and cardiovascular development. Expressed in the brain, where it can mediate the NO-induced release of Ca2+ from intracellular stores in neurons.\r\n\r\nThe E-C coupling involves the mechanical interaction between RyR1 in the SR and DHPR (also known as L-type Ca2+ channel, CPX-3191) in the T-tubule. There is some evidence to suggest that this happens through the direct physical interaction of the two channels.\r\n\r\nFKBP12 binds and co-purifies with RyR1, but the intrinsic isomerase activity is not essential for RyR effects. FKBP is believed to physically stabilize the coordinated gating of the four RyRs in one RyR homotetramer and may be involved in the physical coupling between RyR tetramers. \r\n\r\nRyR1 physically interacts with various other proteins, small molecules and ions that modulate its activity: \r\nLow Ca+2 concentration activates RyR1, by binding to specific high-affinity Ca+2 sites. High Ca+2 concentration inhibits RyR1, by binding to less specific low-affinity Ca+2 sites. S100A1 binds specifically to the purified RyR1 in a Ca2+ dependent manner, at regions overlapping with CaM  binding sites, and enhances the open probability of RyR1 reconstituted in lipid bilayers. TRDN, ASPH, CACNA1S, Homer-1c and ATP stimulates RyR1 channel activity. Calmodulin with bound calcium inhibits the RYR1 channel activity, as is binding to magnesium ions (Mg+2).","predictedComplex":false,"interactors":[{"ac":"EBI-642079","identifier":"E9PZQ0","identifierLink":"https://www.uniprot.org/uniprotkb/E9PZQ0/entry","name":"Ryr1","description":"Ryanodine receptor 1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46399","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3135","complexName":"Ryanodine 1 complex","organismName":"Homo sapiens; 9606","description":"A large homotetrameric intracellular calcium channel predominantly of the skeletal muscle that is crucial for excitation-contraction (E-C) coupling. Following the depolarization of the transverse tubule (T-tubule) membrane, RyR1 opening releases Ca2+ stored in the sarcoplasmic reticulum (SR) into the myoplasm. This increase of cytoplasmic Ca2+ triggers the interaction of actin and myosin that causes contraction of the muscle fibers. Implicated in skeletal muscle development, ossification, dermatogenesis and cardiovascular development. Expressed in the brain, where it can mediate the NO-induced release of Ca2+ from intracellular stores in neurons.\r\n\r\nThe E-C coupling involves the mechanical interaction between RyR1 in the SR and DHPR (also known as L-type Ca2+ channel, CPX-3192) in the T-tubule. There is some evidence to suggest that this happens through the direct physical interaction of the two channels.\r\n\r\nFKBP12 binds and co-purifies with RyR1, but the intrinsic isomerase activity is not essential for RyR effects. FKBP is believed to physically stabilize the coordinated gating of the four RyRs in one RyR homotetramer and may be involved in the physical coupling between RyR tetramers. \r\n\r\nRyR1 physically interacts with various other proteins, small molecules and ions that modulate its activity: \r\nLow Ca+2 concentration activates RyR1, by binding to specific high-affinity Ca+2 sites. High Ca+2 concentration inhibits RyR1, by binding to less specific low-affinity Ca+2 sites. S100A1 binds specifically to the purified RyR1 in a Ca2+ dependent manner, at regions overlapping with CaM  binding sites, and enhances the open probability of RyR1 reconstituted in lipid bilayers. TRDN, ASPH, CACNA1S, Homer-1 and ATP stimulates RyR1 channel activity. Calmodulin with bound calcium inhibits the RYR1 channel activity, as is binding to magnesium ions (Mg+2).","predictedComplex":false,"interactors":[{"ac":"EBI-1221290","identifier":"P21817","identifierLink":"https://www.uniprot.org/uniprotkb/P21817/entry","name":"RYR1","description":"Ryanodine receptor 1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46399","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3136","complexName":"Ryanodine 1 complex","organismName":"Oryctolagus cuniculus; 9986","description":"A large homotetrameric intracellular calcium channel predominantly of the skeletal muscle that is crucial for excitation-contraction (E-C) coupling. Following the depolarization of the transverse tubule (T-tubule) membrane, RyR1 opening releases Ca2+ stored in the sarcoplasmic reticulum (SR) into the myoplasm. This increase of cytoplasmic Ca2+ triggers the interaction of actin and myosin that causes contraction of the muscle fibers. Implicated in skeletal muscle development, ossification, dermatogenesis and cardiovascular development. Expressed in the brain, where it can mediate the NO-induced release of Ca2+ from intracellular stores in neurons.\r\n\r\nThe E-C coupling involves the mechanical interaction between RyR1 in the SR and DHPR (also known as L-type Ca2+ channel, CPX-3189) in the T-tubule. There is some evidence to suggest that this happens through the direct physical interaction of the two channels.\r\n\r\nFKBP12 binds and co-purifies with RyR1, but the intrinsic isomerase activity is not essential for RyR effects. FKBP is believed to physically stabilize the coordinated gating of the four RyRs in one RyR homotetramer and may be involved in the physical coupling between RyR tetramers. \r\n\r\nRyR1 physically interacts with various other proteins, small molecules and ions that modulate its activity: \r\nLow Ca+2 concentration activates RyR1, by binding to specific high-affinity Ca+2 sites. High Ca+2 concentration inhibits RyR1, by binding to less specific low-affinity Ca+2 sites. S100A1 binds specifically to the purified RyR1 in a Ca2+ dependent manner, at regions overlapping with CaM  binding sites, and enhances the open probability of RyR1 reconstituted in lipid bilayers. TRDN, ASPH, CACNA1S and ATP stimulates RyR1 channel activity. Calmodulin with bound calcium inhibits the RYR1 channel activity, as is binding to magnesium ions (Mg+2).","predictedComplex":false,"interactors":[{"ac":"EBI-6477441","identifier":"P11716","identifierLink":"https://www.uniprot.org/uniprotkb/P11716/entry","name":"RYR1","description":"Ryanodine receptor 1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Oryctolagus cuniculus; 9986","xrefs":[]}]},{"complexAC":"CPX-3137","complexName":"Ryanodine 2 complex","organismName":"Mus musculus; 10090","description":"A large homotetrameric intracellular calcium channel predominantly of the cardiac muscle that is crucial for excitation-contraction (E-C) coupling. Following the depolarization of the transverse tubule (T-tubule) membrane, RyR2 opening releases Ca2+ stored in the sarcoplasmic reticulum (SR) into the myoplasm. This increase of cytoplasmic Ca2+ triggers the interaction of actin and myosin that causes contraction of the cardiac muscle fibers. \r\nThe E-C coupling in cardiac muscle involves RyR2 calcium release triggered by  Ca2+ influx due to activation of the L-type calcium channel Cav1.2 (CPX-3194). \r\nRyR2 is required for heart development. Aberrant channel activation can lead to cardiac arrhythmia. RyR2 is also shown to play a role in beta cells survival in vitro.\r\n\r\nRyR2 physically interacts with various other proteins, small molecules and ions that modulate its activity: \r\nLow Ca+2 concentration activates RyR2, by binding to specific high-affinity Ca+2 sites. High Ca+2 concentration inhibits RyR2, by binding to less specific low-affinity Ca+2 sites. PKA binds to RyR2 altering the gating. S100A1 binding enhances the open probability of RyR2. ASPH  and ATP stimulates RyR2 channel activity. Magnesium ions (Mg+2)  inhibits the RyR2 channel activity. Homer-1c binding inhibits RyR2 channel opening. Calmodulin binding may inhibit open basal probability and alter the Ca-dependent activation of RyR2. FKBP binding is believed to physically stabilize the coordinated gating of the four RyRs in one RyR homotetramer and may be involved in the physical coupling between RyR tetramers. Binding to Sorcin decreases open channel probability. CaMKIId binds and phosphorylates RyR2 strongly activating Ca2+ release during both diastole and systole.\r\nAn immunoprecipitation study of recombinant heterologously expressed RyRs provided evidence that RyR2 could form heterotetramers with RyR1 and RyR3. However, the presence of native tissue RyR heterotetramers has not been reported yet.","predictedComplex":false,"interactors":[{"ac":"EBI-643628","identifier":"E9Q401","identifierLink":"https://www.uniprot.org/uniprotkb/E9Q401/entry","name":"Ryr2","description":"Ryanodine receptor 2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46399","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3156","complexName":"Ryanodine 2 complex","organismName":"Homo sapiens; 9606","description":"A large homotetrameric intracellular calcium channel predominantly of the cardiac muscle that is crucial for excitation-contraction (E-C) coupling. Following the depolarization of the transverse tubule (T-tubule) membrane, RyR2 opening releases Ca2+ stored in the sarcoplasmic reticulum (SR) into the myoplasm. This increase of cytoplasmic Ca2+ triggers the interaction of actin and myosin that causes contraction of the cardiac muscle fibers. \r\nThe E-C coupling in cardiac muscle involves RyR2 calcium release triggered by Ca2+ influx due to activation of the L-type calcium channel Cav1.2 (CPX-3195). \r\nRyR2 is required for heart development. Aberrant channel activation can lead to cardiac arrhythmia. RyR2 is also shown to play a role in beta cell survival in vitro.\r\n\r\nRyR2 physically interacts with various other proteins, small molecules and ions that modulate its activity: \r\nLow Ca+2 concentration activates RyR2, by binding to specific high-affinity Ca+2 sites. High Ca+2 concentration inhibits RyR2, by binding to less specific low-affinity Ca+2 sites. PKA binds to RyR2 altering the gating. S100A1 binding enhances the open probability of RyR2. ASPH  and ATP stimulates RyR2 channel activity. Magnesium ions (Mg+2)  inhibits the RyR2 channel activity. Homer-1c binding inhibits RyR2 channel opening. Calmodulin binding may inhibit open basal probability and alter the Ca-dependent activation of RyR2. FKBP binding is believed to physically stabilize the coordinated gating of the four RyRs in one RyR homotetramer and may be involved in the physical coupling between RyR tetramers. Binding to sorcin decreases open channel probability. CaMKIId binds and phosphorylates RyR2 strongly activating Ca2+ release during both diastole and systole.","predictedComplex":false,"interactors":[{"ac":"EBI-1170425","identifier":"Q92736","identifierLink":"https://www.uniprot.org/uniprotkb/Q92736/entry","name":"RYR2","description":"Ryanodine receptor 2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46399","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3157","complexName":"Ryanodine 3 complex","organismName":"Oryctolagus cuniculus; 9986","description":"A large homotetrameric intracellular calcium channel, member of the ryanodine receptors family, responsible for the release of Ca2+ from the SR in muscle cells, thereby triggering muscle fiber contraction. Also responsible for the release of Ca2+ from the ER in non-muscle cell types. Predominantly expressed in the diaphragm muscles, smooth muscle cells and in the brain (mainly in hippocampus, thalamus, Purkinje cells, corpus striatum) and in low levels in many other organs.\r\n\r\nRyR3 physically interacts with other proteins, small molecules and ions that modulate its activity: \r\n\r\nLow Ca+2 concentration activates RyR3, by binding to specific high-affinity Ca+2 sites. High Ca+2 concentration inhibits RyR3, by binding to less specific low-affinity Ca+2 sites. ATP stimulates RyR1 channel activity. Calmodulin with bound calcium inhibits the RyR3 channel activity, as is binding to magnesium ions (Mg+2). Binding to FKBP may physically stabilize the coordinated gating of the four RyRs in one RyR homotetramer.","predictedComplex":false,"interactors":[{"ac":"EBI-9641796","identifier":"Q9TS33-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9TS33-1/entry","name":"RYR3","description":"Ryanodine receptor 3","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Oryctolagus cuniculus; 9986","xrefs":[]}]},{"complexAC":"CPX-3161","complexName":"Ryanodine 3 complex","organismName":"Mus musculus; 10090","description":"A large homotetrameric intracellular calcium channel, member of the ryanodine receptors family, responsible for the release of Ca2+ from the SR in muscle cells, thereby triggering muscle fiber contraction. Also responsible for the release of Ca2+ from the ER in non-muscle cell types. Predominantly expressed in the diaphragm muscles, smooth muscle cells and in the brain (mainly in hippocampus, thalamus, Purkinje cells, corpus striatum) and in low levels in many other organs.\r\n\r\nRyR3 physically interacts with other proteins, small molecules and ions that modulate its activity: \r\n\r\nLow Ca+2 concentration activates RyR3, by binding to specific high-affinity Ca+2 sites. High Ca+2 concentration inhibits RyR3, by binding to less specific low-affinity Ca+2 sites. ATP stimulates RyR1 channel activity. Calmodulin with bound calcium inhibits the RyR3 channel activity, as is binding to magnesium ions (Mg+2). Binding to FKBP may physically stabilize the coordinated gating of the four RyRs in one RyR homotetramer.","predictedComplex":false,"interactors":[{"ac":"EBI-9663179","identifier":"A2AGL3","identifierLink":"https://www.uniprot.org/uniprotkb/A2AGL3/entry","name":"Ryr3","description":"Ryanodine receptor 3","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46399","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3162","complexName":"Ryanodine 3 complex","organismName":"Homo sapiens; 9606","description":"A large homotetrameric intracellular calcium channel, member of the ryanodine receptors family, responsible for the release of Ca2+ from the SR in muscle cells, thereby triggering muscle fiber contraction. Also responsible for the release of Ca2+ from the ER in non-muscle cell types. Predominantly expressed in the diaphragm muscles, smooth muscle cells and in the brain (mainly in hippocampus, thalamus, Purkinje cells, corpus striatum) and in low levels in many other organs.\r\n\r\nRyR3 physically interacts with other proteins, small molecules and ions that modulate its activity: \r\n\r\nLow Ca+2 concentration activates RyR3, by binding to specific high-affinity Ca+2 sites. High Ca+2 concentration inhibits RyR3, by binding to less specific low-affinity Ca+2 sites. ATP stimulates RyR1 channel activity. Calmodulin with bound calcium inhibits the RyR3 channel activity, as is binding to magnesium ions (Mg+2). Binding to FKBP may physically stabilize the coordinated gating of the four RyRs in one RyR homotetramer.","predictedComplex":false,"interactors":[{"ac":"EBI-2692727","identifier":"Q15413","identifierLink":"https://www.uniprot.org/uniprotkb/Q15413/entry","name":"RYR3","description":"Ryanodine receptor 3","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46399","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3138","complexName":"KIF3 complex variant AB","organismName":"Homo sapiens; 9606","description":"Cytoplasmic, kinesin-2 motor complex involved in tethering the chromosomes to the spindle pole and in chromosome movement. Microtubule-based anterograde translocator for membranous organelles. Exhibits plus end-directed microtubule sliding activity (in vitro). \r\nIt is unclear if this dimer exists in vivo or whether it is always in complex with KAP3 (Q92845).","predictedComplex":false,"interactors":[{"ac":"EBI-1104844","identifier":"Q9Y496","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y496/entry","name":"KIF3A","description":"Kinesin-like protein KIF3A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3931791","identifier":"O15066","identifierLink":"https://www.uniprot.org/uniprotkb/O15066/entry","name":"KIF3B","description":"Kinesin-like protein KIF3B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3199","complexName":"KIF3 complex variant AC","organismName":"Homo sapiens; 9606","description":"Cytoplasmic, kinesin-2 motor complex involved in tethering the chromosomes to the spindle pole and in chromosome movement. Microtubule-based anterograde translocator for membranous organelles. Exhibits plus end-directed microtubule sliding activity (in vitro). \r\nIt is unclear if this dimer exists in vivo or whether it is always in complex with KAP3 (Q92845).","predictedComplex":false,"interactors":[{"ac":"EBI-1104844","identifier":"Q9Y496","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y496/entry","name":"KIF3A","description":"Kinesin-like protein KIF3A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1104854","identifier":"O14782","identifierLink":"https://www.uniprot.org/uniprotkb/O14782/entry","name":"KIF3C","description":"Kinesin-like protein KIF3C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3200","complexName":"KIF3 complex variant AC-KAP3","organismName":"Homo sapiens; 9606","description":"Cytoplasmic, kinesin-2 motor complex involved in tethering the chromosomes to the spindle pole and in chromosome movement. Microtubule-based anterograde translocator for membranous organelles. Exhibits plus end-directed microtubule sliding activity (in vitro). This trimeric kinesin motor complex may regulate the membrane binding of the KIF3A/KIF3C dimer (CPX-3199).","predictedComplex":false,"interactors":[{"ac":"EBI-1104844","identifier":"Q9Y496","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y496/entry","name":"KIF3A","description":"Kinesin-like protein KIF3A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1104854","identifier":"O14782","identifierLink":"https://www.uniprot.org/uniprotkb/O14782/entry","name":"KIF3C","description":"Kinesin-like protein KIF3C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-954040","identifier":"Q92845","identifierLink":"https://www.uniprot.org/uniprotkb/Q92845/entry","name":"KIFAP3","description":"Kinesin-associated protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15605","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3201","complexName":"KIF3 complex variant AB-KAP3","organismName":"Homo sapiens; 9606","description":"Cytoplasmic, kinesin-2 motor complex involved in tethering the chromosomes to the spindle pole and in chromosome movement. Microtubule-based anterograde translocator for membranous organelles. Exhibits plus end-directed microtubule sliding activity (in vitro). This trimeric kinesin motor complex may regulate the membrane binding of the KIF3A/KIF3B dimer (CPX-3138).","predictedComplex":false,"interactors":[{"ac":"EBI-1104844","identifier":"Q9Y496","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y496/entry","name":"KIF3A","description":"Kinesin-like protein KIF3A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3931791","identifier":"O15066","identifierLink":"https://www.uniprot.org/uniprotkb/O15066/entry","name":"KIF3B","description":"Kinesin-like protein KIF3B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-954040","identifier":"Q92845","identifierLink":"https://www.uniprot.org/uniprotkb/Q92845/entry","name":"KIFAP3","description":"Kinesin-associated protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15605","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3202","complexName":"KIF3 complex variant AC","organismName":"Mus musculus; 10090","description":"Cytoplasmic, kinesin-2 motor complex involved in tethering the chromosomes to the spindle pole and in chromosome movement. Microtubule-based anterograde translocator for membranous organelles. Exhibits plus end-directed microtubule sliding activity (in vitro). \r\nIt is unclear if this dimer exists in vivo or whether it is always in complex with KAP3 (P70188).","predictedComplex":false,"interactors":[{"ac":"EBI-6169413","identifier":"P28741","identifierLink":"https://www.uniprot.org/uniprotkb/P28741/entry","name":"Kif3a","description":"Kinesin-like protein KIF3A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9688707","identifier":"O35066","identifierLink":"https://www.uniprot.org/uniprotkb/O35066/entry","name":"Kif3c","description":"Kinesin-like protein KIF3C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3203","complexName":"KIF3 complex variant AB","organismName":"Mus musculus; 10090","description":"Cytoplasmic, kinesin-2 motor complex involved in tethering the chromosomes to the spindle pole and in chromosome movement. Microtubule-based anterograde translocator for membranous organelles. Exhibits plus end-directed microtubule sliding activity (in vitro). \r\nIt is unclear if this dimer exists in vivo or whether it is always in complex with KAP3 (P70188).","predictedComplex":false,"interactors":[{"ac":"EBI-6169413","identifier":"P28741","identifierLink":"https://www.uniprot.org/uniprotkb/P28741/entry","name":"Kif3a","description":"Kinesin-like protein KIF3A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6395332","identifier":"Q61771","identifierLink":"https://www.uniprot.org/uniprotkb/Q61771/entry","name":"Kif3b","description":"Kinesin-like protein KIF3B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3204","complexName":"KIF3 complex variant AB-KAP3","organismName":"Mus musculus; 10090","description":"Cytoplasmic, kinesin-2 motor complex involved in tethering the chromosomes to the spindle pole and in chromosome movement. Microtubule-based anterograde translocator for membranous organelles. Exhibits plus end-directed microtubule sliding activity (in vitro). This trimeric kinesin motor complex may regulate the membrane binding of the KIF3A/KIF3B dimer (CPX-3203).","predictedComplex":false,"interactors":[{"ac":"EBI-6169413","identifier":"P28741","identifierLink":"https://www.uniprot.org/uniprotkb/P28741/entry","name":"Kif3a","description":"Kinesin-like protein KIF3A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6169443","identifier":"P70188","identifierLink":"https://www.uniprot.org/uniprotkb/P70188/entry","name":"Kifap3","description":"Kinesin-associated protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15605","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6395332","identifier":"Q61771","identifierLink":"https://www.uniprot.org/uniprotkb/Q61771/entry","name":"Kif3b","description":"Kinesin-like protein KIF3B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3205","complexName":"KIF3 complex variant AC-KAP3","organismName":"Mus musculus; 10090","description":"Cytoplasmic, kinesin-2 motor complex involved in tethering the chromosomes to the spindle pole and in chromosome movement. Microtubule-based anterograde translocator for membranous organelles. Exhibits plus end-directed microtubule sliding activity (in vitro). This trimeric kinesin motor complex may regulate the membrane binding of the KIF3A/KIF3C dimer (CPX-3202).","predictedComplex":false,"interactors":[{"ac":"EBI-6169413","identifier":"P28741","identifierLink":"https://www.uniprot.org/uniprotkb/P28741/entry","name":"Kif3a","description":"Kinesin-like protein KIF3A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6169443","identifier":"P70188","identifierLink":"https://www.uniprot.org/uniprotkb/P70188/entry","name":"Kifap3","description":"Kinesin-associated protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15605","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9688707","identifier":"O35066","identifierLink":"https://www.uniprot.org/uniprotkb/O35066/entry","name":"Kif3c","description":"Kinesin-like protein KIF3C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3140","complexName":"Spaetzle complex","organismName":"Drosophila melanogaster; 7227","description":"The activated form, spaetzle C-106, acts as a ligand for the Toll receptor and involved in development and innate immunity. Binding to Toll activates the Toll signaling pathway and induces expression of the antifungal peptide drosomycin (P41964) in the hemolymph (esp. during gram-positive bacteria or fungal infection). Component of the extracellular signaling pathway that establishes dorsal-ventral polarity in the embryo.","predictedComplex":false,"interactors":[{"ac":"EBI-6379245","identifier":"P48607-PRO_0000022407","identifierLink":"https://www.uniprot.org/uniprotkb/P48607-PRO_0000022407/entry","name":"spz","description":"Protein spaetzle C-106","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]}]},{"complexAC":"CPX-3146","complexName":"Mitochondrial DNA-directed RNA polymerase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Mitochondrial RNA polymerase resides in the mitochondrion and is responsible for transcription of all genes on the mitochondrial genome, both protein- and RNA-coding. Binding of the polymerase complex to the promoter consensus sequence 5-prime-(- 8)ATATAAGTA(+ 1) bends and opens promoter DNA. The ability to initiate transcription at mitochondrial promoters is conferred by the regulatory subunit Mtf1p. The transcriptional activity of mitochondrial RNA polymerase is repressed by the high ATP levels generated during growth on glucose, and activated at low ATP levels during growth on non-fermentable carbon sources.","predictedComplex":false,"interactors":[{"ac":"EBI-11557","identifier":"P14908","identifierLink":"https://www.uniprot.org/uniprotkb/P14908/entry","name":"MTF1","description":"Mitochondrial transcription factor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11727","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15960","identifier":"P13433","identifierLink":"https://www.uniprot.org/uniprotkb/P13433/entry","name":"RPO41","description":"DNA-directed RNA polymerase, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3147","complexName":"PYM-mago-Y14 complex","organismName":"Drosophila melanogaster; 7227","description":"A cytoplasmic protein complex that activates the disassembly of the mago-Y14 (mago-tsu) complex (CPX-3100) from the spliced mRNA during first round of translation, disassembling the exon-exon junction complex independently of the translational machinery. The mago-Y14 complex shuttles between the nucleus, where it is loaded onto specific mRNAs, and the cytoplasm and functions in translational regulation.","predictedComplex":false,"interactors":[{"ac":"EBI-159609","identifier":"P49028","identifierLink":"https://www.uniprot.org/uniprotkb/P49028/entry","name":"mago","description":"Protein mago nashi","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12638","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-162353","identifier":"P82804","identifierLink":"https://www.uniprot.org/uniprotkb/P82804/entry","name":"Pym","description":"Partner of Y14 and mago","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22959","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-172458","identifier":"Q9V535","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V535/entry","name":"tsu","description":"RNA-binding protein 8A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3153","complexName":"PTEN phosphatase complex","organismName":"Homo sapiens; 9606","description":"PTEN is a phospholipid phosphatase, catalyzing the hydrolysis of the second messenger PtdIns (3,4,5)P3. Will also dephosphorylate PtdIns(3,4)P2, PtdIns3P, and Ins(1,3,4,5)P4. Dimerization is critical for its lipid phosphatase function. Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thus modulates cell cycle progression and cell survival. Also active as a dual-specificity protein phosphatase dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins but it is not yet clear if the enzyme is dimeric or monomeric for this activity.","predictedComplex":false,"interactors":[{"ac":"EBI-696162","identifier":"P60484","identifierLink":"https://www.uniprot.org/uniprotkb/P60484/entry","name":"PTEN","description":"Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3154","complexName":"PTEN phosphatase complex","organismName":"Mus musculus; 10090","description":"PTEN is a phospholipid phosphatase, catalyzing the hydrolysis of the second messenger PtdIns (3,4,5)P3. Will also dephosphorylate PtdIns(3,4)P2, PtdIns3P, and Ins(1,3,4,5)P4. Dimerization is critical for its lipid phosphatase function. Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thus modulates cell cycle progression and cell survival. Also active as a dual-specificity protein phosphatase dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins but it is not yet clear if the enzyme is dimeric or monomeric for this activity.","predictedComplex":false,"interactors":[{"ac":"EBI-1186266","identifier":"O08586","identifierLink":"https://www.uniprot.org/uniprotkb/O08586/entry","name":"Pten","description":"Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3152","complexName":"CSL-Notch-Mastermind transcription factor complex","organismName":"Caenorhabditis elegans; 6239","description":"Transcriptional activation complex. Assembles in the nucleus following engagement of a Notch receptor ligand which results in the release of the intracellular portion of Notch (ICN, NICD or Notch-Intra) from the membrane allowing this to translocate to the nucleus. The complex binds to the promoter of genes containing a conserved pair of CSL binding sites in a psuedo-symmetrical head-to-head orientation that are separated by 15-19 base pairs - a Su(H)-paired site or sequence paired site (SPS).","predictedComplex":false,"interactors":[{"ac":"EBI-317579","identifier":"Q09260","identifierLink":"https://www.uniprot.org/uniprotkb/Q09260/entry","name":"sel-8","description":"Protein lag-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-324482","identifier":"V6CLJ5","identifierLink":"https://www.uniprot.org/uniprotkb/V6CLJ5/entry","name":"lag-1","description":"Suppressor of hairless protein homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10665","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-326049","identifier":"P14585","identifierLink":"https://www.uniprot.org/uniprotkb/P14585/entry","name":"lin-12","description":"Protein lin-12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3155","complexName":"NuA4 histone acetyltransferase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Essential gene regulatory acetyltransferase with ATPase, DNA helicase and structural DNA binding activities. NuA4 histone acetyltransferase (HAT) complex is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, histone H2B to form H2BK16ac, histone H2A to form H2AK4ac and H2AK7ac, and histone variant H2A.Z to form H2A.ZK14ac. Acetylation of histone H4 is essential for DNA double-strand break repair through homologous recombination. Involved in cell cycle progression.","predictedComplex":false,"interactors":[{"ac":"EBI-2169","identifier":"P60010","identifierLink":"https://www.uniprot.org/uniprotkb/P60010/entry","name":"ACT1","description":"Actin","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22312","identifier":"P39995","identifierLink":"https://www.uniprot.org/uniprotkb/P39995/entry","name":"EAF5","description":"Chromatin modification-related protein EAF5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-22792","identifier":"P43572","identifierLink":"https://www.uniprot.org/uniprotkb/P43572/entry","name":"EPL1","description":"Enhancer of polycomb-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14898","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23061","identifier":"P53201","identifierLink":"https://www.uniprot.org/uniprotkb/P53201/entry","name":"SWC4","description":"SWR1-complex protein 4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12855","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-24622","identifier":"P38806","identifierLink":"https://www.uniprot.org/uniprotkb/P38806/entry","name":"YNG2","description":"Chromatin modification-related protein YNG2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-24638","identifier":"P38811","identifierLink":"https://www.uniprot.org/uniprotkb/P38811/entry","name":"TRA1","description":"SAGA complex/NuA4 acetyltransferase complex subunit TRA1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25552","identifier":"P47128","identifierLink":"https://www.uniprot.org/uniprotkb/P47128/entry","name":"EAF6","description":"Chromatin modification-related protein EAF6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-28841","identifier":"P53930","identifierLink":"https://www.uniprot.org/uniprotkb/P53930/entry","name":"YAF9","description":"Protein AF-9 homolog","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23195","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28927","identifier":"P53911","identifierLink":"https://www.uniprot.org/uniprotkb/P53911/entry","name":"EAF7","description":"Chromatin modification-related protein EAF7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13581","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2939","identifier":"P80428","identifierLink":"https://www.uniprot.org/uniprotkb/P80428/entry","name":"ARP4","description":"Actin-related protein 4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-35867","identifier":"Q06337","identifierLink":"https://www.uniprot.org/uniprotkb/Q06337/entry","name":"EAF1","description":"Chromatin modification-related protein EAF1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46459","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6281","identifier":"Q12432","identifierLink":"https://www.uniprot.org/uniprotkb/Q12432/entry","name":"EAF3","description":"Chromatin modification-related protein EAF3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10880","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6648","identifier":"Q08649","identifierLink":"https://www.uniprot.org/uniprotkb/Q08649/entry","name":"ESA1","description":"Histone acetyltransferase ESA1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3184","complexName":"EAF5-7-3 nucleosome disassembly/reassembly complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Plays a role in co-transcriptional RNA processing and maturation by associating with the coding region of transcriptionally active genes and affecting RNA polymerase II processivity. Promote the disruption, and subsequent reassembly, of nucleosomes. Also exists as a component of the NuA4 histone acetyltransferase complex (CPX-3155) which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A.","predictedComplex":false,"interactors":[{"ac":"EBI-22312","identifier":"P39995","identifierLink":"https://www.uniprot.org/uniprotkb/P39995/entry","name":"EAF5","description":"Chromatin modification-related protein EAF5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-28927","identifier":"P53911","identifierLink":"https://www.uniprot.org/uniprotkb/P53911/entry","name":"EAF7","description":"Chromatin modification-related protein EAF7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13581","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6281","identifier":"Q12432","identifierLink":"https://www.uniprot.org/uniprotkb/Q12432/entry","name":"EAF3","description":"Chromatin modification-related protein EAF3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10880","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3185","complexName":"Piccolo NuA4 histone acetyltransferase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Histone acetyltransferase complex which is involved in transcriptional activation of selected genes, principally by acetylation of nucleosomal histone H4 and H2A. Strongly prefers chromatin over free histones as substrate. Also acts as the catalytic core of the 1.3-MDa NuA4 histone acetyltransferase complex (CPX-3155).","predictedComplex":false,"interactors":[{"ac":"EBI-22792","identifier":"P43572","identifierLink":"https://www.uniprot.org/uniprotkb/P43572/entry","name":"EPL1","description":"Enhancer of polycomb-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14898","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-24622","identifier":"P38806","identifierLink":"https://www.uniprot.org/uniprotkb/P38806/entry","name":"YNG2","description":"Chromatin modification-related protein YNG2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6648","identifier":"Q08649","identifierLink":"https://www.uniprot.org/uniprotkb/Q08649/entry","name":"ESA1","description":"Histone acetyltransferase ESA1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3158","complexName":"SPOTS complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Serine C-palmitoyltransferase (SPT) catalyzes the first committed step in the biosynthesis of sphingolipids: condensation of serine with palmitoyl-CoA to form 3-ketosphinganine. The catalytic activity depends on LCB1 and LCB2, and is stimulated several-fold by TSC3. The remaining components are believed to play regulatory roles. Mature sphingolipids are an essential component of the plasma membrane. Moreover, several intermediates in sphingolipid metabolism are important signaling molecules involved in control of growth and stress response. Tight regulation of this rate-limiting step in sphingolipid synthesis is therefore critical for lipid homeostasis, membrane biogenesis, protein quality control and trafficking through the secretory pathway. Regulation of sphingolipid synthesis is mediated by phosphorylation of ORM1 and ORM2 as well as by up-regulation of ORM2 protein levels. Sphingolipid depletion activates the TORC2 complex (CPX-1717), which triggers ORM1 and ORM2 phosphorylation by the protein kinase YPK1 (P12688). Inhibition of the nutrient-sensitive TORC1 complex (CPX-1715 /CPX-1716) triggers phosphorylation of ORM proteins by the protein kinase NPR1 (P22211). Increased phosphorylation of ORM proteins reduces their inhibitory activity resulting in stimulation of SPOTS and increased sphingolipid synthesis. In addition, the presence of the phosphoinositide phosphatase SAC1 (P32368) in the SPOTS complex appears to link sphingolipid synthesis to phosphoinositide signaling that controls ER functions and ER-to-Golgi traffic. Thus, the SPOTS complex may be responsible for coordinating sphingolipid homeostasis with a variety of processes that control cell growth and response to nutrients.","predictedComplex":false,"interactors":[{"ac":"EBI-10059","identifier":"P25045","identifierLink":"https://www.uniprot.org/uniprotkb/P25045/entry","name":"LCB1","description":"Serine palmitoyltransferase 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13693","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10067","identifier":"P40970","identifierLink":"https://www.uniprot.org/uniprotkb/P40970/entry","name":"LCB2","description":"Serine palmitoyltransferase 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13693","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12592","identifier":"P53224","identifierLink":"https://www.uniprot.org/uniprotkb/P53224/entry","name":"ORM1","description":"Protein ORM1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12665","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16210","identifier":"P32368","identifierLink":"https://www.uniprot.org/uniprotkb/P32368/entry","name":"SAC1","description":"Phosphatidylinositol-3-phosphatase SAC1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45662","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2097198","identifier":"Q3E790","identifierLink":"https://www.uniprot.org/uniprotkb/Q3E790/entry","name":"TSC3","description":"Serine palmitoyltransferase-regulating protein TSC3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-34916","identifier":"Q06144","identifierLink":"https://www.uniprot.org/uniprotkb/Q06144/entry","name":"ORM2","description":"Protein ORM2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12665","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3159","complexName":"SLX1-SLX4 structure-specific endonuclease complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A structure-specific DNA endonuclease that cleaves the phosphodiester backbone on the 3'-side of the DNA branchpoint of branched DNA substrates including stem-loops and Y-structures, replication forks, 5'- and 3'-flaps, and nicked or intact Holliday junctions and is therefore involved in DNA recombination and repair. It is involved in rDNA copy number regulation and appears to act at the termination of rDNA replication.","predictedComplex":false,"interactors":[{"ac":"EBI-21016","identifier":"P38324","identifierLink":"https://www.uniprot.org/uniprotkb/P38324/entry","name":"SLX1","description":"Structure-specific endonuclease subunit SLX1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR20208","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-37788","identifier":"Q12098","identifierLink":"https://www.uniprot.org/uniprotkb/Q12098/entry","name":"SLX4","description":"Structure-specific endonuclease subunit SLX4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-9097897","identifier":"CHEBI:60240","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60240","name":"divalent metal cation","description":"divalent metal cation","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3163","complexName":"Sulfite reductase complex (NADPH)","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Sulfite reductase is a flavoprotein complex that catalyzes the reduction of sulfite to sulfide in the cysteine and methionine biosynthesis pathway. The activity is also required for sulfate assimilation.","predictedComplex":false,"interactors":[{"ac":"EBI-11476","identifier":"P39692","identifierLink":"https://www.uniprot.org/uniprotkb/P39692/entry","name":"MET10","description":"Sulfite reductase [NADPH] flavoprotein component","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19384","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25702","identifier":"P47169","identifierLink":"https://www.uniprot.org/uniprotkb/P47169/entry","name":"MET5","description":"Sulfite reductase [NADPH] subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11493","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9028779","identifier":"CHEBI:64607","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:64607","name":"fe4s4 iron-sulfur cluster","description":"Fe4S4 iron-sulfur cluster","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9663515","identifier":"CHEBI:58210","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58210","name":"fmn(3-)","description":"FMN(3-)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9678820","identifier":"CHEBI:28599","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:28599","name":"siroheme","description":"siroheme","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3170","complexName":"cdm-RanGTP complex","organismName":"Drosophila melanogaster; 7227","description":"A protein complex that has a role in the transport of proteins and RNAs in and out of the nucleus. Complex forms in the nucleus upon Ran-GTP binding to the cdm component of the nuclear import complex cdm-mago-Y14 (CPX-3171) and causes release of mago-Y14 (mago-tsu) (CPX-3100) for another round of messenger ribonucleoprotein (mRNP) incorporation. cdm translocates back into the cytosol for another round of cdm-mago-Y14 complex formation. The mago-Y14 heterodimer shuttles between the nucleus, where it is loaded onto specific mRNAs, and the cytoplasm and functions in translational regulation.","predictedComplex":false,"interactors":[{"ac":"EBI-170371","identifier":"Q9VEC5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VEC5/entry","name":"cdm","description":"Importin-13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12363","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-191663","identifier":"Q9VZ23","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VZ23/entry","name":"Ran","description":"GTP-binding nuclear protein Ran","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR24071","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-989053","identifier":"CHEBI:15996","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15996","name":"gtp","description":"guanosine triphosphate - GTP","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3171","complexName":"cdm-mago-Y14 complex","organismName":"Drosophila melanogaster; 7227","description":"A nuclear import complex that functions as a nuclear import receptor for the mago-Y14 (mago-tsu) complex (CPX-3100) for each round of messenger ribonucleoprotein (mRNP) complex incorporation and regulation. Complex formation occurs in the cytosol and requires the action of translating ribosomes on the mRNP and the ribosomally associated protein Pym (P82804, in complex CPX-3147). cdm (Imp13) binds to and releases Pym from the mago-Y14 complex. mago-Y14 shuttles between the nucleus, where it is loaded onto specific mRNAs, and the cytoplasm and functions in translational regulation.","predictedComplex":false,"interactors":[{"ac":"EBI-159609","identifier":"P49028","identifierLink":"https://www.uniprot.org/uniprotkb/P49028/entry","name":"mago","description":"Protein mago nashi","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12638","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-170371","identifier":"Q9VEC5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VEC5/entry","name":"cdm","description":"Importin-13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12363","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-172458","identifier":"Q9V535","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V535/entry","name":"tsu","description":"RNA-binding protein 8A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3172","complexName":"EGO complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"The EGO complex is localized to the vacuolar membranes and activates vacuolar membrane associated TORC1 in the presence of preferred nitrogen sources.  It thereby has an important role in regulating cell growth and autophagy by relaying amino acid signals.  Specifically, its subunit GTR1 becomes activated to a GTP-bound form in a downstream response to nutrient signals, causing EGO to interact with and activate TORC1.  EGO is required for recovery from rapamycin-induced growth arrest and positively regulates microautophagy.","predictedComplex":false,"interactors":[{"ac":"EBI-10954475","identifier":"Q3E830","identifierLink":"https://www.uniprot.org/uniprotkb/Q3E830/entry","name":"EGO2","description":"Protein EGO2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-21507","identifier":"P38247","identifierLink":"https://www.uniprot.org/uniprotkb/P38247/entry","name":"SLM4","description":"Protein SLM4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-27062","identifier":"Q02205","identifierLink":"https://www.uniprot.org/uniprotkb/Q02205/entry","name":"MEH1","description":"Protein MEH1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-7954","identifier":"Q00582","identifierLink":"https://www.uniprot.org/uniprotkb/Q00582/entry","name":"GTR1","description":"GTP-binding protein GTR1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11259","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7962","identifier":"P53290","identifierLink":"https://www.uniprot.org/uniprotkb/P53290/entry","name":"GTR2","description":"GTP-binding protein GTR2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11259","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3233","complexName":"GSE complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"GTPase complex that stimulates TORC1 in response to amino acid stimulation. The GSE complex was shown to be localized to late endosomes, and to be required for sorting of GAP1 - a general amino acid permease - to the plasma membrane from endosomes.  Regulates exit from rapamycin-induced growth arrest. GSE shares common components with the EGO complex (CPX-3172).","predictedComplex":false,"interactors":[{"ac":"EBI-10248","identifier":"P34078","identifierLink":"https://www.uniprot.org/uniprotkb/P34078/entry","name":"LTV1","description":"Protein LTV1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21531","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21507","identifier":"P38247","identifierLink":"https://www.uniprot.org/uniprotkb/P38247/entry","name":"SLM4","description":"Protein SLM4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-27062","identifier":"Q02205","identifierLink":"https://www.uniprot.org/uniprotkb/Q02205/entry","name":"MEH1","description":"Protein MEH1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-7954","identifier":"Q00582","identifierLink":"https://www.uniprot.org/uniprotkb/Q00582/entry","name":"GTR1","description":"GTP-binding protein GTR1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11259","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7962","identifier":"P53290","identifierLink":"https://www.uniprot.org/uniprotkb/P53290/entry","name":"GTR2","description":"GTP-binding protein GTR2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11259","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3174","complexName":"raps-insc complex","organismName":"Drosophila melanogaster; 7227","description":"Required for the asymmetric division of neuroblasts. Coordinates asymmetric localization of cell fate determinants with orientation of the mitotic spindle resulting in different daughter cells upon division. Localizes at the apical cortex of the neuroblast: Raps maintains, but does not initiate, Insc apically, while Insc segregates Raps asymmetrically.\r\n\r\nRequires the G protein alpha i subunit (Galphai, P20353) for partial activity resulting in the selective recruitment of Discs large 1 (Dlg1, P31007) but not Mushroom body defect (Mud, Q8IR55). This ensures that the spindle is attached to the cortex (via Dlg) before activation of spindle pulling forces by Dynein/Dynactin (via Mud). The selective recruitment of Dlg1 occurs by a steric mechanism: Insc and Mud compete for binding to the tetratricopeptide repeats (TPRs, IPR019734) of Raps. \r\n\r\nComplex activity appears to be conserved. Mammalian Insc (Q1MX18) functions similar to Insc, GPSM1 (also called AGS3, Q86YR5) and GPSM2 (also called LGN, P81274) to Raps, and NuMA (Q14980) to Mud.","predictedComplex":false,"interactors":[{"ac":"EBI-116643","identifier":"Q9VB22","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VB22/entry","name":"pins","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45954","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-124697","identifier":"Q9W2R4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W2R4/entry","name":"insc","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21386","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3177","complexName":"eIF4E-cup complex","organismName":"Drosophila melanogaster; 7227","description":"Causes translational repression. Prevents assembly of ribosomes at the mRNA by interfacing with a sequence-specific RNA-binding protein leading to recruitment of the CCR4 complex and consequently, reduction of the mRNA's poly(A) tail length. \r\n\r\nRequired for dorso-ventral pattern formation in the embryo: liaises with Bruno (O02374) and Smaug (Q23972), which bind to oskar and nanos mRNAs, respectively, to prevent their translation before posterior localization.","predictedComplex":false,"interactors":[{"ac":"EBI-198574","identifier":"P48598","identifierLink":"https://www.uniprot.org/uniprotkb/P48598/entry","name":"eIF4E1","description":"Eukaryotic translation initiation factor 4E1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-95398","identifier":"Q9VMA3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VMA3/entry","name":"cup","description":"Protein cup","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12269","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3179","complexName":"Slx5-Slx8 SUMO-targeted ubiquitin ligase (STUbL) complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"The Slx5-Slx8 complex is a heterodimeric ubiquitin ligase (E3) that recognizes sumoylated proteins and causes the transfer of ubiquitin from an E2 to its target, attaching polyubiquitin chains to it. The complex has DNA-binding activity and is involved in various cellular processes, including targeting poly-sumoylated proteins for degradation; DNA damage repair and genome stability. The complex is localized to the nucleus and has been implicated in protein quality control of nuclear proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-22661","identifier":"P40072","identifierLink":"https://www.uniprot.org/uniprotkb/P40072/entry","name":"SLX8","description":"E3 ubiquitin-protein ligase complex SLX5-SLX8 subunit SLX8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-8276","identifier":"P32828","identifierLink":"https://www.uniprot.org/uniprotkb/P32828/entry","name":"SLX5","description":"E3 ubiquitin-protein ligase complex SLX5-SLX8 subunit SLX5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28042","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3180","complexName":"Mitochondrial degradosome complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Plays an essential role in mitochondrial RNA turnover, degrading structured RNA  in an ATP-dependent manner.  Helicase activity of the degradosome is more efficient with substrates with 3'-overhangs, and requires the presence of DSS1.\r\nUnprocessed rRNA and mRNA accumulate in cells lacking degradosome activity, however, tRNA maturation is unaffected, indicating that this complex is not directly involved in RNA processing. Instead, the degradosome complex is likely part of the mitochondrial RNA surveillance system, which degrades aberrant and unprocessed RNAs.","predictedComplex":false,"interactors":[{"ac":"EBI-11468","identifier":"P39112","identifierLink":"https://www.uniprot.org/uniprotkb/P39112/entry","name":"DSS1","description":"Exoribonuclease II, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23355","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18594","identifier":"P32580","identifierLink":"https://www.uniprot.org/uniprotkb/P32580/entry","name":"SUV3","description":"ATP-dependent RNA helicase SUV3, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3181","complexName":"aubergine-tudor complex","organismName":"Drosophila melanogaster; 7227","description":"Required for gametogenesis. PIWI proteins associate specifically with PIWI-interacting RNAs (piRNAs), small RNAs expressed predominantly in germlines, and silence transposable DNA elements, thus maintaining the integrity of the genome and the development of gametes. The presence of Tudor in the complex appears to be required for the quality control of transposon-derived piRNAs. Symmetric dimethylated arginines (sDMA) result from methylation of Aub by dPRMT5 (csul, Q9U6Y9) and act as binding sites for Tud domains. This complex accumulates in the P granule (meiotic nuage) of primordial germ cells where it is found in the posterior pole plasm.","predictedComplex":false,"interactors":[{"ac":"EBI-498741","identifier":"P25823","identifierLink":"https://www.uniprot.org/uniprotkb/P25823/entry","name":"tud","description":"Protein tudor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22948","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-98862","identifier":"O76922","identifierLink":"https://www.uniprot.org/uniprotkb/O76922/entry","name":"aub","description":"Protein aubergine","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22891","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3188","complexName":"Polarisome","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Controls thepolarized (unidimensional) cell growth in yeast and other fungi. Required for tip growth and acts as a central hub for coordinating exocytosis with actin cable formation. One of the targets of polarisome is the Rab GTPase SEC4, which associates with secretory vesicles and stimulates their fusion with the exocytic sites at the plasma membrane. Thus, the primary function of polarisome appears to be guiding polarized transport and secretion along actin cables and bringing secretory vesicles to the sites of polarized growth.","predictedComplex":false,"interactors":[{"ac":"EBI-13106","identifier":"P40091","identifierLink":"https://www.uniprot.org/uniprotkb/P40091/entry","name":"PEA2","description":"Protein PEA2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-17803","identifier":"P23201","identifierLink":"https://www.uniprot.org/uniprotkb/P23201/entry","name":"SPA2","description":"Protein SPA2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21601","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28312","identifier":"P48566","identifierLink":"https://www.uniprot.org/uniprotkb/P48566/entry","name":"MSB3","description":"GTPase-activating protein GYP3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-33881","identifier":"Q12317","identifierLink":"https://www.uniprot.org/uniprotkb/Q12317/entry","name":"MSB4","description":"GTPase-activating protein MSB4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3692","identifier":"P41832","identifierLink":"https://www.uniprot.org/uniprotkb/P41832/entry","name":"BNI1","description":"Protein BNI1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3857","identifier":"P41697","identifierLink":"https://www.uniprot.org/uniprotkb/P41697/entry","name":"BUD6","description":"Bud site selection protein 6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22741","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3189","complexName":"Cav1.1 voltage-gated calcium channel complex, CACNA2D1-CACNB1-CACNG1 variant","organismName":"Oryctolagus cuniculus; 9986","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.1 channel is responsible for the excitation-contraction coupling that causes contraction of skeletal muscles in response to changes in membrane potential, relaying an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmic membrane. The action potential-induced conformational changes of the complex activates the type 1 ryanodine receptor ( [RyR1: CPX-3135, RyR3: CPX-3162]), which releases Ca2+ from the sarcoplasmic reticulum, triggering muscle contraction.","predictedComplex":false,"interactors":[{"ac":"EBI-8613624","identifier":"P07293","identifierLink":"https://www.uniprot.org/uniprotkb/P07293/entry","name":"CACNA1S","description":"Voltage-dependent L-type calcium channel subunit alpha-1S","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Oryctolagus cuniculus; 9986","xrefs":[]},{"ac":"EBI-9683785","identifier":"P13806-PRO_0000005007","identifierLink":"https://www.uniprot.org/uniprotkb/P13806-PRO_0000005007/entry","name":"CACNA2D1","description":"Voltage-dependent calcium channel subunit alpha-2-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Oryctolagus cuniculus; 9986","xrefs":[]},{"ac":"EBI-9683796","identifier":"P13806-PRO_0000005008","identifierLink":"https://www.uniprot.org/uniprotkb/P13806-PRO_0000005008/entry","name":"CACNA2D1","description":"Voltage-dependent calcium channel subunit delta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Oryctolagus cuniculus; 9986","xrefs":[]},{"ac":"EBI-9683808","identifier":"P19518","identifierLink":"https://www.uniprot.org/uniprotkb/P19518/entry","name":"CACNG1","description":"Voltage-dependent calcium channel gamma-1 subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Oryctolagus cuniculus; 9986","xrefs":[]},{"ac":"EBI-978604","identifier":"P19517","identifierLink":"https://www.uniprot.org/uniprotkb/P19517/entry","name":"CACNB1","description":"Voltage-dependent L-type calcium channel subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Oryctolagus cuniculus; 9986","xrefs":[]}]},{"complexAC":"CPX-3191","complexName":"Cav1.1 voltage-gated calcium channel complex, CACNA2D1-CACNB1-CACNG1 variant","organismName":"Mus musculus; 10090","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.1 channel is responsible for the excitation-contraction coupling that causes contraction of skeletal muscles in response to changes in membrane potential, relaying an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmic membrane.. The action potential-induced conformational changes of the complex activates the type 1 ryanodine receptor ( [RyR1: CPX-3135, RyR3: CPX-3162]), which releases Ca2+ from the sarcoplasmic reticulum, triggering muscle contraction.","predictedComplex":false,"interactors":[{"ac":"EBI-644833","identifier":"Q8R3Z5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R3Z5/entry","name":"Cacnb1","description":"Voltage-dependent L-type calcium channel subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9686660","identifier":"Q02789","identifierLink":"https://www.uniprot.org/uniprotkb/Q02789/entry","name":"Cacna1s","description":"Voltage-dependent L-type calcium channel subunit alpha-1S","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9686698","identifier":"O08532-PRO_0000005003","identifierLink":"https://www.uniprot.org/uniprotkb/O08532-PRO_0000005003/entry","name":"Cacna2d1","description":"Voltage-dependent calcium channel subunit alpha-2-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-9686707","identifier":"O08532-PRO_0000005004","identifierLink":"https://www.uniprot.org/uniprotkb/O08532-PRO_0000005004/entry","name":"Cacna2d1","description":"Voltage-dependent calcium channel subunit delta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-9686716","identifier":"O70578","identifierLink":"https://www.uniprot.org/uniprotkb/O70578/entry","name":"Cacng1","description":"Voltage-dependent calcium channel gamma-1 subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15025","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3192","complexName":"Cav1.1 voltage-gated calcium channel complex, CACNA2D1-CACNB1-CACNG1 variant","organismName":"Homo sapiens; 9606","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.1 channel is responsible for the excitation-contraction coupling that causes contraction of skeletal muscles in response to changes in membrane potential, relaying an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmic membrane.. The action potential-induced conformational changes of the complex activates the type 1 ryanodine receptor ( [RyR1: CPX-3135, RyR3: CPX-3162]), which releases Ca2+ from the sarcoplasmic reticulum, triggering muscle contraction.","predictedComplex":false,"interactors":[{"ac":"EBI-5329490","identifier":"Q13698","identifierLink":"https://www.uniprot.org/uniprotkb/Q13698/entry","name":"CACNA1S","description":"Voltage-dependent L-type calcium channel subunit alpha-1S","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-947514","identifier":"Q02641","identifierLink":"https://www.uniprot.org/uniprotkb/Q02641/entry","name":"CACNB1","description":"Voltage-dependent L-type calcium channel subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9686780","identifier":"Q06432","identifierLink":"https://www.uniprot.org/uniprotkb/Q06432/entry","name":"CACNG1","description":"Voltage-dependent calcium channel gamma-1 subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15025","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9686800","identifier":"P54289-PRO_0000005001","identifierLink":"https://www.uniprot.org/uniprotkb/P54289-PRO_0000005001/entry","name":"CACNA2D1","description":"Voltage-dependent calcium channel subunit alpha-2-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-9686811","identifier":"P54289-PRO_0000005002","identifierLink":"https://www.uniprot.org/uniprotkb/P54289-PRO_0000005002/entry","name":"CACNA2D1","description":"Voltage-dependent calcium channel subunit delta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-3193","complexName":"Cav1.2 voltage-gated calcium channel complex, CACNA2D1-CACNB2 variant","organismName":"Bos taurus; 9913","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.2 channel is responsible for excitation-contraction (E-C) coupling of cardiac and, to some extent, smooth muscle. It relays an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmatic membrane. More specifically, rapid depolarization-induced conformational changes of the complex stimulates calcium efflux from the sarcoplasmatic reticulum through the Ryanodine 2 complex calcium release channel, which subsequently triggers the contractile apparatus until the calcium concentration is reduced again due to re-uptake into the sarcoplasmic reticulum by the Ca2+-ATPase, ATP2A1 (Q0VCY0).","predictedComplex":false,"interactors":[{"ac":"EBI-9683990","identifier":"Q9MZL5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9MZL5/entry","name":"CACNB2","description":"Voltage-dependent L-type calcium channel subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9684011","identifier":"F1N5T3","identifierLink":"https://www.uniprot.org/uniprotkb/F1N5T3/entry","name":"CACNA1C","description":"Voltage-dependent L-type calcium channel subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9684050","identifier":"F1N7F9","identifierLink":"https://www.uniprot.org/uniprotkb/F1N7F9/entry","name":"CACNA2D1","description":null,"stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR10166","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3194","complexName":"Cav1.2 voltage-gated calcium channel complex, CACNA2D1-CACNB2 variant","organismName":"Mus musculus; 10090","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.2channel is responsible for excitation-contraction (E-C) coupling of cardiac and, to some extent, smooth muscle. It relays an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmatic membrane. More specifically, rapid depolarization-induced conformational changes of  the complex stimulates calcium efflux from the sarcoplasmatic reticulum through the Ryanodine 2 complex  (CPX-3137) calcium release channel, which subsequently triggers the contractile apparatus until the calcium concentration is reduced again due to re-uptake into the sarcoplasmic reticulum by the Ca2+-ATPase, ATP2A1 (Q8R429).","predictedComplex":false,"interactors":[{"ac":"EBI-644904","identifier":"Q01815","identifierLink":"https://www.uniprot.org/uniprotkb/Q01815/entry","name":"Cacna1c","description":"Voltage-dependent L-type calcium channel subunit alpha-1C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9686698","identifier":"O08532-PRO_0000005003","identifierLink":"https://www.uniprot.org/uniprotkb/O08532-PRO_0000005003/entry","name":"Cacna2d1","description":"Voltage-dependent calcium channel subunit alpha-2-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-9686707","identifier":"O08532-PRO_0000005004","identifierLink":"https://www.uniprot.org/uniprotkb/O08532-PRO_0000005004/entry","name":"Cacna2d1","description":"Voltage-dependent calcium channel subunit delta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-9690121","identifier":"Q8CC27","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CC27/entry","name":"Cacnb2","description":"Voltage-dependent L-type calcium channel subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3195","complexName":"Cav1.2 voltage-gated calcium channel complex, CACNA2D1-CACNB2 variant","organismName":"Homo sapiens; 9606","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.2 channel is responsible for excitation-contraction (E-C) coupling of cardiac and, to some extent, smooth muscle. It relays an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmatic membrane. More specifically, rapid depolarization-induced conformational changes of  the complex stimulates calcium efflux from the sarcoplasmatic reticulum through the Ryanodine 2 complex  (CPX-3156) calcium release channel, which subsequently triggers the contractile apparatus until the calcium concentration is reduced again due to re-uptake into the sarcoplasmic reticulum by the Ca2+-ATPase, ATP2A1 (O14983).","predictedComplex":false,"interactors":[{"ac":"EBI-1038838","identifier":"Q13936","identifierLink":"https://www.uniprot.org/uniprotkb/Q13936/entry","name":"CACNA1C","description":"Voltage-dependent L-type calcium channel subunit alpha-1C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2874501","identifier":"Q08289","identifierLink":"https://www.uniprot.org/uniprotkb/Q08289/entry","name":"CACNB2","description":"Voltage-dependent L-type calcium channel subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9686800","identifier":"P54289-PRO_0000005001","identifierLink":"https://www.uniprot.org/uniprotkb/P54289-PRO_0000005001/entry","name":"CACNA2D1","description":"Voltage-dependent calcium channel subunit alpha-2-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-9686811","identifier":"P54289-PRO_0000005002","identifierLink":"https://www.uniprot.org/uniprotkb/P54289-PRO_0000005002/entry","name":"CACNA2D1","description":"Voltage-dependent calcium channel subunit delta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-3196","complexName":"ERMES complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"The ERMES complex serves as a physical connection between the endoplasmic reticulum (ER) and the mitochondrion. The complex, or simply the physical connection provided by the complex, may facilitate transfer of lipids, calcium ions, or other metabolites between the organelles. Mitochondrial nucleoids are located near ERMES, and the complex is required for accurate segregation of the mitochondrial genome. Mutations is any of the complex subunit genes confer aberrant mitochondrial morphology and inheritance.","predictedComplex":false,"interactors":[{"ac":"EBI-10580","identifier":"P18409","identifierLink":"https://www.uniprot.org/uniprotkb/P18409/entry","name":"MDM10","description":"Mitochondrial distribution and morphology protein 10","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28035","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10584","identifier":"Q92328","identifierLink":"https://www.uniprot.org/uniprotkb/Q92328/entry","name":"MDM12","description":"Mitochondrial distribution and morphology protein 12","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28204","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11029","identifier":"P41800","identifierLink":"https://www.uniprot.org/uniprotkb/P41800/entry","name":"MMM1","description":"Maintenance of mitochondrial morphology protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13466","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20685","identifier":"P39722","identifierLink":"https://www.uniprot.org/uniprotkb/P39722/entry","name":"GEM1","description":"Mitochondrial Rho GTPase 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24072","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-24154","identifier":"P53083","identifierLink":"https://www.uniprot.org/uniprotkb/P53083/entry","name":"MDM34","description":"Mitochondrial distribution and morphology protein 34","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28185","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3207","complexName":"Mitochondrial pyruvate dehydrogenase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Mitochondrial matrix enzyme that converts pyruvate to acetyl-CoA and CO2. This provides a metabolic connection between glycolysis, whose end product is pyruvate, and the tricarboxylic acid cycle, which starts with acetyl-CoA. Pyruvate dehydrogenase (PDH) activity is negatively regulated via phosphorylation of its PDA1 subunit. The protein kinases PKP1 (P40530) and PKP2 (P53170) phosphorylate PDA1, and the protein phosphatases PTC5 (Q12511) and PTC6 (P25646) mediate its dephosphorylation.","predictedComplex":false,"interactors":[{"ac":"EBI-1225105","identifier":"CHEBI:16238","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16238","name":"fad","description":"FAD - Flavin adenine dinucleotide","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-12469","identifier":"P12695","identifierLink":"https://www.uniprot.org/uniprotkb/P12695/entry","name":"LAT1","description":"Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial","stochiometry":"minValue: 60, maxValue: 60","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23151","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12475","identifier":"P16387","identifierLink":"https://www.uniprot.org/uniprotkb/P16387/entry","name":"PDA1","description":"Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial","stochiometry":"minValue: 24, maxValue: 24","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11516","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12482","identifier":"P32473","identifierLink":"https://www.uniprot.org/uniprotkb/P32473/entry","name":"PDB1","description":"Pyruvate dehydrogenase E1 component subunit beta, mitochondrial","stochiometry":"minValue: 24, maxValue: 24","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11624","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12489","identifier":"P16451","identifierLink":"https://www.uniprot.org/uniprotkb/P16451/entry","name":"PDX1","description":"Pyruvate dehydrogenase complex protein X component, mitochondrial","stochiometry":"minValue: 12, maxValue: 12","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23151","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5940","identifier":"P09624","identifierLink":"https://www.uniprot.org/uniprotkb/P09624/entry","name":"LPD1","description":"Dihydrolipoyl dehydrogenase, mitochondrial","stochiometry":"minValue: 12, maxValue: 12","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22912","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9691551","identifier":"CHEBI:58937","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58937","name":"thiamine(1+) diphosphate(3-)","description":"thiamine(1+) diphosphate(3-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3208","complexName":"SMAD2-SMAD4 complex","organismName":"Homo sapiens; 9606","description":"A transcription factor complex which binds to the promoters of target genes and recruits co-activators and histone acetyltransferases, such as p300, CBP and P300/CBP-associated factor, facilitating transcription. In response to TGF-beta/activin-family protein binding, TGF-beta type II receptors phosphorylate TGF-beta type I receptors (ALK4, 5 and 7) which in turn phosphorylates SMAD2 on two Ser-465 and Ser-467. This enables binding to SMAD4 to form heteromeric SMAD complexes that enter the nucleus to initiate gene transcription.\r\nBecause of their relatively low DNA-binding affinity, SMAD complexes interact with a wide variety of DNA-binding proteins, crosstalk with other signalling pathways and interaction with other DNA-binding cofactors define the specific binding patterns of SMADs; in addition, interaction with coactivators/corepressors modulates their transcriptional activity.","predictedComplex":false,"interactors":[{"ac":"EBI-1040141","identifier":"Q15796","identifierLink":"https://www.uniprot.org/uniprotkb/Q15796/entry","name":"SMAD2","description":"Mothers against decapentaplegic homolog 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13703","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347263","identifier":"Q13485","identifierLink":"https://www.uniprot.org/uniprotkb/Q13485/entry","name":"SMAD4","description":"Mothers against decapentaplegic homolog 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13703","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3251","complexName":"SMAD2-SMAD4 complex","organismName":"Mus musculus; 10090","description":"A transcription factor complex which binds to the promoters of target genes and recruits co-activators and histone acetyltransferases, such as p300, CBP and P300/CBP-associated factor, facilitating transcription. In response to TGF-beta/activin-family protein binding, TGF-beta type II receptors phosphorylate TGF-beta type I receptors (ALK4, 5 and 7) which in turn phosphorylates Smad2 on two Ser-465 and Ser-467. This enables binding to Smad4 to form heteromeric Smad complexes that enter the nucleus to initiate gene transcription.\r\nBecause of their relatively low DNA-binding affinity, Smad complexes interact with a wide variety of DNA-binding proteins. Crosstalk with other signalling pathways and interaction with other DNA-binding cofactors define the specific binding patterns of Smads; in addition, interaction with coactivators/corepressors modulates their transcriptional activity.","predictedComplex":false,"interactors":[{"ac":"EBI-2337932","identifier":"Q62432","identifierLink":"https://www.uniprot.org/uniprotkb/Q62432/entry","name":"Smad2","description":"Mothers against decapentaplegic homolog 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13703","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5259270","identifier":"P97471","identifierLink":"https://www.uniprot.org/uniprotkb/P97471/entry","name":"Smad4","description":"Mothers against decapentaplegic homolog 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13703","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3252","complexName":"SMAD3-SMAD4 complex","organismName":"Homo sapiens; 9606","description":"A transcription factor complex which binds to the promoters of target genes and recruits co-activators and histone acetyltransferases, such as p300, CBP and P300/CBP-associated factor, facilitating transcription. In response to TGF-beta/activin-family protein binding, TGF-beta type II receptors phosphorylate TGF-beta type I receptors (ALK4, 5 and 7) which in turn phosphorylates SMAD3 on two Ser-423 and Ser-425. This enables binding to SMAD4 to form heteromeric SMAD complexes that enter the nucleus to initiate gene transcription.\r\nBecause of their relatively low DNA-binding affinity, SMAD complexes interact with a wide variety of DNA-binding proteins. Crosstalk with other signalling pathways and interaction with other DNA-binding cofactors define the specific binding patterns of SMADs; in addition, interaction with coactivators/corepressors modulates their transcriptional activity.","predictedComplex":false,"interactors":[{"ac":"EBI-347161","identifier":"P84022","identifierLink":"https://www.uniprot.org/uniprotkb/P84022/entry","name":"SMAD3","description":"Mothers against decapentaplegic homolog 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13703","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347263","identifier":"Q13485","identifierLink":"https://www.uniprot.org/uniprotkb/Q13485/entry","name":"SMAD4","description":"Mothers against decapentaplegic homolog 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13703","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3209","complexName":"Cry1-Per2 complex","organismName":"Mus musculus; 10090","description":"Gradually accumulates in the nucleus to negatively regulate CLOCK-BMAL (CPX-3225, CPX-3228) -dependent transactivation of genes in a delayed negative feedback mechanism which generates circadian rhythms. Phosphorylation of PER2 by CSNK1D/CSNK1E (Q9DC28/Q9JMK2) effects stability and nuclear localisation of the complex. Phosphorylation of CRY1 Ser-71 stimulates the direct binding of FBXL3 (Q8C4V4), targeting it for ubiquitin-mediated degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-1266607","identifier":"P97784","identifierLink":"https://www.uniprot.org/uniprotkb/P97784/entry","name":"Cry1","description":"Cryptochrome-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11455","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1266779","identifier":"O54943","identifierLink":"https://www.uniprot.org/uniprotkb/O54943/entry","name":"Per2","description":"Period circadian protein homolog 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11269","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3219","complexName":"Cry1-Per2 complex","organismName":"Homo sapiens; 9606","description":"Gradually accumulates in the nucleus to negatively regulate CLOCK-BMAL (CPX-3229, CPX-3230) -dependent transactivation of genes in a delayed negative feedback mechanism which generates circadian rhythms. Phosphorylation of PER2 by CSNK1D/CSNK1E (P48730/P49674) effects stability and nuclear localisation of the complex. Phosphorylation of CRY1 Ser-71 stimulates the direct binding of FBXL3 (Q9UKT7), targeting it for ubiquitin-mediated degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-1054296","identifier":"O15055","identifierLink":"https://www.uniprot.org/uniprotkb/O15055/entry","name":"PER2","description":"Period circadian protein homolog 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11269","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-741297","identifier":"Q16526","identifierLink":"https://www.uniprot.org/uniprotkb/Q16526/entry","name":"CRY1","description":"Cryptochrome-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11455","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3210","complexName":"Cry2-Per2 complex","organismName":"Mus musculus; 10090","description":"Gradually accumulates in the nucleus to negatively regulate CLOCK-BMAL (CPX-3225, CPX-3228) -dependent transactivation of genes in a delayed negative feedback mechanism which generates circadian rhythms. Phosphorylation of PER2 by CSNK1D/CSNK1E (Q9DC28/Q9JMK2) effects stability and nuclear localisation of the complex. Phosphorylation of CRY2 Ser-71 stimulates the direct binding of FBXL3 (Q8C4V4), targeting it for ubiquitin-mediated degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-1266619","identifier":"Q9R194","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R194/entry","name":"Cry2","description":"Cryptochrome-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11455","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1266779","identifier":"O54943","identifierLink":"https://www.uniprot.org/uniprotkb/O54943/entry","name":"Per2","description":"Period circadian protein homolog 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11269","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3214","complexName":"Cry2-Per1 complex","organismName":"Mus musculus; 10090","description":"Gradually accumulates in the nucleus to negatively regulate CLOCK-BMAL (CPX-3225, CPX-3228) -dependent transactivation of genes in a delayed negative feedback mechanism which generates circadian rhythms. Phosphorylation of PER1 by CSNK1D/CSNK1E (Q9DC28/Q9JMK2) effects stability and nuclear localisation of the complex. Phosphorylation of CRY2 Ser-71 stimulates the direct binding of FBXL3 (Q8C4V4), targeting it for ubiquitin-mediated degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-1266619","identifier":"Q9R194","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R194/entry","name":"Cry2","description":"Cryptochrome-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11455","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1266764","identifier":"O35973","identifierLink":"https://www.uniprot.org/uniprotkb/O35973/entry","name":"Per1","description":"Period circadian protein homolog 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11269","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3216","complexName":"Cry1-Per1 complex","organismName":"Mus musculus; 10090","description":"Gradually accumulates in the nucleus to negatively regulate CLOCK-BMAL (CPX-3225, CPX-3228) -dependent transactivation of genes in a delayed negative feedback mechanism which generates circadian rhythms. Phosphorylation of PER1 by CSNK1D/CSNK1E (Q9DC28/Q9JMK2) effects stability and nuclear localisation of the complex. Phosphorylation of CRY1 Ser-71 stimulates the direct binding of FBXL3 (Q8C4V4), targeting it for ubiquitin-mediated degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-1266607","identifier":"P97784","identifierLink":"https://www.uniprot.org/uniprotkb/P97784/entry","name":"Cry1","description":"Cryptochrome-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11455","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1266764","identifier":"O35973","identifierLink":"https://www.uniprot.org/uniprotkb/O35973/entry","name":"Per1","description":"Period circadian protein homolog 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11269","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3217","complexName":"Cry1-Per3 complex","organismName":"Mus musculus; 10090","description":"Gradually accumulates in the nucleus to negatively regulate CLOCK-BMAL (CPX-3225, CPX-3228) -dependent transactivation of genes in a delayed negative feedback mechanism which generates circadian rhythms. Phosphorylation of PER3 by CSNK1D/CSNK1E (Q9DC28/Q9JMK2) effects stability and nuclear localisation of the complex. Phosphorylation of CRY1 Ser-71 stimulates the direct binding of FBXL3 (Q8C4V4), targeting it for ubiquitin-mediated degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-1266607","identifier":"P97784","identifierLink":"https://www.uniprot.org/uniprotkb/P97784/entry","name":"Cry1","description":"Cryptochrome-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11455","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9695895","identifier":"O70361","identifierLink":"https://www.uniprot.org/uniprotkb/O70361/entry","name":"Per3","description":"Period circadian protein homolog 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11269","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3218","complexName":"Cry2-Per3 complex","organismName":"Mus musculus; 10090","description":"Gradually accumulates in the nucleus to negatively regulate CLOCK-BMAL (CPX-3225, CPX-3228) -dependent transactivation of genes in a delayed negative feedback mechanism which generates circadian rhythms. Phosphorylation of PER3 by CSNK1D/CSNK1E (Q9DC28/Q9JMK2) effects stability and nuclear localisation of the complex. Phosphorylation of CRY2 Ser-71 stimulates the direct binding of FBXL3 (Q8C4V4), targeting it for ubiquitin-mediated degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-1266619","identifier":"Q9R194","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R194/entry","name":"Cry2","description":"Cryptochrome-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11455","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9695895","identifier":"O70361","identifierLink":"https://www.uniprot.org/uniprotkb/O70361/entry","name":"Per3","description":"Period circadian protein homolog 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11269","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3220","complexName":"CRY2-PER2 complex","organismName":"Homo sapiens; 9606","description":"Gradually accumulates in the nucleus to negatively regulate CLOCK-BMAL (CPX-3229, CPX-3230) -dependent transactivation of genes in a delayed negative feedback mechanism which generates circadian rhythms. Phosphorylation of PER2 by CSNK1D/CSNK1E (P48730/P49674) effects stability and nuclear localisation of the complex. Phosphorylation of CRY2 Ser-71 stimulates the direct binding of FBXL3 (Q9UKT7), targeting it for ubiquitin-mediated degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-1054296","identifier":"O15055","identifierLink":"https://www.uniprot.org/uniprotkb/O15055/entry","name":"PER2","description":"Period circadian protein homolog 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11269","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2212355","identifier":"Q49AN0","identifierLink":"https://www.uniprot.org/uniprotkb/Q49AN0/entry","name":"CRY2","description":"Cryptochrome-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11455","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3221","complexName":"Cry2-Per1 complex","organismName":"Homo sapiens; 9606","description":"Gradually accumulates in the nucleus to negatively regulate CLOCK-BMAL (CPX-3229, CPX-3230) -dependent transactivation of genes in a delayed negative feedback mechanism which generates circadian rhythms. Phosphorylation of PER1 by CSNK1D/CSNK1E (P48730/P49674) effects stability and nuclear localisation of the complex. Phosphorylation of CRY2 Ser-71 stimulates the direct binding of FBXL3 (Q9UKT7), targeting it for ubiquitin-mediated degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-2212355","identifier":"Q49AN0","identifierLink":"https://www.uniprot.org/uniprotkb/Q49AN0/entry","name":"CRY2","description":"Cryptochrome-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11455","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2557276","identifier":"O15534","identifierLink":"https://www.uniprot.org/uniprotkb/O15534/entry","name":"PER1","description":"Period circadian protein homolog 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11269","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3222","complexName":"Cry1-Per1 complex","organismName":"Homo sapiens; 9606","description":"Gradually accumulates in the nucleus to negatively regulate CLOCK-BMAL (CPX-3229, CPX-3230) -dependent transactivation of genes in a delayed negative feedback mechanism which generates circadian rhythms. Phosphorylation of PER1 by CSNK1D/CSNK1E (P48730/P49674) effects stability and nuclear localisation of the complex. Phosphorylation of CRY1 Ser-71 stimulates the direct binding of FBXL3 (Q9UKT7), targeting it for ubiquitin-mediated degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-2557276","identifier":"O15534","identifierLink":"https://www.uniprot.org/uniprotkb/O15534/entry","name":"PER1","description":"Period circadian protein homolog 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11269","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-741297","identifier":"Q16526","identifierLink":"https://www.uniprot.org/uniprotkb/Q16526/entry","name":"CRY1","description":"Cryptochrome-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11455","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3223","complexName":"Cry1-Per3 complex","organismName":"Homo sapiens; 9606","description":"Gradually accumulates in the nucleus to negatively regulate CLOCK-BMAL (CPX-3229, CPX-3230) -dependent transactivation of genes in a delayed negative feedback mechanism which generates circadian rhythms. Phosphorylation of PER3 by CSNK1D/CSNK1E (P48730/P49674) effects stability and nuclear localisation of the complex. Phosphorylation of CRY1 Ser-71 stimulates the direct binding of FBXL3 (Q9UKT7), targeting it for ubiquitin-mediated degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-2827813","identifier":"P56645","identifierLink":"https://www.uniprot.org/uniprotkb/P56645/entry","name":"PER3","description":"Period circadian protein homolog 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11269","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-741297","identifier":"Q16526","identifierLink":"https://www.uniprot.org/uniprotkb/Q16526/entry","name":"CRY1","description":"Cryptochrome-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11455","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3224","complexName":"Cry2-Per3 complex","organismName":"Homo sapiens; 9606","description":"Gradually accumulates in the nucleus to negatively regulate CLOCK-BMAL (CPX-3229, CPX-3230) -dependent transactivation of genes in a delayed negative feedback mechanism which generates circadian rhythms. Phosphorylation of PER3 by CSNK1D/CSNK1E (P48730/P49674) effects stability and nuclear localisation of the complex. Phosphorylation of CRY2 Ser-71 stimulates the direct binding of FBXL3 (Q9UKT7), targeting it for ubiquitin-mediated degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-2212355","identifier":"Q49AN0","identifierLink":"https://www.uniprot.org/uniprotkb/Q49AN0/entry","name":"CRY2","description":"Cryptochrome-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11455","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2827813","identifier":"P56645","identifierLink":"https://www.uniprot.org/uniprotkb/P56645/entry","name":"PER3","description":"Period circadian protein homolog 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11269","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3212","complexName":"Mitotic checkpoint complex, MAD1-MAD2-BUB1-BUB3 subcomplex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"This complex forms during mitosis, as a result of the activation of the spindle checkpoint. BUB3 and BUB1 are associated through the cell cycle, however, the addition of MAD1 is cell cycle dependent. The formation of a stable complex requires the functions of MAD2, BUB3, and MPS1. In addition, a highly conserved Arg-Leu-Lys motif at 653-655 of MAD1 is required for the formation of a complete complex.","predictedComplex":false,"interactors":[{"ac":"EBI-10354","identifier":"P40957","identifierLink":"https://www.uniprot.org/uniprotkb/P40957/entry","name":"MAD1","description":"Spindle assembly checkpoint component MAD1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23168","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10362","identifier":"P40958","identifierLink":"https://www.uniprot.org/uniprotkb/P40958/entry","name":"MAD2","description":"Mitotic spindle checkpoint component MAD2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3816","identifier":"P41695","identifierLink":"https://www.uniprot.org/uniprotkb/P41695/entry","name":"BUB1","description":"Spindle assembly checkpoint serine/threonine-protein kinase BUB1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14030","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3830","identifier":"P26449","identifierLink":"https://www.uniprot.org/uniprotkb/P26449/entry","name":"BUB3","description":"Spindle assembly checkpoint protein BUB3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3213","complexName":"Rhino-Deadlock-Cutoff complex","organismName":"Drosophila melanogaster; 7227","description":"Binds to dual-strand-cluster chromatin, probably via the H3K9me3-binding activity of Rhi, and licenses transcription of dual-strand PIWI interacting RNA (piRNA) source loci. piRNAs are a germline-specific class of small noncoding RNAs that protect the genome of animal germ cells from the action of transposable elements by silencing these via Piwi-piRNA complex formation. Rhi binding brings the putative termination cofactor Cuff in close proximity to the nascent piRNA precursor transcript which it appears to protect from degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-149916","identifier":"Q7JXA8","identifierLink":"https://www.uniprot.org/uniprotkb/Q7JXA8/entry","name":"rhi","description":"Chromo domain-containing protein rhino","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22812","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-151790","identifier":"Q9VIF5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VIF5/entry","name":"del","description":"Protein deadlock","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-185996","identifier":"Q9V629","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V629/entry","name":"cuff","description":"Protein cutoff","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12395","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3215","complexName":"FACT complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A heterodimeric H2A-H2B histone chaperone, that helps reorganize nucleosomes in an ATP independent fashion. It promotes histone removal, deposition and replacement on chromatin. Due to its role in chromatin dynamics, it has a role in many cellular processes related to chromatin: DNA replication, DNA damage and repair, transcription initiation and elongation. The redundant  NHP6A/B proteins(P11632/P11633) are involved in FACT function and supply the DNA binding activity, potentially destabilizing nucleosomes to promote formation of alternative chromatin structures in addition to recruiting FACT.","predictedComplex":false,"interactors":[{"ac":"EBI-27863","identifier":"Q04636","identifierLink":"https://www.uniprot.org/uniprotkb/Q04636/entry","name":"POB3","description":"FACT complex subunit POB3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45849","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4334","identifier":"P32558","identifierLink":"https://www.uniprot.org/uniprotkb/P32558/entry","name":"SPT16","description":"FACT complex subunit SPT16","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13980","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3226","complexName":"Core mediator complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Plays an essential role in gene expression regulation by acting as a bridge between DNA-binding transcription factors and the RNA polymerase II (RNAPII) transcription machinery, serving as a central scaffold within the pre-initiation complex. The Mediator complex is also targeted by sequence-specific, DNA-binding transcription factors and appears to regulate RNAPII at both the initiation and elongation stages of transcription. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and unfolds to an extended conformation and partially surrounds RNAPII specifically interacting with the unphosphorylated form of its C-terminal domain. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.\r\n\r\nReversibly associates with the CKM complex (CPX-1853). Mediator lacking the CKM complex has a stimulatory effect on basal transcription. In contrast, Mediator containing the sub-complex represses basal transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-10667","identifier":"P38782","identifierLink":"https://www.uniprot.org/uniprotkb/P38782/entry","name":"MED6","description":"Mediator of RNA polymerase II transcription subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13104","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10674","identifier":"Q08278","identifierLink":"https://www.uniprot.org/uniprotkb/Q08278/entry","name":"MED7","description":"Mediator of RNA polymerase II transcription subunit 7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21428","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12407","identifier":"P53114","identifierLink":"https://www.uniprot.org/uniprotkb/P53114/entry","name":"NUT1","description":"Mediator of RNA polymerase II transcription subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR35784","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12414","identifier":"Q06213","identifierLink":"https://www.uniprot.org/uniprotkb/Q06213/entry","name":"NUT2","description":"Mediator of RNA polymerase II transcription subunit 10","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13345","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13268","identifier":"P40356","identifierLink":"https://www.uniprot.org/uniprotkb/P40356/entry","name":"PGD1","description":"Mediator of RNA polymerase II transcription subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-15087","identifier":"P19263","identifierLink":"https://www.uniprot.org/uniprotkb/P19263/entry","name":"RGR1","description":"Mediator of RNA polymerase II transcription subunit 14","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12809","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15722","identifier":"P25046","identifierLink":"https://www.uniprot.org/uniprotkb/P25046/entry","name":"ROX3","description":"Mediator of RNA polymerase II transcription subunit 19","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28270","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17172","identifier":"P32259","identifierLink":"https://www.uniprot.org/uniprotkb/P32259/entry","name":"SIN4","description":"Mediator of RNA polymerase II transcription subunit 16","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13224","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17658","identifier":"P38633","identifierLink":"https://www.uniprot.org/uniprotkb/P38633/entry","name":"SOH1","description":"Mediator of RNA polymerase II transcription subunit 31","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13186","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18018","identifier":"P34162","identifierLink":"https://www.uniprot.org/uniprotkb/P34162/entry","name":"SRB2","description":"Mediator of RNA polymerase II transcription subunit 20","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12465","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18025","identifier":"P32569","identifierLink":"https://www.uniprot.org/uniprotkb/P32569/entry","name":"SRB4","description":"Mediator of RNA polymerase II transcription subunit 17","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13114","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18032","identifier":"P32585","identifierLink":"https://www.uniprot.org/uniprotkb/P32585/entry","name":"SRB5","description":"Mediator of RNA polymerase II transcription subunit 18","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18039","identifier":"P32570","identifierLink":"https://www.uniprot.org/uniprotkb/P32570/entry","name":"SRB6","description":"Mediator of RNA polymerase II transcription subunit 22","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-18046","identifier":"P47822","identifierLink":"https://www.uniprot.org/uniprotkb/P47822/entry","name":"SRB7","description":"Mediator of RNA polymerase II transcription subunit 21","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13381","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20932","identifier":"P38304","identifierLink":"https://www.uniprot.org/uniprotkb/P38304/entry","name":"MED8","description":"Mediator of RNA polymerase II transcription subunit 8","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13074","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27213","identifier":"Q99278","identifierLink":"https://www.uniprot.org/uniprotkb/Q99278/entry","name":"MED11","description":"Mediator of RNA polymerase II transcription subunit 11","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31503","identifier":"Q12343","identifierLink":"https://www.uniprot.org/uniprotkb/Q12343/entry","name":"MED4","description":"Mediator of RNA polymerase II transcription subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13208","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32854","identifier":"Q12321","identifierLink":"https://www.uniprot.org/uniprotkb/Q12321/entry","name":"MED1","description":"Mediator of RNA polymerase II transcription subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-37542","identifier":"Q12124","identifierLink":"https://www.uniprot.org/uniprotkb/Q12124/entry","name":"MED2","description":"Mediator of RNA polymerase II transcription subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-5174","identifier":"P33308","identifierLink":"https://www.uniprot.org/uniprotkb/P33308/entry","name":"CSE2","description":"Mediator of RNA polymerase II transcription subunit 9","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-7305","identifier":"P19659","identifierLink":"https://www.uniprot.org/uniprotkb/P19659/entry","name":"GAL11","description":"Mediator of RNA polymerase II transcription subunit 15","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23202","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3227","complexName":"Core mediator complex","organismName":"Homo sapiens; 9606","description":"Plays an essential role in gene expression regulation by acting as a bridge between DNA-binding transcription factors and the RNA polymerase II (RNAPII) transcription machinery, serving as a central scaffold within the pre-initiation complex. The Mediator complex is also targeted by sequence-specific, DNA-binding transcription factors and appears to regulate RNAPII at both the initiation and elongation stages of transcription. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and unfolds to an extended conformation and partially surrounds RNAPII specifically interacting with the unphosphorylated form of its C-terminal domain. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.\r\n\r\nReversibly associates with the CKM complex (CPX-3232, CPX-3263). Mediator lacking the CKM complex has a stimulatory effect on basal transcription. In contrast, Mediator containing the sub-complex represses basal transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-311161","identifier":"Q9ULK4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ULK4/entry","name":"MED23","description":"Mediator of RNA polymerase II transcription subunit 23","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394354","identifier":"Q9BTT4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BTT4/entry","name":"MED10","description":"Mediator of RNA polymerase II transcription subunit 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13345","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394392","identifier":"O95402","identifierLink":"https://www.uniprot.org/uniprotkb/O95402/entry","name":"MED26","description":"Mediator of RNA polymerase II transcription subunit 26","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15201","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394405","identifier":"Q96G25","identifierLink":"https://www.uniprot.org/uniprotkb/Q96G25/entry","name":"MED8","description":"Mediator of RNA polymerase II transcription subunit 8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13074","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394430","identifier":"A0JLT2","identifierLink":"https://www.uniprot.org/uniprotkb/A0JLT2/entry","name":"MED19","description":"Mediator of RNA polymerase II transcription subunit 19","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22536","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394459","identifier":"Q15648","identifierLink":"https://www.uniprot.org/uniprotkb/Q15648/entry","name":"MED1","description":"Mediator of RNA polymerase II transcription subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12881","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394489","identifier":"O60244","identifierLink":"https://www.uniprot.org/uniprotkb/O60244/entry","name":"MED14","description":"Mediator of RNA polymerase II transcription subunit 14","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12809","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394506","identifier":"Q96RN5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96RN5/entry","name":"MED15","description":"Mediator of RNA polymerase II transcription subunit 15","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31804","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394523","identifier":"O75448","identifierLink":"https://www.uniprot.org/uniprotkb/O75448/entry","name":"MED24","description":"Mediator of RNA polymerase II transcription subunit 24","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12898","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394541","identifier":"Q9Y2X0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2X0/entry","name":"MED16","description":"Mediator of RNA polymerase II transcription subunit 16","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13224","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394558","identifier":"Q71SY5","identifierLink":"https://www.uniprot.org/uniprotkb/Q71SY5/entry","name":"MED25","description":"Mediator of RNA polymerase II transcription subunit 25","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12433","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394562","identifier":"Q9NVC6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NVC6/entry","name":"MED17","description":"Mediator of RNA polymerase II transcription subunit 17","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13114","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394603","identifier":"Q6P2C8","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P2C8/entry","name":"MED27","description":"Mediator of RNA polymerase II transcription subunit 27","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13130","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394607","identifier":"Q9NPJ6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPJ6/entry","name":"MED4","description":"Mediator of RNA polymerase II transcription subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13208","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394624","identifier":"O75586","identifierLink":"https://www.uniprot.org/uniprotkb/O75586/entry","name":"MED6","description":"Mediator of RNA polymerase II transcription subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13104","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394632","identifier":"O43513","identifierLink":"https://www.uniprot.org/uniprotkb/O43513/entry","name":"MED7","description":"Mediator of RNA polymerase II transcription subunit 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15498","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394640","identifier":"Q9BUE0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BUE0/entry","name":"MED18","description":"Mediator of RNA polymerase II transcription subunit 18","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394644","identifier":"Q9H944","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H944/entry","name":"MED20","description":"Mediator of RNA polymerase II transcription subunit 20","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12465","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394653","identifier":"Q9NWA0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NWA0/entry","name":"MED9","description":"Mediator of RNA polymerase II transcription subunit 9","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394656","identifier":"Q9NX70","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NX70/entry","name":"MED29","description":"Mediator of RNA polymerase II transcription subunit 29","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28314","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394659","identifier":"Q96HR3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96HR3/entry","name":"MED30","description":"Mediator of RNA polymerase II transcription subunit 30","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31705","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394678","identifier":"Q13503","identifierLink":"https://www.uniprot.org/uniprotkb/Q13503/entry","name":"MED21","description":"Mediator of RNA polymerase II transcription subunit 21","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13381","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394687","identifier":"Q15528","identifierLink":"https://www.uniprot.org/uniprotkb/Q15528/entry","name":"MED22","description":"Mediator of RNA polymerase II transcription subunit 22","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12434","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394704","identifier":"Q9P086","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P086/entry","name":"MED11","description":"Mediator of RNA polymerase II transcription subunit 11","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394707","identifier":"Q9Y3C7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3C7/entry","name":"MED31","description":"Mediator of RNA polymerase II transcription subunit 31","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13186","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-514199","identifier":"Q9H204","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H204/entry","name":"MED28","description":"Mediator of RNA polymerase II transcription subunit 28","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13512","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3264","complexName":"Core mediator complex","organismName":"Mus musculus; 10090","description":"Plays an essential role in gene expression regulation by acting as a bridge between DNA-binding transcription factors and the RNA polymerase II (RNAPII) transcription machinery, serving as a central scaffold within the pre-initiation complex. The Mediator complex is also targeted by sequence-specific, DNA-binding transcription factors and appears to regulate RNAPII at both the initiation and elongation stages of transcription. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and unfolds to an extended conformation and partially surrounds RNAPII specifically interacting with the unphosphorylated form of its C-terminal domain. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.\r\n\r\nReversibly associates with the CKM complex (CPX-3266/\r\nCPX-3267). Mediator lacking the CKM complex has a stimulatory effect on basal transcription. In contrast, Mediator containing the sub-complex represses basal transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-309215","identifier":"Q920D3","identifierLink":"https://www.uniprot.org/uniprotkb/Q920D3/entry","name":"Med28","description":"Mediator of RNA polymerase II transcription subunit 28","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13512","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-309220","identifier":"Q9CQI9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQI9/entry","name":"Med30","description":"Mediator of RNA polymerase II transcription subunit 30","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR31705","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-309355","identifier":"Q9CXU1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CXU1/entry","name":"Med31","description":"Mediator of RNA polymerase II transcription subunit 31","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13186","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-310097","identifier":"Q7TN02","identifierLink":"https://www.uniprot.org/uniprotkb/Q7TN02/entry","name":"Med26","description":"Mediator of RNA polymerase II transcription subunit 26","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15201","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398698","identifier":"Q9R0X0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R0X0/entry","name":"Med20","description":"Mediator of RNA polymerase II transcription subunit 20","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12465","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398761","identifier":"Q8C1S0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C1S0/entry","name":"Med19","description":"Mediator of RNA polymerase II transcription subunit 19","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22536","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5744924","identifier":"A2ABV5","identifierLink":"https://www.uniprot.org/uniprotkb/A2ABV5/entry","name":"Med14","description":"Mediator of RNA polymerase II transcription subunit 14","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12809","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5744951","identifier":"Q8VCD5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VCD5/entry","name":"Med17","description":"Mediator of RNA polymerase II transcription subunit 17","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13114","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5745001","identifier":"Q80YQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q80YQ2/entry","name":"Med23","description":"Mediator of RNA polymerase II transcription subunit 23","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5745029","identifier":"Q99K74","identifierLink":"https://www.uniprot.org/uniprotkb/Q99K74/entry","name":"Med24","description":"Mediator of RNA polymerase II transcription subunit 24","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12898","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5745083","identifier":"Q925J9","identifierLink":"https://www.uniprot.org/uniprotkb/Q925J9/entry","name":"Med1","description":"Mediator of RNA polymerase II transcription subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12881","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5745175","identifier":"Q8VCB2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VCB2/entry","name":"Med25","description":"Mediator of RNA polymerase II transcription subunit 25","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12433","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5745248","identifier":"Q9DB40","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DB40/entry","name":"Med27","description":"Mediator of RNA polymerase II transcription subunit 27","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13130","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5745319","identifier":"Q9CZB6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CZB6/entry","name":"Med7","description":"Mediator of RNA polymerase II transcription subunit 7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15498","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5745356","identifier":"Q9DB91","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DB91/entry","name":"Med29","description":"Mediator of RNA polymerase II transcription subunit 29","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR28314","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5745371","identifier":"Q9CZ82","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CZ82/entry","name":"Med18","description":"Mediator of RNA polymerase II transcription subunit 18","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5745383","identifier":"Q921D4","identifierLink":"https://www.uniprot.org/uniprotkb/Q921D4/entry","name":"Med6","description":"Mediator of RNA polymerase II transcription subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13104","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5745428","identifier":"Q9CQA5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQA5/entry","name":"Med4","description":"Mediator of RNA polymerase II transcription subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13208","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6260816","identifier":"Q6PGF3","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PGF3/entry","name":"Med16","description":"Mediator of RNA polymerase II transcription subunit 16","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13224","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6260880","identifier":"Q9CXU0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CXU0/entry","name":"Med10","description":"Mediator of RNA polymerase II transcription subunit 10","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13345","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6260909","identifier":"Q9D8C6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D8C6/entry","name":"Med11","description":"Mediator of RNA polymerase II transcription subunit 11","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6260935","identifier":"Q924H2","identifierLink":"https://www.uniprot.org/uniprotkb/Q924H2/entry","name":"Med15","description":"Mediator of RNA polymerase II transcription subunit 15","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR31804","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6260960","identifier":"Q9CQ39","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQ39/entry","name":"Med21","description":"Mediator of RNA polymerase II transcription subunit 21","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13381","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-641886","identifier":"Q62276","identifierLink":"https://www.uniprot.org/uniprotkb/Q62276/entry","name":"Med22","description":"Mediator of RNA polymerase II transcription subunit 22","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12434","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7990252","identifier":"Q9D7W5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D7W5/entry","name":"Med8","description":"Mediator of RNA polymerase II transcription subunit 8","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13074","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8400359","identifier":"Q8VCS6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VCS6/entry","name":"Med9","description":"Mediator of RNA polymerase II transcription subunit 9","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR20844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3225","complexName":"CLOCK-BMAL1 transcription complex","organismName":"Mus musculus; 10090","description":"Transcription factor complex which interacts with E-box regulatory elements in target genes, including Period (Per1, Per2, Per3) and Cryptochrome (Cry1, Cry2), to activate their transcription during the daytime. The CRY-PER complexes (CPX-3209, CPX-3210, CPX-3214, CPX-3216, CPX-3217, CPX-3218) then inhibit Clock-Bmal1-driven transcription in a negative feedback loop to generate circadian rhythms.","predictedComplex":false,"interactors":[{"ac":"EBI-644534","identifier":"Q9WTL8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WTL8/entry","name":"Bmal1","description":"Basic helix-loop-helix ARNT-like protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23042","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-79859","identifier":"O08785","identifierLink":"https://www.uniprot.org/uniprotkb/O08785/entry","name":"Clock","description":"Circadian locomoter output cycles protein kaput","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46055","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3228","complexName":"CLOCK-BMAL2 transcription complex","organismName":"Mus musculus; 10090","description":"Transcription factor complex which interacts with E-box regulatory elements in target genes, including Period (Per1, Per2, Per3) and Cryptochrome (Cry1, Cry2), to activate their transcription during the daytime. The Cry-Per-complexes (CPX-3209, CPX-3210, CPX-3214, CPX-3216, CPX-3217, CPX-3218) then inhibit Clock-Bmal2-driven transcription in a negative feedback loop to generate circadian rhythms.","predictedComplex":false,"interactors":[{"ac":"EBI-79859","identifier":"O08785","identifierLink":"https://www.uniprot.org/uniprotkb/O08785/entry","name":"Clock","description":"Circadian locomoter output cycles protein kaput","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46055","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9696862","identifier":"Q2VPD4","identifierLink":"https://www.uniprot.org/uniprotkb/Q2VPD4/entry","name":"Bmal2","description":"Basic helix-loop-helix ARNT-like protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23042","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3229","complexName":"CLOCK-BMAL1 transcription complex","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which interacts with E-box regulatory elements in target genes, including Period (Per1, Per2, Per3) and Cryptochrome (Cry1, Cry2), to activate their transcription during the daytime. The CRY-PER complexes (CPX-3219, CPX-3220, CPX-3221, CPX-3222, CPX-3223, CPX-3224) then inhibit CLOCK-BMAL1-driven transcription in a negative feedback loop to generate circadian rhythms.","predictedComplex":false,"interactors":[{"ac":"EBI-1794206","identifier":"O00327","identifierLink":"https://www.uniprot.org/uniprotkb/O00327/entry","name":"BMAL1","description":"Basic helix-loop-helix ARNT-like protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23042","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1794265","identifier":"O15516","identifierLink":"https://www.uniprot.org/uniprotkb/O15516/entry","name":"CLOCK","description":"Circadian locomoter output cycles protein kaput","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46055","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3230","complexName":"CLOCK-BMAL2 transcription complex","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which interacts with E-box regulatory elements in target genes, including Period (Per1, Per2, Per3) and Cryptochrome (Cry1, Cry2), to activate their transcription during the daytime. The CRY-PER complexes (CPX-3219, CPX-3220, CPX-3221, CPX-3222, CPX-3223, CPX-3224) then inhibit CLOCK-BMAL2-driven transcription in a negative feedback loop to generate circadian rhythms.","predictedComplex":false,"interactors":[{"ac":"EBI-1793513","identifier":"Q8WYA1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WYA1/entry","name":"BMAL2","description":"Basic helix-loop-helix ARNT-like protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23042","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1794265","identifier":"O15516","identifierLink":"https://www.uniprot.org/uniprotkb/O15516/entry","name":"CLOCK","description":"Circadian locomoter output cycles protein kaput","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46055","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3231","complexName":"SEA complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Vacuole associated growth regulator that acts as a GTPase-activating protein (GAP) for GTR1 (Q00582), a Rag GTPase that relays nutrient status to the Target of Rapamycin Complex 1 (CPX-1715, CPX-1716)  One end of the SEA complex is made of the IML1/NPR2/NPR3 trimer (SEACIT), involved in inhibition of TORC1 signaling, while the other end, composed of RTC1/MTC5/SEA4/SEH1/SecEC13 (SEACAT), is involved in the activation of TORC1 signaling by acting as a scaffold for the binding of TORC1 regulators. The complex thus regulates TORC1 signaling and is involved in maintaining vacuolar integrity, regulating autophagy in response to nitrogen starvation.  A putative GEF activity was suggested for NPR2 and NPR3.","predictedComplex":false,"interactors":[{"ac":"EBI-12212","identifier":"P39923","identifierLink":"https://www.uniprot.org/uniprotkb/P39923/entry","name":"NPR2","description":"Nitrogen permease regulator 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12991","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16529","identifier":"Q04491","identifierLink":"https://www.uniprot.org/uniprotkb/Q04491/entry","name":"SEC13","description":"Protein transport protein SEC13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11024","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16940","identifier":"P53011","identifierLink":"https://www.uniprot.org/uniprotkb/P53011/entry","name":"SEH1","description":"Nucleoporin SEH1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11024","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2047093","identifier":"Q08281","identifierLink":"https://www.uniprot.org/uniprotkb/Q08281/entry","name":"RTC1","description":"Restriction of telomere capping protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46200","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21365","identifier":"P38164","identifierLink":"https://www.uniprot.org/uniprotkb/P38164/entry","name":"SEA4","description":"SEH-associated protein 4","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR16453","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-24336","identifier":"P38742","identifierLink":"https://www.uniprot.org/uniprotkb/P38742/entry","name":"NPR3","description":"Nitrogen permease regulator 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13153","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25710","identifier":"P47170","identifierLink":"https://www.uniprot.org/uniprotkb/P47170/entry","name":"IML1","description":"Vacuolar membrane-associated protein IML1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13179","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32422","identifier":"Q03897","identifierLink":"https://www.uniprot.org/uniprotkb/Q03897/entry","name":"MTC5","description":"Maintenance of telomere capping protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46170","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3234","complexName":"SCF-Cdc4 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SCF-Cdc4 is a member of the SCF (Skp1-Cullin-F-box) E3 ubiquitin ligase family, in which the F-box protein, Cdc4, forms the substrate recognition subunit. It is required for both G1/S and G2/M cell cycle transitions, when it ubiquitinates and targets to degradation its substrates such as SIC1, FAR1, CLN1/2 and CLB6. The active complex may be a homodimer.","predictedComplex":false,"interactors":[{"ac":"EBI-19730","identifier":"P14682","identifierLink":"https://www.uniprot.org/uniprotkb/P14682/entry","name":"CDC34","description":"Ubiquitin-conjugating enzyme E2-34 kDa","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31686","identifier":"Q08273","identifierLink":"https://www.uniprot.org/uniprotkb/Q08273/entry","name":"HRT1","description":"RING-box protein HRT1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4090","identifier":"P52286","identifierLink":"https://www.uniprot.org/uniprotkb/P52286/entry","name":"SKP1","description":"Suppressor of kinetochore protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4321","identifier":"Q12018","identifierLink":"https://www.uniprot.org/uniprotkb/Q12018/entry","name":"CDC53","description":"Cell division control protein 53","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4434","identifier":"P07834","identifierLink":"https://www.uniprot.org/uniprotkb/P07834/entry","name":"CDC4","description":"Cell division control protein 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19854","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3241","complexName":"SCF-Grr1 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SCF-Grr1 is a member of the SCF (Skp1-Cullin-F-box) E3 ubiquitin ligase family, in which the F-box protein, Grr1, forms the substrate recognition subunit. It is required for the G1/S cell cycle transition, when it ubiquitinates and targets proteins such as CLN1/2 and GIC2 for degradation. It is a central component in glucose-induced signal transduction, regulating the induction of the glucose transporter Hxt1 via degradation of Mth1 when glucose is abundant. Grr1 is also responsible for the ubiquitination and degradation of several metabolic enzymes and proteins involved in glycolysis and amino-acid biosynthesis.The active complex may be a homodimer.","predictedComplex":false,"interactors":[{"ac":"EBI-19730","identifier":"P14682","identifierLink":"https://www.uniprot.org/uniprotkb/P14682/entry","name":"CDC34","description":"Ubiquitin-conjugating enzyme E2-34 kDa","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31686","identifier":"Q08273","identifierLink":"https://www.uniprot.org/uniprotkb/Q08273/entry","name":"HRT1","description":"RING-box protein HRT1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4090","identifier":"P52286","identifierLink":"https://www.uniprot.org/uniprotkb/P52286/entry","name":"SKP1","description":"Suppressor of kinetochore protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4321","identifier":"Q12018","identifierLink":"https://www.uniprot.org/uniprotkb/Q12018/entry","name":"CDC53","description":"Cell division control protein 53","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7898","identifier":"P24814","identifierLink":"https://www.uniprot.org/uniprotkb/P24814/entry","name":"GRR1","description":"SCF E3 ubiquitin ligase complex F-box protein GRR1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13382","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3242","complexName":"SCF-Mdm30 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SCF-Mdm30 is a member of the SCF (Skp1-Cullin-F-box) E3 ubiquitin ligase family, in which the F-box protein, Mdm30, forms the substrate recognition subunit. The complex is required for the degradation of Fzo1 and Gal80, and is thereby involved in mitochondrial fusion and regulation of galactose metabolism. The active complex may be a homodimer.","predictedComplex":false,"interactors":[{"ac":"EBI-19730","identifier":"P14682","identifierLink":"https://www.uniprot.org/uniprotkb/P14682/entry","name":"CDC34","description":"Ubiquitin-conjugating enzyme E2-34 kDa","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31686","identifier":"Q08273","identifierLink":"https://www.uniprot.org/uniprotkb/Q08273/entry","name":"HRT1","description":"RING-box protein HRT1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31799","identifier":"Q05930","identifierLink":"https://www.uniprot.org/uniprotkb/Q05930/entry","name":"MDM30","description":"Mitochondrial distribution and morphology protein 30","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-4090","identifier":"P52286","identifierLink":"https://www.uniprot.org/uniprotkb/P52286/entry","name":"SKP1","description":"Suppressor of kinetochore protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4321","identifier":"Q12018","identifierLink":"https://www.uniprot.org/uniprotkb/Q12018/entry","name":"CDC53","description":"Cell division control protein 53","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3243","complexName":"SCF-Ufo1 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SCF-Ufo1 is a member of the SCF (Skp1-Cullin-F-box) E3 ubiquitin ligase family, in which the F-box protein, Ufo1, forms the substrate recognition subunit. The complex is required for the degradation of HO and Gal80, thereby involved in mating type switching and regulation of galactose metabolism. The complex may form a homodimer.","predictedComplex":false,"interactors":[{"ac":"EBI-19730","identifier":"P14682","identifierLink":"https://www.uniprot.org/uniprotkb/P14682/entry","name":"CDC34","description":"Ubiquitin-conjugating enzyme E2-34 kDa","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20020","identifier":"Q04511","identifierLink":"https://www.uniprot.org/uniprotkb/Q04511/entry","name":"UFO1","description":"Ubiquitin ligase complex F-box protein UFO1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14381","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31686","identifier":"Q08273","identifierLink":"https://www.uniprot.org/uniprotkb/Q08273/entry","name":"HRT1","description":"RING-box protein HRT1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4090","identifier":"P52286","identifierLink":"https://www.uniprot.org/uniprotkb/P52286/entry","name":"SKP1","description":"Suppressor of kinetochore protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4321","identifier":"Q12018","identifierLink":"https://www.uniprot.org/uniprotkb/Q12018/entry","name":"CDC53","description":"Cell division control protein 53","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3244","complexName":"SCF-Das1 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SCF-Das1 is a member of the SCF (Skp1-Cullin-F-box) E3 ubiquitin ligase family, in which the F-box protein, Das1, forms the substrate recognition subunit. The complex is required for the degradation of MIG2 and Gal80, thereby involved in regulation of galactose metabolism. The complex may form a homodimer.","predictedComplex":false,"interactors":[{"ac":"EBI-19730","identifier":"P14682","identifierLink":"https://www.uniprot.org/uniprotkb/P14682/entry","name":"CDC34","description":"Ubiquitin-conjugating enzyme E2-34 kDa","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26114","identifier":"P47005","identifierLink":"https://www.uniprot.org/uniprotkb/P47005/entry","name":"DAS1","description":"F-box protein DAS1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-31686","identifier":"Q08273","identifierLink":"https://www.uniprot.org/uniprotkb/Q08273/entry","name":"HRT1","description":"RING-box protein HRT1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4090","identifier":"P52286","identifierLink":"https://www.uniprot.org/uniprotkb/P52286/entry","name":"SKP1","description":"Suppressor of kinetochore protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4321","identifier":"Q12018","identifierLink":"https://www.uniprot.org/uniprotkb/Q12018/entry","name":"CDC53","description":"Cell division control protein 53","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3249","complexName":"SCF-MET30 E3 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SCF-Met30 is a member of the SCF (Skp1-Cullin-F-box) E3 ubiquitin ligase family, in which the F-box protein, MET30, forms the substrate recognition subunit. The complex is required for the ubiquitylation of  the transcription factor MET4 (P32389), resulting in its deactivation, and destabilization of the cell cycle inhibitor MET32 (Q12041), thus enabling cell cycle progression. MET4 is the master regulator of genes governing the synthesis of sulfur-containing amino acids, therefore SCF-MET30 coordinates cell cycle progression with biosynthetic pathways of sulfur-containing metabolites, such as methionine, cysteine, and S-adenosylmethionine.  The complex may form a homodimer.","predictedComplex":false,"interactors":[{"ac":"EBI-11507","identifier":"P39014","identifierLink":"https://www.uniprot.org/uniprotkb/P39014/entry","name":"MET30","description":"F-box protein MET30","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19730","identifier":"P14682","identifierLink":"https://www.uniprot.org/uniprotkb/P14682/entry","name":"CDC34","description":"Ubiquitin-conjugating enzyme E2-34 kDa","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31686","identifier":"Q08273","identifierLink":"https://www.uniprot.org/uniprotkb/Q08273/entry","name":"HRT1","description":"RING-box protein HRT1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4090","identifier":"P52286","identifierLink":"https://www.uniprot.org/uniprotkb/P52286/entry","name":"SKP1","description":"Suppressor of kinetochore protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4321","identifier":"Q12018","identifierLink":"https://www.uniprot.org/uniprotkb/Q12018/entry","name":"CDC53","description":"Cell division control protein 53","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3250","complexName":"SCF-Dia2 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SCF-Dia2 is a member of the SCF (Skp1-Cullin-F-box) E3 ubiquitin ligase family, in which the F-box protein, Dia2, forms the substrate recognition subunit. The complex may form a homodimer. SCF-Dia2 is involved in a number of cellular processes: it has been associated with replication stress response and is considered part of the replisome progression complex responsible for fork stability. CSF-Dia2 has also been linked to part of the intra-S phase DNA damage checkpoint. It is also involved in transcriptional silencing at telomeres and mating type loci, as well as regulating transcription by mediating assembly of the RSC complex. It is required for the degradation of Cdc6 in G1.","predictedComplex":false,"interactors":[{"ac":"EBI-19730","identifier":"P14682","identifierLink":"https://www.uniprot.org/uniprotkb/P14682/entry","name":"CDC34","description":"Ubiquitin-conjugating enzyme E2-34 kDa","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31686","identifier":"Q08273","identifierLink":"https://www.uniprot.org/uniprotkb/Q08273/entry","name":"HRT1","description":"RING-box protein HRT1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31943","identifier":"Q08496","identifierLink":"https://www.uniprot.org/uniprotkb/Q08496/entry","name":"DIA2","description":"Protein DIA2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-4090","identifier":"P52286","identifierLink":"https://www.uniprot.org/uniprotkb/P52286/entry","name":"SKP1","description":"Suppressor of kinetochore protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4321","identifier":"Q12018","identifierLink":"https://www.uniprot.org/uniprotkb/Q12018/entry","name":"CDC53","description":"Cell division control protein 53","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3253","complexName":"SCF-Ylr352w ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SCF-Ylr352w  is a member of the SCF (Skp1-Cullin-F-box) E3 ubiquitin ligase family, in which the F-box protein, Lug1, forms the substrate recognition subunit. The cellular role of this complex is unknown.  The complex may form a homodimer.","predictedComplex":false,"interactors":[{"ac":"EBI-19730","identifier":"P14682","identifierLink":"https://www.uniprot.org/uniprotkb/P14682/entry","name":"CDC34","description":"Ubiquitin-conjugating enzyme E2-34 kDa","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31686","identifier":"Q08273","identifierLink":"https://www.uniprot.org/uniprotkb/Q08273/entry","name":"HRT1","description":"RING-box protein HRT1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-35627","identifier":"Q06479","identifierLink":"https://www.uniprot.org/uniprotkb/Q06479/entry","name":"yl352","description":"F-box protein YLR352W","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13318","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4090","identifier":"P52286","identifierLink":"https://www.uniprot.org/uniprotkb/P52286/entry","name":"SKP1","description":"Suppressor of kinetochore protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4321","identifier":"Q12018","identifierLink":"https://www.uniprot.org/uniprotkb/Q12018/entry","name":"CDC53","description":"Cell division control protein 53","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3254","complexName":"SCF-Saf1 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SCF-Saf1 is a member of the SCF (Skp1-Cullin-F-box) E3 ubiquitin ligase family, in which the F-box protein, Saf1, forms the substrate recognition subunit. The complex is required for the ubiquitylation of Aah1 and several vacuolar/lysosomal enzymes.  The complex may form a homodimer.","predictedComplex":false,"interactors":[{"ac":"EBI-19730","identifier":"P14682","identifierLink":"https://www.uniprot.org/uniprotkb/P14682/entry","name":"CDC34","description":"Ubiquitin-conjugating enzyme E2-34 kDa","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21172","identifier":"P38352","identifierLink":"https://www.uniprot.org/uniprotkb/P38352/entry","name":"SAF1","description":"SCF-associated factor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45982","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31686","identifier":"Q08273","identifierLink":"https://www.uniprot.org/uniprotkb/Q08273/entry","name":"HRT1","description":"RING-box protein HRT1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4090","identifier":"P52286","identifierLink":"https://www.uniprot.org/uniprotkb/P52286/entry","name":"SKP1","description":"Suppressor of kinetochore protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4321","identifier":"Q12018","identifierLink":"https://www.uniprot.org/uniprotkb/Q12018/entry","name":"CDC53","description":"Cell division control protein 53","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3255","complexName":"SCF-Hrt3 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SCF-Hrt3 is a member of the SCF (Skp1-Cullin-F-box) E3 ubiquitin ligase family, in which the F-box protein, Hrt3, forms the substrate recognition subunit. The complex is involved in the cellular response to methylmercury. The complex may form a homodimer.","predictedComplex":false,"interactors":[{"ac":"EBI-19730","identifier":"P14682","identifierLink":"https://www.uniprot.org/uniprotkb/P14682/entry","name":"CDC34","description":"Ubiquitin-conjugating enzyme E2-34 kDa","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30029","identifier":"Q12347","identifierLink":"https://www.uniprot.org/uniprotkb/Q12347/entry","name":"HRT3","description":"F-box protein HRT3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12874","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31686","identifier":"Q08273","identifierLink":"https://www.uniprot.org/uniprotkb/Q08273/entry","name":"HRT1","description":"RING-box protein HRT1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4090","identifier":"P52286","identifierLink":"https://www.uniprot.org/uniprotkb/P52286/entry","name":"SKP1","description":"Suppressor of kinetochore protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4321","identifier":"Q12018","identifierLink":"https://www.uniprot.org/uniprotkb/Q12018/entry","name":"CDC53","description":"Cell division control protein 53","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3238","complexName":"SUMO activating enzyme complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SUMO activating complex provides an E1-like activity that catalyzes the first step in conjugation of Smt3 (SUMO) to proteins (sumoylation). The activated Smt3 is then transferred to the E2-like SUMO conjugating enzyme Ubc9. In subsequent steps, Smt3 is covalently attached to lysine residues on target proteins by one of the E3-like SUMO ligases that include Siz1, Mms21, Cst9, and Nfi1. Attachment of Smt3 alters protein-protein and protein-DNA interactions, as well as subcellular localization of the target proteins, among which are septins, several DNA repair proteins, and cell division regulators, therefore affecting chromosome segregation, cell cycle control, and likely many other regulatory pathways.","predictedComplex":false,"interactors":[{"ac":"EBI-15107","identifier":"Q06624","identifierLink":"https://www.uniprot.org/uniprotkb/Q06624/entry","name":"AOS1","description":"DNA damage tolerance protein RHC31","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19710","identifier":"P52488","identifierLink":"https://www.uniprot.org/uniprotkb/P52488/entry","name":"UBA2","description":"Ubiquitin-activating enzyme E1-like","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3239","complexName":"Kv4.2-KChIP2 channel complex","organismName":"Homo sapiens; 9606","description":"Member of the transient outward (A-type), rapidly inactivating voltage-gated potassium channels, also called the D member of the Shal-related voltage-gated potassium channels. A transmembrane channel specific for potassium and sensitive to voltage changes in the cell's membrane potential, composed of alpha and beta subunits. Alpha subunit (Kv4.2), is a potassium voltage-gated channel subfamily D member 2 protein. Beta subunit is an auxiliary, regulatory subunit, called Kv channel-interacting protein 2 (KChIP2) that modulates channel inactivation kinetics and rate of recovery from inactivation in a calcium-dependent manner. During action potentials, the channel plays a crucial role in returning the depolarized cell to a resting state (repolarisation phase). It contributes to the cardiac transient outward  current I(TO) in the heart and the somatodendritic A-type current  I(SA) in neurons.These currents operate at subthreshold membrane potentials to control the excitability of neurons and cardiac myocytes.","predictedComplex":false,"interactors":[{"ac":"EBI-1052975","identifier":"Q9NS61","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NS61/entry","name":"KCNIP2","description":"A-type potassium channel modulatory protein KCNIP2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23055","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1646745","identifier":"Q9NZV8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZV8/entry","name":"KCND2","description":"A-type voltage-gated potassium channel KCND2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11537","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3261","complexName":"Kv4.2-KChIP2 channel complex","organismName":"Mus musculus; 10090","description":"Member of the transient outward (A-type), rapidly inactivating voltage-gated potassium channels, also called the D member of the Shal-related voltage-gated potassium channels. A transmembrane channel specific for potassium and sensitive to voltage changes in the cell's membrane potential, composed of alpha and beta subunits. Alpha subunit (Kv4.2), is a potassium voltage-gated channel subfamily D member 2 protein. Beta subunit is an auxiliary, regulatory subunit, called Kv channel-interacting protein 2 (KChIP2) that modulates channels inactivation kinetics and rate of recovery from inactivation in a calcium-dependent manner. During action potentials, the channel plays a crucial role in returning the depolarized cell to a resting state (repolarisation phase). It contributes to the cardiac transient outward  current I(TO) in the heart and the somatodendritic A-type current  I(SA) in neurons.These   currents operate at subthreshold membrane potentials to control the excitability of neurons and cardiac myocytes.","predictedComplex":false,"interactors":[{"ac":"EBI-959779","identifier":"Q9Z0V2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0V2/entry","name":"Kcnd2","description":"A-type voltage-gated potassium channel KCND2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11537","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9843825","identifier":"Q9JJ69","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JJ69/entry","name":"Kcnip2","description":"A-type potassium channel modulatory protein KCNIP2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23055","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3248","complexName":"Asi ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"The Asi complex resides in the nuclear inner membrane and ubiquitinates proteins to target them for degradation, as part of the endoplasmic reticulum-associated degradation (ERAD) pathway. It targets two types of substrate: misfolded nuclear inner membrane proteins; and proteins that participate in sterol biosynthesis, including ERG11 (lanosterol 14-alpha-demethylase) and NSG1, a regulator of sterol biosynthesis. The Asi complex has an important role in regulation of the response to extracellular amino acids, by mediating degradation of the transcription factor Stp1.","predictedComplex":false,"interactors":[{"ac":"EBI-27241","identifier":"P54074","identifierLink":"https://www.uniprot.org/uniprotkb/P54074/entry","name":"ASI1","description":"ERAD-associated E3 ubiquitin-protein ligase ASI1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22696","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28603","identifier":"P53983","identifierLink":"https://www.uniprot.org/uniprotkb/P53983/entry","name":"ASI3","description":"Probable ERAD-associated E3 ubiquitin-protein ligase ASI1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22696","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28975","identifier":"P53895","identifierLink":"https://www.uniprot.org/uniprotkb/P53895/entry","name":"ASI2","description":"Protein ASI2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-3256","complexName":"Kv4.3-KChIP1 channel complex","organismName":"Homo sapiens; 9606","description":"Member of the transient outward (A-type), rapidly inactivating voltage-gated potassium channels, also called the D member of the Shal-related voltage-gated potassium channels. A transmembrane channel specific for potassium and sensitive to voltage changes in the cell's membrane potential, composed of alpha and beta subunits. Alpha subunit (Kv4.3), is a potassium voltage-gated channel subfamily D member 3 protein. Beta subunit is an auxiliary, regulatory subunit, called Kv channel-interacting protein 1 (KChIP1) that modulates channels density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent manner. During action potentials, the channel plays a crucial role in returning the depolarized cell to a resting state (repolarisation phase). It contributes to the cardiac transient outward current I(TO) in the heart and the somatodendritic A-type current  I(SA) in neurons.These currents operate at subthreshold membrane potentials to control the excitability of neurons and cardiac myocytes.","predictedComplex":false,"interactors":[{"ac":"EBI-2120635","identifier":"Q9NZI2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZI2/entry","name":"KCNIP1","description":"A-type potassium channel modulatory protein KCNIP1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23055","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9825212","identifier":"Q9UK17","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK17/entry","name":"KCND3","description":"A-type voltage-gated potassium channel KCND3","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11537","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26624","complexName":"Fatty acid synthase complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the synthesis of the 16-carbon saturated fatty acid palmitate from acetyl-Coenzyme A (acetyl-CoA) and malonyl-CoA, in the presence of NADPH. Complex is a key component in de novo lipogenesis (DNL), a process essential in mammals to produce fatty acids for membrane formation, energy storage, cell signalling and protein modifications.","predictedComplex":false,"interactors":[{"ac":"EBI-356658","identifier":"P49327","identifierLink":"https://www.uniprot.org/uniprotkb/P49327/entry","name":"FASN","description":"Fatty acid synthase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43775","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8785164","identifier":"CHEBI:16474","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16474","name":"nadph","description":"NADPH","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26625","complexName":"Adaptor complex AP-1","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Plays a central role in clathrin-coated vesicle formation by coupling coat assembly and cargo collection. Binds short linear motifs on cargo proteins and incorporates them into the clathrin coat of forming vesicles. Mediates the bi-directional transfer of membrane proteins between the trans-Golgi network and the early endosome.","predictedComplex":false,"interactors":[{"ac":"EBI-1542474","identifier":"Q9HFE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HFE5/entry","name":"apm1","description":"AP-1 complex subunit mu-1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67105904","identifier":"Q9UU81","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UU81/entry","name":"apl4","description":"AP-1 complex subunit gamma-1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR22780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67105963","identifier":"O43079","identifierLink":"https://www.uniprot.org/uniprotkb/O43079/entry","name":"apl2","description":"AP-1 complex subunit beta-1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67105989","identifier":"Q9P7N2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P7N2/entry","name":"vas2","description":"AP-1 complex subunit sigma-1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26626","complexName":"Adaptor complex AP-2","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Adaptor complex that orchestrates the formation of membrane coats that mediate cargo selection and vesicle budding, for example by linking clathrin to the membrane surface of trans-Golgi network vesicles. AP-2 is involved in plasma membrane to endosome traffic.","predictedComplex":false,"interactors":[{"ac":"EBI-64040019","identifier":"Q09718","identifierLink":"https://www.uniprot.org/uniprotkb/Q09718/entry","name":"apm4","description":"AP-2 complex subunit mu","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67106014","identifier":"Q9C0W7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9C0W7/entry","name":"apl3","description":"AP-2 complex subunit alpha","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR22780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67106067","identifier":"O43005","identifierLink":"https://www.uniprot.org/uniprotkb/O43005/entry","name":"apl1","description":"AP-2 complex subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67106092","identifier":"Q9Y7L6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y7L6/entry","name":"aps2","description":"AP-2 complex subunit sigma","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26627","complexName":"Adaptor complex AP-3","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Adaptor complex that orchestrates the formation of membrane coats that mediate cargo selection and vesicle budding, for example by linking clathrin to the membrane surface of trans-Golgi network vesicles. AP-3 is associated with endosomes and, to a less extent, the trans-Golgi network and appears to function independently of clathrin. Drosophila AP-3 genes were first linked to defects in the biogenesis of visual pigment granules.","predictedComplex":false,"interactors":[{"ac":"EBI-21242183","identifier":"O13939","identifierLink":"https://www.uniprot.org/uniprotkb/O13939/entry","name":"apl6","description":"AP-3 complex subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67106117","identifier":"Q9UTL8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UTL8/entry","name":"apl5","description":"AP-3 complex subunit delta","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR22781","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67106151","identifier":"O94669","identifierLink":"https://www.uniprot.org/uniprotkb/O94669/entry","name":"apm3","description":"AP-3 complex subunit mu","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67106175","identifier":"Q09905","identifierLink":"https://www.uniprot.org/uniprotkb/Q09905/entry","name":"aps3","description":"AP-3 complex subunit sigma","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26628","complexName":"Fatty acid synthase complex","organismName":"Mus musculus; 10090","description":"Catalyzes the synthesis of the 16-carbon saturated fatty acid palmitate from acetyl-Coenzyme A (acetyl-CoA) and malonyl-CoA, in the presence of NADPH. Complex is a key component in de novo lipogenesis (DNL), a process essential in mammals to produce fatty acids for membrane formation, energy storage, cell signalling and protein modifications.","predictedComplex":false,"interactors":[{"ac":"EBI-773277","identifier":"P19096","identifierLink":"https://www.uniprot.org/uniprotkb/P19096/entry","name":"Fasn","description":"Fatty acid synthase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR43775","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8785164","identifier":"CHEBI:16474","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16474","name":"nadph","description":"NADPH","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26630","complexName":"Fatty acid synthase complex","organismName":"Sus scrofa; 9823","description":"Catalyzes the synthesis of the 16-carbon saturated fatty acid palmitate from acetyl-Coenzyme A (acetyl-CoA) and malonyl-CoA, in the presence of NADPH. Complex is a key component in de novo lipogenesis (DNL), a process essential in mammals to produce fatty acids for membrane formation, energy storage, cell signalling and protein modifications.","predictedComplex":false,"interactors":[{"ac":"EBI-26895143","identifier":"A5YV76","identifierLink":"https://www.uniprot.org/uniprotkb/A5YV76/entry","name":"FASN","description":"Fatty acid synthase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Sus scrofa; 9823","xrefs":[]},{"ac":"EBI-8785164","identifier":"CHEBI:16474","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16474","name":"nadph","description":"NADPH","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26631","complexName":"ESCRT-0 complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"The ESCRT machinery consists of ESCRT-0 (this complex), -I , -II , -III  and -IV (VPS4 complex) and is required for the downregulation of cell-surface receptors and for the final membrane scission step during endocytosis. ESCRT-0 binds PI3P on endosomes and ubiquitinated cargo via VPS27, recruiting clathrin and sequestering ubiquitylated cargo in clathrin-coated microdomains. HSE1 recruits ESCRT-1 and initiates the multivesicular body (MVB) pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-67108120","identifier":"O13821","identifierLink":"https://www.uniprot.org/uniprotkb/O13821/entry","name":"sst4","description":"Vacuolar protein sorting-associated protein 27","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR47794","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67108152","identifier":"O74749","identifierLink":"https://www.uniprot.org/uniprotkb/O74749/entry","name":"hse1","description":"Class E vacuolar protein-sorting machinery protein hse1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR45929","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26632","complexName":"DCPS decapping scavenger complex","organismName":"Homo sapiens; 9606","description":"Decapping complex which catalyzes the degradation of the residual cap structure following 3'->5' mRNA decay, to prevent the premature decapping of the capped long mRNA and misincorporation of methylated nucleotides in nucleic acids, thereby averting accumulation of intermediates that might interfere with RNA processing, export, and translation. Hydrolyzes cap analog structures such as 7-methylguanosine nucleoside triphosphate (m7GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides), releasing m7G monophosphate (m7Gp) and diphosphate terminated oligo mRNA (ppRNA).","predictedComplex":false,"interactors":[{"ac":"EBI-3917181","identifier":"Q96C86","identifierLink":"https://www.uniprot.org/uniprotkb/Q96C86/entry","name":"DCPS","description":"m7GpppX diphosphatase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12978","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26633","complexName":"TAS1R2-TAS1R3 type 1 taste receptor complex","organismName":"Homo sapiens; 9606","description":"A class C G-protein-coupled receptor (GPCR) heterodimer which senses sweet compounds. The receptor is expressed in specialized taste receptor cells in the taste bud and also in tissues involved in the  regulation of energy metabolism such as adipose tissue, endocrine cells of the gut and the beta-islet cells of the pancreas signal through GNAT-3-containing (gustducin) G-protein heterotrimers, initiating downstream physiological responses.","predictedComplex":false,"interactors":[{"ac":"EBI-54560348","identifier":"Q8TE23","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TE23/entry","name":"TAS1R2","description":"Taste receptor type 1 member 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24061","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-54721553","identifier":"Q7RTX0","identifierLink":"https://www.uniprot.org/uniprotkb/Q7RTX0/entry","name":"TAS1R3","description":"Taste receptor type 1 member 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24061","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26634","complexName":"Dcps decapping scavenger complex","organismName":"Mus musculus; 10090","description":"Decapping complex which catalyzes the degradation of the residual cap structure following 3'->5' mRNA decay, to prevent the premature decapping of the capped long mRNA and misincorporation of methylated nucleotides in nucleic acids, thereby averting accumulation of intermediates that might interfere with RNA processing, export, and translation. Hydrolyzes cap analog structures such as 7-methylguanosine nucleoside triphosphate (m7GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides), releasing m7G monophosphate (m7Gp) and diphosphate terminated oligo mRNA (ppRNA).","predictedComplex":false,"interactors":[{"ac":"EBI-8318510","identifier":"Q9DAR7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DAR7/entry","name":"Dcps","description":"m7GpppX diphosphatase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12978","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26635","complexName":"TAS1R1-TAS1R3 type 1 taste receptor complex","organismName":"Homo sapiens; 9606","description":"A class C G-protein-coupled receptor (GPCR) heterodimer which senses umami taste stimulus (the taste of monosodium glutamate). The receptor is expressed in specialized taste receptor cells in the taste bud and signal primarily through the G-alpha subunit of gustducin (GNAT3, GNB1, GNG13), initiating downstream physiological responses","predictedComplex":false,"interactors":[{"ac":"EBI-54721553","identifier":"Q7RTX0","identifierLink":"https://www.uniprot.org/uniprotkb/Q7RTX0/entry","name":"TAS1R3","description":"Taste receptor type 1 member 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24061","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67107683","identifier":"Q7RTX1","identifierLink":"https://www.uniprot.org/uniprotkb/Q7RTX1/entry","name":"TAS1R1","description":"Taste receptor type 1 member 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24061","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26636","complexName":"Mitochondrial glycine dehydrogenase complex","organismName":"Homo sapiens; 9606","description":"Catalyzes glycine degradation. GLDC, the glycine cleavage system protein P binds to the alpha-amino group of glycine through its pyridoxal phosphate cofactor, releases CO2 and transfers the remaining methylamine moiety to the lipoamide cofactor, GCSH (P23434), the glycine cleavage system H protein.\r\n\r\nMutations in GLDC are associated with glycine encephalopathy. Also considered a useful biomarker in the diagnosis of stomach cancer.","predictedComplex":false,"interactors":[{"ac":"EBI-2509907","identifier":"P23378","identifierLink":"https://www.uniprot.org/uniprotkb/P23378/entry","name":"GLDC","description":"Glycine dehydrogenase (decarboxylating), mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11773","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8852014","identifier":"CHEBI:597326","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:597326","name":"pyridoxal 5'-phosphate(2-)","description":"pyridoxal 5'-phosphate(2-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26637","complexName":"Cytoplasmic thioredoxin reductase 1 complex","organismName":"Homo sapiens; 9606","description":"Flavoprotein complex which reduces thioredoxin/TXN (P10599) to its dithiol-containing form. The complex is present in the cytoplasm in various tissues and is involved in the regulation of cellular redox reactions, growth and differentiation. Essential for oxygen radical scavenging to protect cells from radical oxygen species (ROS), and thereby cellular dysfunction. \r\n\r\nBinding to NADPH, results in the transportation of electrons from NADPH via FAD to the disulfide region in the N-terminal active site, and from there onwards to the C-terminal redox center of the adjacent subunit, where substrate reduction occurs.","predictedComplex":false,"interactors":[{"ac":"EBI-716617","identifier":"Q16881","identifierLink":"https://www.uniprot.org/uniprotkb/Q16881/entry","name":"TXNRD1","description":"Thioredoxin reductase 1, cytoplasmic","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26638","complexName":"Mitochondrial thioredoxin reductase 2 complex","organismName":"Homo sapiens; 9606","description":"Flavoprotein complex which reduces thioredoxin/TXN (P10599) to its dithiol-containing form. The complex is present in mitochondria in various tissues and is involved in the regulation of cellular redox reactions, growth and differentiation. Essential for mitochondrial oxygen radical scavenging to protect mitochondria from radical oxygen species (ROS), and thereby cellular dysfunction. \r\n\r\nBinding to NADPH, results in the transportation of electrons from NADPH via FAD to the disulfide region in the N-terminal active site, and from there onwards to the C-terminal redox center of the adjacent subunit, where substrate reduction occurs.","predictedComplex":false,"interactors":[{"ac":"EBI-10763091","identifier":"Q9NNW7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NNW7/entry","name":"TXNRD2","description":"Thioredoxin reductase 2, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26639","complexName":"Spermatid-associated thioredoxin reductase 3 complex","organismName":"Homo sapiens; 9606","description":"Flavoprotein complex which reduces thioredoxin/TXN (P10599) to its dithiol-containing form. The complex is involved in the regulation of cellular redox reactions, growth and differentiation. Essential for maintaining thiol redox homeostasis to protect sperm from radical oxygen species (ROS) which are particularly susceptible during critical phases of sperm development. \r\n\r\nBinding to NADPH, results in the transportation of electrons from NADPH via FAD to the disulfide region in the N-terminal active site, and from there onwards to the C-terminal redox center of the adjacent subunit, where substrate reduction occurs.\r\n\r\nLargely restricted to the testis, TXNRD3 is thought to be involved in the process of sperm maturation.","predictedComplex":false,"interactors":[{"ac":"EBI-18122152","identifier":"Q86VQ6","identifierLink":"https://www.uniprot.org/uniprotkb/Q86VQ6/entry","name":"TXNRD3","description":"Thioredoxin reductase 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26640","complexName":"Signal recognition particle","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"A conserved ribonucleoprotein particle, which includes in its structure a small cytoplasmic RNA (scRNA). In co-translational targeting of membrane and secretory proteins, SRP recognizes signal sequences as soon as they emerge from the ribosomal polypeptide exit tunnel and binds to the ribosome-nascent chain complex (RNC), leading to retardation of peptide elongation. The SRP-RNC complex is targeted to the endoplasmic reticulum (ER) membrane by interaction with the SRP receptor (SR).  After docking to the membrane, the RNC is transferred to the protein-conducting channel, the translocon, and protein synthesis continues. The SRP-SR complex dissociates from the ribosome and, as a result of GTP hydrolysis, SRP and SR dissociate from each other. The genes encoding scR1 and SRP54 are not essential for growth, although SRP-deficient cells grow poorly, suggesting that an alternative, SRP-independent targeting pathway(s) to the ER membrane exists.","predictedComplex":false,"interactors":[{"ac":"EBI-67124216","identifier":"Q9P372","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P372/entry","name":"srp14","description":"Signal recognition particle subunit srp14","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12013","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67124270","identifier":"O13804","identifierLink":"https://www.uniprot.org/uniprotkb/O13804/entry","name":"ye07","description":"Uncharacterized protein C17H9.07","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12834","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67124285","identifier":"O94407","identifierLink":"https://www.uniprot.org/uniprotkb/O94407/entry","name":"sec65","description":"Signal recognition particle sec65 subunit","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR17453","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67124300","identifier":"O59787","identifierLink":"https://www.uniprot.org/uniprotkb/O59787/entry","name":"srp72","description":"Signal recognition particle subunit srp72","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR14094","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67124317","identifier":"O74436","identifierLink":"https://www.uniprot.org/uniprotkb/O74436/entry","name":"srp68","description":"Signal recognition particle subunit srp68","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12860","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67124335","identifier":"URS0000D656E3_4896","identifierLink":"http://rnacentral.org/rna/URS0000D656E3_4896","name":"(fission yeast) 7sl signal recognition particle component","description":"Schizosaccharomyces pombe (fission yeast) 7SL signal recognition particle component","stochiometry":null,"interactorType":"long non-coding ribonucleic acid","organismName":"Schizosaccharomyces pombe; 4896","xrefs":[]},{"ac":"EBI-7169286","identifier":"P21565","identifierLink":"https://www.uniprot.org/uniprotkb/P21565/entry","name":"srp54","description":"Signal recognition particle subunit SRP54","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11564","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26641","complexName":"Signal recognition particle","organismName":"Caenorhabditis elegans; 6239","description":"A conserved ribonucleoprotein particle, which includes in its structure a small cytoplasmic RNA (scRNA). In co-translational targeting of membrane and secretory proteins, SRP recognizes signal sequences as soon as they emerge from the ribosomal polypeptide exit tunnel and binds to the ribosome-nascent chain complex (RNC), leading to retardation of peptide elongation. The SRP-RNC complex is targeted to the endoplasmic reticulum (ER) membrane by interaction with the SRP receptor (SR).  After docking to the membrane, the RNC is transferred to the protein-conducting channel, the translocon, and protein synthesis continues. The SRP-SR complex dissociates from the ribosome and, as a result of GTP hydrolysis, SRP and SR dissociate from each other. The genes encoding scR1 and SRP54 are not essential for growth, although SRP-deficient cells grow poorly, suggesting that an alternative, SRP-independent targeting pathway(s) to the ER membrane exists.","predictedComplex":false,"interactors":[{"ac":"EBI-2421303","identifier":"P34642","identifierLink":"https://www.uniprot.org/uniprotkb/P34642/entry","name":"srp09","description":"Signal recognition particle 9 kDa protein","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12834","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-320390","identifier":"O16927","identifierLink":"https://www.uniprot.org/uniprotkb/O16927/entry","name":"srp14","description":"Signal recognition particle 14 kDa protein","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12013","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67124344","identifier":"P91240","identifierLink":"https://www.uniprot.org/uniprotkb/P91240/entry","name":"srpa-72","description":"Signal recognition particle subunit SRP72","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR14094","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67124384","identifier":"Q20822","identifierLink":"https://www.uniprot.org/uniprotkb/Q20822/entry","name":"srpa-68","description":"Signal recognition particle subunit SRP68","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12860","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67124402","identifier":"G5EE80","identifierLink":"https://www.uniprot.org/uniprotkb/G5EE80/entry","name":"g5ee80","description":"Signal recognition particle 54 kDa protein","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11564","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67124429","identifier":"O61749","identifierLink":"https://www.uniprot.org/uniprotkb/O61749/entry","name":"srp19","description":"Probable signal recognition particle 19 kDa protein","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR17453","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67124442","identifier":null,"identifierLink":null,"name":"7sl_caeel","description":"7sl signal recognition particle component","stochiometry":null,"interactorType":"long non-coding ribonucleic acid","organismName":"Caenorhabditis elegans; 6239","xrefs":[]}]},{"complexAC":"CPX-26642","complexName":"U2 small nuclear ribonucleoprotein auxiliary factor complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Ribonucleoprotein complex that recognizes an consensus AG-dinucleotide at the splice site junction and a preceding polypyrimidine tract and recruits the U2 small nuclear ribonucleoprotein particle (snRNP) of the spliceosome during the removal of intervening sequences (introns) separating protein-coding regions within pre-mRNAs.","predictedComplex":false,"interactors":[{"ac":"EBI-1024157","identifier":"P36629","identifierLink":"https://www.uniprot.org/uniprotkb/P36629/entry","name":"prp2","description":"Splicing factor U2AF 59 kDa subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1564162","identifier":"Q09176","identifierLink":"https://www.uniprot.org/uniprotkb/Q09176/entry","name":"u2af1","description":"Splicing factor U2AF 23 kDa subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12620","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26643","complexName":"Klp5-Klp6 kinesin complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Kinesin motor complex which associates with mcp1 (O94452) to walk along the lattice of interphase microtubules (iMTs). Accumulates at iMT plus ends behind the Tea2 complex (CPX-26644) where it is prevented from accessing the plus end by the presence of Tea2. The complex may then either displace the Tea2 complex from the plus end, triggering MT catastrophe, or initiate MT depolymerisation resulting in the loss of the Tea2 complex and the GTP cap.","predictedComplex":false,"interactors":[{"ac":"EBI-1561745","identifier":"O59751","identifierLink":"https://www.uniprot.org/uniprotkb/O59751/entry","name":"klp6","description":"Kinesin-like protein 6","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1561765","identifier":"O14343","identifierLink":"https://www.uniprot.org/uniprotkb/O14343/entry","name":"klp5","description":"Kinesin-like protein 5","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26644","complexName":"Tea2 microtubule plus-end tracking complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Kinesin motor complex which acts as a microtubule plus-end tracking (MPET) system crucial for establishing cell polarity by asymmetrically transporting polarity markers to the cellular cortex.","predictedComplex":false,"interactors":[{"ac":"EBI-1002268","identifier":"Q10113","identifierLink":"https://www.uniprot.org/uniprotkb/Q10113/entry","name":"mal3","description":"Microtubule integrity protein mal3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10623","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1102463","identifier":"P79065","identifierLink":"https://www.uniprot.org/uniprotkb/P79065/entry","name":"tip1","description":"Tip elongation protein 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR18916","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1107767","identifier":"Q1MTQ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q1MTQ1/entry","name":"tea2","description":"Kinesin-like protein tea2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR47968","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26645","complexName":"Tea1-Tea4 signaling complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Binds to the microtubule plus end by interaction with the Tea2 complex (CPX-26644). Signals from the tip cortex to  polarisome proteins which play a role in positioning polarized growth through the formation of actin cables.","predictedComplex":false,"interactors":[{"ac":"EBI-1099982","identifier":"O60132","identifierLink":"https://www.uniprot.org/uniprotkb/O60132/entry","name":"tea4","description":"Tip elongation aberrant protein Tea4","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR47775","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-875376","identifier":"P87061","identifierLink":"https://www.uniprot.org/uniprotkb/P87061/entry","name":"tea1","description":"Tip elongation aberrant protein 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23244","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26646","complexName":"DUOX1-DUOXA1 dual oxidase complex","organismName":"Mus musculus; 10090","description":"Calcium-dependent NADPH oxidase which catalyzes cross-membrane electron transfer resulting in the production of hydrogen peroxide (H2O2). Electrons are transferred from NADPH to FAD, then to a heme molecule on the cytoplasmic side of the membrane to Phe-1097 of DUOX1, and finally to the heme group on the extracellular side of the membrane where they react with oxygen. Required for the H2O2-dependent activity of thyroperoxidase (P07202) which catalyzes the three steps of thyroid hormone biosynthesis. May also have an antimicrobial role at mucosal surfases such as salivary glands in the trachea and play a role in wound response at the airway epithelium.","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-27037542","identifier":"A2AQ92","identifierLink":"https://www.uniprot.org/uniprotkb/A2AQ92/entry","name":"Duox1","description":"NAD(P)H oxidase (H2O2-forming)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11972","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27037594","identifier":"Q8VE49","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VE49/entry","name":"Duoxa1","description":"Dual oxidase maturation factor 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR31158","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26647","complexName":"HMG-CoA reductase complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the conversion of 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) to mevalonate in a four-electron oxidoreduction, the rate-limiting step in isoprenoid biosynthesis, including that of cholesterol (CHEBI:16113). Regulated through a negative feedback loop mediated by mevalonate-derived sterols and non-sterol metabolites.\r\n\r\nTargeted by HMG-CoA reductase inhibitors (statins, CHEBI:87631) to lower serum cholesterol in the treatment of hypercholesterolemia and thereby preventing cardiovascular disease.","predictedComplex":false,"interactors":[{"ac":"EBI-465513","identifier":"P04035","identifierLink":"https://www.uniprot.org/uniprotkb/P04035/entry","name":"HMGCR","description":"3-hydroxy-3-methylglutaryl-coenzyme A reductase","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10572","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26649","complexName":"Follicle Stimulating Hormone, type 1 receptor complex","organismName":"Homo sapiens; 9606","description":"Gonadotropin-receptor complex. Follicle stimulating hormone (FSH) mediates a diverse range of functions by binding to one of four FSH receptor (FSHR) isoforms. Canonical FSHR (FSHR-1) is expressed on the granulosa cell surface in ovaries and the Sertoli cell surface in testes. FSHR-1 activation leads to dissociation of the heterotrimeric inhibitory G (Gi) protein resulting in Gi-alpha activation of adenylyl cyclase and a consequent elevation in cyclic adenosine monophosphate (cAMP) levels and a consequent increase in steroid production necessary for follicular growth and ovulation in women.\r\n\r\nThe canonical FSHR (FSHR-1) is expressed only in ovarian granulosa and testicular Sertoli cells and its primary function is to participate in follicular development and granulosa cell differentiation.\r\n\r\nLoss-of-function in the FSH-FSHR pathway is linked to hypogonadism characterized by absent or incomplete sexual maturation by the expected age, as well as amenorrhea-associated ovarian dysgenesis and ovarian cancer.","predictedComplex":false,"interactors":[{"ac":"EBI-12510998","identifier":"CPX-665","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-665","name":"Follicle-stimulating hormone complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-15999714","identifier":"P23945-1","identifierLink":"https://www.uniprot.org/uniprotkb/P23945-1/entry","name":"FSHR","description":"Follicle-stimulating hormone receptor","stochiometry":"minValue: 1, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-26650","complexName":"Follicle Stimulating Hormone, type 2 dominant negative receptor complex","organismName":"Homo sapiens; 9606","description":"Gonadotropin dominant negative receptor complex. Follicle stimulating hormone (FSH) mediates a diverse range of functions by binding to one of four FSH receptor (FSHR) isoforms. The physiological significance of the alternatively-spliced isoform 2 FSHR (FSHR-2) is yet to be determined, and while it binds FSH with high affinity, it lacks the ability to activate inhibitory G (Gi) proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-12510998","identifier":"CPX-665","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-665","name":"Follicle-stimulating hormone complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-67142965","identifier":"P23945-2","identifierLink":"https://www.uniprot.org/uniprotkb/P23945-2/entry","name":"FSHR","description":"Isoform Short of Follicle-stimulating hormone receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-26651","complexName":"Follicle Stimulating Hormone, type 3 receptor complex","organismName":"Homo sapiens; 9606","description":"Gonadotropin-receptor complex. Follicle stimulating hormone (FSH) mediates a diverse range of functions by binding to one of four FSH receptor (FSHR) isoforms. Follicle stimulating receptor isoform 3 (FSHR-3) binds FSH promoting mitotic activity and cell growth by activating the MAPK-ERK pathway in granulosa cells in a cyclic adenosine monophosphate (cAMP)-independent manner. MAPK-ERK activation regulates cell proliferation (including ovarian stem cells) through the modulation of calcium-dependent channels.\r\n\r\nFSHR-3 is thought to be the dominant form in developing follicles and ovarian stem cells.","predictedComplex":false,"interactors":[{"ac":"EBI-12510998","identifier":"CPX-665","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-665","name":"Follicle-stimulating hormone complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-67143115","identifier":"P23945-3","identifierLink":"https://www.uniprot.org/uniprotkb/P23945-3/entry","name":"FSHR","description":"Isoform 3 of Follicle-stimulating hormone receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-26653","complexName":"Follicle Stimulating Hormone, type 4 soluble receptor complex","organismName":"Homo sapiens; 9606","description":"Gonadotropin-receptor complex. Follicle stimulating hormone (FSH) mediates a diverse range of functions by binding to one of four FSH receptor (FSHR) isoforms. The alternatively-spliced isoform 4 FSHR (FSHR-4) may function like a prohormone of the active molecule but its physiological significance is yet to be determined.","predictedComplex":false,"interactors":[{"ac":"EBI-12510998","identifier":"CPX-665","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-665","name":"Follicle-stimulating hormone complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-67143164","identifier":"P23945-4","identifierLink":"https://www.uniprot.org/uniprotkb/P23945-4/entry","name":"FSHR","description":"Isoform 4 of Follicle-stimulating hormone receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-26654","complexName":"Phosphopantothenoylcysteine decarboxylase","organismName":"Arabidopsis thaliana; 3702","description":"Catalyzes decarboxylation of 4'-phosphopantothenoylcysteine to yield 4'-phosphopantetheine; the third step in the biosynthesis of Coenzyme A (CoA). The synthesis of CoA involves the phosphorylation of pantothenate (vitamin B5) to 4'-phosphopantothenate, to which a cysteine is then added to form 4'-phospho-N-pantothenoylcysteine (PCC). PPC is decarboxylated to 4'-phosphopantetheine by phosphopantothenoylcysteine decarboxylase (this complex). 4'-phosphopantetheine is adenylylated to form dephospho-CoA which is then phosphorylated to form coenzyme A.","predictedComplex":false,"interactors":[{"ac":"EBI-67144128","identifier":"Q9SWE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9SWE5/entry","name":"HAL3A","description":"Phosphopantothenoylcysteine decarboxylase","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR14359","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8786278","identifier":"CHEBI:17621","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:17621","name":"fmn","description":"FMN","stochiometry":"minValue: 3, maxValue: 3","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26655","complexName":"HAUS complex","organismName":"Xenopus laevis; 8355","description":"Regulates mitotic spindle assembly and centrosome integrity and is required for completion of cytokinesis. The complex interacts with the gamma-tubulin ring complex and this interaction is required for spindle assembly. May regulate microtubule nucleation events to control neuronal development.","predictedComplex":false,"interactors":[{"ac":"EBI-11608744","identifier":"B1H1T5","identifierLink":"https://www.uniprot.org/uniprotkb/B1H1T5/entry","name":"haus7.S","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Xenopus laevis; 8355","xrefs":[{"identifier":"PTHR14352","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11608970","identifier":"A0JPI0","identifierLink":"https://www.uniprot.org/uniprotkb/A0JPI0/entry","name":"haus6.L","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Xenopus laevis; 8355","xrefs":[{"identifier":"PTHR16151","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11609017","identifier":"Q6INL9","identifierLink":"https://www.uniprot.org/uniprotkb/Q6INL9/entry","name":"haus2.L","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Xenopus laevis; 8355","xrefs":[{"identifier":"PTHR16039","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11609203","identifier":"Q4V7I1","identifierLink":"https://www.uniprot.org/uniprotkb/Q4V7I1/entry","name":"haus4.L","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Xenopus laevis; 8355","xrefs":[{"identifier":"PTHR16219","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67144621","identifier":"A0A8J1L9M8","identifierLink":"https://www.uniprot.org/uniprotkb/A0A8J1L9M8/entry","name":"haus1.L","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Xenopus laevis; 8355","xrefs":[{"identifier":"PTHR31570","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67144642","identifier":"Q6DCY9","identifierLink":"https://www.uniprot.org/uniprotkb/Q6DCY9/entry","name":"haus3","description":"HAUS augmin-like complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Xenopus laevis; 8355","xrefs":[{"identifier":"PTHR19378","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67144665","identifier":"A0A1L8FPI2","identifierLink":"https://www.uniprot.org/uniprotkb/A0A1L8FPI2/entry","name":"haus5.L","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Xenopus laevis; 8355","xrefs":[{"identifier":"PTHR28588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67144683","identifier":"Q0IHJ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q0IHJ3/entry","name":"haus8","description":"HAUS augmin-like complex subunit 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Xenopus laevis; 8355","xrefs":[]}]},{"complexAC":"CPX-26656","complexName":"Luminal surveillance complex","organismName":"Homo sapiens; 9606","description":"Recognizes the protein determinant required for ER-associated degradation (ERAD) of mis-folded proteins, recruiting substrates to SYVN1-associated machinery, and activating downstream events that commit substrates for degradation. The complex recognizes misfolded glycoproteins independent of their glycosylation status and brings them to the downstream ubiquitination/extraction machinery. However the commitment step to destruction requires the lectin ERLEC1, which recognizes the glycan species found on terminally misfolded proteins.\r\n\r\nFailure of ERAD-mediated degradation leads to the accumulation of misfolded proteins in neurons, a pathological feature of neurodegenerative diseases, including Alzheimer’s disease, Parkinson’s and Amyotrophic Lateral Sclerosis. SYVN1-associated mutations have also been reported to cause embryonic lethality, developmental delay and other disorders post-birth.","predictedComplex":false,"interactors":[{"ac":"EBI-1023677","identifier":"Q96DZ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q96DZ1/entry","name":"ERLEC1","description":"Endoplasmic reticulum lectin 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15414","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358766","identifier":"Q9UBV2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UBV2/entry","name":"SEL1L","description":"Protein sel-1 homolog 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-947849","identifier":"Q86TM6","identifierLink":"https://www.uniprot.org/uniprotkb/Q86TM6/entry","name":"SYVN1","description":"E3 ubiquitin-protein ligase synoviolin","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22763","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26657","complexName":"SPO11 meiotic recombination initiation complex","organismName":"Homo sapiens; 9606","description":"Catalyzed by SPO11, the complex mediates DNA cleavage to generate double-strand breaks (DSBs) to initiate meiotic recombination. Complex promotes the relaxation of negative and positive supercoiled DNA and DNA decatenation through cleavage and ligation cycles.\r\n\r\nMutations in SPO11 cause defects in meiotic recombination.","predictedComplex":false,"interactors":[{"ac":"EBI-12550116","identifier":"Q9Y5K1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5K1/entry","name":"SPO11","description":"Meiotic recombination protein SPO11","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10848","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67148298","identifier":"Q8N6T0-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N6T0-1/entry","name":"TOP6BL","description":"Isoform 3 of Type 2 DNA topoisomerase 6 subunit B-like","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26658","complexName":"SPO11 meiotic recombination initiation complex","organismName":"Mus musculus; 10090","description":"Catalyzed by SPO11, the complex mediates DNA cleavage to generate double-strand breaks (DSBs) to initiate meiotic recombination. Complex promotes the relaxation of negative and positive supercoiled DNA and DNA decatenation through cleavage and ligation cycles.","predictedComplex":false,"interactors":[{"ac":"EBI-16200997","identifier":"J3QMY9","identifierLink":"https://www.uniprot.org/uniprotkb/J3QMY9/entry","name":"Top6bl","description":"Type 2 DNA topoisomerase 6 subunit B-like","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14652","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16201014","identifier":"Q9WTK8-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WTK8-1/entry","name":"Spo11","description":"Meiotic recombination protein SPO11","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26659","complexName":"SPO11 meiotic recombination initiation complex","organismName":"Arabidopsis thaliana; 3702","description":"Catalyzed by SPO11-1/SPO11-2, the complex mediates DNA cleavage to generate double-strand breaks (DSBs) to initiate meiotic recombination. Complex promotes the relaxation of negative and positive supercoiled DNA and DNA decatenation through cleavage and ligation cycles. Complex promotes relaxation of negative and positive supercoiled DNA and DNA decatenation through cleavage and ligation cycles.","predictedComplex":false,"interactors":[{"ac":"EBI-1540725","identifier":"Q9M4A2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9M4A2/entry","name":"SPO11-1","description":"Meiotic recombination protein SPO11-1","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR10848","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16200362","identifier":"Q5Q0E6","identifierLink":"https://www.uniprot.org/uniprotkb/Q5Q0E6/entry","name":"MTOPVIB","description":"Type 2 DNA topoisomerase 6 subunit B-like","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR36722","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1772309","identifier":"Q9M4A1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9M4A1/entry","name":"SPO11-2","description":"Meiotic recombination protein SPO11-2","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR10848","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26660","complexName":"GTPase KRAS - Son of sevenless homolog 1 complex","organismName":"Homo sapiens; 9606","description":"A RAS GTPase complex responsible for intracellular transduction of signals received through cell-surface receptor tyrosine kinases. KRAS and SOS1 allosterically activate each other: binding of inactive KRAS.GDP to SOS1 stimulates SOS1 nucleotide exchange activity which in turn leads to KRAS binding GTP in place of GDP.\r\n\r\nKRAS accounts for around 85% of RAS-related mutations which lead to several cancers (including pancreatic, colon and small intestine) and rasopathies and of these, the more abundant KRAS-4B isoform (P01116-2) is dominant.","predictedComplex":false,"interactors":[{"ac":"EBI-297487","identifier":"Q07889","identifierLink":"https://www.uniprot.org/uniprotkb/Q07889/entry","name":"SOS1","description":"Son of sevenless homolog 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23113","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-367415","identifier":"P01116","identifierLink":"https://www.uniprot.org/uniprotkb/P01116/entry","name":"KRAS","description":"GTPase KRas","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24070","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-989053","identifier":"CHEBI:15996","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15996","name":"gtp","description":"guanosine triphosphate - GTP","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26662","complexName":"SPO11 DNA endo-reduplication complex","organismName":"Arabidopsis thaliana; 3702","description":"Involved in chromatin organization and endoreduplication in somatic cells, with the latter process contributing to both the increase in level as well as variation in nuclear ploidy levels. Complex plays crucial roles in plant growth and development, including cell-elongation processes mediated by brassinosteroids.","predictedComplex":false,"interactors":[{"ac":"EBI-1772104","identifier":"Q9LZ03","identifierLink":"https://www.uniprot.org/uniprotkb/Q9LZ03/entry","name":"TOP6A","description":"DNA topoisomerase 6 subunit A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR10848","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1772132","identifier":"Q9C5V6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9C5V6/entry","name":"TOP6B","description":"DNA topoisomerase 6 subunit B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR10871","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26664","complexName":"SPO11, meiotic recombination initiation complex","organismName":"Drosophila melanogaster; 7227","description":"Catalyzed by mei-W68, the complex mediates DNA cleavage to generate double-strand breaks (DSBs) to initiate meiotic recombination in female drosophila. Recombination is absent in male drosophila, suggesting that this mei-W68-complex is not required for male meiosis. May also play a role in mitosis.","predictedComplex":false,"interactors":[{"ac":"EBI-102811","identifier":"Q9VS36","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VS36/entry","name":"mei-P22","description":"Meiotic recombination protein P22","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-496850","identifier":"Q7KPA5","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KPA5/entry","name":"mei-W68","description":"Meiotic recombination protein W68","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10848","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26665","complexName":"Casein kinase II complex","organismName":"Drosophila melanogaster; 7227","description":"Serine/threonine-protein kinase that phosphorylates substrates containing acidic residues both N- and C-terminal to the phosphorylated serine or threonine. CK2 plays an important role in Notch signaling during development of two sensory organs (eye and bristle), through its targeting of the bHLH transcription factors E(spl)m5-HLH (P13096), E(spl)m7-HLH (P13097) and E(spl)m8-HLH (P13098).","predictedComplex":false,"interactors":[{"ac":"EBI-128120","identifier":"P08182","identifierLink":"https://www.uniprot.org/uniprotkb/P08182/entry","name":"CkIIbeta","description":"Casein kinase II subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-93115","identifier":"P08181","identifierLink":"https://www.uniprot.org/uniprotkb/P08181/entry","name":"CkIIalpha","description":"Casein kinase II subunit alpha","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR24054","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26666","complexName":"GNAI1-GPSM2-NUMA1, spindle orientation complex","organismName":"Homo sapiens; 9606","description":"Coordinates cell polarization and spindle orientation during asymmetrical cell division in progenitor cells. Localizes dynein to the cell cortex to direct spindle positioning, and ensures levels of the dynein-dynactin motor protein complex at the plasma membrane is appropriate.\r\n\r\nGPSM2 partially co-localizes with NUMA1 at spindle poles during mitosis. NUMA1 binding to GPSM2 is a mutually exclusive process, where INSC (Q1MX18) can displace NUMA1 from GPSM2.","predictedComplex":false,"interactors":[{"ac":"EBI-521611","identifier":"Q14980","identifierLink":"https://www.uniprot.org/uniprotkb/Q14980/entry","name":"NUMA1","description":"Nuclear mitotic apparatus protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18902","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-618639","identifier":"P63096","identifierLink":"https://www.uniprot.org/uniprotkb/P63096/entry","name":"GNAI1","description":"Guanine nucleotide-binding protein G(i) subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10218","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-618655","identifier":"P81274","identifierLink":"https://www.uniprot.org/uniprotkb/P81274/entry","name":"GPSM2","description":"G-protein-signaling modulator 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45954","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26667","complexName":"Phosphopantothenoylcysteine synthetase complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the second step in the biosynthesis of coenzyme A (CoA) from vitamin B5, in which cysteine is conjugated to 4′-phosphopantothenate to form 4′-phosphopantothenoylcysteine. \r\n\r\nThe biosynthesis of CoA from pantothenate involves five universally conserved steps. First, pantothenate is phosphorylated by pantothenate kinases (CPX-26668). In the second step, 4′-phosphopantothenate is conjugated with cysteine by phosphopantothenoylcysteine synthetase (this complex). The resulting intermediate is then converted to 4′-phosphopantetheine by phosphopantothenoylcysteine decarboxylase (see CPX-26563). The final two steps are catalyzed by phosphopantetheine adenylyltransferase (COASY, Q13057), which adenylates 4′-phosphopantetheine to form dephospho-CoA, followed by phosphorylation of dephospho-CoA by dephospho-CoA kinase (also COASY) to yield the final CoA product.","predictedComplex":false,"interactors":[{"ac":"EBI-2827176","identifier":"Q9HAB8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HAB8/entry","name":"PPCS","description":"Phosphopantothenate--cysteine ligase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12290","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26668","complexName":"Pantothenate kinase 1 complex","organismName":"Homo sapiens; 9606","description":"Critical regulator of intracellular levels of coenzyme A (CoA). Catalyzes the first and rate-limiting step in CoA biosynthesis by phosphorylating pantothenate to produce 4′-phosphopantothenate. \r\n\r\nThe biosynthesis of CoA from pantothenate involves five universally conserved steps. First, pantothenate is phosphorylated by a pantothenate kinase (this complex, see also CPX-26669, CPX-26670). In the second step, 4′-phosphopantothenate is conjugated with cysteine by phosphopantothenoylcysteine synthetase (see CPX-26667). The resulting intermediate is then converted to 4′-phosphopantetheine by phosphopantothenoylcysteine decarboxylase (see CPX-26563). The final two steps are catalyzed by phosphopantetheine adenylyltransferase (COASY, Q13057), which adenylates 4′-phosphopantetheine to form dephospho-CoA, followed by phosphorylation of dephospho-CoA by dephospho-CoA kinase (also COASY) to yield the final CoA product.\r\n\r\nComplex is expressed in liver, kidney, and heart tissues, and its expression is key to controlling the cellular level of CoA.","predictedComplex":false,"interactors":[{"ac":"EBI-67153468","identifier":"Q8TE04-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TE04-1/entry","name":"PANK1","description":"Isoform 1 of Pantothenate kinase 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-26669","complexName":"Mitochondrial Pantothenate kinase 2 complex","organismName":"Homo sapiens; 9606","description":"Critical regulator of intracellular levels of coenzyme A (CoA). Mitochondrial complex that catalyzes the first and rate-limiting step in CoA biosynthesis by phosphorylating pantothenate to produce 4′-phosphopantothenate. \r\n\r\nThe biosynthesis of CoA from pantothenate involves five universally conserved steps. First, pantothenate is phosphorylated by a pantothenate kinase (this complex, see also CPX-26668, CPX-26670, CPX-26671). In the second step, 4′-phosphopantothenate is conjugated with cysteine by phosphopantothenoylcysteine synthetase (see CPX-26667). The resulting intermediate is then converted to 4′-phosphopantetheine by phosphopantothenoylcysteine decarboxylase (see CPX-26563). The final two steps are catalyzed by phosphopantetheine adenylyltransferase (COASY, Q13057), which adenylates 4′-phosphopantetheine to form dephospho-CoA, followed by phosphorylation of dephospho-CoA by dephospho-CoA kinase (also COASY) to yield the final CoA product.\r\n\r\nMutations in PANK2 is implicated in Pantothenate-kinase-associated neurodegeneration (PKAN), a rare genetic disease and a form of neurodegeneration with brain iron accumulation (NBIA).","predictedComplex":false,"interactors":[{"ac":"EBI-67158858","identifier":"Q9BZ23-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BZ23-1/entry","name":"PANK2","description":"Isoform 1 of Pantothenate kinase 2, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-26670","complexName":"Cytoplasmic Pantothenate kinase 2 complex","organismName":"Homo sapiens; 9606","description":"Critical regulator of intracellular levels of coenzyme A (CoA). Cytoplasmic complex that catalyzes the first and rate-limiting step in CoA biosynthesis by phosphorylating pantothenate to produce 4′-phosphopantothenate. \r\n\r\nThe biosynthesis of CoA from pantothenate involves five universally conserved steps. First, pantothenate is phosphorylated by a pantothenate kinase (this complex, see also CPX-26668, CPX-26669, CPX-26671). In the second step, 4′-phosphopantothenate is conjugated with cysteine by phosphopantothenoylcysteine synthetase (see CPX-26667). The resulting intermediate is then converted to 4′-phosphopantetheine by phosphopantothenoylcysteine decarboxylase (see CPX-26563). The final two steps are catalyzed by phosphopantetheine adenylyltransferase (COASY, Q13057), which adenylates 4′-phosphopantetheine to form dephospho-CoA, followed by phosphorylation of dephospho-CoA by dephospho-CoA kinase (also COASY) to yield the final CoA product.\r\n\r\nMutations in PANK2 is implicated in Pantothenate-kinase-associated neurodegeneration (PKAN), a rare genetic disease and a form of neurodegeneration with brain iron accumulation (NBIA).","predictedComplex":false,"interactors":[{"ac":"EBI-67158850","identifier":"Q9BZ23-4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BZ23-4/entry","name":"PANK2","description":"Pantothenate kinase 2, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-26671","complexName":"Pantothenate kinase 3 complex","organismName":"Homo sapiens; 9606","description":"Critical regulator of intracellular levels of coenzyme A (CoA). Complex catalyzes the first and rate-limiting step in CoA biosynthesis by phosphorylating pantothenate to produce 4′-phosphopantothenate. \r\n\r\nThe biosynthesis of CoA from pantothenate involves five universally conserved steps. First, pantothenate is phosphorylated by a pantothenate kinase (this complex, see also CPX-26668, CPX-26669, CPX-26670). In the second step, 4′-phosphopantothenate is conjugated with cysteine by phosphopantothenoylcysteine synthetase (see CPX-26667). The resulting intermediate is then converted to 4′-phosphopantetheine by phosphopantothenoylcysteine decarboxylase (see CPX-26563). The final two steps are catalyzed by phosphopantetheine adenylyltransferase (COASY, Q13057), which adenylates 4′-phosphopantetheine to form dephospho-CoA, followed by phosphorylation of dephospho-CoA by dephospho-CoA kinase (also COASY) to yield the final CoA product.\r\n\r\nMutations in PANK2 is implicated in Pantothenate-kinase-associated neurodegeneration (PKAN), a rare genetic disease and a form of neurodegeneration with brain iron accumulation (NBIA).","predictedComplex":false,"interactors":[{"ac":"EBI-41428008","identifier":"Q9H999","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H999/entry","name":"PANK3","description":"Pantothenate kinase 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12280","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-12912","complexName":"BCAR1-CRK-SH2D3C, focal adhesion regulator complex","organismName":"Homo sapiens; 9606","description":"Focal adhesion regulator complex. SH2D3C acts as an adaptor to bridge Cas family protein BCAR1 (a scaffolding protein) with the signalling molecule CRK to form a signalling hub which regulates integrin-mediated cell adhesion, spreading and migration.","predictedComplex":false,"interactors":[{"ac":"EBI-702093","identifier":"P56945","identifierLink":"https://www.uniprot.org/uniprotkb/P56945/entry","name":"BCAR1","description":"Breast cancer anti-estrogen resistance protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10654","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-745980","identifier":"Q8N5H7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N5H7/entry","name":"SH2D3C","description":"SH2 domain-containing protein 3C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14247","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-886","identifier":"P46108","identifierLink":"https://www.uniprot.org/uniprotkb/P46108/entry","name":"CRK","description":"Adapter molecule crk","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19969","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26673","complexName":"FTH1-FTL, Ferritin complex","organismName":"Homo sapiens; 9606","description":"Critical for storing and releasing iron in a controlled manner to maintain iron homeostasis and protect cells from oxidative damage. Intracellularly, it preserves iron in a non-toxic and readily available form, but it is also abundantly found in circlulation. \r\n\r\nA heteromeric complex is necessary for optimal functioning, with FTH1 and FTL co-assembling into different types of isoferritins, which are either more acidic (heavy chain rich) or more basic (Light chain rich). However, the two are not interchangeable; FTH1 has a metal-binding site and exhibits ferroxidase activity catalysing the oxidation of Fe2+ to Fe3+, so that iron can be safely stored inside the ferritin cavity, whereas FTL lacks ferroxidase activity. Instead, it helps with iron nucleation and stabilises the assembled ferritin shell, helping in iron storage and retention. \r\n\r\nFerriting degradation allows the cell to reutilize iron, and occurs primarily through ferritinophagy, a selective form of autophagy mediated by the cargo receptor NCOA4 (see CPX-14323).","predictedComplex":false,"interactors":[{"ac":"EBI-11472102","identifier":"CHEBI:24875","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:24875","name":"iron cation","description":"iron cation","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-713259","identifier":"P02794","identifierLink":"https://www.uniprot.org/uniprotkb/P02794/entry","name":"FTH1","description":"Ferritin heavy chain","stochiometry":"minValue: 1, maxValue: 23","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11431","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-713279","identifier":"P02792","identifierLink":"https://www.uniprot.org/uniprotkb/P02792/entry","name":"FTL","description":"Ferritin light chain","stochiometry":"minValue: 1, maxValue: 23","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11431","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26674","complexName":"Huntingtin-HAP40 endosomal complex","organismName":"Drosophila melanogaster; 7227","description":"The HTT-HAP40 complex plays several key biological roles, including maintaining protein stability, regulating intracellular transport, and modulating cellular homeostasis. The complex acts as a RAB5 (Q9V3I2) effector, regulating early endosome motility by by recruiting kinesins to facilitate anterograde motility along microtubules, thereby affecting intracellular cargo transport and membrane dynamics.","predictedComplex":false,"interactors":[{"ac":"EBI-120379","identifier":"Q9VXR6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VXR6/entry","name":"Hap40","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR16797","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3411082","identifier":"Q9V3N4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V3N4/entry","name":"htt","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10170","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-15113","complexName":"cFLIP-CASP8-FADD complex","organismName":"Homo sapiens; 9606","description":"Anti-apoptosis regulator complex. Complex regulates death receptor (DR)-mediated apoptosis and RIPK1 (Q13546)-mediated necroptosis. However, its function remains controversial, where a hierarchical death-effector domain (DED) assembly mechanism is thought to confer resistance to both DR-mediated and DR-independent death signaling in tumor cells with elevated CFLAR levels. The catalytic activity of the cFLIP-CASP8-FADD complex blocks RIPK3-dependent signaling (including necrosis) by cleaving RIPK1, whilst CFLAR blocks RIPK3-independent apoptosis promoted by the FADD-caspase-8 complex.","predictedComplex":false,"interactors":[{"ac":"EBI-494804","identifier":"Q13158","identifierLink":"https://www.uniprot.org/uniprotkb/Q13158/entry","name":"FADD","description":"FAS-associated death domain protein","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-514941","identifier":"O15519","identifierLink":"https://www.uniprot.org/uniprotkb/O15519/entry","name":"CFLAR","description":"CASP8 and FADD-like apoptosis regulator","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10454","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-78060","identifier":"Q14790","identifierLink":"https://www.uniprot.org/uniprotkb/Q14790/entry","name":"CASP8","description":"Caspase-8","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10454","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26675","complexName":"INSR, insulin receptor complex","organismName":"Homo sapiens; 9606","description":"Insulin (P01308) binding tyrosine kinase receptor complex. Regulates glucose homeostasis and normal human growth. Initiates key signalling pathways upon insulin binding. Activation of INSR leads to autophosphorylation and recruitment of insulin receptor substrates (IRS proteins), which in turn activate the PI3K-AKT and MAPK pathways, thereby regulating critical metabolic functions such as glucose uptake (via GLUT4 translocation), glycogen synthesis, lipid metabolism, and inhibition of hepatic glucose production. INSR also influences physiological processes including growth, development, and bone formation, partly through interactions with the growth hormone/IGF. INSR function is tightly regulated by internalization and recycling mechanisms, and its dysfunction can result in severe insulin resistance syndromes or contribute to the pathogenesis of diabetes mellitus.","predictedComplex":false,"interactors":[{"ac":"EBI-10818032","identifier":"P06213-PRO_0000016689","identifierLink":"https://www.uniprot.org/uniprotkb/P06213-PRO_0000016689/entry","name":"INSR","description":"Insulin receptor subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-67171059","identifier":"P06213-PRO_0000016687","identifierLink":"https://www.uniprot.org/uniprotkb/P06213-PRO_0000016687/entry","name":"INSR","description":"Insulin receptor subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-26677","complexName":"Insulin-like growth factor 1 receptor complex","organismName":"Homo sapiens; 9606","description":"Receptor tyrosine kinase that mediates cellular responses to IGF1 (P05019) and IGF2 (P01344). Upon ligand binding, IGF1R undergoes conformational changes that activate its intrinsic kinase activity, triggering downstream signalling pathways involved in cell growth, differentiation, metabolism, and survival. IGF1R plays critical roles in development, tissue homeostasis, and cancer progression by regulating proliferation and preventing apoptosis.\r\n\r\nIGF1R binds insulin only weakly and with limited physiological relevance. IGF1R-INSR hybrid receptor's (CPX-16536), insulin binding affinity and signalling are intermediate but generally reduced compared to INSR receptors (CPX-26675).","predictedComplex":false,"interactors":[{"ac":"EBI-22054038","identifier":"P08069-PRO_0000016682","identifierLink":"https://www.uniprot.org/uniprotkb/P08069-PRO_0000016682/entry","name":"IGF1R","description":"Insulin-like growth factor 1 receptor beta chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-67171102","identifier":"P08069-PRO_0000016681","identifierLink":"https://www.uniprot.org/uniprotkb/P08069-PRO_0000016681/entry","name":"IGF1R","description":"Insulin-like growth factor 1 receptor alpha chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-26678","complexName":"INS-INSR receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Glucose-regulating complex. Upon binding with high affinity to INS, INSR undergoes major conformational shift from an autoinhibited, inverted-U shape to an active T-shaped conformation. Conformational rearrangement brings the membrane-proximal regions and intracellular kinase domains into close proximity, enabling trans-autophosphorylation and signal initiation. Once activated, INSR triggers downstream signalling pathways, including the PI3K-AKT and MAPK cascades, that regulate glucose uptake, lipid metabolism, protein synthesis, cell growth, and survival, thus playing a critical role in maintaining metabolic and systemic homeostasis.","predictedComplex":false,"interactors":[{"ac":"EBI-12685818","identifier":"P01308-PRO_0000015821","identifierLink":"https://www.uniprot.org/uniprotkb/P01308-PRO_0000015821/entry","name":"INS","description":"Insulin A chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-12685833","identifier":"P01308-PRO_0000015819","identifierLink":"https://www.uniprot.org/uniprotkb/P01308-PRO_0000015819/entry","name":"INS","description":"Insulin B chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-67170992","identifier":"CPX-26675","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-26675","name":"INSR, insulin receptor complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-15604","complexName":"VCP-remodelling complex","organismName":"Homo sapiens; 9606","description":"Lysine-specific methyltransferase that catalyzes the trimethylation of Lys-315 of VCP. ASPSCR1 enables the disassembly of VCP allowing the methyltransferase VCPKMT to bind and trimethylate VCP at the lysine side chain, which is deeply buried inside functional VCP hexamers. VCP is an ATPase involved in a number of cellular functions, including endoplasmic reticulum associated degradation (ERAD), membrane fusion, protein degradation and transcription factor regulation. Maintains cellular homeostasis under both physiological and stress conditions. Its activity is essential for clearing misfolded or damaged proteins, resolving stalled replication forks, terminating transcription complexes, and regulating the turnover of membrane-bound and nuclear signalling factors.","predictedComplex":false,"interactors":[{"ac":"EBI-18393784","identifier":"Q9H867","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H867/entry","name":"VCPKMT","description":"Protein N-lysine methyltransferase METTL21D","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14614","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1993677","identifier":"Q9BZE9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BZE9/entry","name":"ASPSCR1","description":"Tether containing UBX domain for GLUT4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46467","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30813205","identifier":"CHEBI:59789","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:59789","name":"s-adenosyl-l-methionine zwitterion","description":"S-adenosyl-L-methionine zwitterion","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-355164","identifier":"P55072","identifierLink":"https://www.uniprot.org/uniprotkb/P55072/entry","name":"VCP","description":"Transitional endoplasmic reticulum ATPase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26680","complexName":"Positive transcription elongation factor B complex, cdk9-pch1","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"A serine kinase complex that phosphorylates Ser-2 and Ser-5 of the rpb1 subunit (P36594) of RNA polymerase II (RNA Pol II) heptapeptide repeat, thus positively regulating productive mRNA elongation through the gene body after promoter-proximal pausing of RNA Pol II .","predictedComplex":false,"interactors":[{"ac":"EBI-443557","identifier":"Q96WV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q96WV9/entry","name":"cdk9","description":"Probable cyclin-dependent kinase 9","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-443575","identifier":"O74627","identifierLink":"https://www.uniprot.org/uniprotkb/O74627/entry","name":"pch1","description":"Cyclin pch1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26682","complexName":"Glycoprotein hormone receptor complex, GPA2-GPB5 variant","organismName":"Caenorhabditis elegans; 6239","description":"Leucine-rich-repeat-containing G-protein-coupled receptor. Required for normal body size and acts through activation of the glycoprotein hormone receptor ortholog FSHR-1 (G5EG04).","predictedComplex":false,"interactors":[{"ac":"EBI-67171580","identifier":"A7DT38","identifierLink":"https://www.uniprot.org/uniprotkb/A7DT38/entry","name":"gplb-1","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11515","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67171604","identifier":"A0T3A2","identifierLink":"https://www.uniprot.org/uniprotkb/A0T3A2/entry","name":"a0t3a2","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]}]},{"complexAC":"CPX-26683","complexName":"Mitochondrial pyruvate dehydrogenase complex, Pdha1 variant","organismName":"Drosophila melanogaster; 7227","description":"The pyruvate dehydrogenase complex (PDC) catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). The eukaryotic Pyruvate Dehydrogenase Complex (PDC) is a multi-enzyme complex organized around a dodecahedral core formed by the dihydrolipoyl transacetylase (E2) component. To this core, multiple copies of the thiamin diphosphate-dependent pyruvate dehydrogenase (E1) component, the FAD-containing dihydrolipoamide dehydrogenase (E3) component, and one to two copies each of pyruvate dehydrogenase kinase (PDK) and pyruvate dehydrogenase phosphatase (PDP, which comprises a catalytic and regulatory subunit) are tethered via non-covalent interactions. The PDC functions in the mitochondrial matrix to catalyze the oxidative decarboxylation of pyruvate to produce acetyl-CoA and NADH and as such is the gate-keeper enzyme that links glycolysis to the Krebs cycle and lipogenic pathways.","predictedComplex":false,"interactors":[{"ac":"EBI-110434","identifier":"Q9VVL7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVL7/entry","name":"Dld","description":"Dihydrolipoyl dehydrogenase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22912","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-143435","identifier":"P91622","identifierLink":"https://www.uniprot.org/uniprotkb/P91622/entry","name":"Pdk","description":"[Pyruvate dehydrogenase (acetyl-transferring)] kinase, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11947","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-161034","identifier":"Q9W3Q1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W3Q1/entry","name":"Pdp","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13832","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-163004","identifier":"Q7K5K3","identifierLink":"https://www.uniprot.org/uniprotkb/Q7K5K3/entry","name":"Pdhb","description":"Pyruvate dehydrogenase E1 component subunit beta, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11624","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16416616","identifier":"CHEBI:83088","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:83088","name":"(r)-lipoate","description":"(R)-lipoate","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-277228","identifier":"Q9VM14","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VM14/entry","name":"Dlat","description":"dihydrolipoyllysine-residue acetyltransferase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23151","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2890572","identifier":"Q9W4K8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W4K8/entry","name":"Pdpr","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67172388","identifier":"Q7KVX1","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KVX1/entry","name":"Pdha1","description":"Pyruvate dehydrogenase E1 component subunit alpha","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11516","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9691551","identifier":"CHEBI:58937","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58937","name":"thiamine(1+) diphosphate(3-)","description":"thiamine(1+) diphosphate(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26684","complexName":"Mitochondrial pyruvate dehydrogenase complex, Pdha2 variant","organismName":"Drosophila melanogaster; 7227","description":"The pyruvate dehydrogenase complex (PDC) catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). The eukaryotic Pyruvate Dehydrogenase Complex (PDC) is a multi-enzyme complex organized around a dodecahedral core formed by the dihydrolipoyl transacetylase (E2) component. To this core, multiple copies of the thiamin diphosphate-dependent pyruvate dehydrogenase (E1) component, the FAD-containing dihydrolipoamide dehydrogenase (E3) component, and one to two copies each of pyruvate dehydrogenase kinase (PDK) and pyruvate dehydrogenase phosphatase (PDP, which comprises a catalytic and regulatory subunit) are tethered via non-covalent interactions. The PDC functions in the mitochondrial matrix to catalyze the oxidative decarboxylation of pyruvate to produce acetyl-CoA and NADH and as such is the gate-keeper enzyme that links glycolysis to the Krebs cycle and lipogenic pathways.","predictedComplex":false,"interactors":[{"ac":"EBI-110434","identifier":"Q9VVL7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVL7/entry","name":"Dld","description":"Dihydrolipoyl dehydrogenase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22912","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-143435","identifier":"P91622","identifierLink":"https://www.uniprot.org/uniprotkb/P91622/entry","name":"Pdk","description":"[Pyruvate dehydrogenase (acetyl-transferring)] kinase, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11947","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-161034","identifier":"Q9W3Q1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W3Q1/entry","name":"Pdp","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13832","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-163004","identifier":"Q7K5K3","identifierLink":"https://www.uniprot.org/uniprotkb/Q7K5K3/entry","name":"Pdhb","description":"Pyruvate dehydrogenase E1 component subunit beta, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11624","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16416616","identifier":"CHEBI:83088","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:83088","name":"(r)-lipoate","description":"(R)-lipoate","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-277228","identifier":"Q9VM14","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VM14/entry","name":"Dlat","description":"dihydrolipoyllysine-residue acetyltransferase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23151","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2890572","identifier":"Q9W4K8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W4K8/entry","name":"Pdpr","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-86476","identifier":"Q9W4H4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W4H4/entry","name":"Pdha2","description":"Pyruvate dehydrogenase E1 component subunit alpha","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11516","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9691551","identifier":"CHEBI:58937","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58937","name":"thiamine(1+) diphosphate(3-)","description":"thiamine(1+) diphosphate(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26685","complexName":"Mitochondrial 2-oxoisovalerate dehydrogenase complex","organismName":"Drosophila melanogaster; 7227","description":"Catalyzes the conversion of alpha-keto acids derived from the branched-chain amino acids leucine, isoleucine and valine. to acyl-CoA and CO2, a step in the catabolism of branched chain amino acids.","predictedComplex":false,"interactors":[{"ac":"EBI-110434","identifier":"Q9VVL7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVL7/entry","name":"Dld","description":"Dihydrolipoyl dehydrogenase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22912","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-137358","identifier":"Q9VXY3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VXY3/entry","name":"Dbct","description":"Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 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The complex may also contribute to the unwinding of strand invasion after extension of the invading 3' end by DNA synthesis to promote DSB repair by synthesis-dependent strand annealing, as well as reversal of strand invasion prior to 3' end extension.","predictedComplex":false,"interactors":[{"ac":"EBI-16123681","identifier":"Q09811","identifierLink":"https://www.uniprot.org/uniprotkb/Q09811/entry","name":"rqh1","description":"ATP-dependent DNA helicase hus2/rqh1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13710","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67173874","identifier":"O60126","identifierLink":"https://www.uniprot.org/uniprotkb/O60126/entry","name":"top3","description":"DNA topoisomerase 3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11390","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67173903","identifier":"Q10160","identifierLink":"https://www.uniprot.org/uniprotkb/Q10160/entry","name":"rmi1","description":"RecQ-mediated genome instability protein 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]}]},{"complexAC":"CPX-26687","complexName":"Retromer complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"A coat complex that mediates the recycling of transmembrane proteins from endosomes to the trans-Golgi network. Functions in endosomal membrane protein sorting and transport for endosome-to-Golgi retrieval. Involved in the retrieval of  a vacuolar protein sorting vps10 (O42930) protein, from endosome for retrograde transport to the trans-Golgi network.","predictedComplex":false,"interactors":[{"ac":"EBI-67173932","identifier":"Q9C0U7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9C0U7/entry","name":"vps5","description":"Vacuolar protein sorting-associated protein vps5","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10555","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67173997","identifier":"Q9URW7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9URW7/entry","name":"vps17","description":"Vacuolar protein sorting-associated protein 17","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR47433","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67174020","identifier":"Q9UTI5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UTI5/entry","name":"vps29","description":"Vacuolar protein sorting-associated protein 29","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11124","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67174037","identifier":"O74552","identifierLink":"https://www.uniprot.org/uniprotkb/O74552/entry","name":"vps35","description":"Vacuolar protein sorting-associated protein 35","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11099","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67174054","identifier":"Q10243","identifierLink":"https://www.uniprot.org/uniprotkb/Q10243/entry","name":"vps26","description":"Vacuolar protein sorting-associated protein 26","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12233","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26688","complexName":"Ribonuclease MRP complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Multifunctional ribonucleoprotein (RNP) complex that is involved in the maturation of various types of RNA including ribosomal RNA.","predictedComplex":false,"interactors":[{"ac":"EBI-67174070","identifier":"Q9UT91","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UT91/entry","name":"rmp1","description":"Ribonuclease MRP protein subunit rmp1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR37792","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67174210","identifier":"O94306","identifierLink":"https://www.uniprot.org/uniprotkb/O94306/entry","name":"ycgj","description":"Uncharacterized protein C16C4.19","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR14742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67174272","identifier":"Q9UTA4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UTA4/entry","name":"pop1","description":"Ribonucleases P/MRP protein subunit pop1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR22731","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67174292","identifier":"O74450","identifierLink":"https://www.uniprot.org/uniprotkb/O74450/entry","name":"pop3","description":"Ribonucleases P/MRP protein subunit pop3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28272","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67174306","identifier":"G2TRL5","identifierLink":"https://www.uniprot.org/uniprotkb/G2TRL5/entry","name":"new2","description":"Uncharacterized protein new2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-67174317","identifier":"O94251","identifierLink":"https://www.uniprot.org/uniprotkb/O94251/entry","name":"pop7","description":"Ribonucleases P/MRP protein subunit POP7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15314","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67174336","identifier":"Q7Z996","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z996/entry","name":"pop8","description":"Probable ribonucleases P protein subunit pop8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28173","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67174354","identifier":"Q9UU90","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UU90/entry","name":"pop5","description":"Ribonuclease P/MRP protein subunit POP5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15441","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67189416","identifier":"P87120","identifierLink":"https://www.uniprot.org/uniprotkb/P87120/entry","name":"rnp3","description":"Probable ribonuclease P protein subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 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9606","description":"Complex is critical for storing and releasing iron in a controlled manner, thereby maintaining iron homeostasis and protecting cells from oxidative damage. Intracellularly, it preserves iron in a non-toxic, soluble, and readily available form, but ferritin is also found in circulation, particularly in the serum, where its level reflects body iron stores.\r\n\r\nComplex contains a metal-binding ferroxidase center that catalyzes the oxidation of Fe2+ to Fe3+, allowing iron to be safely stored inside the ferritin cavity. This heavy-chain-rich complex supports rapid iron oxidation and detoxification, whereas complexes containing both heavy and light chains favor long-term iron mineral storage (CPX-26673). In the nucleus, heavy-chain ferritin helps protect DNA and chromatin from iron-mediated oxidative damage while maintaining local iron balance.\r\n\r\nFerritin degradation enables the cell to reutilize stored iron and occurs primarily through ferritinophagy, a selective form of autophagy mediated by the cargo receptor NCOA4 (see complex CPX-14323).","predictedComplex":false,"interactors":[{"ac":"EBI-11472102","identifier":"CHEBI:24875","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:24875","name":"iron cation","description":"iron cation","stochiometry":"minValue: 48, maxValue: 48","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-713259","identifier":"P02794","identifierLink":"https://www.uniprot.org/uniprotkb/P02794/entry","name":"FTH1","description":"Ferritin heavy chain","stochiometry":"minValue: 24, maxValue: 24","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11431","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-20447","complexName":"Cortical microtubule stabilization complex, KANK2 variant","organismName":"Homo sapiens; 9606","description":"Tethers microtubule plus ends to the cell cortex, linking microtubule dynamics with cell adhesion and polarity. By anchoring microtubules at sites of exocytosis, cell migration, and neuronal morphogenesis, the complex ensures proper cytoskeletal organization and spatial coordination of cellular processes. Complex also clusters strongly around focal adhesions at the leading cell edge and promote their disassembly. \r\n\r\nDisruption of complex components KANK2, PPFIBP1, or KIF21A leads to defects in microtubule organization, focal adhesion turnover, and cell motility. Moreover, pathogenic mutations, such as those in KIF21A associated with congenital fibrosis of the extraocular muscles (CFEOM) or in KANK2 linked to nephrotic syndrome, disturb this regulatory interface, underscoring the complex’s essential role in coordinating cytoskeletal dynamics with cellular function.","predictedComplex":false,"interactors":[{"ac":"EBI-1044755","identifier":"Q8IUD2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IUD2/entry","name":"ERC1","description":"ELKS/Rab6-interacting/CAST family member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18861","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1045582","identifier":"Q86W92","identifierLink":"https://www.uniprot.org/uniprotkb/Q86W92/entry","name":"PPFIBP1","description":"Liprin-beta-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12587","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2556193","identifier":"Q63ZY3","identifierLink":"https://www.uniprot.org/uniprotkb/Q63ZY3/entry","name":"KANK2","description":"KN motif and ankyrin repeat domain-containing protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24168","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2691397","identifier":"Q7Z4S6","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z4S6/entry","name":"KIF21A","description":"Kinesin-like protein KIF21A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2798483","identifier":"Q86SQ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q86SQ0/entry","name":"PHLDB2","description":"Pleckstrin homology-like domain family B member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12156","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-745426","identifier":"Q13136","identifierLink":"https://www.uniprot.org/uniprotkb/Q13136/entry","name":"PPFIA1","description":"Liprin-alpha-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12587","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-913476","identifier":"Q7Z460","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z460/entry","name":"CLASP1","description":"CLIP-associating protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21567","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-913524","identifier":"O75122","identifierLink":"https://www.uniprot.org/uniprotkb/O75122/entry","name":"CLASP2","description":"CLIP-associating protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21567","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26690","complexName":"Cortical microtubule stabilization complex, KANK1 variant","organismName":"Homo sapiens; 9606","description":"Tethers microtubule plus ends to the cell cortex, linking microtubule dynamics with cell adhesion and polarity. By anchoring microtubules at sites of exocytosis, cell migration, and neuronal morphogenesis, the complex ensures proper cytoskeletal organization and spatial coordination of cellular processes. Complex also clusters strongly around focal adhesions at the leading cell edge and promote their disassembly. \r\n\r\nDisruption of complex components KANK1, PPFIBP1, or KIF21A leads to defects in microtubule organization, focal adhesion turnover, and cell motility. Moreover, pathogenic mutations, such as those in KIF21A associated with congenital fibrosis of the extraocular muscles (CFEOM), disturb this regulatory interface, underscoring the complex’s essential role in coordinating cytoskeletal dynamics with cellular function.","predictedComplex":false,"interactors":[{"ac":"EBI-1044755","identifier":"Q8IUD2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IUD2/entry","name":"ERC1","description":"ELKS/Rab6-interacting/CAST family member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18861","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1045582","identifier":"Q86W92","identifierLink":"https://www.uniprot.org/uniprotkb/Q86W92/entry","name":"PPFIBP1","description":"Liprin-beta-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12587","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2556221","identifier":"Q14678","identifierLink":"https://www.uniprot.org/uniprotkb/Q14678/entry","name":"KANK1","description":"KN motif and ankyrin repeat domain-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24168","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2691397","identifier":"Q7Z4S6","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z4S6/entry","name":"KIF21A","description":"Kinesin-like protein KIF21A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2798483","identifier":"Q86SQ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q86SQ0/entry","name":"PHLDB2","description":"Pleckstrin homology-like domain family B member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12156","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-745426","identifier":"Q13136","identifierLink":"https://www.uniprot.org/uniprotkb/Q13136/entry","name":"PPFIA1","description":"Liprin-alpha-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12587","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-913476","identifier":"Q7Z460","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z460/entry","name":"CLASP1","description":"CLIP-associating protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21567","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-913524","identifier":"O75122","identifierLink":"https://www.uniprot.org/uniprotkb/O75122/entry","name":"CLASP2","description":"CLIP-associating protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21567","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-23940","complexName":"XIAP-CASP7 apoptosis regulatory complex","organismName":"Homo sapiens; 9606","description":"XIAP binds CASP7 preventing execution of apoptotic programs, particularly when CASP3 (P42574) is deficient and CASP7 is essential. Disruption of this complex restores CASP7 activity and promotes cell death.\r\n\r\nAlterations in apoptotic pathways have been implicated in several diseases, including cancer, autoimmune diseases, and developmental disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-12735963","identifier":"P55210-PRO_0000004619","identifierLink":"https://www.uniprot.org/uniprotkb/P55210-PRO_0000004619/entry","name":"CASP7","description":"Caspase-7 subunit p11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-12735969","identifier":"P55210-PRO_0000004617","identifierLink":"https://www.uniprot.org/uniprotkb/P55210-PRO_0000004617/entry","name":"CASP7","description":"Caspase-7 subunit p20","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-517127","identifier":"P98170","identifierLink":"https://www.uniprot.org/uniprotkb/P98170/entry","name":"XIAP","description":"E3 ubiquitin-protein ligase XIAP","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26693","complexName":"KRAS-RAF1, MAPK-cascade signal initiation complex","organismName":"Homo sapiens; 9606","description":"Serine/threonine kinase complex which reg complex which regulates diverse cellular processes, including proliferation, differentiation, and survival. Active, membrane-bound KRAS binds and recruits RAF1 to the membrane, initiating the canonical KRAS-RAF1-MEK-ERK, MAPK signalling cascade. RAF1 activation (via dimerization) leads to sequential phosphorylation of MEK and then ERK. Activated ERK moves into the nucleus to regulate gene expression through phosphorylation of transcription factors. \r\n\r\nMutations that maintain KRAS in its active, GTP-bound state drive constitutive MAPK pathway signaling and promote oncogenesis; KRAS represents the most frequently mutated oncogene in human cancers, accounting for approximately 80% of RAS-driven tumors.","predictedComplex":false,"interactors":[{"ac":"EBI-25820308","identifier":"CHEBI:37565","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:37565","name":"gtp(4-)","description":"GTP(4-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-365996","identifier":"P04049","identifierLink":"https://www.uniprot.org/uniprotkb/P04049/entry","name":"RAF1","description":"RAF proto-oncogene serine/threonine-protein kinase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44329","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-367415","identifier":"P01116","identifierLink":"https://www.uniprot.org/uniprotkb/P01116/entry","name":"KRAS","description":"GTPase KRas","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24070","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26694","complexName":"KRAS-PIK3CA cellular-homeostasis regulatory complex","organismName":"Homo sapiens; 9606","description":"Phosphatidylinositol 3-kinase (PI3K) activation complex which acts as a molecular switch maintaining cellular homeostasis by coordinating a broad range of essential processes, including glucose absorption, anabolic metabolism, cell growth, and survival. Once active, PIK3CA phosphorylates its substrate, PIP2 (ChEBI:18348), to generate PIP3 (ChEBI:16618), which in turn activates downstream signalling, including the AKT-mTOR pathway. This promotes cell survival by inhibiting pro-apoptotic factors, stimulate cell growth and proliferation through mTORC1 activation, and regulates metabolism by enhancing glucose uptake and glycolysis.\r\n\r\nMutations in KRAS and PIK3CA are implicated in various cancers. Notably, in endometrial carcinogenesis, KRAS and PIK3CA mutations are mutually exclusive and inversely correlated, suggesting that alterations in either gene may play equivalent roles in tumour development.","predictedComplex":false,"interactors":[{"ac":"EBI-367415","identifier":"P01116","identifierLink":"https://www.uniprot.org/uniprotkb/P01116/entry","name":"KRAS","description":"GTPase KRas","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24070","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67189923","identifier":"P42336-PRO_0000088785","identifierLink":"https://www.uniprot.org/uniprotkb/P42336-PRO_0000088785/entry","name":"PIK3CA","description":"Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-26695","complexName":"MRAS-PIK3CA cellular-homeostasis regulatory complex","organismName":"Homo sapiens; 9606","description":"Phosphatidylinositol 3-kinase (PI3K) activation complex which acts as a molecular switch maintaining cellular homeostasis by coordinating a broad range of essential processes, including glucose absorption, anabolic metabolism, cell growth, and survival. Once active, PIK3CA phosphorylates its substrate, PIP2 (ChEBI:18348), to generate PIP3 (ChEBI:16618), which in turn activates downstream signalling, including the AKT-mTOR pathway. This promotes cell survival by inhibiting pro-apoptotic factors, stimulate cell growth and proliferation through mTORC1 activation, and regulates metabolism by enhancing glucose uptake and glycolysis.\r\n\r\nMutations in MRAS and PIK3CA are implicated in various cancers.","predictedComplex":false,"interactors":[{"ac":"EBI-67189923","identifier":"P42336-PRO_0000088785","identifierLink":"https://www.uniprot.org/uniprotkb/P42336-PRO_0000088785/entry","name":"PIK3CA","description":"Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-968728","identifier":"O14807","identifierLink":"https://www.uniprot.org/uniprotkb/O14807/entry","name":"MRAS","description":"Ras-related protein M-Ras","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24070","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26696","complexName":"SMG5-SMG7, nonsense-mediated decay complex","organismName":"Homo sapiens; 9606","description":"The complex binds phosphorylated UPF1 (Q92900), the central NMD effector, with high affinity and recruits decay factors to the target mRNA through SMG7, thereby promoting target degradation via the nonsense-mediated decay (NMD) pathway, an mRNA quality control mechanism that detects and degrades aberrant transcripts containing premature translation termination codons (PTCs). Recognition of UPF1 by the complex enables the recruitment of protein phosphatase 2A (PPP2CA; P67775), which promotes UPF1 dephosphorylation, a step required for NMD progression.","predictedComplex":false,"interactors":[{"ac":"EBI-3400861","identifier":"Q9UPR3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UPR3/entry","name":"SMG5","description":"Nonsense-mediated mRNA decay factor SMG5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15696","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-719830","identifier":"Q92540","identifierLink":"https://www.uniprot.org/uniprotkb/Q92540/entry","name":"SMG7","description":"Nonsense-mediated mRNA decay factor SMG7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15696","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26697","complexName":"UPF core mRNA surveillance complex, UPF3A variant","organismName":"Homo sapiens; 9606","description":"Core effector and catalytic module in nonsense-mediated decay (NMD), an mRNA surveillance pathway that recognizes and degrades transcripts harboring premature termination codons (PTCs). Interaction with the exon-junction complex (EJC) enhances the efficiency of PTC recognition by coupling translation termination to UPF1 activation. This activation promotes the recruitment of mRNA decay factors that mediate deadenylation, decapping, and exonucleolytic degradation of aberrant transcripts.\r\n\r\nUPF3 paralogs, UPF3A/UPF3B act in a cross-regulatory feedback circuit, buffering NMD in response to environmental and genetic perturbations. UPF3A and UPF3B (Q9BZI7) competitively bind UPF2; UPF3B, activates NMD while UPF3A is generally a less potent activator of NMD, except in cells lacking UPF3B. This mechanism extends to cell type-specific control of NMD by being differentially engaged in the complex across cell types.","predictedComplex":false,"interactors":[{"ac":"EBI-372073","identifier":"Q9HAU5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HAU5/entry","name":"UPF2","description":"Regulator of nonsense transcripts 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12839","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373471","identifier":"Q92900","identifierLink":"https://www.uniprot.org/uniprotkb/Q92900/entry","name":"UPF1","description":"Regulator of nonsense transcripts 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10887","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-521530","identifier":"Q9H1J1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H1J1/entry","name":"UPF3A","description":"Regulator of nonsense transcripts 3A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13112","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26698","complexName":"UPF core mRNA surveillance complex, UPF3B variant","organismName":"Homo sapiens; 9606","description":"Core effector and catalytic module in nonsense-mediated decay (NMD), an mRNA surveillance pathway that recognizes and degrades transcripts harboring premature termination codons (PTCs). Interaction with the exon-junction complex (EJC) enhances the efficiency of PTC recognition by coupling translation termination to UPF1 activation. This activation promotes the recruitment of mRNA decay factors that mediate deadenylation, decapping, and exonucleolytic degradation of aberrant transcripts.\r\n\r\nUPF3 paralogs, UPF3A/UPF3B act in a cross-regulatory feedback circuit, buffering NMD in response to environmental and genetic perturbations. UPF3A (Q9H1J1) and UPF3B competitively bind UPF2; UPF3B, activates NMD while UPF3A is generally a less potent activator of NMD, except in cells lacking UPF3B. This mechanism extends to cell type-specific control of NMD by being differentially engaged in the complex across cell types.","predictedComplex":false,"interactors":[{"ac":"EBI-372073","identifier":"Q9HAU5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HAU5/entry","name":"UPF2","description":"Regulator of nonsense transcripts 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12839","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372780","identifier":"Q9BZI7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BZI7/entry","name":"UPF3B","description":"Regulator of nonsense transcripts 3B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13112","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373471","identifier":"Q92900","identifierLink":"https://www.uniprot.org/uniprotkb/Q92900/entry","name":"UPF1","description":"Regulator of nonsense transcripts 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10887","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26705","complexName":"AR-EFCAB6-PARK7 androgen regulating complex","organismName":"Homo sapiens; 9606","description":"Dihydrotestosterone regulating complex. EFCAB6 directly interacts with both PARK7 and the androgen receptor (AR) in a testosterone-dependent manner, facilitating the formation of a ternary complex in cells. In prostate cells, AR activity can be repressed by EFCAB6, which acts as a regulatory partner. PARK7 modulates AR activity in a hormone-dependent manner by binding to EFCAB6, and forming a complex that relieves this repression, thereby enhancing AR transactivation. Physiologically, this interaction allows cells to fine-tune AR signalling in response to hormonal cues, balancing gene expression programs involved in growth, differentiation, and cellular homeostasis.","predictedComplex":false,"interactors":[{"ac":"EBI-1164361","identifier":"Q99497","identifierLink":"https://www.uniprot.org/uniprotkb/Q99497/entry","name":"PARK7","description":"Parkinson disease protein 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48094","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12548860","identifier":"Q5THR3","identifierLink":"https://www.uniprot.org/uniprotkb/Q5THR3/entry","name":"EFCAB6","description":"EF-hand calcium-binding domain-containing protein 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20875","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-608057","identifier":"P10275","identifierLink":"https://www.uniprot.org/uniprotkb/P10275/entry","name":"AR","description":"Androgen receptor","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26706","complexName":"CLTA-CLTC-CKAP5-TACC3, mitotic spindle organizing complex","organismName":"Homo sapiens; 9606","description":"Complex stabilizes the mitotic spindle by crosslinking adjacent microtubules within kinetochore fibres, enhancing their mechanical integrity and suppressing microtubule-catastrophe events. This stabilization is essential for maintaining spindle architecture and strengthening kinetochore-microtubule attachments, thereby ensuring accurate chromosome segregation during mitosis.","predictedComplex":false,"interactors":[{"ac":"EBI-2554984","identifier":"Q9Y6A5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6A5/entry","name":"TACC3","description":"Transforming acidic coiled-coil-containing protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13924","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-310585","identifier":"Q14008","identifierLink":"https://www.uniprot.org/uniprotkb/Q14008/entry","name":"CKAP5","description":"Cytoskeleton-associated protein 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12609","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67190270","identifier":"CPX-26707","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-26707","name":"Clathrin, endocytosis-mediating complex, CLTA variant","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-26707","complexName":"Clathrin, endocytosis-mediating complex, CLTA variant","organismName":"Homo sapiens; 9606","description":"Building block of the polyhedral coat of coated pits and vesicles, forming a polymeric mechanical scaffold on the vesicle surface. Endocytosis-mediating complex; involved in the intracellular trafficking of a wide range of cargo, clathrin is a major route for internalization of many membrane lipids and proteins. Clathrin is also involved in various cellular and biological processes such as chromosomal segregation during mitosis and organelle biogenesis.\r\n\r\nWhile clathrin's heavy chain is well-conserved, light-chain specificity is said to be both tissue and specific-specific, and there is some suggestion that lattices formed from mixtures of clathrin with CLTA (CPX-26707) and CLTB have different assembly properties and are more efficient in membrane deformation compared to lattices with only one type of neuronal light chain.","predictedComplex":false,"interactors":[{"ac":"EBI-1171169","identifier":"P09496","identifierLink":"https://www.uniprot.org/uniprotkb/P09496/entry","name":"CLTA","description":"Clathrin light chain A","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-354967","identifier":"Q00610","identifierLink":"https://www.uniprot.org/uniprotkb/Q00610/entry","name":"CLTC","description":"Clathrin heavy chain 1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10292","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26708","complexName":"Clathrin, endocytosis-mediating complex, CLTA variant","organismName":"Bos taurus; 9913","description":"Building block of the polyhedral coat of coated pits and vesicles, forming a polymeric mechanical scaffold on the vesicle surface. \r\nEndocytosis-mediating complex; involved in the intracellular trafficking of a wide range of cargo, clathrin-coated vesicles are major carriers of lipids and proteins between intracellular membrane-bound compartments. Clathrin is also involved in various cellular and biological processes, such as chromosomal segregation during mitosis and organelle biogenesis.\r\n\r\nWhile clathrin's heavy chain is well-conserved, light-chain specificity is said to be both tissue and specific-specific, and there is some suggestion that lattices formed from mixtures of clathrin with CLTA (CPX-26707) and CLTB have different assembly properties and are more efficient in membrane deformation compared to lattices with only one type of neuronal light chain.","predictedComplex":false,"interactors":[{"ac":"EBI-448355","identifier":"P49951","identifierLink":"https://www.uniprot.org/uniprotkb/P49951/entry","name":"CLTC","description":"Clathrin heavy chain 1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR10292","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7374562","identifier":"P04973","identifierLink":"https://www.uniprot.org/uniprotkb/P04973/entry","name":"CLTA","description":"Clathrin light chain A","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR10639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26709","complexName":"Clathrin, endocytosis-mediating complex, CLTB variant","organismName":"Bos taurus; 9913","description":"Building block of the polyhedral coat of coated pits and vesicles, forming a polymeric mechanical scaffold on the vesicle surface. Endocytosis-mediating complex; involved in the intracellular trafficking of a wide range of cargo, clathrin-coated vesicles are major carriers of lipids and proteins between intracellular membrane-bound compartments. Clathrin is also involved in various cellular and biological processes, such as chromosomal segregation during mitosis and organelle biogenesis.\r\n\r\nWhile clathrin's heavy chain is well-conserved, light-chain specificity is said to be both tissue and specific-specific, and there is some suggestion that lattices formed from mixtures of clathrin with CLTA (CPX-26707) and CLTB have different assembly properties and are more efficient in membrane deformation compared to lattices with only one type of neuronal light chain.","predictedComplex":false,"interactors":[{"ac":"EBI-448355","identifier":"P49951","identifierLink":"https://www.uniprot.org/uniprotkb/P49951/entry","name":"CLTC","description":"Clathrin heavy chain 1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR10292","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7374462","identifier":"P04975","identifierLink":"https://www.uniprot.org/uniprotkb/P04975/entry","name":"CLTB","description":"Clathrin light chain B","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR10639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26710","complexName":"Clathrin, endocytosis-mediating complex, CLTB variant","organismName":"Homo sapiens; 9606","description":"Building block of the polyhedral coat of coated pits and vesicles, forming a polymeric mechanical scaffold on the vesicle surface. Endocytosis-mediating complex; involved in the intracellular trafficking of a wide range of cargo, clathrin is a major route for internalization of many membrane lipids and proteins. Clathrin is also involved in various cellular and biological processes such as chromosomal segregation during mitosis and organelle biogenesis.\r\n\r\nWhile clathrin's heavy chain is well-conserved, light-chain specificity is said to be both tissue and specific-specific, and there is some suggestion that lattices formed from mixtures of clathrin with CLTA (CPX-26707) and CLTB have different assembly properties and are more efficient in membrane deformation compared to lattices with only one type of neuronal light chain.","predictedComplex":false,"interactors":[{"ac":"EBI-354967","identifier":"Q00610","identifierLink":"https://www.uniprot.org/uniprotkb/Q00610/entry","name":"CLTC","description":"Clathrin heavy chain 1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10292","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-726598","identifier":"P09497","identifierLink":"https://www.uniprot.org/uniprotkb/P09497/entry","name":"CLTB","description":"Clathrin light chain B","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26711","complexName":"CLTB-CLTC-CKAP5-TACC3, mitotic spindle organizing complex","organismName":"Homo sapiens; 9606","description":"Complex stabilizes the mitotic spindle by crosslinking adjacent microtubules within kinetochore fibres, enhancing their mechanical integrity and suppressing microtubule-catastrophe events. This stabilization is essential for maintaining spindle architecture and strengthening kinetochore-microtubule attachments, thereby ensuring accurate chromosome segregation during mitosis.","predictedComplex":false,"interactors":[{"ac":"EBI-2554984","identifier":"Q9Y6A5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6A5/entry","name":"TACC3","description":"Transforming acidic coiled-coil-containing protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13924","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-310585","identifier":"Q14008","identifierLink":"https://www.uniprot.org/uniprotkb/Q14008/entry","name":"CKAP5","description":"Cytoskeleton-associated protein 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12609","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67191228","identifier":"CPX-26710","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-26710","name":"Clathrin, endocytosis-mediating complex, CLTB variant","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-26714","complexName":"Inhibitor of acetyltransferases complex","organismName":"Homo sapiens; 9606","description":"Histone acetylation suppressor complex which inhibits HAT/co-activator-mediated acetylation by masking core histones and nucleosomes. Plays a regulatory role in chromatin modification and serves as a distinct mechanism of transcriptional regulation.\r\n\r\nImpairment of histone acetylation is causally linked to the cognitive decline in Alzheimer's disease.","predictedComplex":false,"interactors":[{"ac":"EBI-359234","identifier":"P39687","identifierLink":"https://www.uniprot.org/uniprotkb/P39687/entry","name":"ANP32A","description":"Acidic leucine-rich nuclear phosphoprotein 32 family member A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5452920","identifier":"Q01105-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q01105-1/entry","name":"SET","description":"Protein SET","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-7481343","identifier":"Q01105-2","identifierLink":"https://www.uniprot.org/uniprotkb/Q01105-2/entry","name":"SET","description":"Protein SET","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-26715","complexName":"SET complex","organismName":"Homo sapiens; 9606","description":"Multifunctional chromatin-associated complex which translocates from the endoplasmic reticulum to the nucleus in response to superoxide generation by granzyme A to maintain cellular homeostasis. Regulates both genome stability and chromatin structure, and apoptotic pathways. Participates in nucleosome remodelling and transcriptional repression through the histone-chaperone and histone acetyltransferase inhibitory activities of SET and ANP32A, while HMGB2 contributes DNA-bending and chromatin-architectural functions that facilitate access to regulatory regions. APEX1 provides base-excision repair activity, and TREX1 contributes 3'->5' exonuclease function, enabling coordinated processing of damaged or mislocalized DNA. NME1 supports the complex through nucleotide homeostasis and metastasis-suppressor signalling roles. Implicated in genomic stress responses, autoimmunity, and oncogenic transformation.\r\n\r\nGranzymes released from cytotoxic cells are thought to shift the activity of the SET complex from a role in base-excision repair to one that promotes cell death. Under non-granzyme conditions, the complex may participate in DNA repair responses to oxidative damage. Granzymes drive apoptosis by blocking the complex’s base-excision repair activity and inducing widespread DNA damage.","predictedComplex":false,"interactors":[{"ac":"EBI-1048805","identifier":"P27695","identifierLink":"https://www.uniprot.org/uniprotkb/P27695/entry","name":"APEX1","description":"DNA repair nuclease/redox regulator APEX1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22748","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1057009","identifier":"P26583","identifierLink":"https://www.uniprot.org/uniprotkb/P26583/entry","name":"HMGB2","description":"High mobility group protein B2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48112","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16822261","identifier":"Q9NSU2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NSU2/entry","name":"TREX1","description":"Three-prime repair exonuclease 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13058","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359234","identifier":"P39687","identifierLink":"https://www.uniprot.org/uniprotkb/P39687/entry","name":"ANP32A","description":"Acidic leucine-rich nuclear phosphoprotein 32 family member A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-741141","identifier":"P15531","identifierLink":"https://www.uniprot.org/uniprotkb/P15531/entry","name":"NME1","description":"Nucleoside diphosphate kinase A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11349","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7481343","identifier":"Q01105-2","identifierLink":"https://www.uniprot.org/uniprotkb/Q01105-2/entry","name":"SET","description":"Protein SET","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6124","complexName":"TIM22 mitochondrial inner membrane twin-pore carrier translocase complex","organismName":"Homo sapiens; 9606","description":"Mediates the insertion and lateral release of multi-spanning membrane precursor proteins into the mitochondrial inner membrane in a membrane potential-dependent manner following translocation into the mitochondrion. Most mitochondrial proteins are synthesized in the cytosol, imported into mitochondria, sorted to one of the four sub-mitochondrial compartments, where they function, and attain their functional native conformation, which is often facilitated by assembly into the membrane or a multi-protein complex.","predictedComplex":false,"interactors":[{"ac":"EBI-10974729","identifier":"Q9BSF4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BSF4/entry","name":"TIMM29","description":"Mitochondrial import inner membrane translocase subunit Tim29","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21435","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1200370","identifier":"Q9Y5J7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5J7/entry","name":"TIMM9","description":"Mitochondrial import inner membrane translocase subunit Tim9","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13172","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1200382","identifier":"Q9Y5J6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5J6/entry","name":"TIMM10B","description":"Mitochondrial import inner membrane translocase subunit Tim10 B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13172","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1200391","identifier":"P62072","identifierLink":"https://www.uniprot.org/uniprotkb/P62072/entry","name":"TIMM10","description":"Mitochondrial import inner membrane translocase subunit Tim10","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11038","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1200494","identifier":"Q9Y584","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y584/entry","name":"TIMM22","description":"Mitochondrial import inner membrane translocase subunit Tim22","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14110","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2269837","identifier":"Q53H12","identifierLink":"https://www.uniprot.org/uniprotkb/Q53H12/entry","name":"AGK","description":"Acylglycerol kinase, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12358","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26719","complexName":"SHOC1-SPO16-TEX11, meiotic recombination facilitating complex","organismName":"Homo sapiens; 9606","description":"Plays a key role in facilitating meiotic recombination by binding and stabilizing early recombination intermediates. Required for the elongation of the synaptonemal complex (CPX-2461).\r\n\r\nLoss-of-function mutations result in defects in the formation of crossovers and the synaptonemal complex, leading to zipper-like structures between homologous pairs and causing meiotic arrest, chromosome mis-segregation, and infertility.","predictedComplex":false,"interactors":[{"ac":"EBI-2836330","identifier":"Q5VXU9","identifierLink":"https://www.uniprot.org/uniprotkb/Q5VXU9/entry","name":"SHOC1","description":"Protein shortage in chiasmata 1 ortholog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR35668","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-54698213","identifier":"Q5VVC0","identifierLink":"https://www.uniprot.org/uniprotkb/Q5VVC0/entry","name":"SPO16","description":"Protein SPO16 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31408","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742397","identifier":"Q8IYF3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IYF3/entry","name":"TEX11","description":"Testis-expressed protein 11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26720","complexName":"M1AP-SHOC1-SPO16-TEX11, male-linked meiotic recombination facilitating complex","organismName":"Homo sapiens; 9606","description":"Complex promotes crossover formation and meiotic progression in males.\r\n\r\nDisruption of M1AP leads to a reduced number of recombination intermediates and class I crossover which in turn results in meiotic metaphase I arrest and impairs male fertility; indeed, loss-of-function of any of the complex components leads to meiotic arrest and male infertility.","predictedComplex":false,"interactors":[{"ac":"EBI-67203231","identifier":"CPX-26719","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-26719","name":"SHOC1-SPO16-TEX11, meiotic recombination facilitating complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-748182","identifier":"Q8TC57","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TC57/entry","name":"M1AP","description":"Meiosis 1 arrest protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28642","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26721","complexName":"G3BP1-USP10, deubiquitinase complex","organismName":"Homo sapiens; 9606","description":"Deubiquitinase complex with a key role in the ribosome-associated quality control (RQC) pathway. USP10 plays a key role in regulating the ubiquitylation of the ribosomal proteins RPS2 (P15880) and RPS3 (P23396), with prolonged ubiquitylation of RPS2/RPS3 driving the selective degradation of 40S ribosomal proteins through a pathway that is independent of canonical autophagy. \r\n\r\nThe complex also plays a role in stress granule (SG) regulation. The complex suppresses SG formation, and can impair stress recovery, increasing apoptosis and exacerbating disease. USP10 acts as a negative regulator of stress-granule assembly by lowering G3BP1 valence, thereby preventing G3BP1 from undergoing liquid-liquid phase separation (LLPS) and forming stress granules.","predictedComplex":false,"interactors":[{"ac":"EBI-1047359","identifier":"Q13283","identifierLink":"https://www.uniprot.org/uniprotkb/Q13283/entry","name":"G3BP1","description":"Ras GTPase-activating protein-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10693","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2510389","identifier":"Q14694","identifierLink":"https://www.uniprot.org/uniprotkb/Q14694/entry","name":"USP10","description":"Ubiquitin carboxyl-terminal hydrolase 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24006","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26723","complexName":"G3BP2-USP10, deubiquitinase complex","organismName":"Homo sapiens; 9606","description":"Deubiquitinase complex with a key role in the ribosome-associated quality control (RQC) pathway. USP10 plays a key role in regulating the ubiquitylation of the ribosomal proteins RPS2 (P15880) and RPS3 (P23396), with prolonged ubiquitylation of RPS2/RPS3 driving the selective degradation of 40S ribosomal proteins through a pathway that is independent of canonical autophagy.  \r\n\r\nThe complex also plays a role in stress granule (SG) regulation. Complex suppresses SG formation, and can impair stress recovery, increasing apoptosis and exacerbating disease. USP10 acts as a negative regulator of stress-granule assembly by lowering G3BP2 valence, thereby preventing G3BP2 from undergoing liquid-liquid phase separation (LLPS) and forming stress granules. \r\n\r\nThe USP10-G3BP2 interaction is thought to inhibit apoptosis under stress conditions, including in prostate cancer. USP10 deubiquitinates and stabilizes G3BP2, which suppresses TP53 (P04637) activity and consequently promotes the AR (P10275) signalling pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-1044298","identifier":"Q9UN86","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UN86/entry","name":"G3BP2","description":"Ras GTPase-activating protein-binding protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10693","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2510389","identifier":"Q14694","identifierLink":"https://www.uniprot.org/uniprotkb/Q14694/entry","name":"USP10","description":"Ubiquitin carboxyl-terminal hydrolase 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24006","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26724","complexName":"Clathrin complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Building block of the polyhedral coat of coated pits and vesicles, forming a polymeric mechanical scaffold on the vesicle surface. Clathrin-coated  vesicles participate in selective protein  transport  processes from the plasma membrane and  the Golgi complex, including endocytosis, sorting of newly made lysosomal proteins, secretory granule formation and localization of certain Golgi membrane proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-2477461","identifier":"Q9USP6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9USP6/entry","name":"clc1","description":"Clathrin light chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-70796608","identifier":"Q10161","identifierLink":"https://www.uniprot.org/uniprotkb/Q10161/entry","name":"chc1","description":"Probable clathrin heavy chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10292","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26725","complexName":"Clathrin, endocytosis-mediating complex, CLTA-CLTB mixed lattice variant","organismName":"Bos taurus; 9913","description":"Building block of the polyhedral coat of coated pits and vesicles, forming a polymeric mechanical scaffold on the vesicle surface. \r\nEndocytosis-mediating complex; involved in the intracellular trafficking of a wide range of cargo, clathrin-coated vesicles are major carriers of lipids and proteins between intracellular membrane-bound compartments. Clathrin is also involved in various cellular and biological processes, such as chromosomal segregation during mitosis and organelle biogenesis.\r\n\r\nWhile clathrin's heavy chain is well-conserved, light-chain specificity is said to be both tissue and specific-specific, and there is some suggestion that lattices formed from mixtures of clathrin with CLTA (CPX-26707) and CLTB (CPX-26709) have different assembly properties and are more efficient in membrane deformation compared to lattices with only one type of neuronal light chain.","predictedComplex":false,"interactors":[{"ac":"EBI-448355","identifier":"P49951","identifierLink":"https://www.uniprot.org/uniprotkb/P49951/entry","name":"CLTC","description":"Clathrin heavy chain 1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR10292","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7374462","identifier":"P04975","identifierLink":"https://www.uniprot.org/uniprotkb/P04975/entry","name":"CLTB","description":"Clathrin light chain B","stochiometry":"minValue: 1, maxValue: 2","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR10639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7374562","identifier":"P04973","identifierLink":"https://www.uniprot.org/uniprotkb/P04973/entry","name":"CLTA","description":"Clathrin light chain A","stochiometry":"minValue: 1, maxValue: 2","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR10639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26726","complexName":"Clathrin, endocytosis-mediating complex, CLTA-CLTB mixed lattice variant","organismName":"Homo sapiens; 9606","description":"Building block of the polyhedral coat of coated pits and vesicles, forming a polymeric mechanical scaffold on the vesicle surface. Endocytosis-mediating complex; involved in the intracellular trafficking of a wide range of cargo, clathrin is a major route for internalization of many membrane lipids and proteins. Clathrin is also involved in various cellular and biological processes such as chromosomal segregation during mitosis and organelle biogenesis.\r\n\r\nWhile clathrin's heavy chain is well-conserved, light-chain specificity is said to be both tissue and specific-specific, and there is some suggestion that lattices formed from mixtures of clathrin with CLTA (CPX-26707) and CLTB (CPX-26710) have different assembly properties and are more efficient in membrane deformation compared to lattices with only one type of neuronal light chain.","predictedComplex":false,"interactors":[{"ac":"EBI-1171169","identifier":"P09496","identifierLink":"https://www.uniprot.org/uniprotkb/P09496/entry","name":"CLTA","description":"Clathrin light chain A","stochiometry":"minValue: 1, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-354967","identifier":"Q00610","identifierLink":"https://www.uniprot.org/uniprotkb/Q00610/entry","name":"CLTC","description":"Clathrin heavy chain 1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10292","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-726598","identifier":"P09497","identifierLink":"https://www.uniprot.org/uniprotkb/P09497/entry","name":"CLTB","description":"Clathrin light chain B","stochiometry":"minValue: 1, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26727","complexName":"CHL1-CTF4 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Functions as a replisome-organizing module that coordinates DNA replication fork progression with sister chromatid cohesion establishment during S phase. CTF4 acts as a replisomal interaction hub, recruiting the CHL1 helicase to the CMG helicase (CPX-297) via a conserved binding motif shared with GINS (CPX-1641) and DNA polymerase-alpha. This coupling links DNA unwinding to lagging-strand priming, promoting efficient replication, particularly under conditions of nucleotide depletion.","predictedComplex":false,"interactors":[{"ac":"EBI-4600","identifier":"P22516","identifierLink":"https://www.uniprot.org/uniprotkb/P22516/entry","name":"CHL1","description":"ATP-dependent DNA helicase CHL1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11472","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5209","identifier":"Q01454","identifierLink":"https://www.uniprot.org/uniprotkb/Q01454/entry","name":"CTF4","description":"DNA polymerase alpha-binding protein","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26728","complexName":"SET3C histone deacetylase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Histone deacetylase complex important in regulating gene induction and repression. Required to repress early/middle sporulation genes during meiosis.","predictedComplex":false,"interactors":[{"ac":"EBI-2477865","identifier":"O94640","identifierLink":"https://www.uniprot.org/uniprotkb/O94640/entry","name":"sir2","description":"NAD-dependent histone deacetylase sir2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11085","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32717409","identifier":"CHEBI:57540","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57540","name":"nad(1-)","description":"NAD(1-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-70796682","identifier":"Q10362","identifierLink":"https://www.uniprot.org/uniprotkb/Q10362/entry","name":"set3","description":"SET domain-containing protein 3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR46462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-70796707","identifier":"O74845","identifierLink":"https://www.uniprot.org/uniprotkb/O74845/entry","name":"hif2","description":"Set3 complex subunit hif2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR22846","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-70796725","identifier":"Q10369","identifierLink":"https://www.uniprot.org/uniprotkb/Q10369/entry","name":"ydbj","description":"Uncharacterized protein C22E12.19","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26729","complexName":"SED5-SLY1 SNARE chaperone complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SNARE regulatory complex which controls vesicle-mediated membrane trafficking between the endoplasmic reticulum (ER) and Golgi apparatus in yeast. SLY1 binds directly to the N-terminal region of SED5, an essential syntaxin, stabilizing it and facilitating the assembly of SNARE complexes that drive membrane fusion.  The SLY1 N-lobe is anchored to SED5 on the target organelle while the SlLY1 regulatory loop binds the incoming vesicle’s lipid bilayer This interaction enhances the specificity and efficiency of vesicle docking and fusion, thereby ensuring proper intracellular transport and maintaining cellular organization.","predictedComplex":false,"interactors":[{"ac":"EBI-16930","identifier":"Q01590","identifierLink":"https://www.uniprot.org/uniprotkb/Q01590/entry","name":"SED5","description":"Integral membrane protein SED5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17387","identifier":"P22213","identifierLink":"https://www.uniprot.org/uniprotkb/P22213/entry","name":"SLY1","description":"Protein SLY1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11679","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26730","complexName":"Cdr2 medial cortical node complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Acts to control cell division by regulating cell surface area and thus size-dependent control of entry into mitosis. Forms punctate structures (nodes) on the medial cortex to regulate the wee1 protein kinase  which phosphorylates and inhibits Cdk1, preventing mitotic entry during interphase.","predictedComplex":false,"interactors":[{"ac":"EBI-15683908","identifier":"P07527","identifierLink":"https://www.uniprot.org/uniprotkb/P07527/entry","name":"wee1","description":"Mitosis inhibitor protein kinase wee1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11042","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4319869","identifier":"P87050","identifierLink":"https://www.uniprot.org/uniprotkb/P87050/entry","name":"cdr2","description":"Mitosis inducer protein kinase cdr2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR24343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-70798328","identifier":"P07334","identifierLink":"https://www.uniprot.org/uniprotkb/P07334/entry","name":"cdr1","description":"Mitosis inducer protein kinase cdr1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR24343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-70800267","identifier":"Q9Y7Z2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y7Z2/entry","name":"arf6","description":"ADP-ribosylation factor 6","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11711","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26731","complexName":"ERG25-ERG26-ERG27 ergosterol biosynthesis complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Ergosterol biosynthesis complex. The ERG25-ERG26-ERG27 multienzyme complex is formed primarily in the endoplasmic reticulum (ER) during the late stages of the ergosterol synthesis pathway, which involves the conversion of lanosterol to zymosterol through a series of demethylation, reduction, and desaturation reactions. Ergosterol is essential for mitochondrial DNA maintenance, and is also an immunoactive lipid which induces host cell pyroptosis, a necrotic and inflammatory programmed cell death. Ergosterol abundance is critical for yeast stress adaptation, including hypoxic and iron deficiency responses in yeast.\r\n\r\nLoss-of-function of complex components within the late pathway is thought to be lethal and lead to sterol auxotrophy.","predictedComplex":false,"interactors":[{"ac":"EBI-38132","identifier":"Q12452","identifierLink":"https://www.uniprot.org/uniprotkb/Q12452/entry","name":"ERG27","description":"3-keto-steroid reductase ERG27","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43647","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6506","identifier":"P53045","identifierLink":"https://www.uniprot.org/uniprotkb/P53045/entry","name":"ERG25","description":"C-4 methylsterol oxidase ERG25","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11863","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6514","identifier":"P53199","identifierLink":"https://www.uniprot.org/uniprotkb/P53199/entry","name":"ERG26","description":"Sterol-4-alpha-carboxylate 3-dehydrogenase ERG26, decarboxylating","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10366","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9641","complexName":"Mitochondrial respiratory chain complex IV","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Terminal oxidase of the electron transport chain in mitochondria. It accepts electrons from cytochrome c to reduce the oxygen to water and pumps two protons from the matrix side to the intermembrane space. Electrons originating from reduced cytochrome c in the intermembrane space  are transferred via the dinuclear copper center of mt:CoII and heme A of mt:CoI to the active site in mt:CoI, a binuclear center formed by heme A3  and a second copper atom. The binuclear center  reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the intermembrane space and 4 protons from the mitochondrial matrix.","predictedComplex":false,"interactors":[{"ac":"EBI-12592690","identifier":"CHEBI:23378","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:23378","name":"copper cation","description":"copper cation","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-55030863","identifier":"P21534","identifierLink":"https://www.uniprot.org/uniprotkb/P21534/entry","name":"cox2","description":"Cytochrome c oxidase subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR22888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55030887","identifier":"P07657","identifierLink":"https://www.uniprot.org/uniprotkb/P07657/entry","name":"cox1","description":"Cytochrome c oxidase subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10422","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55030907","identifier":"O74471","identifierLink":"https://www.uniprot.org/uniprotkb/O74471/entry","name":"cox13","description":"Cytochrome c oxidase subunit 13, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11504","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55030924","identifier":"O94581","identifierLink":"https://www.uniprot.org/uniprotkb/O94581/entry","name":"cox12","description":"Cytochrome c oxidase subunit 12, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR46281","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55030955","identifier":"Q9P4W1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P4W1/entry","name":"cox8","description":"Cytochrome c oxidase polypeptide VIII, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13313","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55030970","identifier":"G2TRP5","identifierLink":"https://www.uniprot.org/uniprotkb/G2TRP5/entry","name":"cox7","description":"Cytochrome c oxidase subunit 7","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-55030984","identifier":"O74988","identifierLink":"https://www.uniprot.org/uniprotkb/O74988/entry","name":"cox5","description":"Cytochrome c oxidase polypeptide 5, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10707","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55030999","identifier":"Q9UTF6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UTF6/entry","name":"cox6","description":"Cytochrome c oxidase subunit 6, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR14200","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55031015","identifier":"P14575","identifierLink":"https://www.uniprot.org/uniprotkb/P14575/entry","name":"cox3","description":"Cytochrome c oxidase subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11403","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55031030","identifier":"O94705","identifierLink":"https://www.uniprot.org/uniprotkb/O94705/entry","name":"cox9","description":"Cytochrome c oxidase subunit 9, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-7593610","identifier":"P79010","identifierLink":"https://www.uniprot.org/uniprotkb/P79010/entry","name":"cox4","description":"Cytochrome c oxidase subunit 4, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10122","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26732","complexName":"Myosin class II complex, MYL1-MYL2-MYH1 variant","organismName":"Homo sapiens; 9606","description":"Building block of the fast skeletal muscle class II myosin bipolar filament, responsible for ATP-dependent sliding of actin filaments during muscle contraction. Forms a hexameric motor complex composed of two myosin heavy chains (MHC) associated with two essential light chains (MLC) and two regulatory light chains (MLC-2). The myosin heavy chain motor domains mediate ATP-dependent interaction with F-actin, while the neck region, stabilized by bound light chains, acts as a rigid lever arm that amplifies conformational changes within the motor domain into a large mechanical power stroke, generating force and directed movement along actin filaments.","predictedComplex":false,"interactors":[{"ac":"EBI-366238","identifier":"P12882","identifierLink":"https://www.uniprot.org/uniprotkb/P12882/entry","name":"MYH1","description":"Myosin-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5653459","identifier":"P05976","identifierLink":"https://www.uniprot.org/uniprotkb/P05976/entry","name":"MYL1","description":"Myosin light chain 1/3, skeletal muscle isoform","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-725770","identifier":"P10916","identifierLink":"https://www.uniprot.org/uniprotkb/P10916/entry","name":"MYL2","description":"Myosin regulatory light chain 2, ventricular/cardiac muscle isoform","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23049","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26733","complexName":"Myosin class II complex, MYH11-MYL6-MYL11 variant","organismName":"Gallus gallus; 9031","description":"Building block of conventional class II myosin motor complex which forms the basic units of contraction in smooth muscle myosin. Forms a hexameric motor complex composed of two myosin heavy chains (MHC) associated with two essential light chains (MLC) and two regulatory light chains (MLC-2) which couples ATP hydrolysis in the myosin motor domain to directed sliding of actin filaments. The essential and regulatory light chains bound to the myosin neck stabilize the lever arm and modulate force transduction, enabling the heavy chain to generate contractile force in smooth muscle cells.","predictedComplex":false,"interactors":[{"ac":"EBI-1027073","identifier":"P02607","identifierLink":"https://www.uniprot.org/uniprotkb/P02607/entry","name":"MYL6","description":"Myosin light polypeptide 6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[{"identifier":"PTHR23048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1027098","identifier":"P10587","identifierLink":"https://www.uniprot.org/uniprotkb/P10587/entry","name":"MYH11","description":"Myosin-11","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[{"identifier":"PTHR45615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-70804568","identifier":"P02609","identifierLink":"https://www.uniprot.org/uniprotkb/P02609/entry","name":"MYL11","description":"Myosin regulatory light chain 11","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[{"identifier":"PTHR23049","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26734","complexName":"Inward rectifier potassium channel 13 complex","organismName":"Homo sapiens; 9606","description":"Inward rectifier potassium channel that mediates potassium ion flux across the plasma membrane. Contributes to the maintenance of membrane potential and potassium homeostasis, particularly in epithelial and retinal cells. Displays weak inward rectification, low single-channel conductance, and reduced sensitivity to classical inward rectifier blockers compared with other Kir channels. Plays an essential role in epithelial potassium recycling and in maintaining the ionic environment of the retina; loss of channel function disrupts retinal physiology and leads to inherited retinal degenerative disorders. Throught to be particularly abundant in the Purkinje cell layer of the cerebellum and pyramidal cells of the hippocampus.","predictedComplex":false,"interactors":[{"ac":"EBI-70807649","identifier":"O60928","identifierLink":"https://www.uniprot.org/uniprotkb/O60928/entry","name":"KCNJ13","description":"Inward rectifier potassium channel 13","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-26736","complexName":"Eukaryotic translation initiation factor 2B complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Plays a critical regulatory role in eukaryotic translation initiation. Acts as a guanine nucleotide exchange factor (GEF) catalyzing the exchange of GDP on eIF2-GDP for GTP, thus reactivating eIF2 and allowing subsequent rounds of translation initiation. This activity is inhibited by the when phosphorylated eIF2 (alpha subunit) binds to eIF2B. Phosphorylation of eIF2 occurs in response to nutrient starvation and thus prevents further protein synthesis. eIF2B also acts as a GDP dissociation inhibitor (GDI) displacement factor that can recruit eIF2 from the eIF2.GDP/eIF5 GDI complex prior to GEF action.","predictedComplex":false,"interactors":[{"ac":"EBI-16198490","identifier":"Q9UT76","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UT76/entry","name":"tif222","description":"Translation initiation factor eIF2B subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR45859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16198511","identifier":"P56288","identifierLink":"https://www.uniprot.org/uniprotkb/P56288/entry","name":"tif223","description":"Translation initiation factor eIF2B subunit gamma","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR45989","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16198531","identifier":"Q09924","identifierLink":"https://www.uniprot.org/uniprotkb/Q09924/entry","name":"tif224","description":"Translation initiation factor eIF2B subunit delta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10233","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16198550","identifier":"P56287","identifierLink":"https://www.uniprot.org/uniprotkb/P56287/entry","name":"tif225","description":"Translation initiation factor eIF2B subunit epsilon","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR45887","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1793476","identifier":"Q9USP0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9USP0/entry","name":"gcn3","description":"Translation initiation factor eIF2B subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR45860","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8609","complexName":"GluK1-GluK2-GluK5 glutamate ionotropic kainate-type receptor complex","organismName":"Rattus norvegicus; 10116","description":"An ionotropic glutamate receptor which localizes either post-synaptically to drive synaptic depolarization or pre-synaptically to regulate neurotransmitter release. Belonging to the kainate-type glutamate receptors (KARs) sub-family, GluKs are ligand-gated cation channels activated by the neurotransmitter l-glutamate. GluKs play complex roles in neural development and CNS function.","predictedComplex":false,"interactors":[{"ac":"EBI-15612757","identifier":"P22756","identifierLink":"https://www.uniprot.org/uniprotkb/P22756/entry","name":"Grik1","description":"Glutamate receptor ionotropic, kainate 1","stochiometry":"minValue: 1, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48421334","identifier":"Q63273","identifierLink":"https://www.uniprot.org/uniprotkb/Q63273/entry","name":"Grik5","description":"Glutamate receptor ionotropic, kainate 5","stochiometry":"minValue: 1, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7809795","identifier":"P42260","identifierLink":"https://www.uniprot.org/uniprotkb/P42260/entry","name":"Grik2","description":"Glutamate receptor ionotropic, kainate 2","stochiometry":"minValue: 1, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8610","complexName":"GluK1-GluK2-GluK3-GluK5 glutamate ionotropic kainate-type receptor complex","organismName":"Rattus norvegicus; 10116","description":"An ionotropic glutamate receptor which localizes either post-synaptically to drive synaptic depolarization or pre-synaptically to regulate neurotransmitter release. Belonging to the kainate-type glutamate receptors (KARs) sub-family, GluKs are ligand-gated cation channels activated by the neurotransmitter l-glutamate. GluKs play complex roles in neural development and CNS function.","predictedComplex":false,"interactors":[{"ac":"EBI-15612757","identifier":"P22756","identifierLink":"https://www.uniprot.org/uniprotkb/P22756/entry","name":"Grik1","description":"Glutamate receptor ionotropic, kainate 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48420651","identifier":"P42264","identifierLink":"https://www.uniprot.org/uniprotkb/P42264/entry","name":"Grik3","description":"Glutamate receptor ionotropic, kainate 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48421334","identifier":"Q63273","identifierLink":"https://www.uniprot.org/uniprotkb/Q63273/entry","name":"Grik5","description":"Glutamate receptor ionotropic, kainate 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7809795","identifier":"P42260","identifierLink":"https://www.uniprot.org/uniprotkb/P42260/entry","name":"Grik2","description":"Glutamate receptor ionotropic, kainate 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8611","complexName":"GluK3 glutamate ionotropic kainate-type receptor complex","organismName":"Rattus norvegicus; 10116","description":"An ionotropic glutamate receptor which localizes either post-synaptically to drive synaptic depolarization or pre-synaptically to regulate neurotransmitter release. Belonging to the kainate-type glutamate receptors (KARs) sub-family, GluKs are ligand-gated cation channels activated by the neurotransmitter l-glutamate. GluKs play complex roles in neural development and CNS function.","predictedComplex":false,"interactors":[{"ac":"EBI-48420651","identifier":"P42264","identifierLink":"https://www.uniprot.org/uniprotkb/P42264/entry","name":"Grik3","description":"Glutamate receptor ionotropic, kainate 3","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8612","complexName":"GluK1-GluK5 glutamate ionotropic kainate-type receptor complex","organismName":"Rattus norvegicus; 10116","description":"An ionotropic glutamate receptor which localizes either post-synaptically to drive synaptic depolarization or pre-synaptically to regulate neurotransmitter release. Belonging to the kainate-type glutamate receptors (KARs) sub-family, GluKs are ligand-gated cation channels activated by the neurotransmitter l-glutamate. GluKs play complex roles in neural development and CNS function.\r\n\r\nGluKs 1-3 can assemble in any combination of homo- or heterotetrameic structures to form functions ion channels but GluKs 4-5  are obligate heterotetramers which require GluKs 1-3 to reach the neuronal surface.","predictedComplex":false,"interactors":[{"ac":"EBI-15612757","identifier":"P22756","identifierLink":"https://www.uniprot.org/uniprotkb/P22756/entry","name":"Grik1","description":"Glutamate receptor ionotropic, kainate 1","stochiometry":"minValue: 2, maxValue: 3","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48421334","identifier":"Q63273","identifierLink":"https://www.uniprot.org/uniprotkb/Q63273/entry","name":"Grik5","description":"Glutamate receptor ionotropic, kainate 5","stochiometry":"minValue: 1, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8613","complexName":"GluK1-GluK3 glutamate ionotropic kainate-type receptor complex","organismName":"Rattus norvegicus; 10116","description":"An ionotropic glutamate receptor which localizes either post-synaptically to drive synaptic depolarization or pre-synaptically to regulate neurotransmitter release. Belonging to the kainate-type glutamate receptors (KARs) sub-family, GluKs are ligand-gated cation channels activated by the neurotransmitter l-glutamate. GluKs play complex roles in neural development and CNS function.","predictedComplex":false,"interactors":[{"ac":"EBI-15612757","identifier":"P22756","identifierLink":"https://www.uniprot.org/uniprotkb/P22756/entry","name":"Grik1","description":"Glutamate receptor ionotropic, kainate 1","stochiometry":"minValue: 1, maxValue: 3","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48420651","identifier":"P42264","identifierLink":"https://www.uniprot.org/uniprotkb/P42264/entry","name":"Grik3","description":"Glutamate receptor ionotropic, kainate 3","stochiometry":"minValue: 1, maxValue: 3","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8614","complexName":"GluK2-GluK3 glutamate ionotropic kainate-type receptor complex","organismName":"Rattus norvegicus; 10116","description":"An ionotropic glutamate receptor which localizes either post-synaptically to drive synaptic depolarization or pre-synaptically to regulate neurotransmitter release. Belonging to the kainate-type glutamate receptors (KARs) sub-family, GluKs are ligand-gated cation channels activated by the neurotransmitter l-glutamate. GluKs play complex roles in neural development and CNS function.","predictedComplex":false,"interactors":[{"ac":"EBI-48420651","identifier":"P42264","identifierLink":"https://www.uniprot.org/uniprotkb/P42264/entry","name":"Grik3","description":"Glutamate receptor ionotropic, kainate 3","stochiometry":"minValue: 1, maxValue: 3","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7809795","identifier":"P42260","identifierLink":"https://www.uniprot.org/uniprotkb/P42260/entry","name":"Grik2","description":"Glutamate receptor ionotropic, kainate 2","stochiometry":"minValue: 1, maxValue: 3","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8615","complexName":"GluK3-GluK5 glutamate ionotropic kainate-type receptor complex","organismName":"Rattus norvegicus; 10116","description":"An ionotropic glutamate receptor which localizes either post-synaptically to drive synaptic depolarization or pre-synaptically to regulate neurotransmitter release. Belonging to the kainate-type glutamate receptors (KARs) sub-family, GluKs are ligand-gated cation channels activated by the neurotransmitter l-glutamate. GluKs play complex roles in neural development and CNS function.","predictedComplex":false,"interactors":[{"ac":"EBI-48420651","identifier":"P42264","identifierLink":"https://www.uniprot.org/uniprotkb/P42264/entry","name":"Grik3","description":"Glutamate receptor ionotropic, kainate 3","stochiometry":"minValue: 1, maxValue: 3","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48421334","identifier":"Q63273","identifierLink":"https://www.uniprot.org/uniprotkb/Q63273/entry","name":"Grik5","description":"Glutamate receptor ionotropic, kainate 5","stochiometry":"minValue: 1, maxValue: 3","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8616","complexName":"GluK1 glutamate ionotropic kainate-type receptor complex","organismName":"Rattus norvegicus; 10116","description":"An ionotropic glutamate receptor which localizes either post-synaptically to drive synaptic depolarization or pre-synaptically to regulate neurotransmitter release. Belonging to the kainate-type glutamate receptors (KARs) sub-family, GluKs are ligand-gated cation channels activated by the neurotransmitter L-glutamate. GluKs play complex roles in neural development and CNS function.","predictedComplex":false,"interactors":[{"ac":"EBI-15612757","identifier":"P22756","identifierLink":"https://www.uniprot.org/uniprotkb/P22756/entry","name":"Grik1","description":"Glutamate receptor ionotropic, kainate 1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8618","complexName":"Mitochondrial proton-transporting ATP synthase complex","organismName":"Drosophila melanogaster; 7227","description":"Acts to convert the energy of oxidation-reduction reactions of the electron transport chain (respiration) to the phosphorylation of ADP. The synthesis of ATP is coupled to the respiratory chain via the proton potential. The ATP synthase is a molecular motor composed of two separable parts: F1 and Fo. The F1 portion contains the catalytic sites for ATP synthesis and protrudes into the mitochondrial matrix. Fo forms a proton turbine that is embedded in the inner membrane and connected to the rotor of F1. The flux of protons flowing down a potential gradient powers the rotation of the rotor driving the synthesis of ATP. Thus, the flow of protons though Fo is coupled to the synthesis of ATP. May also play a role in Ca(2+)-induced Ca(2+) release from the mitochondria.","predictedComplex":false,"interactors":[{"ac":"EBI-114220","identifier":"Q9W141","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W141/entry","name":"ATPsynF","description":"Putative ATP synthase subunit f, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13080","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-119937","identifier":"O77134","identifierLink":"https://www.uniprot.org/uniprotkb/O77134/entry","name":"ATPsynE","description":"ATP synthase F(0) complex subunit e, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12427","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-123738","identifier":"Q94516","identifierLink":"https://www.uniprot.org/uniprotkb/Q94516/entry","name":"ATPsynB","description":"ATP synthase subunit b, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 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The synthesis of ATP is coupled to the respiratory chain via the proton potential. The ATP synthase is a molecular motor composed of two separable parts: F1 and Fo. The F1 portion contains the catalytic sites for ATP synthesis and protrudes into the mitochondrial matrix. Fo forms a proton turbine that is embedded in the inner membrane and connected to the rotor of F1. The flux of protons flowing down a potential gradient powers the rotation of the rotor driving the synthesis of ATP. Thus, the flow of protons though Fo is coupled to the synthesis of ATP. May also play a role in Ca(2+)-induced Ca(2+) release from the mitochondria.","predictedComplex":false,"interactors":[{"ac":"EBI-113067","identifier":"Q9VR93","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VR93/entry","name":"atpmk","description":"ATP synthase membrane subunit K, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR34038","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-114220","identifier":"Q9W141","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W141/entry","name":"ATPsynF","description":"Putative ATP synthase subunit f, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13080","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-119447","identifier":"Q9VH24","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VH24/entry","name":"ATPsynepsilonL","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 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It accepts electrons from cytochrome c to reduce the oxygen to water and pumps two protons from the matrix side to the intermembrane space. Electrons originating from reduced cytochrome c in the intermembrane space  are transferred via the dinuclear copper center of mt:CoII and heme A of mt:CoI to the active site in mt:CoI, a binuclear center formed by heme A3  and a second copper atom.. The binuclear center  reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the intermembrane space and 4 protons from the mitochondrial matrix.","predictedComplex":false,"interactors":[{"ac":"EBI-105449","identifier":"Q9VHS2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VHS2/entry","name":"COX7A","description":"Cytochrome c oxidase subunit 7A, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10510","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-125326","identifier":"Q9VIQ8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VIQ8/entry","name":"COX4","description":"Cytochrome c oxidase subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10707","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12592690","identifier":"CHEBI:23378","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:23378","name":"copper cation","description":"copper cation","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; 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It accepts electrons from cytochrome c to reduce the oxygen to water and pumps two protons from the matrix side to the intermembrane space. Electrons originating from reduced cytochrome c in the intermembrane space  are transferred via the dinuclear copper center of mt:CoII and heme A of mt:CoI to the active site in mt:CoI, a binuclear center formed by heme A3  and a second copper atom.. The binuclear center  reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the intermembrane space and 4 protons from the mitochondrial matrix.","predictedComplex":false,"interactors":[{"ac":"EBI-100442","identifier":"Q8T4H8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8T4H8/entry","name":"COX4L","description":"Cytochrome c oxidase subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10707","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12592690","identifier":"CHEBI:23378","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:23378","name":"copper cation","description":"copper cation","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-143553","identifier":"Q9VP19","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VP19/entry","name":"COX8","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR16717","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-150838","identifier":"Q8SYJ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8SYJ2/entry","name":"ND-MLRQ","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14256","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-155593","identifier":"Q9VWD1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VWD1/entry","name":"COX6B","description":"Cytochrome c oxidase subunit","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11387","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-180123","identifier":"Q94514","identifierLink":"https://www.uniprot.org/uniprotkb/Q94514/entry","name":"COX5A","description":"Cytochrome c oxidase subunit 5A, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14200","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26812698","identifier":"Q4QPY7","identifierLink":"https://www.uniprot.org/uniprotkb/Q4QPY7/entry","name":"COX6AL","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11504","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48426154","identifier":"Q9VVG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVG5/entry","name":"COX7B","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22133","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48426194","identifier":"P00399","identifierLink":"https://www.uniprot.org/uniprotkb/P00399/entry","name":"mt:CoI","description":"Cytochrome c oxidase subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10422","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48426223","identifier":"P00408","identifierLink":"https://www.uniprot.org/uniprotkb/P00408/entry","name":"mt:CoII","description":"Cytochrome c oxidase subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48426249","identifier":"P00417","identifierLink":"https://www.uniprot.org/uniprotkb/P00417/entry","name":"mt:CoIII","description":"Cytochrome c oxidase subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11403","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48426379","identifier":"Q9VVU8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVU8/entry","name":"COX6AL2","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11504","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48426399","identifier":"X2JD93","identifierLink":"https://www.uniprot.org/uniprotkb/X2JD93/entry","name":"COX6CL","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR48416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48426413","identifier":"Q9VHR9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VHR9/entry","name":"COX7AL","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10510","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48426436","identifier":"A0A0B4LF36","identifierLink":"https://www.uniprot.org/uniprotkb/A0A0B4LF36/entry","name":"COX7CL","description":"Cytochrome c oxidase subunit 7C, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13313","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50432544","identifier":"Q9VMB8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VMB8/entry","name":"COX5BL","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10122","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-8622","complexName":"Mitochondrial respiratory chain complex II","organismName":"Drosophila melanogaster; 7227","description":"Key role in aerobic respiration, in which mitochondrial enzymes accept electrons from electron carriers reduced in glycolysis and the tricarboxylic acid cycle. Catalyzes the oxidation of succinate to fumarate as part of tricarboxylic acid cycle and and transfers the electrons to coenzyme Q of the respiratory chain to form ubiquinol. Under most conditions the electrons are used to reduce oxygen, allowing ATP synthesis. SDHA and SDHB form the catalytic dimer that is anchored to the matrix surface of the mitochondrial inner membrane by SDHC and SDHD, integral membrane proteins of the membrane dimer. Electrons flow from succinate to the FAD, and sequentially through the [2Fe:2S], the [4Fe:4S], and the [3Fe:4S] clusters. From there, electrons enter the membrane dimer which contains a b-type heme and the active site for ubiquinone reduction.","predictedComplex":false,"interactors":[{"ac":"EBI-103859","identifier":"Q9VGS3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VGS3/entry","name":"SdhC","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10978","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11297461","identifier":"CHEBI:21137","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:21137","name":"tri-mu-sulfido-mu3-sulfido-triiron","description":"tri-mu-sulfido-mu3-sulfido-triiron","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-136047","identifier":"P21914","identifierLink":"https://www.uniprot.org/uniprotkb/P21914/entry","name":"SdhB","description":"Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11921","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-152453","identifier":"Q94523","identifierLink":"https://www.uniprot.org/uniprotkb/Q94523/entry","name":"SdhA","description":"Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11632","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-161866","identifier":"Q9VCI5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VCI5/entry","name":"SdhD","description":"Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13337","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-46449825","identifier":"CHEBI:190135","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:190135","name":"di-mu-sulfido-diiron","description":"di-mu-sulfido-diiron","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-8623","complexName":"miRNA RISC complex, TNRC6A variant","organismName":"Homo sapiens; 9606","description":"Incorporates one strand of a micro RNA (miRNA) and uses this as a template for recognizing complementary mRNA. During strand selection, one of the miRNA strands is selected and anchored into the AGO protein, while the other strand is unwound and targeted for degradation, a process which involved a nick created by AGO2 to which the C3PO complex (CPX-890) is recruited. Base-pairing complementation by the guide strand binds the RISC complex to its target mRNA. Binding to a perfectly complementary mRNA generally results in silencing due to endonucleolytic cleavage of the mRNA specifically by AGO2. Binding of RISC to a partially complementary mRNA results in silencing through inhibition of translation which does not require endonuclease activity.The TNRC6 scaffolding protein acts to recruit other proteins which repress the translation of the target mRNA and accelerate mRNA decay.","predictedComplex":false,"interactors":[{"ac":"EBI-2267883","identifier":"Q9H9G7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H9G7/entry","name":"AGO3","description":"Protein argonaute-3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22891","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2269696","identifier":"Q9HCK5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HCK5/entry","name":"AGO4","description":"Protein argonaute-4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22891","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2269715","identifier":"Q8NDV7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NDV7/entry","name":"TNRC6A","description":"Trinucleotide repeat-containing gene 6A protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-527363","identifier":"Q9UL18","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UL18/entry","name":"AGO1","description":"Protein argonaute-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22891","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-528269","identifier":"Q9UKV8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UKV8/entry","name":"AGO2","description":"Protein argonaute-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22891","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-134","complexName":"RISC-loading complex, TARBP2 variant","organismName":"Homo sapiens; 9606","description":"Binds to precursor miRNAs (pre-miRNAs). DICER then cleaves approximately 22 nucleotides from the 5' end of the stem-loop to form mature  double-stranded miRNAs. The duplex miRNA is then loaded onto Argonaute (AGO) proteins which, with the scaffolding proteins TNRC6, form the RNA-induced silencing complex (RISC). During this loading process, the passenger strand is removed from the RNA duplex leaving the guide strand. May also process pre-siRNAs.","predictedComplex":false,"interactors":[{"ac":"EBI-395506","identifier":"Q9UPY3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UPY3/entry","name":"DICER1","description":"Endoribonuclease Dicer","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14950","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-978581","identifier":"Q15633","identifierLink":"https://www.uniprot.org/uniprotkb/Q15633/entry","name":"TARBP2","description":"RISC-loading complex subunit TARBP2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46205","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-135","complexName":"RISC-loading complex, TARBP2 variant","organismName":"Mus musculus; 10090","description":"Binds to precursor miRNAs (pre-miRNAs). DICER then cleaves approximately 22 nucleotides from the 5' end of the stem-loop to form mature  double-stranded miRNAs. The duplex miRNA is then loaded onto Argonaute (AGO) proteins which, with the scaffolding proteins TNRC6, form the RNA-induced silencing complex (RISC). During this loading process, the passenger strand is removed from the RNA duplex leaving the guide strand. May also process pre-siRNAs..","predictedComplex":false,"interactors":[{"ac":"EBI-2644020","identifier":"P97473","identifierLink":"https://www.uniprot.org/uniprotkb/P97473/entry","name":"Tarbp2","description":"RISC-loading complex subunit TARBP2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46205","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2644051","identifier":"Q8R418","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R418/entry","name":"Dicer1","description":"Endoribonuclease Dicer","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14950","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1072","complexName":"RISC-loading complex, PRKRA variant","organismName":"Homo sapiens; 9606","description":"Binds to precursor miRNAs (pre-miRNAs). DICER then cleaves approximately 22 nucleotides from the 5' end of the stem-loop to form mature  double-stranded miRNAs. The duplex miRNA is then loaded onto Argonaute (AGO) proteins which, with the scaffolding proteins TNRC6, form the RNA-induced silencing complex (RISC). During this loading process, the passenger strand is removed from the RNA duplex leaving the guide strand. May also process pre-siRNAs.","predictedComplex":false,"interactors":[{"ac":"EBI-395506","identifier":"Q9UPY3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UPY3/entry","name":"DICER1","description":"Endoribonuclease Dicer","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14950","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-713955","identifier":"O75569","identifierLink":"https://www.uniprot.org/uniprotkb/O75569/entry","name":"PRKRA","description":"Interferon-inducible double-stranded RNA-dependent protein kinase activator A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46205","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1073","complexName":"RISC-loading complex, PRKRA variant","organismName":"Mus musculus; 10090","description":"Binds to precursor miRNAs (pre-miRNAs). DICER then cleaves approximately 22 nucleotides from the 5' end of the stem-loop to form mature  double-stranded miRNAs. The duplex miRNA is then loaded onto Argonaute (AGO) proteins which, with the scaffolding proteins TNRC6, form the RNA-induced silencing complex (RISC). During this loading process, the passenger strand is removed from the RNA duplex leaving the guide strand. May also process pre-siRNAs.","predictedComplex":false,"interactors":[{"ac":"EBI-2644051","identifier":"Q8R418","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R418/entry","name":"Dicer1","description":"Endoribonuclease Dicer","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14950","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8313024","identifier":"Q9WTX2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WTX2/entry","name":"Prkra","description":"Interferon-inducible double-stranded RNA-dependent protein kinase activator A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46205","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8624","complexName":"miRNA RISC complex, TNRC6B variant","organismName":"Homo sapiens; 9606","description":"Incorporates one strand of a micro RNA (miRNA) and uses this as a template for recognizing complementary mRNA. During strand selection, one of the miRNA strands is selected and anchored into the AGO protein, while the other strand is unwound and targeted for degradation, a process which involved a nick created by AGO2 to which the C3PO complex (CPX-890) is recruited. Base-pairing complementation by the guide strand binds the RISC complex to its target mRNA. Binding to a perfectly complementary mRNA generally results in silencing due to endonucleolytic cleavage of the mRNA specifically by AGO2. Binding of RISC to a partially complementary mRNA results in silencing through inhibition of translation which does not require endonuclease activity.The TNRC6 scaffolding protein acts to recruit other proteins which repress the translation of the target mRNA and accelerate mRNA decay.","predictedComplex":false,"interactors":[{"ac":"EBI-2267883","identifier":"Q9H9G7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H9G7/entry","name":"AGO3","description":"Protein argonaute-3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22891","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2269696","identifier":"Q9HCK5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HCK5/entry","name":"AGO4","description":"Protein argonaute-4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22891","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-527363","identifier":"Q9UL18","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UL18/entry","name":"AGO1","description":"Protein argonaute-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22891","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-528269","identifier":"Q9UKV8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UKV8/entry","name":"AGO2","description":"Protein argonaute-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22891","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-947158","identifier":"Q9UPQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UPQ9/entry","name":"TNRC6B","description":"Trinucleotide repeat-containing gene 6B protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8625","complexName":"miRNA RISC complex, TNRC6C variant","organismName":"Homo sapiens; 9606","description":"Incorporates one strand of a micro RNA (miRNA) and uses this as a template for recognizing complementary mRNA. During strand selection, one of the miRNA strands is selected and anchored into the AGO protein, while the other strand is unwound and targeted for degradation, a process which involved a nick created by AGO2 to which the C3PO complex (CPX-890) is recruited. Base-pairing complementation by the guide strand binds the RISC complex to its target mRNA. Binding to a perfectly complementary mRNA generally results in silencing due to endonucleolytic cleavage of the mRNA specifically by AGO2. Binding of RISC to a partially complementary mRNA results in silencing through inhibition of translation which does not require endonuclease activity.The TNRC6 scaffolding protein acts to recruit other proteins which repress the translation of the target mRNA and accelerate mRNA decay.","predictedComplex":false,"interactors":[{"ac":"EBI-2267883","identifier":"Q9H9G7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H9G7/entry","name":"AGO3","description":"Protein argonaute-3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22891","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2269696","identifier":"Q9HCK5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HCK5/entry","name":"AGO4","description":"Protein argonaute-4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22891","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52312184","identifier":"Q9HCJ0-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HCJ0-1/entry","name":"TNRC6C","description":"Trinucleotide repeat-containing gene 6C protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-527363","identifier":"Q9UL18","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UL18/entry","name":"AGO1","description":"Protein argonaute-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22891","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-528269","identifier":"Q9UKV8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UKV8/entry","name":"AGO2","description":"Protein argonaute-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22891","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8627","complexName":"Mitochondrial respiratory chain complex II, testis-specific variant","organismName":"Drosophila melanogaster; 7227","description":"Key role in aerobic respiration, in which mitochondrial enzymes accept electrons from electron carriers reduced in glycolysis and the tricarboxylic acid cycle. Catalyzes the oxidation of succinate to fumarate as part of tricarboxylic acid cycle and and transfers the electrons to coenzyme Q of the respiratory chain to form ubiquinol. Under most conditions the electrons are used to reduce oxygen, allowing ATP synthesis. SDHA and SDHB form the catalytic dimer that is anchored to the matrix surface of the mitochondrial inner membrane by SDHC and SDHD, integral membrane proteins of the membrane dimer. Electrons flow from succinate to the FAD, and sequentially through the [2Fe:2S], the [4Fe:4S], and the [3Fe:4S] clusters. From there, electrons enter the membrane dimer which contains a b-type heme and the active site for ubiquinone reduction.","predictedComplex":false,"interactors":[{"ac":"EBI-11297461","identifier":"CHEBI:21137","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:21137","name":"tri-mu-sulfido-mu3-sulfido-triiron","description":"tri-mu-sulfido-mu3-sulfido-triiron","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-130149","identifier":"Q9VGT9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VGT9/entry","name":"SdhCL","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10978","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15108503","identifier":"Q8SX97","identifierLink":"https://www.uniprot.org/uniprotkb/Q8SX97/entry","name":"SdhAL","description":"Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11632","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-161866","identifier":"Q9VCI5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VCI5/entry","name":"SdhD","description":"Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13337","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-169783","identifier":"Q9VWN3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VWN3/entry","name":"SdhBL","description":"Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11921","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-46449825","identifier":"CHEBI:190135","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:190135","name":"di-mu-sulfido-diiron","description":"di-mu-sulfido-diiron","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-8628","complexName":"Mitochondrial respiratory chain complex I","organismName":"Drosophila melanogaster; 7227","description":"Catalyses the first step of electron transport by the oxidation of NADH, thus providing two electrons for the reduction of ubiquinone. Electron transfer is coupled with the translocation of protons across the membrane, generating a proton motive force.","predictedComplex":false,"interactors":[{"ac":"EBI-103427","identifier":"Q94511","identifierLink":"https://www.uniprot.org/uniprotkb/Q94511/entry","name":"ND-75","description":"NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-106163","identifier":"Q9VJZ4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VJZ4/entry","name":"ND-B22","description":"NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12868","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-107132","identifier":"Q9VMU0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VMU0/entry","name":"ND-13A","description":"NADH dehydrogenase [ubiquinone] iron-sulfur protein 6, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 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May play a role as a Ca2+-modulated Na+ leak channel.","predictedComplex":false,"interactors":[{"ac":"EBI-17247926","identifier":"Q9NY72","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NY72/entry","name":"SCN3B","description":"Sodium channel regulatory subunit beta-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10546","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23705473","identifier":"Q8IWT1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IWT1/entry","name":"SCN4B","description":"Sodium channel regulatory subunit beta-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13869","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-44443060","identifier":"Q01118","identifierLink":"https://www.uniprot.org/uniprotkb/Q01118/entry","name":"SCN7A","description":"Sodium channel protein type 7 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8693","complexName":"Nax cation channel complex, SCN1B-SCN4B variant","organismName":"Homo sapiens; 9606","description":"Ion channel that may be non-selective for monovalent cations, inhibited by extracellular calcium, and sensitive to classical NaV channel blockers, such as tetrodotoxin. May play a role as a Ca2+-modulated Na+ leak channel.","predictedComplex":false,"interactors":[{"ac":"EBI-20771086","identifier":"Q07699","identifierLink":"https://www.uniprot.org/uniprotkb/Q07699/entry","name":"SCN1B","description":"Sodium channel regulatory subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10546","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23705473","identifier":"Q8IWT1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IWT1/entry","name":"SCN4B","description":"Sodium channel regulatory subunit beta-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13869","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-44443060","identifier":"Q01118","identifierLink":"https://www.uniprot.org/uniprotkb/Q01118/entry","name":"SCN7A","description":"Sodium channel protein type 7 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8694","complexName":"Nax cation channel complex, SCN1B-SCN2B variant","organismName":"Homo sapiens; 9606","description":"Ion channel that may be non-selective for monovalent cations, inhibited by extracellular calcium, and sensitive to classical NaV channel blockers, such as tetrodotoxin. May play a role as a Ca2+-modulated Na+ leak channel.","predictedComplex":false,"interactors":[{"ac":"EBI-20771086","identifier":"Q07699","identifierLink":"https://www.uniprot.org/uniprotkb/Q07699/entry","name":"SCN1B","description":"Sodium channel regulatory subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10546","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21671881","identifier":"O60939","identifierLink":"https://www.uniprot.org/uniprotkb/O60939/entry","name":"SCN2B","description":"Sodium channel regulatory subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13869","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-44443060","identifier":"Q01118","identifierLink":"https://www.uniprot.org/uniprotkb/Q01118/entry","name":"SCN7A","description":"Sodium channel protein type 7 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8695","complexName":"F-actin capping protein complex, CAPZA1 variant","organismName":"Homo sapiens; 9606","description":"Caps the barbed end of the actin filament  in a Ca(2+)-independent manner thereby blocking the exchange of subunits at these ends. The complex is an essential component for the reconstitution of movement powered by actin polymerization and is important for actin assembly and cell motility.","predictedComplex":false,"interactors":[{"ac":"EBI-353595","identifier":"P47756","identifierLink":"https://www.uniprot.org/uniprotkb/P47756/entry","name":"CAPZB","description":"F-actin-capping protein subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355586","identifier":"P52907","identifierLink":"https://www.uniprot.org/uniprotkb/P52907/entry","name":"CAPZA1","description":"F-actin-capping protein subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10653","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8696","complexName":"F-actin capping protein complex, CAPZA2 variant","organismName":"Homo sapiens; 9606","description":"Caps the barbed end of the actin filament  in a Ca(2+)-independent manner thereby blocking the exchange of subunits at these ends. The complex is an essential component for the reconstitution of movement powered by actin polymerization and is important for actin assembly and cell motility.","predictedComplex":false,"interactors":[{"ac":"EBI-353595","identifier":"P47756","identifierLink":"https://www.uniprot.org/uniprotkb/P47756/entry","name":"CAPZB","description":"F-actin-capping protein subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-762451","identifier":"P47755","identifierLink":"https://www.uniprot.org/uniprotkb/P47755/entry","name":"CAPZA2","description":"F-actin-capping protein subunit alpha-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10653","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8699","complexName":"Cav1.1 voltage-gated calcium channel complex, CACNA2D1-CACNB2-CACNG1 variant","organismName":"Homo sapiens; 9606","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.1 channel is responsible for the excitation-contraction coupling that causes contraction of skeletal muscles in response to changes in membrane potential, relaying an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmic membrane. The action potential-induced conformational changes of the complex activates the type 1 ryanodine receptor (P21817), which releases Ca2+ from the sarcoplasmic reticulum, triggering muscle contraction.","predictedComplex":false,"interactors":[{"ac":"EBI-2874501","identifier":"Q08289","identifierLink":"https://www.uniprot.org/uniprotkb/Q08289/entry","name":"CACNB2","description":"Voltage-dependent L-type calcium channel subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5329490","identifier":"Q13698","identifierLink":"https://www.uniprot.org/uniprotkb/Q13698/entry","name":"CACNA1S","description":"Voltage-dependent L-type calcium channel subunit alpha-1S","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9686780","identifier":"Q06432","identifierLink":"https://www.uniprot.org/uniprotkb/Q06432/entry","name":"CACNG1","description":"Voltage-dependent calcium channel gamma-1 subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15025","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9686800","identifier":"P54289-PRO_0000005001","identifierLink":"https://www.uniprot.org/uniprotkb/P54289-PRO_0000005001/entry","name":"CACNA2D1","description":"Voltage-dependent calcium channel subunit alpha-2-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-9686811","identifier":"P54289-PRO_0000005002","identifierLink":"https://www.uniprot.org/uniprotkb/P54289-PRO_0000005002/entry","name":"CACNA2D1","description":"Voltage-dependent calcium channel subunit delta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-8701","complexName":"GABA-A receptor, alpha-5/beta-3 complex","organismName":"Homo sapiens; 9606","description":"Anion-selective, ligand-gated ion channel. GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel. Acts as the main driver of fast inhibitory neurotransmission in the nervous system.\r\n\r\nGABA-A receptor assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nPredominantly expressed in the cerebral cortex, the GABA-A, alpha-5 receptor subtypes constitute less than 5% of the entire receptor population but up to 25% of the receptor subtype are located in the crucial learning and memory-associated area of the brain; the hippocampus.\r\n \r\nLargely absent at GABAergic synapses, exhibit little synaptic phasic inhibition, but abundant in the dendritic regions of extrasynaptic sites, and mediate tonic inhibition with continuously occurring smaller amplitude.\r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets:\r\n\r\n1) Positive allosteric modulation of GABA-A alpha-5 receptor subtypes can selectively decrease hippocampal activity and reverse psychosis-like physiological and behavioural changes in rats; may potentially help treat patients with post-traumatic stress disorder (PTSD) and comorbid psychosis; allopregnanolone (CHEBI:50169), a naturally occurring progesterone derivative, is a positive allosteric modulator referred to as brexanolone when used for the medical treatment of moderate to severe postpartum depression.\r\n\r\n2) Negative-allosteric modulators for reducing their tonic inhibition have been shown to enhance learning and memory in neurological disorders such as schizophrenia, Down syndrome, and autism with a possible alternative benzodiazepine binding site.","predictedComplex":false,"interactors":[{"ac":"EBI-6258252","identifier":"P28472","identifierLink":"https://www.uniprot.org/uniprotkb/P28472/entry","name":"GABRB3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008566","identifier":"P31644","identifierLink":"https://www.uniprot.org/uniprotkb/P31644/entry","name":"GABRA5","description":"Gamma-aminobutyric acid receptor subunit alpha-5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8702","complexName":"GABA-A receptor, alpha2-beta1-gamma2 complex","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states.\r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-2685723","identifier":"P47869","identifierLink":"https://www.uniprot.org/uniprotkb/P47869/entry","name":"GABRA2","description":"Gamma-aminobutyric acid receptor subunit alpha-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3914848","identifier":"P18505","identifierLink":"https://www.uniprot.org/uniprotkb/P18505/entry","name":"GABRB1","description":"Gamma-aminobutyric acid receptor subunit beta-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008430","identifier":"P18507","identifierLink":"https://www.uniprot.org/uniprotkb/P18507/entry","name":"GABRG2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8721","complexName":"GABA-A receptor, alpha3-beta1-gamma2 complex","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states.\r\n\r\nGABA-A alpha-3 receptor subtypes undergo pre-mRNA editing by adenosine desaminase (ADAR) resulting in reduced cell surface expression and the total number of alpha-3 subunits, suggesting that editing plays a role in receptor trafficking.\r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-1763805","identifier":"P34903","identifierLink":"https://www.uniprot.org/uniprotkb/P34903/entry","name":"GABRA3","description":"Gamma-aminobutyric acid receptor subunit alpha-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3914848","identifier":"P18505","identifierLink":"https://www.uniprot.org/uniprotkb/P18505/entry","name":"GABRB1","description":"Gamma-aminobutyric acid receptor subunit beta-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008430","identifier":"P18507","identifierLink":"https://www.uniprot.org/uniprotkb/P18507/entry","name":"GABRG2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8723","complexName":"GABA-A receptor, alpha4-beta1-gamma2 complex","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-3909227","identifier":"P48169","identifierLink":"https://www.uniprot.org/uniprotkb/P48169/entry","name":"GABRA4","description":"Gamma-aminobutyric acid receptor subunit alpha-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3914848","identifier":"P18505","identifierLink":"https://www.uniprot.org/uniprotkb/P18505/entry","name":"GABRB1","description":"Gamma-aminobutyric acid receptor subunit beta-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008430","identifier":"P18507","identifierLink":"https://www.uniprot.org/uniprotkb/P18507/entry","name":"GABRG2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8724","complexName":"GABA-A receptor, alpha5-beta1-gamma2 complex","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptor assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nPredominantly expressed in the cerebral cortex, the GABA-A, alpha-5 receptor subtypes constitute less than 5% of the entire receptor population but up to 25% of the receptor subtype are located in the crucial learning and memory-associated area of the brain; the hippocampus.\r\n \r\nLargely absent at GABAergic synapses, exhibit little synaptic phasic inhibition, but abundant in the dendritic regions of extrasynaptic sites, and mediate tonic inhibition with continuously occurring smaller amplitude.\r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets:\r\n\r\n1) Positive allosteric modulation of GABA-A alpha-5 receptor subtypes can selectively decrease hippocampal activity and reverse psychosis-like physiological and behavioural changes in rats; may potentially help treat patients with post-traumatic stress disorder (PTSD) and comorbid psychosis; allopregnanolone (CHEBI:50169), a naturally occurring progesterone derivative, is a PAM referred to as brexanolone when used for the medical treatment of moderate to severe postpartum depression.\r\n\r\n2) Negative-allosteric modulators for reducing their tonic inhibition have been shown to enhance learning and memory in neurological disorders such as schizophrenia, Down syndrome, and autism with a possible alternative benzodiazepine binding site.","predictedComplex":false,"interactors":[{"ac":"EBI-3914848","identifier":"P18505","identifierLink":"https://www.uniprot.org/uniprotkb/P18505/entry","name":"GABRB1","description":"Gamma-aminobutyric acid receptor subunit beta-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008430","identifier":"P18507","identifierLink":"https://www.uniprot.org/uniprotkb/P18507/entry","name":"GABRG2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008566","identifier":"P31644","identifierLink":"https://www.uniprot.org/uniprotkb/P31644/entry","name":"GABRA5","description":"Gamma-aminobutyric acid receptor subunit alpha-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8725","complexName":"Cav1.1 voltage-gated calcium channel complex, CACNA2D1-CACNB3-CACNG1 variant","organismName":"Homo sapiens; 9606","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.1 channel is responsible for the excitation-contraction coupling that causes contraction of skeletal muscles in response to changes in membrane potential, relaying an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmic membrane. The action potential-induced conformational changes of the complex activates the type 1 ryanodine receptor (P21817), which releases Ca2+ from the sarcoplasmic reticulum, triggering muscle contraction.","predictedComplex":false,"interactors":[{"ac":"EBI-1184651","identifier":"P54284","identifierLink":"https://www.uniprot.org/uniprotkb/P54284/entry","name":"CACNB3","description":"Voltage-dependent L-type calcium channel subunit beta-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5329490","identifier":"Q13698","identifierLink":"https://www.uniprot.org/uniprotkb/Q13698/entry","name":"CACNA1S","description":"Voltage-dependent L-type calcium channel subunit alpha-1S","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9686780","identifier":"Q06432","identifierLink":"https://www.uniprot.org/uniprotkb/Q06432/entry","name":"CACNG1","description":"Voltage-dependent calcium channel gamma-1 subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15025","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9686800","identifier":"P54289-PRO_0000005001","identifierLink":"https://www.uniprot.org/uniprotkb/P54289-PRO_0000005001/entry","name":"CACNA2D1","description":"Voltage-dependent calcium channel subunit alpha-2-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-9686811","identifier":"P54289-PRO_0000005002","identifierLink":"https://www.uniprot.org/uniprotkb/P54289-PRO_0000005002/entry","name":"CACNA2D1","description":"Voltage-dependent calcium channel subunit delta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-8726","complexName":"Cav1.1 voltage-gated calcium channel complex, CACNA2D1-CACNB4-CACNG1 variant","organismName":"Homo sapiens; 9606","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.1 channel is responsible for the excitation-contraction coupling that causes contraction of skeletal muscles in response to changes in membrane potential, relaying an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmic membrane. The action potential-induced conformational changes of the complex activates the type 1 ryanodine receptor (P21817), which releases Ca2+ from the sarcoplasmic reticulum, triggering muscle contraction.","predictedComplex":false,"interactors":[{"ac":"EBI-5329490","identifier":"Q13698","identifierLink":"https://www.uniprot.org/uniprotkb/Q13698/entry","name":"CACNA1S","description":"Voltage-dependent L-type calcium channel subunit alpha-1S","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714838","identifier":"O00305","identifierLink":"https://www.uniprot.org/uniprotkb/O00305/entry","name":"CACNB4","description":"Voltage-dependent L-type calcium channel subunit beta-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9686780","identifier":"Q06432","identifierLink":"https://www.uniprot.org/uniprotkb/Q06432/entry","name":"CACNG1","description":"Voltage-dependent calcium channel gamma-1 subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15025","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9686800","identifier":"P54289-PRO_0000005001","identifierLink":"https://www.uniprot.org/uniprotkb/P54289-PRO_0000005001/entry","name":"CACNA2D1","description":"Voltage-dependent calcium channel subunit alpha-2-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-9686811","identifier":"P54289-PRO_0000005002","identifierLink":"https://www.uniprot.org/uniprotkb/P54289-PRO_0000005002/entry","name":"CACNA2D1","description":"Voltage-dependent calcium channel subunit delta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-8727","complexName":"GABA-A receptor alpha6-beta1-gamma2 complex","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptor assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-3914848","identifier":"P18505","identifierLink":"https://www.uniprot.org/uniprotkb/P18505/entry","name":"GABRB1","description":"Gamma-aminobutyric acid receptor subunit beta-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008430","identifier":"P18507","identifierLink":"https://www.uniprot.org/uniprotkb/P18507/entry","name":"GABRG2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008507","identifier":"Q16445","identifierLink":"https://www.uniprot.org/uniprotkb/Q16445/entry","name":"GABRA6","description":"Gamma-aminobutyric acid receptor subunit alpha-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8729","complexName":"GABA-A receptor, alpha1-beta3 complex","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine (BZD) receptor and opening a chloride ion-selective pore. \r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states.\r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.\r\n\r\nGABA-A alpha/beta receptors comprise a sizeable population of extrasynaptic receptors known for tonic inhibition and share common properties regardless of the specific alpha or beta subtype. Two distinct traits of tonic inhibition include: 1) a low open-channel probability (Po) in response to GABA to avoid over-damping neuronal circuitry. 2) high sensitivity to inhibition by endogenous Zn2+, with alpha/beta receptors being the most sensitive of all isoforms, with physiological and pathological consequences during development and in conditions such as temporal lobe epilepsy.","predictedComplex":false,"interactors":[{"ac":"EBI-6258252","identifier":"P28472","identifierLink":"https://www.uniprot.org/uniprotkb/P28472/entry","name":"GABRB3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6258308","identifier":"P14867","identifierLink":"https://www.uniprot.org/uniprotkb/P14867/entry","name":"GABRA1","description":"Gamma-aminobutyric acid receptor subunit alpha-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8730","complexName":"Mitochondrial respiratory chain complex III","organismName":"Drosophila melanogaster; 7227","description":"Key role in aerobic respiration, in which mitochondrial enzymes accept electrons from electron carriers reduced in glycolysis and the tricarboxylic acid cycle. Ubiquinol-cytochrome c reductase pumps protons into the intermembrane space, creating an electrochemical gradient. This is achieved by oxidizing ubiquinol (ubihydroquinone) which reacts from the membrane phase, reducing cytochrome c in the intermembrane space, and using the free energy change to transport H+ ions across the membrane from the matrix to the inter membrane space. Quinol oxidation occurs in a bifurcated reaction, in which one electron is transferred to a high potential chain and the other to a low potential chain. The high potential chain, consisting of the iron sulfur protein, cyt c1 and cyt c2, transfers the first electron from quinol to an acceptor (cytochrome oxidase). The low potential chain consists of two cyt b hemes, which serve as a pathway through which electrons are transferred across the coupling membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-114079","identifier":"Q9VFF0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VFF0/entry","name":"UQCR-C1","description":"Mitochondrial-processing peptidase subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11851","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-115758","identifier":"Q9VXI6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VXI6/entry","name":"UQCR-14","description":"Cytochrome b-c1 complex subunit 7","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12022","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-154162","identifier":"Q9VQ29","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VQ29/entry","name":"RFeSP","description":"Cytochrome b-c1 complex subunit Rieske, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-166508","identifier":"Q9VV75","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VV75/entry","name":"UQCR-C2","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11851","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-177772","identifier":"Q9VRL0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VRL0/entry","name":"Cyt-c1","description":"Cytochrome c1, heme protein, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-193226","identifier":"Q9VVH5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVH5/entry","name":"UQCR-Q","description":"Cytochrome b-c1 complex subunit 8","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46449825","identifier":"CHEBI:190135","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:190135","name":"di-mu-sulfido-diiron","description":"di-mu-sulfido-diiron","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-48440283","identifier":"A8Y535","identifierLink":"https://www.uniprot.org/uniprotkb/A8Y535/entry","name":"UQCR-11","description":"Cytochrome b-c1 complex subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15336","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48440302","identifier":"P18935","identifierLink":"https://www.uniprot.org/uniprotkb/P18935/entry","name":"mt:Cyt-b","description":"Cytochrome b","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19271","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-83821","identifier":"Q500Y7","identifierLink":"https://www.uniprot.org/uniprotkb/Q500Y7/entry","name":"UQCR-6.4","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15420","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-84498","identifier":"Q9XY35","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XY35/entry","name":"ox","description":"Cytochrome b-c1 complex subunit 9","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12980","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8731","complexName":"GABA-A receptor, beta3-gamma2 complex","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGamma subunit-containing receptors of the central nervous system (CNS) localize both synaptically and extrasynaptically and bind GABA with lower affinity and desensitize more rapidly than delta subtype-containing receptors.\r\n\r\nAssemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states.\r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-6258252","identifier":"P28472","identifierLink":"https://www.uniprot.org/uniprotkb/P28472/entry","name":"GABRB3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008430","identifier":"P18507","identifierLink":"https://www.uniprot.org/uniprotkb/P18507/entry","name":"GABRG2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8732","complexName":"GABA-A receptor, beta3-delta complex","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA-A receptor (beta-3/delta) binding to histamine (CHEBI:35678) is thought to promote wakefulness.\r\n\r\nAssemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. Their many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-6258252","identifier":"P28472","identifierLink":"https://www.uniprot.org/uniprotkb/P28472/entry","name":"GABRB3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744352","identifier":"O14764","identifierLink":"https://www.uniprot.org/uniprotkb/O14764/entry","name":"GABRD","description":"Gamma-aminobutyric acid receptor subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8736","complexName":"ERAP1-ERAP2 endoplasmic reticulum aminopeptidase complex","organismName":"Homo sapiens; 9606","description":"Zn2+ aminopeptidases required for peptide trimming. Generates antigenic peptides from N-terminally elongated precursors to fit them to the correct length required for presentation on MHC class I molecules May also degrade some antigenic peptides to lengths too short to allow binding onto MHC-I. Both enzymes are active as monomers however heterodimer formation could result in synergistic effects, in that ERAP1 shows a preference for hydrophbic N-terminal amino acids, ERAP2 for positively charged and also ERAP1 cleaves peptides longer than 9 amino acids, while ERAP2 can efficiently trim shorter peptides","predictedComplex":false,"interactors":[{"ac":"EBI-2834295","identifier":"Q6P179","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P179/entry","name":"ERAP2","description":"Endoplasmic reticulum aminopeptidase 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11533","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-299412","identifier":"Q9NZ08","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZ08/entry","name":"ERAP1","description":"Endoplasmic reticulum aminopeptidase 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11533","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-8737","complexName":"Mitochondrial respiratory chain complex III, testis-specific variant","organismName":"Drosophila melanogaster; 7227","description":"Key role in aerobic respiration, in which mitochondrial enzymes accept electrons from electron carriers reduced in glycolysis and the tricarboxylic acid cycle. Ubiquinol-cytochrome c reductase pumps protons into the intermembrane space, creating an electrochemical gradient. This is achieved by oxidizing ubiquinol (ubihydroquinone) which reacts from the membrane phase, reducing cytochrome c in the intermembrane space, and using the free energy change to transport H+ ions across the membrane from the matrix to the inter membrane space. Quinol oxidation occurs in a bifurcated reaction, in which one electron is transferred to a high potential chain and the other to a low potential chain. The high potential chain, consisting of the iron sulfur protein, cyt c1 and cyt c2, transfers the first electron from quinol to an acceptor (cytochrome oxidase). The low potential chain consists of two cyt b hemes, which serve as a pathway through which electrons are transferred across the coupling membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-114079","identifier":"Q9VFF0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VFF0/entry","name":"UQCR-C1","description":"Mitochondrial-processing peptidase subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11851","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-154162","identifier":"Q9VQ29","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VQ29/entry","name":"RFeSP","description":"Cytochrome b-c1 complex subunit Rieske, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-166508","identifier":"Q9VV75","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VV75/entry","name":"UQCR-C2","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11851","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-172603","identifier":"Q9VAM8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VAM8/entry","name":"Cyt-c1L","description":"Cytochrome c1, heme protein, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-179632","identifier":"Q9VAW7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VAW7/entry","name":"UQCR-14L","description":"Cytochrome b-c1 complex subunit 7","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12022","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-193226","identifier":"Q9VVH5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVH5/entry","name":"UQCR-Q","description":"Cytochrome b-c1 complex subunit 8","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46449825","identifier":"CHEBI:190135","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:190135","name":"di-mu-sulfido-diiron","description":"di-mu-sulfido-diiron","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-48440302","identifier":"P18935","identifierLink":"https://www.uniprot.org/uniprotkb/P18935/entry","name":"mt:Cyt-b","description":"Cytochrome b","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19271","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48440816","identifier":"Q4QPY6","identifierLink":"https://www.uniprot.org/uniprotkb/Q4QPY6/entry","name":"UQCR-11L","description":"Cytochrome b-c1 complex subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15336","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48440833","identifier":"M9NFG6","identifierLink":"https://www.uniprot.org/uniprotkb/M9NFG6/entry","name":"UQCR-6.4L","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15420","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-84498","identifier":"Q9XY35","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XY35/entry","name":"ox","description":"Cytochrome b-c1 complex subunit 9","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12980","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8738","complexName":"Oligosaccharyltransferase complex B, TUCS3 variant","organismName":"Homo sapiens; 9606","description":"Oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc3Man9GlcNAc2 in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs post-translocationally. 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N-glycosylation occurs post-translocationally. 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The action potential-induced conformational changes of the complex activates the type 1 ryanodine receptor ( [RyR1: CPX-3135, RyR3: CPX-3162]), which releases Ca2+ from the sarcoplasmic reticulum, triggering muscle contraction.","predictedComplex":false,"interactors":[{"ac":"EBI-48446589","identifier":"Q9NY47-PRO_0000304637","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NY47-PRO_0000304637/entry","name":"CACNA2D2","description":"Voltage-dependent calcium channel subunit alpha-2/delta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-48446668","identifier":"Q9NY47-PRO_0000304639","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NY47-PRO_0000304639/entry","name":"CACNA2D2","description":"Voltage-dependent calcium channel subunit delta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-5329490","identifier":"Q13698","identifierLink":"https://www.uniprot.org/uniprotkb/Q13698/entry","name":"CACNA1S","description":"Voltage-dependent L-type calcium channel subunit alpha-1S","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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Forms an extensive protein-protein and protein-RNA interaction network within early ribosome assembly intermediates in the nucleolus, thereby potentially serving as a hub for stabilizing or remodeling ribonucleoprotein neighborhoods during 60S subunit biogenesis","predictedComplex":false,"interactors":[{"ac":"EBI-13145","identifier":"P53261","identifierLink":"https://www.uniprot.org/uniprotkb/P53261/entry","name":"NOP7","description":"Pescadillo homolog","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12221","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28098","identifier":"Q04660","identifierLink":"https://www.uniprot.org/uniprotkb/Q04660/entry","name":"ERB1","description":"Ribosome biogenesis protein ERB1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR17605","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29589","identifier":"Q12024","identifierLink":"https://www.uniprot.org/uniprotkb/Q12024/entry","name":"YTM1","description":"Ribosome biogenesis protein YTM1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19855","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1863","complexName":"TAP42-RRD1-SIT4 phosphatase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A serine/threonine protein phosphatase complex that plays a major role in TOR1/2 (P35169/P32600)-mediated signaling and gene expression. Rapamycin causes release of the phosphatase-RRD dimer from TAP42.","predictedComplex":false,"interactors":[{"ac":"EBI-13707","identifier":"P20604","identifierLink":"https://www.uniprot.org/uniprotkb/P20604/entry","name":"SIT4","description":"Serine/threonine-protein phosphatase PP1-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-18926","identifier":"Q04372","identifierLink":"https://www.uniprot.org/uniprotkb/Q04372/entry","name":"TAP42","description":"Type 2A phosphatase-associated protein 42","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10933","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25278","identifier":"P40454","identifierLink":"https://www.uniprot.org/uniprotkb/P40454/entry","name":"RRD1","description":"Serine/threonine-protein phosphatase 2A activator 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10012","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1864","complexName":"SIT4-SAP155 phosphatase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Serine/threonine phosphatase complex which forms in response to nutrient deprivation, mediates G1 to S cell cycle progression and a number of signaling events controlled by the target of rapamycin TOR signaling cascade including growth, budding, NCR gene expression and GCN2-regulated translation.","predictedComplex":false,"interactors":[{"ac":"EBI-13707","identifier":"P20604","identifierLink":"https://www.uniprot.org/uniprotkb/P20604/entry","name":"SIT4","description":"Serine/threonine-protein phosphatase PP1-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 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Before the commencement of replication, the cohesin complex (CPX-1408) is loaded onto DNA. The arms of the Smc1/3 molecules embrace the DNA, thereby forming a ring of approx. 40 nm diameter. The head domains of Smc1 and Smc3 are locked together by Scc1. Cohesion might be generated as the replication fork passes through the ring, entrapping both sister chromatids inside. At the metaphase to anaphase transition, Scc1 is cleaved by separase, thereby opening the lock of the Smc1/3 head domains. The ring opens and sister chromatids can be pulled to opposite spindle poles.","predictedComplex":false,"interactors":[{"ac":"EBI-16655","identifier":"Q12158","identifierLink":"https://www.uniprot.org/uniprotkb/Q12158/entry","name":"MCD1","description":"Sister chromatid cohesion protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12585","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16667","identifier":"P40541","identifierLink":"https://www.uniprot.org/uniprotkb/P40541/entry","name":"IRR1","description":"Cohesin subunit SCC3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11199","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17402","identifier":"P32908","identifierLink":"https://www.uniprot.org/uniprotkb/P32908/entry","name":"SMC1","description":"Structural maintenance of chromosomes protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR18937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17423","identifier":"P47037","identifierLink":"https://www.uniprot.org/uniprotkb/P47037/entry","name":"SMC3","description":"Structural maintenance of chromosomes protein 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43977","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1868","complexName":"SCC2-SCC4 cohesin loader complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for the stable association of the cohesin complex (CPX-1867) with DNA and ensures its enrichment at the mitotic spindle of the centromere thus ensuring correct segregation of the sister chromatids into the daughter cells during cell replication. The RSC chromatin remodeling complex (CPX-1889/CPX-1888) recruits budding yeast SCC2/SCC4 to broad nucleosome-free regions and thhe SCC2/SCC4 complex cooperates with RSC to maintain nucleosome depletion at its binding sites.","predictedComplex":false,"interactors":[{"ac":"EBI-16662","identifier":"Q04002","identifierLink":"https://www.uniprot.org/uniprotkb/Q04002/entry","name":"SCC2","description":"Sister chromatid cohesion protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21704","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16679","identifier":"P40090","identifierLink":"https://www.uniprot.org/uniprotkb/P40090/entry","name":"SCC4","description":"MAU2 chromatid cohesion factor homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1869","complexName":"Nuclear condensin complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Essential for the structural organization of chromosomes during their segregation by the mitotic spindle. Condensin subunits localize along the axial core of pachytene chromosomes and probably introduce positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases.","predictedComplex":false,"interactors":[{"ac":"EBI-17412","identifier":"P38989","identifierLink":"https://www.uniprot.org/uniprotkb/P38989/entry","name":"SMC2","description":"Structural maintenance of chromosomes protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43941","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17430","identifier":"Q12267","identifierLink":"https://www.uniprot.org/uniprotkb/Q12267/entry","name":"SMC4","description":"Structural maintenance of chromosomes protein 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 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9606","xrefs":[{"identifier":"PTHR10410","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712982","identifier":"Q9UBW8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UBW8/entry","name":"COPS7A","description":"COP9 signalosome complex subunit 7a","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15350","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-725197","identifier":"Q13098","identifierLink":"https://www.uniprot.org/uniprotkb/Q13098/entry","name":"GPS1","description":"COP9 signalosome complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14145","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742413","identifier":"Q9BT78","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BT78/entry","name":"COPS4","description":"COP9 signalosome complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10855","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1871","complexName":"COP9 signalosome variant 2","organismName":"Homo sapiens; 9606","description":"Essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2.","predictedComplex":false,"interactors":[{"ac":"EBI-1050386","identifier":"P61201","identifierLink":"https://www.uniprot.org/uniprotkb/P61201/entry","name":"COPS2","description":"COP9 signalosome complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2510102","identifier":"Q99627","identifierLink":"https://www.uniprot.org/uniprotkb/Q99627/entry","name":"COPS8","description":"COP9 signalosome complex subunit 8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13339","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2510162","identifier":"Q9H9Q2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H9Q2/entry","name":"COPS7B","description":"COP9 signalosome complex subunit 7b","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15350","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350590","identifier":"Q9UNS2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UNS2/entry","name":"COPS3","description":"COP9 signalosome complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10758","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-486838","identifier":"Q7L5N1","identifierLink":"https://www.uniprot.org/uniprotkb/Q7L5N1/entry","name":"COPS6","description":"COP9 signalosome complex subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10540","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-594661","identifier":"Q92905","identifierLink":"https://www.uniprot.org/uniprotkb/Q92905/entry","name":"COPS5","description":"COP9 signalosome complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10410","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-725197","identifier":"Q13098","identifierLink":"https://www.uniprot.org/uniprotkb/Q13098/entry","name":"GPS1","description":"COP9 signalosome complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14145","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742413","identifier":"Q9BT78","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BT78/entry","name":"COPS4","description":"COP9 signalosome complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10855","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1872","complexName":"MRX double-strand break repair complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Endo- and exonuclease complex that plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis  via non-homologous end joining and homologous recombination.. The complex possesses both single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11. Mre11 and Rad50 form an ATP-regulated nuclease that senses DSBs and tethers DNA via long Rad50 coiled-coil domains. Required for the formation of the DSB catalysed by the transesterase SPO11 (P23179) protein and subsequently removes covalently attached Spo11 from the 5' extremity of the breaks through its nuclease activity, to allow further break resection. The MRX complex also plays a role during meiosis in bridging DNA molecules together and in sensing SPO11 DSB and activating the DNA damage checkpoint. Clips double-stranded DNA in the vicinity of protein-blocked DNA ends.","predictedComplex":false,"interactors":[{"ac":"EBI-11255","identifier":"P32829","identifierLink":"https://www.uniprot.org/uniprotkb/P32829/entry","name":"MRE11","description":"Double-strand break repair protein MRE11","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14700","identifier":"P12753","identifierLink":"https://www.uniprot.org/uniprotkb/P12753/entry","name":"RAD50","description":"DNA repair protein RAD50","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR18867","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-20599","identifier":"P33301","identifierLink":"https://www.uniprot.org/uniprotkb/P33301/entry","name":"XRS2","description":"DNA repair protein XRS2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1873","complexName":"Nucleolar ribonuclease P complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Responsible for the 5' endonucleolytic cleavage of precursor tRNAs (pre-tRNAs), catalyzing phosphodiester bond hydrolysis to remove approximately 12 leader nucleotides to yield mature tRNAs. The RNA subunit of the nucleolar RNase P is a catalytically active ribozyme that is capable of both recognizing and cleaving substrates efficiently and accurately. The protein component serves as an absolutely required cofactor.","predictedComplex":false,"interactors":[{"ac":"EBI-11621275","identifier":"URS0000413C32_559292","identifierLink":"http://rnacentral.org/rna/URS0000413C32_559292","name":"rpr1 yeast","description":"RNaseP RNA RPR1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"ribonucleic acid","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-13621","identifier":"P41812","identifierLink":"https://www.uniprot.org/uniprotkb/P41812/entry","name":"POP1","description":"Ribonucleases P/MRP protein subunit POP1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22731","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13638","identifier":"P53833","identifierLink":"https://www.uniprot.org/uniprotkb/P53833/entry","name":"POP3","description":"Ribonucleases P/MRP protein subunit POP3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28272","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13646","identifier":"P38336","identifierLink":"https://www.uniprot.org/uniprotkb/P38336/entry","name":"POP4","description":"RNases MRP/P 32.9 kDa subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13348","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13654","identifier":"P28005","identifierLink":"https://www.uniprot.org/uniprotkb/P28005/entry","name":"POP5","description":"Ribonuclease P/MRP protein subunit POP5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR48414","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13662","identifier":"P53218","identifierLink":"https://www.uniprot.org/uniprotkb/P53218/entry","name":"POP6","description":"Ribonucleases P/MRP protein subunit POP6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-13670","identifier":"P38291","identifierLink":"https://www.uniprot.org/uniprotkb/P38291/entry","name":"POP7","description":"Ribonucleases P/MRP protein subunit POP7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28256","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13678","identifier":"P38208","identifierLink":"https://www.uniprot.org/uniprotkb/P38208/entry","name":"POP8","description":"Ribonucleases P/MRP protein subunit POP8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28173","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15968","identifier":"P38786","identifierLink":"https://www.uniprot.org/uniprotkb/P38786/entry","name":"RPP1","description":"Ribonuclease P/MRP protein subunit RPP1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25408","identifier":"P40571","identifierLink":"https://www.uniprot.org/uniprotkb/P40571/entry","name":"RPR2","description":"Ribonuclease P protein subunit RPR2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1874","complexName":"Platelet-derived growth factor AA complex","organismName":"Homo sapiens; 9606","description":"A-chain of the platelet-derived growth factor (PDGF). Binds to and activates PDGF receptor alpha subunit (PDGFRalpha, P16234) by inducing receptor dimerisation and tyrosine phosphorylation. Is a potent mitogen for cells of mesenchymal origin. Plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Required for normal lung alveolar septum formation during embryogenesis, normal development of the gastrointestinal tract, normal development of Leydig cells and spermatogenesis. Required for normal oligodendrocyte development and normal myelination in the spinal cord and cerebellum. Plays an important role in wound healing.","predictedComplex":false,"interactors":[{"ac":"EBI-2881386","identifier":"P04085","identifierLink":"https://www.uniprot.org/uniprotkb/P04085/entry","name":"PDGFA","description":"Platelet-derived growth factor subunit A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2881","complexName":"PDGF receptor alpha - PDGF-AA complex","organismName":"Homo sapiens; 9606","description":"Platelet-derived growth factor (PDGF) receptor alpha (PDGFRalpha) that is activated by its bound ligand, PDGF A-chain. PDGFRalpha is a tyrosine-protein kinase that acts as a cell-surface receptor for PDGFA, and its related B- and C-chains, PDGFB (P01127) and PDGFC (Q9NRA1). It autophosphorylates on multiple tyrosines upon ligand binding, initiating several signalling cascades and phosphorylation of downstream targets. Is a potent mitogen for cells of mesenchymal origin. Plays an essential role in the regulation of embryonic development, cell proliferation, survival and chemotaxis. Required for normal lung alveolar septum formation during embryogenesis, normal development of the gastrointestinal tract, normal development of Leydig cells and spermatogenesis. Required for normal oligodendrocyte development and normal myelination in the spinal cord and cerebellum. Plays an important role in wound healing.","predictedComplex":false,"interactors":[{"ac":"EBI-2861522","identifier":"P16234","identifierLink":"https://www.uniprot.org/uniprotkb/P16234/entry","name":"PDGFRA","description":"Platelet-derived growth factor receptor alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2881386","identifier":"P04085","identifierLink":"https://www.uniprot.org/uniprotkb/P04085/entry","name":"PDGFA","description":"Platelet-derived growth factor subunit A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2893","complexName":"Platelet-derived growth factor AA complex","organismName":"Mus musculus; 10090","description":"A-chain of the platelet-derived growth factor (PDGF). Binds to and actives PDGF receptor alpha subunit (PDGFRalpha, P26618) by inducing receptor dimerisation and tyrosine phosphorylation. Is a potent mitogen for cells of mesenchymal origin. Plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Required for normal lung alveolar septum formation during embryogenesis, normal development of the gastrointestinal tract, normal development of Leydig cells and spermatogenesis. Required for normal oligodendrocyte development and normal myelination in the spinal cord and cerebellum. Plays an important role in wound healing.","predictedComplex":false,"interactors":[{"ac":"EBI-9097402","identifier":"P20033","identifierLink":"https://www.uniprot.org/uniprotkb/P20033/entry","name":"Pdgfa","description":"Platelet-derived growth factor subunit A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2899","complexName":"PDGF receptor alpha - PDGF-AA complex","organismName":"Mus musculus; 10090","description":"Platelet-derived growth factor (PDGF) receptor alpha (PDGFRalpha) that is activated by its bound ligand, PDGF A-chain. PDGFRalpha is a tyrosine-protein kinase that acts as a cell-surface receptor for PDGFA, and its related B- and C-chains, PDGFB (P31240) and PDGFC (Q8CI19). It autophosphorylates on multiple tyrosines upon ligand binding initiating several signalling cascades and phosphorylation of downstream targets. Is a potent mitogen for cells of mesenchymal origin. Plays an essential role in the regulation of embryonic development, cell proliferation, survival and chemotaxis. Required for normal lung alveolar septum formation during embryogenesis, normal development of the gastrointestinal tract, normal development of Leydig cells and spermatogenesis. Required for normal oligodendrocyte development and normal myelination in the spinal cord and cerebellum. Plays an important role in wound healing.","predictedComplex":false,"interactors":[{"ac":"EBI-7290093","identifier":"P26618","identifierLink":"https://www.uniprot.org/uniprotkb/P26618/entry","name":"Pdgfra","description":"Platelet-derived growth factor receptor alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9097402","identifier":"P20033","identifierLink":"https://www.uniprot.org/uniprotkb/P20033/entry","name":"Pdgfa","description":"Platelet-derived growth factor subunit A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1875","complexName":"Platelet-derived growth factor AB complex","organismName":"Homo sapiens; 9606","description":"A- and B-chain of the platelet-derived growth factor (PDGF). Binds to and activates PDGF receptor alpha (PDGFRalpha, P16234) and beta (PDGFRbeta, P09619) subunits by inducing receptor dimerisation and tyrosine phosphorylation. Is a potent mitogen for cells of mesenchymal origin. Plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Plays an important role in wound healing.","predictedComplex":false,"interactors":[{"ac":"EBI-1554925","identifier":"P01127","identifierLink":"https://www.uniprot.org/uniprotkb/P01127/entry","name":"PDGFB","description":"Platelet-derived growth factor subunit B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2881386","identifier":"P04085","identifierLink":"https://www.uniprot.org/uniprotkb/P04085/entry","name":"PDGFA","description":"Platelet-derived growth factor subunit A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2900","complexName":"Platelet-derived growth factor AB complex","organismName":"Mus musculus; 10090","description":"A- and B-chain of the platelet-derived growth factor (PDGF). Binds to and activates PDGF receptor alpha (PDGFRalpha, P26618) and beta (PDGFRbeta, P05622) subunits by inducing receptor dimerisation and tyrosine phosphorylation. Is a potent mitogen for cells of mesenchymal origin. Plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Plays an important role in wound healing.","predictedComplex":false,"interactors":[{"ac":"EBI-9097402","identifier":"P20033","identifierLink":"https://www.uniprot.org/uniprotkb/P20033/entry","name":"Pdgfa","description":"Platelet-derived growth factor subunit A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9101509","identifier":"P31240","identifierLink":"https://www.uniprot.org/uniprotkb/P31240/entry","name":"Pdgfb","description":"Platelet-derived growth factor subunit B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1876","complexName":"Platelet-derived growth factor BB complex","organismName":"Homo sapiens; 9606","description":"A-chain of the platelet-derived growth factor (PDGF). Binds to and activates PDGF receptor alpha (PDGFRalpha, P16234) and beta (PDGFRbeta, P09619) subunits by inducing receptor dimerisation and tyrosine phosphorylation. Is a potent mitogen for cells of mesenchymal origin. Plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing.","predictedComplex":false,"interactors":[{"ac":"EBI-1554925","identifier":"P01127","identifierLink":"https://www.uniprot.org/uniprotkb/P01127/entry","name":"PDGFB","description":"Platelet-derived growth factor subunit B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2879","complexName":"Platelet-derived growth factor CC complex","organismName":"Homo sapiens; 9606","description":"C-chain of the platelet-derived growth factor (PDGF). Binds to and activates PDGF receptor alpha (PDGFRalpha, P16234) and beta (PDGFRbeta, P09619) subunits by inducing receptor dimerisation and tyrosine phosphorylation. Is a potent mitogen for cells of mesenchymal origin. Plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Required for normal skeleton formation during embryonic development, especially for normal development of the craniofacial skeleton and for normal development of the palate. Required for normal skin morphogenesis during embryonic development. Plays an important role in wound healing, where it appears to be involved in three stages: inflammation, proliferation and remodeling. Plays an important role in angiogenesis and blood vessel development. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintenance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function.","predictedComplex":false,"interactors":[{"ac":"EBI-8833587","identifier":"Q9NRA1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NRA1/entry","name":"PDGFC","description":"Platelet-derived growth factor C","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2880","complexName":"Platelet-derived growth factor DD complex","organismName":"Homo sapiens; 9606","description":"D-chain of the platelet-derived growth factor (PDGF). Binds to and activates PDGF receptor alpha (PDGFRalpha, P16234) and beta (PDGFRbeta, P09619) subunits by inducing receptor dimerisation and tyrosine phosphorylation. Is a potent mitogen for cells of mesenchymal origin. Plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Plays an important role in wound healing. Induces macrophage recruitment, increased interstitial pressure, and blood vessel maturation during angiogenesis. Can initiate events that lead to a mesangial proliferative glomerulonephritis, including influx of monocytes and macrophages and production of extracellular matrix","predictedComplex":false,"interactors":[{"ac":"EBI-9076600","identifier":"Q9GZP0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9GZP0/entry","name":"PDGFD","description":"Platelet-derived growth factor D","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2882","complexName":"PDGF receptor beta - PDGF-BB complex","organismName":"Homo sapiens; 9606","description":"Platelet-derived growth factor (PDGF) receptor beta (PDGFRbeta) that is activated by its bound ligand, PDGF B-chain. PDGFRbeta is a tyrosine-protein kinase that acts as a cell-surface receptor for PDGFB, and its related C- and D-chains, PDGFC (Q9NRA1) and PDGFD (Q9GZP0). It autophosphorylates on multiple tyrosines upon ligand binding initiating several signalling cascades and phosphorylation of downstream targets. Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing.","predictedComplex":false,"interactors":[{"ac":"EBI-1554925","identifier":"P01127","identifierLink":"https://www.uniprot.org/uniprotkb/P01127/entry","name":"PDGFB","description":"Platelet-derived growth factor subunit B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-641237","identifier":"P09619","identifierLink":"https://www.uniprot.org/uniprotkb/P09619/entry","name":"PDGFRB","description":"Platelet-derived growth factor receptor beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2883","complexName":"PDGF receptor alpha-beta - PDGF-BB complex","organismName":"Homo sapiens; 9606","description":"Platelet-derived growth factor (PDGF) receptors alpha and beta (PDGFRalpha-beta) that are activated by their bound ligand, PDGF B-chain. PDGFRalpha-beta is a tyrosine-protein kinase that acts as a cell-surface receptor for PDGFB, and its related C- and D-chains, PDGFC (Q9NRA1) and PDGFD (Q9GZP0). It autophosphorylates on multiple tyrosines upon ligand binding initiating several signalling cascades and phosphorylation of downstream targets. Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing.","predictedComplex":false,"interactors":[{"ac":"EBI-1554925","identifier":"P01127","identifierLink":"https://www.uniprot.org/uniprotkb/P01127/entry","name":"PDGFB","description":"Platelet-derived growth factor subunit B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2861522","identifier":"P16234","identifierLink":"https://www.uniprot.org/uniprotkb/P16234/entry","name":"PDGFRA","description":"Platelet-derived growth factor receptor alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-641237","identifier":"P09619","identifierLink":"https://www.uniprot.org/uniprotkb/P09619/entry","name":"PDGFRB","description":"Platelet-derived growth factor receptor beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2884","complexName":"PDGF receptor alpha - PDGF-BB complex","organismName":"Homo sapiens; 9606","description":"Platelet-derived growth factor (PDGF) receptor alpha (PDGFRalpha) that is activated by its bound ligand, PDGF B-chain. PDGFRalpha is a tyrosine-protein kinase that acts as a cell-surface receptor for PDGFB, and its related A- and C-chains, PDGFA (P04085) and PDGFC (Q9NRA1). It autophosphorylates on multiple tyrosines upon ligand binding initiating several signalling cascades and phosphorylation of downstream targets. Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing.","predictedComplex":false,"interactors":[{"ac":"EBI-1554925","identifier":"P01127","identifierLink":"https://www.uniprot.org/uniprotkb/P01127/entry","name":"PDGFB","description":"Platelet-derived growth factor subunit B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2861522","identifier":"P16234","identifierLink":"https://www.uniprot.org/uniprotkb/P16234/entry","name":"PDGFRA","description":"Platelet-derived growth factor receptor alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2885","complexName":"PDGF receptor alpha - PDGF-AB complex","organismName":"Homo sapiens; 9606","description":"Platelet-derived growth factor (PDGF) receptor alpha (PDGFRalpha) that is activated by its bound ligand, PDGF-AB dimer (CPX-1875). PDGFRalpha is a tyrosine-protein kinase that acts as a cell-surface receptor for PDGFA and PDGFB, and its related C-chain, PDGFC (Q9NRA1). It autophosphorylates on multiple tyrosines upon ligand binding initiating several signalling cascades and phosphorylation of downstream targets. Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal lung alveolar septum formation during embryogenesis, normal development of the gastrointestinal tract, normal development of Leydig cells and spermatogenesis. Required for normal oligodendrocyte development and normal myelination in the spinal cord and cerebellum. Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing.","predictedComplex":false,"interactors":[{"ac":"EBI-1554925","identifier":"P01127","identifierLink":"https://www.uniprot.org/uniprotkb/P01127/entry","name":"PDGFB","description":"Platelet-derived growth factor subunit B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2861522","identifier":"P16234","identifierLink":"https://www.uniprot.org/uniprotkb/P16234/entry","name":"PDGFRA","description":"Platelet-derived growth factor receptor alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2881386","identifier":"P04085","identifierLink":"https://www.uniprot.org/uniprotkb/P04085/entry","name":"PDGFA","description":"Platelet-derived growth factor subunit A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2886","complexName":"PDGF receptor beta - PDGF-AB complex","organismName":"Homo sapiens; 9606","description":"Platelet-derived growth factor (PDGF) receptor beta (PDGFRbeta) that is activated by its bound ligand, PDGF-AB dimer (CPX-1875). PDGFRbeta is a tyrosine-protein kinase that acts as a cell-surface receptor for PDGF-AB, and its related C- and D-chains, PDGFC (Q9NRA1) and PDGFD (Q9GZP0). It autophosphorylates on multiple tyrosines upon ligand binding initiating several signalling cascades and phosphorylation of downstream targets. Plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal lung alveolar septum formation during embryogenesis, normal development of the gastrointestinal tract, normal development of Leydig cells and spermatogenesis. Required for normal oligodendrocyte development and normal myelination in the spinal cord and cerebellum. Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing.","predictedComplex":false,"interactors":[{"ac":"EBI-1554925","identifier":"P01127","identifierLink":"https://www.uniprot.org/uniprotkb/P01127/entry","name":"PDGFB","description":"Platelet-derived growth factor subunit B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2881386","identifier":"P04085","identifierLink":"https://www.uniprot.org/uniprotkb/P04085/entry","name":"PDGFA","description":"Platelet-derived growth factor subunit A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-641237","identifier":"P09619","identifierLink":"https://www.uniprot.org/uniprotkb/P09619/entry","name":"PDGFRB","description":"Platelet-derived growth factor receptor beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2887","complexName":"PDGF receptor alpha - PDGF-CC complex","organismName":"Homo sapiens; 9606","description":"Platelet-derived growth factor (PDGF) receptor alpha (PDGFRalpha) that is activated by its bound ligand, PDGF C-chain. PDGFRalpha is a tyrosine-protein kinase that acts as a cell-surface receptor for PDGFC, and its related A- and B-chains, PDGFA (P04085) and PDGFB (P01127). It autophosphorylates on multiple tyrosines upon ligand binding initiating several signalling cascades and phosphorylation of downstream targets. Is a potent mitogen for cells of mesenchymal origin. Plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Required for normal skeleton formation during embryonic development, especially for normal development of the craniofacial skeleton and for normal development of the palate. Required for normal skin morphogenesis during embryonic development. Plays an important role in wound healing, where it appears to be involved in three stages: inflammation, proliferation and remodeling. Plays an important role in angiogenesis and blood vessel development. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintenance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function.","predictedComplex":false,"interactors":[{"ac":"EBI-2861522","identifier":"P16234","identifierLink":"https://www.uniprot.org/uniprotkb/P16234/entry","name":"PDGFRA","description":"Platelet-derived growth factor receptor alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8833587","identifier":"Q9NRA1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NRA1/entry","name":"PDGFC","description":"Platelet-derived growth factor C","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2888","complexName":"PDGF receptor alpha-beta - PDGF-CC complex","organismName":"Homo sapiens; 9606","description":"Platelet-derived growth factor (PDGF) receptors alpha and beta (PDGFRalpha-beta) that are activated by their bound ligand, PDGF C-chain. PDGFRalpha-beta is a tyrosine-protein kinase that acts as a cell-surface receptor for PDGFC, and its related B- and D-chains, PDGFB (P01127) and PDGFD (Q9GZP0). It autophosphorylates on multiple tyrosines upon ligand binding initiating several signalling cascades and phosphorylation of downstream targets. Is a potent mitogen for cells of mesenchymal origin. Plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Required for normal skeleton formation during embryonic development, especially for normal development of the craniofacial skeleton and for normal development of the palate. Required for normal skin morphogenesis during embryonic development. Plays an important role in wound healing, where it appears to be involved in three stages: inflammation, proliferation and remodeling. Plays an important role in angiogenesis and blood vessel development. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintenance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function.","predictedComplex":false,"interactors":[{"ac":"EBI-2861522","identifier":"P16234","identifierLink":"https://www.uniprot.org/uniprotkb/P16234/entry","name":"PDGFRA","description":"Platelet-derived growth factor receptor alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-641237","identifier":"P09619","identifierLink":"https://www.uniprot.org/uniprotkb/P09619/entry","name":"PDGFRB","description":"Platelet-derived growth factor receptor beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8833587","identifier":"Q9NRA1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NRA1/entry","name":"PDGFC","description":"Platelet-derived growth factor C","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2889","complexName":"PDGF receptor beta - PDGF-DD complex","organismName":"Homo sapiens; 9606","description":"Platelet-derived growth factor (PDGF) receptor beta (PDGFRbeta) that is activated by its bound ligand, PDGF D-chain. PDGFRbeta is a tyrosine-protein kinase that acts as a cell-surface receptor for PDGFB, and its related B- and C-chains, PDGFB (P01127) and PDGFC (Q9NRA1). It autophosphorylates on multiple tyrosines upon ligand binding initiating several signalling cascades and phosphorylation of downstream targets. Plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Plays an important role in wound healing. Induces macrophage recruitment, increased interstitial pressure, and blood vessel maturation during angiogenesis. Can initiate events that lead to a mesangial proliferative glomerulonephritis, including influx of monocytes and macrophages and production of extracellular matrix","predictedComplex":false,"interactors":[{"ac":"EBI-641237","identifier":"P09619","identifierLink":"https://www.uniprot.org/uniprotkb/P09619/entry","name":"PDGFRB","description":"Platelet-derived growth factor receptor beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9076600","identifier":"Q9GZP0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9GZP0/entry","name":"PDGFD","description":"Platelet-derived growth factor D","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2890","complexName":"PDGF receptor alpha-beta - PDGF-DD complex","organismName":"Homo sapiens; 9606","description":"Platelet-derived growth factor (PDGF) receptors alpha and beta (PDGFRalpha-beta) that is activated by its bound ligand, PDGF D-chain. PDGFRalpha-beta is a tyrosine-protein kinase that acts as a cell-surface receptor for PDGFD, and its related B- and C-chains, PDGFB (P01127) and PDGFC (Q9NRA1). It autophosphorylates on multiple tyrosines upon ligand binding initiating several signalling cascades and phosphorylation of downstream targets. Plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Plays an important role in wound healing. Induces macrophage recruitment, increased interstitial pressure, and blood vessel maturation during angiogenesis. Can initiate events that lead to a mesangial proliferative glomerulonephritis, including influx of monocytes and macrophages and production of extracellular matrix","predictedComplex":false,"interactors":[{"ac":"EBI-2861522","identifier":"P16234","identifierLink":"https://www.uniprot.org/uniprotkb/P16234/entry","name":"PDGFRA","description":"Platelet-derived growth factor receptor alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-641237","identifier":"P09619","identifierLink":"https://www.uniprot.org/uniprotkb/P09619/entry","name":"PDGFRB","description":"Platelet-derived growth factor receptor beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9076600","identifier":"Q9GZP0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9GZP0/entry","name":"PDGFD","description":"Platelet-derived growth factor D","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2891","complexName":"PDGF receptor beta - PDGF-CC complex","organismName":"Homo sapiens; 9606","description":"Platelet-derived growth factor (PDGF) receptors beta (PDGFRbeta) that is activated by its bound ligand, PDGF C-chain. PDGFRbeta is a tyrosine-protein kinase that acts as a cell-surface receptor for PDGFC, and its related B- and D-chains, PDGFB (P01127) and PDGFD (Q9GZP0). It autophosphorylates on multiple tyrosines upon ligand binding initiating several signalling cascades and phosphorylation of downstream targets. Is a potent mitogen for cells of mesenchymal origin. Plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Required for normal skeleton formation during embryonic development, especially for normal development of the craniofacial skeleton and for normal development of the palate. Required for normal skin morphogenesis during embryonic development. Plays an important role in wound healing, where it appears to be involved in three stages: inflammation, proliferation and remodeling. Plays an important role in angiogenesis and blood vessel development. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintenance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function.","predictedComplex":false,"interactors":[{"ac":"EBI-641237","identifier":"P09619","identifierLink":"https://www.uniprot.org/uniprotkb/P09619/entry","name":"PDGFRB","description":"Platelet-derived growth factor receptor beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8833587","identifier":"Q9NRA1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NRA1/entry","name":"PDGFC","description":"Platelet-derived growth factor C","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2892","complexName":"PDGF receptor alpha-beta - PDGF-AB complex","organismName":"Homo sapiens; 9606","description":"Platelet-derived growth factor (PDGF) receptors alpha and beta (PDGFRalpha-beta) that are activated by their bound ligand, PDGF-AB. PDGFRalpha-beta is a tyrosine-protein kinase that acts as a cell-surface receptor for PDGF-AB, and its related C- and D-chains, PDGFC (Q9NRA1) and PDGFD (Q9GZP0). It autophosphorylates on multiple tyrosines upon ligand binding initiating several signalling cascades and phosphorylation of downstream targets. Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing.","predictedComplex":false,"interactors":[{"ac":"EBI-1554925","identifier":"P01127","identifierLink":"https://www.uniprot.org/uniprotkb/P01127/entry","name":"PDGFB","description":"Platelet-derived growth factor subunit B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2861522","identifier":"P16234","identifierLink":"https://www.uniprot.org/uniprotkb/P16234/entry","name":"PDGFRA","description":"Platelet-derived growth factor receptor alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2881386","identifier":"P04085","identifierLink":"https://www.uniprot.org/uniprotkb/P04085/entry","name":"PDGFA","description":"Platelet-derived growth factor subunit A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-641237","identifier":"P09619","identifierLink":"https://www.uniprot.org/uniprotkb/P09619/entry","name":"PDGFRB","description":"Platelet-derived growth factor receptor beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2901","complexName":"PDGF receptor alpha - PDGF-AB complex","organismName":"Mus musculus; 10090","description":"Platelet-derived growth factor (PDGF) receptor alpha (PDGFRalpha) that is activated by its bound ligand, PDGF-AB dimer (CPX-1875). PDGFRalpha is a tyrosine-protein kinase that acts as a cell-surface receptor for PDGFA and PDGFB, and its related C-chain, PDGFC (Q9NRA1). It autophosphorylates on multiple tyrosines upon ligand binding initiating several signalling cascades and phosphorylation of downstream targets. Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal lung alveolar septum formation during embryogenesis, normal development of the gastrointestinal tract, normal development of Leydig cells and spermatogenesis. Required for normal oligodendrocyte development and normal myelination in the spinal cord and cerebellum. Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing.","predictedComplex":false,"interactors":[{"ac":"EBI-7290093","identifier":"P26618","identifierLink":"https://www.uniprot.org/uniprotkb/P26618/entry","name":"Pdgfra","description":"Platelet-derived growth factor receptor alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9097402","identifier":"P20033","identifierLink":"https://www.uniprot.org/uniprotkb/P20033/entry","name":"Pdgfa","description":"Platelet-derived growth factor subunit A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9101509","identifier":"P31240","identifierLink":"https://www.uniprot.org/uniprotkb/P31240/entry","name":"Pdgfb","description":"Platelet-derived growth factor subunit B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2903","complexName":"PDGF receptor alpha-beta - PDGF-AB complex","organismName":"Mus musculus; 10090","description":"Platelet-derived growth factor (PDGF) receptors alpha and beta (PDGFRalpha-beta) that are activated by their bound ligand, PDGF-AB. PDGFRalpha-beta is a tyrosine-protein kinase that acts as a cell-surface receptor for PDGF-AB, and its related C- and D-chains, PDGFC (Q8CI19) and PDGFD (Q925I7). It autophosphorylates on multiple tyrosines upon ligand binding initiating several signalling cascades and phosphorylation of downstream targets. Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing.","predictedComplex":false,"interactors":[{"ac":"EBI-1554855","identifier":"P05622","identifierLink":"https://www.uniprot.org/uniprotkb/P05622/entry","name":"Pdgfrb","description":"Platelet-derived growth factor receptor beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7290093","identifier":"P26618","identifierLink":"https://www.uniprot.org/uniprotkb/P26618/entry","name":"Pdgfra","description":"Platelet-derived growth factor receptor alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9097402","identifier":"P20033","identifierLink":"https://www.uniprot.org/uniprotkb/P20033/entry","name":"Pdgfa","description":"Platelet-derived growth factor subunit A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9101509","identifier":"P31240","identifierLink":"https://www.uniprot.org/uniprotkb/P31240/entry","name":"Pdgfb","description":"Platelet-derived growth factor subunit B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2904","complexName":"PDGF receptor beta - PDGF-AB complex","organismName":"Mus musculus; 10090","description":"Platelet-derived growth factor (PDGF) receptor beta (PDGFRbeta) that is activated by its bound ligand, PDGF-AB dimer (CPX-1875). PDGFRbeta is a tyrosine-protein kinase that acts as a cell-surface receptor for PDGF-AB, and its related C- and D-chains, PDGFC (Q8CI19) and PDGFD (Q925I7). It autophosphorylates on multiple tyrosines upon ligand binding initiating several signalling cascades and phosphorylation of downstream targets. Plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal lung alveolar septum formation during embryogenesis, normal development of the gastrointestinal tract, normal development of Leydig cells and spermatogenesis. Required for normal oligodendrocyte development and normal myelination in the spinal cord and cerebellum. Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing.","predictedComplex":false,"interactors":[{"ac":"EBI-1554855","identifier":"P05622","identifierLink":"https://www.uniprot.org/uniprotkb/P05622/entry","name":"Pdgfrb","description":"Platelet-derived growth factor receptor beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9097402","identifier":"P20033","identifierLink":"https://www.uniprot.org/uniprotkb/P20033/entry","name":"Pdgfa","description":"Platelet-derived growth factor subunit A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9101509","identifier":"P31240","identifierLink":"https://www.uniprot.org/uniprotkb/P31240/entry","name":"Pdgfb","description":"Platelet-derived growth factor subunit B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2905","complexName":"Platelet-derived growth factor BB complex","organismName":"Mus musculus; 10090","description":"A-chain of the platelet-derived growth factor (PDGF). Binds to and activates PDGF receptor alpha (PDGFRalpha, P26618) and beta (PDGFRbeta, P05622) subunits by inducing receptor dimerisation and tyrosine phosphorylation. Is a potent mitogen for cells of mesenchymal origin. Plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing.","predictedComplex":false,"interactors":[{"ac":"EBI-9101509","identifier":"P31240","identifierLink":"https://www.uniprot.org/uniprotkb/P31240/entry","name":"Pdgfb","description":"Platelet-derived growth factor subunit B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2906","complexName":"PDGF receptor alpha - PDGF-BB complex","organismName":"Mus musculus; 10090","description":"Platelet-derived growth factor (PDGF) receptor alpha (PDGFRalpha) that is activated by its bound ligand, PDGF B-chain. PDGFRalpha is a tyrosine-protein kinase that acts as a cell-surface receptor for PDGFB, and its related A- and C-chains, PDGFA (P20033) and PDGFC (Q8CI19). It autophosphorylates on multiple tyrosines upon ligand binding initiating several signalling cascades and phosphorylation of downstream targets. Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing.","predictedComplex":false,"interactors":[{"ac":"EBI-7290093","identifier":"P26618","identifierLink":"https://www.uniprot.org/uniprotkb/P26618/entry","name":"Pdgfra","description":"Platelet-derived growth factor receptor alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9101509","identifier":"P31240","identifierLink":"https://www.uniprot.org/uniprotkb/P31240/entry","name":"Pdgfb","description":"Platelet-derived growth factor subunit B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2907","complexName":"PDGF receptor alpha-beta - PDGF-BB complex","organismName":"Mus musculus; 10090","description":"Platelet-derived growth factor (PDGF) receptors alpha and beta (PDGFRalpha-beta) that are activated by their bound ligand, PDGF B-chain. PDGFRalpha-beta is a tyrosine-protein kinase that acts as a cell-surface receptor for PDGFB, and its related C- and D-chains, PDGFC (Q8CI19) and PDGFD (Q925I7). It autophosphorylates on multiple tyrosines upon ligand binding initiating several signalling cascades and phosphorylation of downstream targets. Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing.","predictedComplex":false,"interactors":[{"ac":"EBI-1554855","identifier":"P05622","identifierLink":"https://www.uniprot.org/uniprotkb/P05622/entry","name":"Pdgfrb","description":"Platelet-derived growth factor receptor beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7290093","identifier":"P26618","identifierLink":"https://www.uniprot.org/uniprotkb/P26618/entry","name":"Pdgfra","description":"Platelet-derived growth factor receptor alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9101509","identifier":"P31240","identifierLink":"https://www.uniprot.org/uniprotkb/P31240/entry","name":"Pdgfb","description":"Platelet-derived growth factor subunit B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2908","complexName":"PDGF receptor beta - PDGF-BB complex","organismName":"Mus musculus; 10090","description":"Platelet-derived growth factor (PDGF) receptor beta (PDGFRbeta) that is activated by its bound ligand, PDGF B-chain. PDGFRbeta is a tyrosine-protein kinase that acts as a cell-surface receptor for PDGFB, and its related C- and D-chains, PDGFC (Q8CI19) and PDGFD (Q925I7). It autophosphorylates on multiple tyrosines upon ligand binding initiating several signalling cascades and phosphorylation of downstream targets. Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central nervous system, skin, lung, heart and placenta. Required for normal blood vessel development, and for normal development of kidney glomeruli. Plays an important role in wound healing.","predictedComplex":false,"interactors":[{"ac":"EBI-1554855","identifier":"P05622","identifierLink":"https://www.uniprot.org/uniprotkb/P05622/entry","name":"Pdgfrb","description":"Platelet-derived growth factor receptor beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9101509","identifier":"P31240","identifierLink":"https://www.uniprot.org/uniprotkb/P31240/entry","name":"Pdgfb","description":"Platelet-derived growth factor subunit B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2909","complexName":"Platelet-derived growth factor CC complex","organismName":"Mus musculus; 10090","description":"C-chain of the platelet-derived growth factor (PDGF). Binds to and activates PDGF receptor alpha (PDGFRalpha, P26618) and beta (PDGFRbeta, P05622) subunits by inducing receptor dimerisation and tyrosine phosphorylation. Is a potent mitogen for cells of mesenchymal origin. Plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Required for normal skeleton formation during embryonic development, especially for normal development of the craniofacial skeleton and for normal development of the palate. Required for normal skin morphogenesis during embryonic development. Plays an important role in wound healing, where it appears to be involved in three stages: inflammation, proliferation and remodeling. Plays an important role in angiogenesis and blood vessel development. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintenance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function.","predictedComplex":false,"interactors":[{"ac":"EBI-9102033","identifier":"Q8CI19","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CI19/entry","name":"Pdgfc","description":"Platelet-derived growth factor C","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2912","complexName":"PDGF receptor alpha - PDGF-CC complex","organismName":"Mus musculus; 10090","description":"Platelet-derived growth factor (PDGF) receptor alpha (PDGFRalpha) that is activated by its bound ligand, PDGF C-chain. PDGFRalpha is a tyrosine-protein kinase that acts as a cell-surface receptor for PDGFC, and its related A- and B-chains, PDGFA (P20033) and PDGFB (P31240). It autophosphorylates on multiple tyrosines upon ligand binding initiating several signalling cascades and phosphorylation of downstream targets. Is a potent mitogen for cells of mesenchymal origin. Plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Required for normal skeleton formation during embryonic development, especially for normal development of the craniofacial skeleton and for normal development of the palate. Required for normal skin morphogenesis during embryonic development. Plays an important role in wound healing, where it appears to be involved in three stages: inflammation, proliferation and remodeling. Plays an important role in angiogenesis and blood vessel development. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintenance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function.","predictedComplex":false,"interactors":[{"ac":"EBI-7290093","identifier":"P26618","identifierLink":"https://www.uniprot.org/uniprotkb/P26618/entry","name":"Pdgfra","description":"Platelet-derived growth factor receptor alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9102033","identifier":"Q8CI19","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CI19/entry","name":"Pdgfc","description":"Platelet-derived growth factor C","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2913","complexName":"PDGF receptor alpha-beta - PDGF-CC complex","organismName":"Mus musculus; 10090","description":"Platelet-derived growth factor (PDGF) receptors alpha and beta (PDGFRalpha-beta) that are activated by their bound ligand, PDGF C-chain. PDGFRalpha-beta is a tyrosine-protein kinase that acts as a cell-surface receptor for PDGFC, and its related B- and D-chains, PDGFB (P31240) and PDGFD (Q925I7). It autophosphorylates on multiple tyrosines upon ligand binding initiating several signalling cascades and phosphorylation of downstream targets. Is a potent mitogen for cells of mesenchymal origin. Plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Required for normal skeleton formation during embryonic development, especially for normal development of the craniofacial skeleton and for normal development of the palate. Required for normal skin morphogenesis during embryonic development. Plays an important role in wound healing, where it appears to be involved in three stages: inflammation, proliferation and remodeling. Plays an important role in angiogenesis and blood vessel development. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintenance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function.","predictedComplex":false,"interactors":[{"ac":"EBI-1554855","identifier":"P05622","identifierLink":"https://www.uniprot.org/uniprotkb/P05622/entry","name":"Pdgfrb","description":"Platelet-derived growth factor receptor beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7290093","identifier":"P26618","identifierLink":"https://www.uniprot.org/uniprotkb/P26618/entry","name":"Pdgfra","description":"Platelet-derived growth factor receptor alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9102033","identifier":"Q8CI19","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CI19/entry","name":"Pdgfc","description":"Platelet-derived growth factor C","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2914","complexName":"PDGF receptor beta - PDGF-CC complex","organismName":"Mus musculus; 10090","description":"Platelet-derived growth factor (PDGF) receptors beta (PDGFRbeta) that is activated by its bound ligand, PDGF C-chain. PDGFRbeta is a tyrosine-protein kinase that acts as a cell-surface receptor for PDGFC, and its related B- and D-chains, PDGFB (P31240) and PDGFD (Q925I7). It autophosphorylates on multiple tyrosines upon ligand binding initiating several signalling cascades and phosphorylation of downstream targets. Is a potent mitogen for cells of mesenchymal origin. Plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Required for normal skeleton formation during embryonic development, especially for normal development of the craniofacial skeleton and for normal development of the palate. Required for normal skin morphogenesis during embryonic development. Plays an important role in wound healing, where it appears to be involved in three stages: inflammation, proliferation and remodeling. Plays an important role in angiogenesis and blood vessel development. Involved in fibrotic processes, in which transformation of interstitial fibroblasts into myofibroblasts plus collagen deposition occurs. The CUB domain has mitogenic activity in coronary artery smooth muscle cells, suggesting a role beyond the maintenance of the latency of the PDGF domain. In the nucleus, PDGFC seems to have additional function.","predictedComplex":false,"interactors":[{"ac":"EBI-1554855","identifier":"P05622","identifierLink":"https://www.uniprot.org/uniprotkb/P05622/entry","name":"Pdgfrb","description":"Platelet-derived growth factor receptor beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9102033","identifier":"Q8CI19","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CI19/entry","name":"Pdgfc","description":"Platelet-derived growth factor C","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2915","complexName":"Platelet-derived growth factor DD complex","organismName":"Mus musculus; 10090","description":"D-chain of the platelet-derived growth factor (PDGF). Binds to and activates PDGF receptor alpha (PDGFRalpha, P26618) and beta (PDGFRbeta, P05622) subunits by inducing receptor dimerisation and tyrosine phosphorylation. Is a potent mitogen for cells of mesenchymal origin. Plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Plays an important role in wound healing. Induces macrophage recruitment, increased interstitial pressure, and blood vessel maturation during angiogenesis. Can initiate events that lead to a mesangial proliferative glomerulonephritis, including influx of monocytes and macrophages and production of extracellular matrix","predictedComplex":false,"interactors":[{"ac":"EBI-9102539","identifier":"Q925I7","identifierLink":"https://www.uniprot.org/uniprotkb/Q925I7/entry","name":"Pdgfd","description":"Platelet-derived growth factor D","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2916","complexName":"PDGF receptor alpha-beta - PDGF-DD complex","organismName":"Mus musculus; 10090","description":"Platelet-derived growth factor (PDGF) receptors alpha and beta (PDGFRalpha-beta) that is activated by its bound ligand, PDGF D-chain. PDGFRalpha-beta is a tyrosine-protein kinase that acts as a cell-surface receptor for PDGFB, and its related B- and C-chains, PDGFB (P31240) and PDGFC (Q8CI19). It autophosphorylates on multiple tyrosines upon ligand binding initiating several signalling cascades and phosphorylation of downstream targets. Plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Plays an important role in wound healing. Induces macrophage recruitment, increased interstitial pressure, and blood vessel maturation during angiogenesis. Can initiate events that lead to a mesangial proliferative glomerulonephritis, including influx of monocytes and macrophages and production of extracellular matrix","predictedComplex":false,"interactors":[{"ac":"EBI-1554855","identifier":"P05622","identifierLink":"https://www.uniprot.org/uniprotkb/P05622/entry","name":"Pdgfrb","description":"Platelet-derived growth factor receptor beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7290093","identifier":"P26618","identifierLink":"https://www.uniprot.org/uniprotkb/P26618/entry","name":"Pdgfra","description":"Platelet-derived growth factor receptor alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9102539","identifier":"Q925I7","identifierLink":"https://www.uniprot.org/uniprotkb/Q925I7/entry","name":"Pdgfd","description":"Platelet-derived growth factor D","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2917","complexName":"PDGF receptor beta - PDGF-DD complex","organismName":"Mus musculus; 10090","description":"Platelet-derived growth factor (PDGF) receptor beta (PDGFRbeta) that is activated by its bound ligand, PDGF D-chain. PDGFRbeta is a tyrosine-protein kinase that acts as a cell-surface receptor for PDGFB, and its related B- and C-chains, PDGFB (P31240) and PDGFC (Q8CI19). It autophosphorylates on multiple tyrosines upon ligand binding initiating several signalling cascades and phosphorylation of downstream targets. Plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Plays an important role in wound healing. Induces macrophage recruitment, increased interstitial pressure, and blood vessel maturation during angiogenesis. Can initiate events that lead to a mesangial proliferative glomerulonephritis, including influx of monocytes and macrophages and production of extracellular matrix","predictedComplex":false,"interactors":[{"ac":"EBI-1554855","identifier":"P05622","identifierLink":"https://www.uniprot.org/uniprotkb/P05622/entry","name":"Pdgfrb","description":"Platelet-derived growth factor receptor beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9102539","identifier":"Q925I7","identifierLink":"https://www.uniprot.org/uniprotkb/Q925I7/entry","name":"Pdgfd","description":"Platelet-derived growth factor D","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1877","complexName":"LUBAC ubiquitin ligase complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the synthesis of linear ubiquitin chains, conjugating linear polyubiquitin chains through the N-terminal Met of ubiquitin and linking to substrates. Plays a key role in inflammatory response through the activation of NF-kappa-B and inflammsone activation, protection from programmed cell death and autophagy.","predictedComplex":false,"interactors":[{"ac":"EBI-2340624","identifier":"Q9BYM8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BYM8/entry","name":"RBCK1","description":"RanBP-type and C3HC4-type zinc finger-containing protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22770","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3942966","identifier":"Q9H0F6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H0F6/entry","name":"SHARPIN","description":"Sharpin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22770","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-948111","identifier":"Q96EP0","identifierLink":"https://www.uniprot.org/uniprotkb/Q96EP0/entry","name":"RNF31","description":"E3 ubiquitin-protein ligase RNF31","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16004","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1878","complexName":"Replication protein A complex, RPA2 variant","organismName":"Homo sapiens; 9606","description":"Single-stranded DNA binding protein complex involved in all processes that involve single-stranded DNA (ssDNA) by binding to and protecting exposed ssDNA from nucleases and preventing formation of secondary structures. Forms a physical platform to recruit other factors to the DNA including those involved in DNA damage signaling, DNA repair, and DNA replication. RPA protects against inappropriate telomere recombination, and upon telomere uncapping, prevents cell proliferation by a checkpoint-independent pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-621389","identifier":"P27694","identifierLink":"https://www.uniprot.org/uniprotkb/P27694/entry","name":"RPA1","description":"Replication protein A 70 kDa DNA-binding subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23273","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-621404","identifier":"P15927","identifierLink":"https://www.uniprot.org/uniprotkb/P15927/entry","name":"RPA2","description":"Replication protein A 32 kDa subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13989","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-621428","identifier":"P35244","identifierLink":"https://www.uniprot.org/uniprotkb/P35244/entry","name":"RPA3","description":"Replication protein A 14 kDa subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15114","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1879","complexName":"Replication protein A complex, RPA4 variant","organismName":"Homo sapiens; 9606","description":"Single-stranded DNA binding protein complex involved in processes that involve single-stranded DNA (ssDNA) by binding to and protecting exposed ssDNA from nucleases and preventing formation of secondary structures. Forms a physical platform to recruit other factors to the DNA involved in DNA repair. Involved in DNA repair via support for DNA synthesis by DNA polymerase delta (CPX-2097) in the presence of PCNA (CPX-538) and RFC (CPX-415). The complex does not play a role in chromosomal DNA replication or cell cycle progression through S-phase. This appears to be due to a reduced interaction with DNA polymerase alpha:primase (CPX-2087), required for DNA replication initiation.","predictedComplex":false,"interactors":[{"ac":"EBI-2856301","identifier":"Q13156","identifierLink":"https://www.uniprot.org/uniprotkb/Q13156/entry","name":"RPA4","description":"Replication protein A 30 kDa subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13989","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-621389","identifier":"P27694","identifierLink":"https://www.uniprot.org/uniprotkb/P27694/entry","name":"RPA1","description":"Replication protein A 70 kDa DNA-binding subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23273","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-621428","identifier":"P35244","identifierLink":"https://www.uniprot.org/uniprotkb/P35244/entry","name":"RPA3","description":"Replication protein A 14 kDa subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15114","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1880","complexName":"Nuclear origin recognition complex","organismName":"Homo sapiens; 9606","description":"Binds and encircles origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not yet been identified. ORC recruits CDC6 and CDT1 to promote the loading of the MCM2-7 mini-chromosome maintenance complex (CPX-2940) onto chromatin to form the pre-replication complex necessary to initiate DNA replication. ORC is dynamically assembled and disassembled during the cell cycle. The complex is formed in an ATP-dependent manner at the exit from anaphase of mitosis and the complex binds to chromatin in an ORC1-dependent manner. ORC is disassembled in S phase, either by degradation of ORC1 or by a process involving ATP hydrolysis in the complex. ORC1 is thought to be regenerated and to cooperate with ORC4 to initiate a new cycle of pre-RC formation.","predictedComplex":false,"interactors":[{"ac":"EBI-374840","identifier":"Q9Y5N6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5N6/entry","name":"ORC6","description":"Origin recognition complex subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13394","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-374847","identifier":"Q13415","identifierLink":"https://www.uniprot.org/uniprotkb/Q13415/entry","name":"ORC1","description":"Origin recognition complex subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10763","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-374889","identifier":"O43929","identifierLink":"https://www.uniprot.org/uniprotkb/O43929/entry","name":"ORC4","description":"Origin recognition complex subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12087","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-374916","identifier":"Q9UBD5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UBD5/entry","name":"ORC3","description":"Origin recognition complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12748","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-374928","identifier":"O43913","identifierLink":"https://www.uniprot.org/uniprotkb/O43913/entry","name":"ORC5","description":"Origin recognition complex subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12705","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-374957","identifier":"Q13416","identifierLink":"https://www.uniprot.org/uniprotkb/Q13416/entry","name":"ORC2","description":"Origin recognition complex subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14052","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1915","complexName":"Nuclear origin recognition complex","organismName":"Mus musculus; 10090","description":"Binds and encircles origins of replication. DNA-binding is ATP-dependent, however specific DNA sequences that define origins of replication have not yet been identified. ORC recruits CDC6 and CDT1 to promote the loading of the MCM2-7 mini-chromosome maintenance complex (CPX-2940) onto chromatin to form the pre-replication complex necessary to initiate DNA replication. ORC is dynamically assembled and disassembled during the cell cycle. The complex is formed in an ATP-dependent manner at the exit from anaphase of mitosis and the complex binds to chromatin in an ORC1-dependent manner. ORC is disassemnbled in S phase, either by degradation of ORC1 or by a process involving ATP hydrolysis in the complex. ORC1 is thought to be regenerated and to cooperate with ORC4 to initiate a new cycle of pre-RC formation.","predictedComplex":false,"interactors":[{"ac":"EBI-3870607","identifier":"Q9WUV0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WUV0/entry","name":"Orc5","description":"Origin recognition complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12705","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-457142","identifier":"Q60862","identifierLink":"https://www.uniprot.org/uniprotkb/Q60862/entry","name":"Orc2","description":"Origin recognition complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14052","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6171366","identifier":"Q9WUJ8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WUJ8/entry","name":"Orc6","description":"Origin recognition complex subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13394","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6171377","identifier":"O88708","identifierLink":"https://www.uniprot.org/uniprotkb/O88708/entry","name":"Orc4","description":"Origin recognition complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12087","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6171392","identifier":"Q9JK30","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JK30/entry","name":"Orc3","description":"Origin recognition complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12748","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-773812","identifier":"Q9Z1N2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z1N2/entry","name":"Orc1","description":"Origin recognition complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10763","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1881","complexName":"Phosphatidylinositol 3-kinase complex, class III, type I","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes phosphorylation of phosphatidyl inositol, one of the major phospholipids in the cell, specifically at the d-3 position of the inositol ring, to generate PtdIns(3)P (CHEBI:17283). The formation of PtdIns(3)P is crucial for membrane recruitment of ATG proteins and the early stage of autophagosome formation","predictedComplex":false,"interactors":[{"ac":"EBI-20347","identifier":"P22219","identifierLink":"https://www.uniprot.org/uniprotkb/P22219/entry","name":"VPS15","description":"Serine/threonine-protein kinase VPS15","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR17583","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20405","identifier":"P22543","identifierLink":"https://www.uniprot.org/uniprotkb/P22543/entry","name":"VPS34","description":"Phosphatidylinositol 3-kinase VPS34","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2670","identifier":"Q02948","identifierLink":"https://www.uniprot.org/uniprotkb/Q02948/entry","name":"VPS30","description":"Vacuolar protein sorting-associated protein 30","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12768","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2699","identifier":"P38270","identifierLink":"https://www.uniprot.org/uniprotkb/P38270/entry","name":"ATG14","description":"Autophagy-related protein 14","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-35873","identifier":"Q05789","identifierLink":"https://www.uniprot.org/uniprotkb/Q05789/entry","name":"ATG38","description":"PtdIns3K complex I subunit atg38","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1882","complexName":"HAP1 transcriptional repressor complex, SSA1 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Represses the transcriptional activity of HAP1 in the absence of haem. When haem concentration increases, haem enhances the interaction of Hsp90 with HAP1 and binds to AP1, causing conformational changes in the multi-chaperone-HAP1 complex and leading to HAP1 activation.","predictedComplex":false,"interactors":[{"ac":"EBI-10420","identifier":"P25491","identifierLink":"https://www.uniprot.org/uniprotkb/P25491/entry","name":"YDJ1","description":"Mitochondrial protein import protein MAS5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16401534","identifier":"P0CE41","identifierLink":"https://www.uniprot.org/uniprotkb/P0CE41/entry","name":"HAP1","description":"Heme-responsive zinc finger transcription factor HAP1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31944","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18084","identifier":"P25567","identifierLink":"https://www.uniprot.org/uniprotkb/P25567/entry","name":"SRO9","description":"RNA-binding protein SRO9","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22792","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8591","identifier":"P10591","identifierLink":"https://www.uniprot.org/uniprotkb/P10591/entry","name":"SSA1","description":"Heat shock protein SSA1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1883","complexName":"HAP1 transcriptional repressor complex, SSA2 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Represses the transcriptional activity of HAP1 in the absence of haem. When haem concentration increases, haem enhances the interaction of Hsp90 with HAP1 and binds to HAP1, causing conformational changes in the multi-chaperone-HAP1 complex and leading to HAP1 activation.","predictedComplex":false,"interactors":[{"ac":"EBI-10420","identifier":"P25491","identifierLink":"https://www.uniprot.org/uniprotkb/P25491/entry","name":"YDJ1","description":"Mitochondrial protein import protein MAS5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16401534","identifier":"P0CE41","identifierLink":"https://www.uniprot.org/uniprotkb/P0CE41/entry","name":"HAP1","description":"Heme-responsive zinc finger transcription factor HAP1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31944","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18084","identifier":"P25567","identifierLink":"https://www.uniprot.org/uniprotkb/P25567/entry","name":"SRO9","description":"RNA-binding protein SRO9","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22792","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8603","identifier":"P10592","identifierLink":"https://www.uniprot.org/uniprotkb/P10592/entry","name":"SSA2","description":"Heat shock protein SSA2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1884","complexName":"HDA1 histone deacetylase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Class II histone deacetylase, recruited to specific promoter loci through sequence-specific DNA-binding proteins, for example the TUP1 repressor (P16649), and subsequently precisely modifies adjacent nucleosomes at the lysine residues of histones H2B and H3 to repress transcription. Also deacetylates the N-terminal tails of the histones via a nonspecific DNA-binding mechanism.","predictedComplex":false,"interactors":[{"ac":"EBI-32800","identifier":"Q06629","identifierLink":"https://www.uniprot.org/uniprotkb/Q06629/entry","name":"HDA2","description":"HDA1 complex subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31882","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-38663","identifier":"Q06623","identifierLink":"https://www.uniprot.org/uniprotkb/Q06623/entry","name":"HDA3","description":"HDA1 complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8206","identifier":"P53973","identifierLink":"https://www.uniprot.org/uniprotkb/P53973/entry","name":"HDA1","description":"Histone deacetylase HDA1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1885","complexName":"NineTeen complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for spliceosome activation, associates with the spliceosome after the release of U1 and U4 to stabilize the association of U5 and U6 with the spliceosome. The NTC plays an important role in promoting or stabilizing high-specificity interactions between U6 and the 5' splice site and between U5 and the exon sequence at the splice junctions after U1 and U4 have dissociated","predictedComplex":false,"interactors":[{"ac":"EBI-20921","identifier":"P38302","identifierLink":"https://www.uniprot.org/uniprotkb/P38302/entry","name":"NTC20","description":"Pre-mRNA-splicing factor NTC20","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-23308","identifier":"P53277","identifierLink":"https://www.uniprot.org/uniprotkb/P53277/entry","name":"SYF2","description":"Pre-mRNA-splicing factor SYF2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-476","identifier":"Q03654","identifierLink":"https://www.uniprot.org/uniprotkb/Q03654/entry","name":"CEF1","description":"Pre-mRNA-splicing factor CEF1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45885","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-484","identifier":"Q12309","identifierLink":"https://www.uniprot.org/uniprotkb/Q12309/entry","name":"CLF1","description":"Pre-mRNA-splicing factor CLF1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11246","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-493","identifier":"P32523","identifierLink":"https://www.uniprot.org/uniprotkb/P32523/entry","name":"PRP19","description":"Pre-mRNA-processing factor 19","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43995","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-540","identifier":"Q04048","identifierLink":"https://www.uniprot.org/uniprotkb/Q04048/entry","name":"SYF1","description":"Pre-mRNA-splicing factor SYF1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11246","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-818","identifier":"Q06091","identifierLink":"https://www.uniprot.org/uniprotkb/Q06091/entry","name":"SNT309","description":"Pre-mRNA-splicing factor SNT309","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-9382","identifier":"P21374","identifierLink":"https://www.uniprot.org/uniprotkb/P21374/entry","name":"ISY1","description":"Pre-mRNA-splicing factor ISY1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1886","complexName":"Post-mRNA release spliceosomal complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes disassembly of the spliceosome in an ATP-dependent manner, separating U2, U5, U6, NTC (NineTeen Complex, CPX-1885), and lariat-intron.","predictedComplex":false,"interactors":[{"ac":"EBI-26362","identifier":"P36118","identifierLink":"https://www.uniprot.org/uniprotkb/P36118/entry","name":"NTR2","description":"Pre-mRNA-splicing factor NTR2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-505","identifier":"P53131","identifierLink":"https://www.uniprot.org/uniprotkb/P53131/entry","name":"PRP43","description":"Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP43","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR18934","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-576","identifier":"Q06411","identifierLink":"https://www.uniprot.org/uniprotkb/Q06411/entry","name":"SPP382","description":"Pre-mRNA-splicing factor SPP382","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23329","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1888","complexName":"RSC chromatin remodelling complex, variant RSC2","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Member of the SWI/SNF family of ATP-dependent chromatin remodelers with a role in contributing to the integrity of centromeric DNA. The RSC complex is generally recruited to RNA polymerase III promoters and is specifically recruited to RNA polymerase II promoters by transcriptional activators and repressors where it is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. The remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, the RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. It is also involved in non-homologous end joining.","predictedComplex":false,"interactors":[{"ac":"EBI-12202","identifier":"P32832","identifierLink":"https://www.uniprot.org/uniprotkb/P32832/entry","name":"NPL6","description":"Chromatin structure-remodeling complex subunit RSC7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22597","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16198","identifier":"Q06488","identifierLink":"https://www.uniprot.org/uniprotkb/Q06488/entry","name":"RSC2","description":"Chromatin structure-remodeling complex subunit RSC2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR16062","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16204","identifier":"Q02206","identifierLink":"https://www.uniprot.org/uniprotkb/Q02206/entry","name":"RSC4","description":"Chromatin structure-remodeling complex subunit RSC4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR16062","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18410","identifier":"P32597","identifierLink":"https://www.uniprot.org/uniprotkb/P32597/entry","name":"STH1","description":"Nuclear protein STH1/NPS1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21189","identifier":"P38210","identifierLink":"https://www.uniprot.org/uniprotkb/P38210/entry","name":"LDB7","description":"Chromatin structure-remodeling complex protein RSC14","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-21941","identifier":"P25632","identifierLink":"https://www.uniprot.org/uniprotkb/P25632/entry","name":"RSC6","description":"Chromatin structure-remodeling complex protein RSC6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22058","identifier":"Q06639","identifierLink":"https://www.uniprot.org/uniprotkb/Q06639/entry","name":"RSC3","description":"Chromatin structure-remodeling complex protein RSC3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31069","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23005","identifier":"P43609","identifierLink":"https://www.uniprot.org/uniprotkb/P43609/entry","name":"RSC8","description":"Chromatin structure-remodeling complex protein RSC8","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23637","identifier":"P53330","identifierLink":"https://www.uniprot.org/uniprotkb/P53330/entry","name":"RTT102","description":"Regulator of Ty1 transposition protein 102","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-24549","identifier":"P38781","identifierLink":"https://www.uniprot.org/uniprotkb/P38781/entry","name":"RSC30","description":"Chromatin structure-remodeling complex protein RSC30","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31069","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27977","identifier":"Q03124","identifierLink":"https://www.uniprot.org/uniprotkb/Q03124/entry","name":"RSC9","description":"Chromatin structure-remodeling complex subunit RSC9","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22970","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2962","identifier":"Q12406","identifierLink":"https://www.uniprot.org/uniprotkb/Q12406/entry","name":"ARP7","description":"Actin-related protein 7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2972","identifier":"Q05123","identifierLink":"https://www.uniprot.org/uniprotkb/Q05123/entry","name":"ARP9","description":"Actin-like protein ARP9","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-35813","identifier":"Q06168","identifierLink":"https://www.uniprot.org/uniprotkb/Q06168/entry","name":"SFH1","description":"Chromatin structure-remodeling complex subunit SFH1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-36549","identifier":"Q07979","identifierLink":"https://www.uniprot.org/uniprotkb/Q07979/entry","name":"RSC58","description":"Chromatin structure-remodeling complex protein RSC58","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24341","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8717","identifier":"Q9URQ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9URQ5/entry","name":"HTL1","description":"High temperature lethal protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1889","complexName":"RSC chromatin remodelling complex, variant RSC1","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Member of the SWI/SNF family of ATP-dependent chromatin remodelers with a role in contributing to the integrity of centromeric DNA. The RSC complex is generally recruited to RNA polymerase III promoters and is specifically recruited to RNA polymerase II promoters by transcriptional activators and repressors where it is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. The remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, the RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton. It is also involved in non-homologous end joining.","predictedComplex":false,"interactors":[{"ac":"EBI-12202","identifier":"P32832","identifierLink":"https://www.uniprot.org/uniprotkb/P32832/entry","name":"NPL6","description":"Chromatin structure-remodeling complex subunit RSC7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22597","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16192","identifier":"P53236","identifierLink":"https://www.uniprot.org/uniprotkb/P53236/entry","name":"RSC1","description":"Chromatin structure-remodeling complex subunit RSC1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR16062","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16204","identifier":"Q02206","identifierLink":"https://www.uniprot.org/uniprotkb/Q02206/entry","name":"RSC4","description":"Chromatin structure-remodeling complex subunit RSC4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR16062","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18410","identifier":"P32597","identifierLink":"https://www.uniprot.org/uniprotkb/P32597/entry","name":"STH1","description":"Nuclear protein STH1/NPS1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21189","identifier":"P38210","identifierLink":"https://www.uniprot.org/uniprotkb/P38210/entry","name":"LDB7","description":"Chromatin structure-remodeling complex protein RSC14","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-21941","identifier":"P25632","identifierLink":"https://www.uniprot.org/uniprotkb/P25632/entry","name":"RSC6","description":"Chromatin structure-remodeling complex protein RSC6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22058","identifier":"Q06639","identifierLink":"https://www.uniprot.org/uniprotkb/Q06639/entry","name":"RSC3","description":"Chromatin structure-remodeling complex protein RSC3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31069","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23005","identifier":"P43609","identifierLink":"https://www.uniprot.org/uniprotkb/P43609/entry","name":"RSC8","description":"Chromatin structure-remodeling complex protein RSC8","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23637","identifier":"P53330","identifierLink":"https://www.uniprot.org/uniprotkb/P53330/entry","name":"RTT102","description":"Regulator of Ty1 transposition protein 102","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-24549","identifier":"P38781","identifierLink":"https://www.uniprot.org/uniprotkb/P38781/entry","name":"RSC30","description":"Chromatin structure-remodeling complex protein RSC30","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31069","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27977","identifier":"Q03124","identifierLink":"https://www.uniprot.org/uniprotkb/Q03124/entry","name":"RSC9","description":"Chromatin structure-remodeling complex subunit RSC9","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22970","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2962","identifier":"Q12406","identifierLink":"https://www.uniprot.org/uniprotkb/Q12406/entry","name":"ARP7","description":"Actin-related protein 7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2972","identifier":"Q05123","identifierLink":"https://www.uniprot.org/uniprotkb/Q05123/entry","name":"ARP9","description":"Actin-like protein ARP9","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-35813","identifier":"Q06168","identifierLink":"https://www.uniprot.org/uniprotkb/Q06168/entry","name":"SFH1","description":"Chromatin structure-remodeling complex subunit SFH1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-36549","identifier":"Q07979","identifierLink":"https://www.uniprot.org/uniprotkb/Q07979/entry","name":"RSC58","description":"Chromatin structure-remodeling complex protein RSC58","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24341","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8717","identifier":"Q9URQ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9URQ5/entry","name":"HTL1","description":"High temperature lethal protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1890","complexName":"Exocyst complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Recruited to sites of active exocytosis and membrane expansion, where it mediates the tethering of secretory vesicles to the plasma membrane in preparation for soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein receptor (SNARE)-mediated membrane fusion. The exocyst is localized to the emerging bud tip, where it mediates exocytosis for the asymmetric expansion of daughter cell surfaces during polarized cell growth. During cytokinesis, the exocyst is localized to the mother–daughter cell junction to mediate abscission. The targeting of secretory vesicles to the plasma membrane involves direct interactions of the exocyst with PI(4,5)P2. In addition, a number of small GTP-binding proteins interact with components of the exocyst and regulate the assembly, localization, and function of this complex.","predictedComplex":false,"interactors":[{"ac":"EBI-16504","identifier":"Q06245","identifierLink":"https://www.uniprot.org/uniprotkb/Q06245/entry","name":"SEC10","description":"Exocyst complex component SEC10","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12100","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16543","identifier":"P22224","identifierLink":"https://www.uniprot.org/uniprotkb/P22224/entry","name":"SEC15","description":"Exocyst complex component SEC15","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12702","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16850","identifier":"P33332","identifierLink":"https://www.uniprot.org/uniprotkb/P33332/entry","name":"SEC3","description":"Exocyst complex component SEC3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR16092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16865","identifier":"P89102","identifierLink":"https://www.uniprot.org/uniprotkb/P89102/entry","name":"SEC5","description":"Exocyst complex component SEC5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13043","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16874","identifier":"P32844","identifierLink":"https://www.uniprot.org/uniprotkb/P32844/entry","name":"SEC6","description":"Exocyst complex component SEC6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21292","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16896","identifier":"P32855","identifierLink":"https://www.uniprot.org/uniprotkb/P32855/entry","name":"SEC8","description":"Exocyst complex component SEC8","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14146","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21567","identifier":"P38261","identifierLink":"https://www.uniprot.org/uniprotkb/P38261/entry","name":"EXO84","description":"Exocyst complex component EXO84","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21426","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6717","identifier":"P19658","identifierLink":"https://www.uniprot.org/uniprotkb/P19658/entry","name":"EXO70","description":"Exocyst complex component EXO70","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12542","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1891","complexName":"RPB4-RPB7 subcomplex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Shuttles between the nucleus and cytoplasm and mediates both transcription and the two major cytoplasmic mRNA decay pathways, enhancing the deadenylation process of specific mRNAs. Interacts with components of the translation initiation factor 3 (eIF3), and is required for efficient translation initiation. Efficient translation in the cytoplasm depends on association of RPB4/7 with RNA polymerase II (CPX-2662) in the nucleus.","predictedComplex":false,"interactors":[{"ac":"EBI-15777","identifier":"P20433","identifierLink":"https://www.uniprot.org/uniprotkb/P20433/entry","name":"RPB4","description":"DNA-directed RNA polymerase II subunit RPB4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21297","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15790","identifier":"P34087","identifierLink":"https://www.uniprot.org/uniprotkb/P34087/entry","name":"RPB7","description":"DNA-directed RNA polymerase II subunit RPB7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12709","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1893","complexName":"MPP10 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for early co-transcriptional events in ribosome biogenesis, acting as an RNA chaperone to initiate ribosome assembly. IMP3 protein directly associates with the first 70 nucleotides of the U3 snoRNA, with a stem-loop structure within the hinge region, and thereby directs the preassembled MPP10 complex to the U3 preprocessome. A sub-unit of the small subunit (SSU) processome,  a 2.2 MDa ribonucleoprotein complex involved in the processing, assembly and maturation of nascent pre-ribosomal RNA to form the small ribosomal subunit. The SSU processome is a giant particle composed of numerous ribosome assembly factors, including the UTP-A (CPX-1409), UTP-B (CPX-1410), UTP-C (CPX-772/CPX-771/CPX-773) and MPP10 complexes, the U3 small nucleolar ribonucleoprotein (snoRNP) and many individual proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-11168","identifier":"P47083","identifierLink":"https://www.uniprot.org/uniprotkb/P47083/entry","name":"MPP10","description":"U3 small nucleolar RNA-associated protein MPP10","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR17039","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9237","identifier":"P32899","identifierLink":"https://www.uniprot.org/uniprotkb/P32899/entry","name":"IMP3","description":"U3 small nucleolar ribonucleoprotein protein IMP3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11831","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9243","identifier":"P53941","identifierLink":"https://www.uniprot.org/uniprotkb/P53941/entry","name":"IMP4","description":"U3 small nucleolar ribonucleoprotein protein IMP4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22734","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1894","complexName":"COP9 signalosome complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes. Plays a role in the regulation of the mating pheromone response.","predictedComplex":false,"interactors":[{"ac":"EBI-25069","identifier":"P40512","identifierLink":"https://www.uniprot.org/uniprotkb/P40512/entry","name":"PCI8","description":"Cop9 signalosome complex subunit 11","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14145","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28044","identifier":"Q04368","identifierLink":"https://www.uniprot.org/uniprotkb/Q04368/entry","name":"CSI1","description":"Cop9 signalosome-interactor 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-32238","identifier":"Q12348","identifierLink":"https://www.uniprot.org/uniprotkb/Q12348/entry","name":"RRI2","description":"COP9 signalosome complex subunit 10","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-33535","identifier":"Q03981","identifierLink":"https://www.uniprot.org/uniprotkb/Q03981/entry","name":"CSN9","description":"COP9 signalosome complex subunit 9","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15350","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-37511","identifier":"Q12468","identifierLink":"https://www.uniprot.org/uniprotkb/Q12468/entry","name":"RRI1","description":"COP9 signalosome complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10410","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-763","identifier":"P47130","identifierLink":"https://www.uniprot.org/uniprotkb/P47130/entry","name":"CSN12","description":"Cop9 signalosome complex subunit 12","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12732","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1895","complexName":"mRNA cleavage factor complex CFIA","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for the posttranscriptional maturation of mRNA 3' ends. CFI binds signal sequences at the 3' end of yeast mRNA. and is required for correct positioning of a larger protein complex, CPF (CPX-1053), which contains the catalytic subunits executing mRNA cleavage and polyadenylation. CFI (CPX-1896) and CFII recognize the processing signals of the RNA and perform the endonucleolytic cleavage, whereas CFI, polyadenylation factor I (PFI), and the single-polypeptide PAP1 are required for the polyadenylation step.  CFIA forms a stable sub-complex","predictedComplex":false,"interactors":[{"ac":"EBI-12980","identifier":"P39081","identifierLink":"https://www.uniprot.org/uniprotkb/P39081/entry","name":"PCF11","description":"Protein PCF11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15921","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15632","identifier":"P25298","identifierLink":"https://www.uniprot.org/uniprotkb/P25298/entry","name":"RNA14","description":"mRNA 3'-end-processing protein RNA14","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19980","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15640","identifier":"P25299","identifierLink":"https://www.uniprot.org/uniprotkb/P25299/entry","name":"RNA15","description":"mRNA 3'-end-processing protein RNA15","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45735","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29732","identifier":"Q08685","identifierLink":"https://www.uniprot.org/uniprotkb/Q08685/entry","name":"CLP1","description":"mRNA cleavage and polyadenylation factor CLP1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12755","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1896","complexName":"mRNA cleavage factor complex CFI","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for the posttranscriptional maturation of mRNA 3' ends. CFI binds signal sequences at the 3' end of yeast mRNA. and is required for correct positioning of a larger protein complex, CFI and CFII recognize the processing signals of the RNA and perform the endonucleolytic cleavage, whereas CFI, polyadenylation factor I (PFI), and the single-polypeptide PAP1 are required for the polyadenylation step. CFIA (CPX-1895) forms a stable sub-complex.","predictedComplex":false,"interactors":[{"ac":"EBI-11783","identifier":"Q99383","identifierLink":"https://www.uniprot.org/uniprotkb/Q99383/entry","name":"HRP1","description":"Nuclear polyadenylated RNA-binding protein 4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR48031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12980","identifier":"P39081","identifierLink":"https://www.uniprot.org/uniprotkb/P39081/entry","name":"PCF11","description":"Protein PCF11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15921","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15632","identifier":"P25298","identifierLink":"https://www.uniprot.org/uniprotkb/P25298/entry","name":"RNA14","description":"mRNA 3'-end-processing protein RNA14","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19980","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15640","identifier":"P25299","identifierLink":"https://www.uniprot.org/uniprotkb/P25299/entry","name":"RNA15","description":"mRNA 3'-end-processing protein RNA15","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45735","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29732","identifier":"Q08685","identifierLink":"https://www.uniprot.org/uniprotkb/Q08685/entry","name":"CLP1","description":"mRNA cleavage and polyadenylation factor CLP1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12755","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1897","complexName":"Fused-Smurf ubiquitin ligase complex","organismName":"Drosophila melanogaster; 7227","description":"Regulates ubiquitination and proteolysis of the BMP receptor Thickveins in cystoblasts, potentially by controlling Tkv ubiquitination and degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-133520","identifier":"Q9V853","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V853/entry","name":"Smurf","description":"E3 ubiquitin-protein ligase Smurf1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11254","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-165536","identifier":"P23647","identifierLink":"https://www.uniprot.org/uniprotkb/P23647/entry","name":"fu","description":"Serine/threonine-protein kinase fused","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22983","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1898","complexName":"CBF3 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Binds to the CDEIII DNA element, conserved between all yeast chromosomes, early in kinetochore assembly and acts as the the primary determinant of assembly. Binding of the CBF3 complex and presence of the unique N-terminal tails of the two CSE4 (P36012) molecules in the nucleosome could cooperate to induce a sharp bending of the centromeric DNA, thus creating a C-loop structure in which the CSE4 nucleosome is proximal to the plus end of the kinetochore. Alternatively, CSE4-nucleosomes are part of the highly phased array of nucleosomes on either side of the CEN-sequence, while CFB3 occupies CDEIII and additional Ndc10 molecules occupy the CDEII sites to form an extended binding platform. microtubule","predictedComplex":false,"interactors":[{"ac":"EBI-4069","identifier":"P32504","identifierLink":"https://www.uniprot.org/uniprotkb/P32504/entry","name":"CBF2","description":"Centromere DNA-binding protein complex CBF3 subunit A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-4077","identifier":"P40969","identifierLink":"https://www.uniprot.org/uniprotkb/P40969/entry","name":"CEP3","description":"Centromere DNA-binding protein complex CBF3 subunit B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31001","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4085","identifier":"P35203","identifierLink":"https://www.uniprot.org/uniprotkb/P35203/entry","name":"CTF13","description":"Centromere DNA-binding protein complex CBF3 subunit C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-4090","identifier":"P52286","identifierLink":"https://www.uniprot.org/uniprotkb/P52286/entry","name":"SKP1","description":"Suppressor of kinetochore protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1901","complexName":"Peroxisomal receptor export module complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Processive protein translocase that mediates the ATP-dependent relocation and recycling of the peroxisomal targeting signal import receptor PEX5 (P35056) from the peroxisomal membrane to the cytosol, where it is then available for another round of protein import. The PEX1-PEX6 heterohexamer acts as a p97/CDC48-like  ATPase that threads monoubiquitinated PEX5 through its central pore.","predictedComplex":false,"interactors":[{"ac":"EBI-13155","identifier":"P24004","identifierLink":"https://www.uniprot.org/uniprotkb/P24004/entry","name":"PEX1","description":"Peroxisomal ATPase PEX1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13178","identifier":"P33760","identifierLink":"https://www.uniprot.org/uniprotkb/P33760/entry","name":"PEX6","description":"Peroxisomal ATPase PEX6","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31849","identifier":"Q08215","identifierLink":"https://www.uniprot.org/uniprotkb/Q08215/entry","name":"PEX15","description":"Peroxisomal membrane protein PEX15","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1903","complexName":"PEX2-PEX10-PEX12 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"E3 ubiquitin-ligase complex which forms a retrotranslocation channel required for the export of the PEX5 peroxisomal import -receptor from peroxisomes to the cytosol, promoting PEX5 (P35056) recycling. When receptor recycling is compromised, the receptor is polyubiquitylated by the complex, extracted from the ligase channel by another ATPase, and degraded by the proteasome.","predictedComplex":false,"interactors":[{"ac":"EBI-13160","identifier":"P32800","identifierLink":"https://www.uniprot.org/uniprotkb/P32800/entry","name":"PEX2","description":"Peroxisomal biogenesis factor 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-13194","identifier":"Q05568","identifierLink":"https://www.uniprot.org/uniprotkb/Q05568/entry","name":"PEX10","description":"Peroxisome biogenesis factor 10","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23350","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2077297","identifier":"Q04370","identifierLink":"https://www.uniprot.org/uniprotkb/Q04370/entry","name":"PEX12","description":"Peroxisome assembly protein 12","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1904","complexName":"Peroxisomal PEX13-PEX14-PEX17 docking complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Facilitates the peroxoisomal-membrane docking of cargo-loaded, peroxisomal targeting signal type 1 (PTS1) and PTS2 proteins. Proteins designated for peroxisomes are synthezised on cytosolic ribosomes and are recognised  by the receptor PEX5 (P35056)  via their PTS1 or the PEX7-PEX18 receptor complex via their PTS2  The receptor-cargo-complexes bind to the docking-complex at the peroxisomal membrane. It is assumed that the binding between the docking complex and cargo-loaded receptors leads to the formation of a transient pore.","predictedComplex":false,"interactors":[{"ac":"EBI-13206","identifier":"P80667","identifierLink":"https://www.uniprot.org/uniprotkb/P80667/entry","name":"PEX13","description":"Peroxisomal membrane protein PEX13","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19332","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13212","identifier":"P53112","identifierLink":"https://www.uniprot.org/uniprotkb/P53112/entry","name":"PEX14","description":"Peroxisomal membrane protein PEX14","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23058","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13218","identifier":"P40155","identifierLink":"https://www.uniprot.org/uniprotkb/P40155/entry","name":"PEX17","description":"Peroxisomal membrane protein PEX17","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1905","complexName":"Peroxisomal PEX7-PEX18 receptor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Receptor complex which recognises peroxisomal targeting signal type 2 containing proteins  synthezised on cytosolic ribosomes. The receptor-cargo complex is then transported from the cytosol to the peroxisomal docking complex (CPX-1904).","predictedComplex":false,"interactors":[{"ac":"EBI-13183","identifier":"P39108","identifierLink":"https://www.uniprot.org/uniprotkb/P39108/entry","name":"PEX7","description":"Peroxisomal targeting signal 2 receptor","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46027","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-24803","identifier":"P38855","identifierLink":"https://www.uniprot.org/uniprotkb/P38855/entry","name":"PEX18","description":"Peroxisomal membrane protein PEX18","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1906","complexName":"Peroxisomal PEX7-PEX21 receptor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Receptor complex which recognises peroxisomal targeting signal type 2 containing proteins  synthezised on cytosolic ribosomes. The receptor-cargo complex is then transported from the cytosol to the peroxisomal docking complex (CPX-1904).","predictedComplex":false,"interactors":[{"ac":"EBI-13183","identifier":"P39108","identifierLink":"https://www.uniprot.org/uniprotkb/P39108/entry","name":"PEX7","description":"Peroxisomal targeting signal 2 receptor","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46027","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23549","identifier":"P50091","identifierLink":"https://www.uniprot.org/uniprotkb/P50091/entry","name":"PEX21","description":"Peroxisomal protein PEX21","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1908","complexName":"BBSome complex","organismName":"Homo sapiens; 9606","description":"The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor (P61006/Q92930), which localizes to the basal body and contacts the BBSome. RAB8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/RABIN8, the guanosyl exchange factor (GEF) for RAB8 and then the RAB8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog pathway regulation.","predictedComplex":false,"interactors":[{"ac":"EBI-1805484","identifier":"Q8NFJ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NFJ9/entry","name":"BBS1","description":"BBSome complex member BBS1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20870","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1805814","identifier":"Q96RK4","identifierLink":"https://www.uniprot.org/uniprotkb/Q96RK4/entry","name":"BBS4","description":"BBSome complex member BBS4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44186","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1806001","identifier":"Q8IWZ6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IWZ6/entry","name":"BBS7","description":"BBSome complex member BBS7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16074","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2826852","identifier":"Q3SYG4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3SYG4/entry","name":"BBS9","description":"Protein PTHB1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20991","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2892417","identifier":"A8MTZ0","identifierLink":"https://www.uniprot.org/uniprotkb/A8MTZ0/entry","name":"BBIP1","description":"BBSome-interacting protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28596","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2892592","identifier":"Q8N3I7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N3I7/entry","name":"BBS5","description":"BBSome complex member BBS5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2892638","identifier":"Q8TAM2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAM2/entry","name":"TTC8","description":"Tetratricopeptide repeat protein 8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-748297","identifier":"Q9BXC9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BXC9/entry","name":"BBS2","description":"BBSome complex member BBS2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32465","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1909","complexName":"BBSome complex","organismName":"Mus musculus; 10090","description":"The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor (P55258/P61028), which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to Rab3ip/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the Ltzl1, controls Smo ciliary trafficking and contributes to the sonic hedgehog pathway regulation.","predictedComplex":false,"interactors":[{"ac":"EBI-20975868","identifier":"J3QMK2","identifierLink":"https://www.uniprot.org/uniprotkb/J3QMK2/entry","name":"Bbip1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR28596","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2892836","identifier":"Q3V3N7","identifierLink":"https://www.uniprot.org/uniprotkb/Q3V3N7/entry","name":"Bbs1","description":"BBSome complex member BBS1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR20870","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2892863","identifier":"Q9CWF6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CWF6/entry","name":"Bbs2","description":"BBSome complex member BBS2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR32465","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2892887","identifier":"Q8C1Z7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C1Z7/entry","name":"Bbs4","description":"BBSome complex member BBS4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR44186","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2892924","identifier":"Q8K2G4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K2G4/entry","name":"Bbs7","description":"BBSome complex member BBS7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16074","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6127679","identifier":"Q9CZQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CZQ9/entry","name":"Bbs5","description":"BBSome complex member BBS5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6127691","identifier":"Q811G0","identifierLink":"https://www.uniprot.org/uniprotkb/Q811G0/entry","name":"Bbs9","description":"Protein PTHB1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR20991","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6127721","identifier":"Q8VD72","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VD72/entry","name":"Ttc8","description":"Tetratricopeptide repeat protein 8","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR44177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1907","complexName":"Ripoptosome","organismName":"Homo sapiens; 9606","description":"Intracellular complex whose formation can induce either the extrinsic apoptotic signaling pathway or necroptosis. Central components are RIPK1 and CASP8, linked through FADD. Formation induced upon stimulation of membrane-bound receptors (TRAIL, CD95 or TLR3) and dependent on depletion of IAP (inhibitor-of-apoptosis) proteins caused by cytokine stimulation, cellular stress or treatment with IAP antagonists. Can recruit different isoforms of IAPs, such as cFLIPs or cFLIPl. Can induce necroptosis or apoptosis, depending on the composition of heterodimers of CASP8 and cFLIP isoforms: predominance of CASP8-CASP8 homodimers induces apoptosis, predominance of CASP8-cFLIP heterodimers induces necroptosis. RIPK3 seems to be dowstream target when the complex induces necroptosis.","predictedComplex":false,"interactors":[{"ac":"EBI-358507","identifier":"Q13546","identifierLink":"https://www.uniprot.org/uniprotkb/Q13546/entry","name":"RIPK1","description":"Receptor-interacting serine/threonine-protein kinase 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44329","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-494804","identifier":"Q13158","identifierLink":"https://www.uniprot.org/uniprotkb/Q13158/entry","name":"FADD","description":"FAS-associated death domain protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-78060","identifier":"Q14790","identifierLink":"https://www.uniprot.org/uniprotkb/Q14790/entry","name":"CASP8","description":"Caspase-8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10454","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1914","complexName":"Ripoptosome","organismName":"Mus musculus; 10090","description":"Intracellular complex whose formation can induce either the extrinsic apoptotic signaling pathway or necroptosis. Central components are RIPK1 and CASP8, linked through FADD. Formation induced upon stimulation of membrane-bound receptors (TRAIL, CD95 or TLR3) and dependent on depletion of IAP (inhibitor-of-apoptosis) proteins caused by cytokine stimulation, cellular stress or treatment with IAP antagonists. Can recruit different isoforms of IAPs, such as cFLIPs or cFLIPl. Can induce necroptosis or apoptosis, depending on the composition of heterodimers of CASP8 and cFLIP isoforms: predominance of CASP8-CASP8 homodimers induces apoptosis, predominance of CASP8-cFLIP heterodimers induces necroptosis. RIPK3 seems to be downstream target when the complex induces necroptosis.","predictedComplex":false,"interactors":[{"ac":"EBI-524415","identifier":"Q61160","identifierLink":"https://www.uniprot.org/uniprotkb/Q61160/entry","name":"Fadd","description":"FAS-associated death domain protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-529119","identifier":"Q60855","identifierLink":"https://www.uniprot.org/uniprotkb/Q60855/entry","name":"Ripk1","description":"Receptor-interacting serine/threonine-protein kinase 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR44329","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-851690","identifier":"O89110","identifierLink":"https://www.uniprot.org/uniprotkb/O89110/entry","name":"Casp8","description":"Caspase-8","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10454","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1910","complexName":"BLOC-1 complex","organismName":"Homo sapiens; 9606","description":"Critical for melanosome biogenesis and also implicated in neurological function and disease. Implicated in the formation and/or maturation of tubular vesicular intermediates between endosomes and lysosome-related organelles. Possible role in intracellular protein trafficking.","predictedComplex":false,"interactors":[{"ac":"EBI-296723","identifier":"O95295","identifierLink":"https://www.uniprot.org/uniprotkb/O95295/entry","name":"SNAPIN","description":"SNARE-associated protein Snapin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348630","identifier":"P78537","identifierLink":"https://www.uniprot.org/uniprotkb/P78537/entry","name":"BLOC1S1","description":"Biogenesis of lysosome-related organelles complex 1 subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465781","identifier":"Q9UL45","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UL45/entry","name":"BLOC1S6","description":"Biogenesis of lysosome-related organelles complex 1 subunit 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31328","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465804","identifier":"Q96EV8","identifierLink":"https://www.uniprot.org/uniprotkb/Q96EV8/entry","name":"DTNBP1","description":"Dysbindin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465852","identifier":"Q9NUP1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NUP1/entry","name":"BLOC1S4","description":"Biogenesis of lysosome-related organelles complex 1 subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16230","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465861","identifier":"Q8TDH9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TDH9/entry","name":"BLOC1S5","description":"Biogenesis of lysosome-related organelles complex 1 subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31784","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465872","identifier":"Q6QNY1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6QNY1/entry","name":"BLOC1S2","description":"Biogenesis of lysosome-related organelles complex 1 subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46479","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465930","identifier":"Q6QNY0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6QNY0/entry","name":"BLOC1S3","description":"Biogenesis of lysosome-related organelles complex 1 subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31974","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1913","complexName":"BLOC-1 complex","organismName":"Mus musculus; 10090","description":"Critical for melanosome biogenesis and also implicated in neurological function and disease. Implicated in the formation and/or maturation of tubular vesicular intermediates between endosomes and lysosome-related organelles. Possible role in intracellular protein trafficking.","predictedComplex":false,"interactors":[{"ac":"EBI-6170232","identifier":"Q8VED2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VED2/entry","name":"Bloc1s4","description":"Biogenesis of lysosome-related organelles complex 1 subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16230","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6170242","identifier":"Q9R0C0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R0C0/entry","name":"Bloc1s6","description":"Biogenesis of lysosome-related organelles complex 1 subunit 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR31328","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6170267","identifier":"Q9CWG9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CWG9/entry","name":"Bloc1s2","description":"Biogenesis of lysosome-related organelles complex 1 subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46479","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6170282","identifier":"Q8R015","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R015/entry","name":"Bloc1s5","description":"Biogenesis of lysosome-related organelles complex 1 subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR31784","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6170299","identifier":"Q5U5M8","identifierLink":"https://www.uniprot.org/uniprotkb/Q5U5M8/entry","name":"Bloc1s3","description":"Biogenesis of lysosome-related organelles complex 1 subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR31974","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6170320","identifier":"Q9Z266","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z266/entry","name":"Snapin","description":"SNARE-associated protein Snapin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR31305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6170351","identifier":"O55102","identifierLink":"https://www.uniprot.org/uniprotkb/O55102/entry","name":"Bloc1s1","description":"Biogenesis of lysosome-related organelles complex 1 subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-643186","identifier":"Q91WZ8","identifierLink":"https://www.uniprot.org/uniprotkb/Q91WZ8/entry","name":"Dtnbp1","description":"Dysbindin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1916","complexName":"Fibrinogen","organismName":"Mus musculus; 10090","description":"Soluble glycoprotein synthesized by hepatocytes which participates in the final step of blood coagulation. Converted to fibrin in a reaction catalyzed by thrombin, which releases fibrinopeptides A  and B from amino-termini of the alpha and beta chains to produce fibrin monomers.","predictedComplex":false,"interactors":[{"ac":"EBI-1634324","identifier":"Q8K0E8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K0E8/entry","name":"Fgb","description":"Fibrinogen beta chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR19143","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6252659","identifier":"E9PV24","identifierLink":"https://www.uniprot.org/uniprotkb/E9PV24/entry","name":"Fga","description":"Fibrinogen alpha chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR47221","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6252682","identifier":"Q8VCM7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VCM7/entry","name":"Fgg","description":"Fibrinogen gamma chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR19143","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1917","complexName":"Phosphatidylinositol 3-kinase complex class IA, p110alpha/p85beta","organismName":"Homo sapiens; 9606","description":"Uses PI(4,5)P2 as a substrate to generate the product PI(3,4,5)P3 which initiates major signaling pathways downstream. Performs a central role in cellular signaling, mediating responses to growth factors and extracellular stimuli. Engaged by beta-1 integrin/Fak/Src to mediate signaling for the suppression of anoikis. This variant is found to be ubiquitously expressed in human cells.","predictedComplex":false,"interactors":[{"ac":"EBI-2116585","identifier":"P42336","identifierLink":"https://www.uniprot.org/uniprotkb/P42336/entry","name":"PIK3CA","description":"Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-346930","identifier":"O00459","identifierLink":"https://www.uniprot.org/uniprotkb/O00459/entry","name":"PIK3R2","description":"Phosphatidylinositol 3-kinase regulatory subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10155","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1918","complexName":"Phosphatidylinositol 3-kinase complex class IA, p110alpha/p55gamma","organismName":"Homo sapiens; 9606","description":"Uses 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate/PI(4,5)P2 (CHEBI:18348) as a substrate to generate the product 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate/PI(3,4,5)P3 (CHEBI:16618) which initiates major signaling pathways downstream. Performs a central role in cellular signaling, mediating responses to growth factors and extracellular stimuli. Engaged by beta-1 integrin/Fak/Src to mediate signaling for the suppression of anoikis. This variant is found to be ubiquitously expressed in human cells.","predictedComplex":false,"interactors":[{"ac":"EBI-2116585","identifier":"P42336","identifierLink":"https://www.uniprot.org/uniprotkb/P42336/entry","name":"PIK3CA","description":"Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-79893","identifier":"Q92569","identifierLink":"https://www.uniprot.org/uniprotkb/Q92569/entry","name":"PIK3R3","description":"Phosphatidylinositol 3-kinase regulatory subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10155","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1919","complexName":"Complement component C1q complex","organismName":"Homo sapiens; 9606","description":"Recognition unit of the classical pathway of complement which associates with the Ca2+ - dependent C1r(2)-C1s(2) tetramer to form C1 (CPX-1920), the first component of the classical complement system. The complex's role in C1 is the recognition of immune complexes, or other molecules, which trigger the classical pathway of the complement system. Independent of complement activation C1q appears to have additional roles in homeostasis and cellular development, superoxide (O2-) production by neutrophils, blood coagulation and neurological synapse pruning.","predictedComplex":false,"interactors":[{"ac":"EBI-1220209","identifier":"P02745","identifierLink":"https://www.uniprot.org/uniprotkb/P02745/entry","name":"C1QA","description":"Complement C1q subcomponent subunit A","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15427","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1220222","identifier":"P02747","identifierLink":"https://www.uniprot.org/uniprotkb/P02747/entry","name":"C1QC","description":"Complement C1q subcomponent subunit C","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15427","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2813376","identifier":"P02746","identifierLink":"https://www.uniprot.org/uniprotkb/P02746/entry","name":"C1QB","description":"Complement C1q subcomponent subunit B","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15427","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1920","complexName":"Complement C1 complex","organismName":"Homo sapiens; 9606","description":"The first component of the classical serum complement system. In the presence of calcium, the C1q complex (CPX-1919) associates with the C1S-C1R-C1R-C1S tetramer. When C1q binds to an activating target, a conformational change triggers the auto-activation of the associated C1R protease (converting the pro-enzyme into an activated form), which activates C1S. C1S then cleaves the Arg-|-Ala bond in complement component C4 to form C4a and C4b, and the Lys(or Arg)-|-Lys bond in complement component C2 to form C2a and C2b which in turn form C3 convertase complexes C4bC2a-A (CPX-5675) and C4bC2a-B.","predictedComplex":false,"interactors":[{"ac":"EBI-10889493","identifier":"P00736-PRO_0000027578","identifierLink":"https://www.uniprot.org/uniprotkb/P00736-PRO_0000027578/entry","name":"C1R","description":"Complement C1r subcomponent heavy chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-10889498","identifier":"P00736-PRO_0000027579","identifierLink":"https://www.uniprot.org/uniprotkb/P00736-PRO_0000027579/entry","name":"C1R","description":"Complement C1r subcomponent light chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-22196148","identifier":"P09871-PRO_0000027587","identifierLink":"https://www.uniprot.org/uniprotkb/P09871-PRO_0000027587/entry","name":"C1S","description":"Complement C1s subcomponent heavy chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-22196153","identifier":"P09871-PRO_0000027588","identifierLink":"https://www.uniprot.org/uniprotkb/P09871-PRO_0000027588/entry","name":"C1S","description":"Complement C1s subcomponent light chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-6264901","identifier":"CPX-1919","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-1919","name":"Complement component C1q complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-2107","complexName":"MacAB-TolC ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"Tripartite, ATP-dependent efflux pump spanning the entire cell membrane system. Drives the efflux of antibiotics and other toxins (specifically macrolide compounds containing 14- and 15-membered lactones). May also play a role in the transport of glycolipids.","predictedComplex":false,"interactors":[{"ac":"EBI-1125580","identifier":"P75831","identifierLink":"https://www.uniprot.org/uniprotkb/P75831/entry","name":"macB","description":"Macrolide export ATP-binding/permease protein MacB","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30572","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-551961","identifier":"P75830","identifierLink":"https://www.uniprot.org/uniprotkb/P75830/entry","name":"macA","description":"Macrolide export protein MacA","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30469","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-875614","identifier":"P02930","identifierLink":"https://www.uniprot.org/uniprotkb/P02930/entry","name":"tolC","description":"Outer membrane protein TolC","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3099","complexName":"FtsQBL complex","organismName":"Escherichia coli (strain K12); 83333","description":"Sub-complex of the divisome, required for cell division. FtsQBL appears to form independently of the divisome and is hypothesized to link cytoplasmic to periplasmic events during cell division through a multitude of transient interactions. May have a structural role as a scaffold in the assembly of the divisome recruiting late divisome components.","predictedComplex":false,"interactors":[{"ac":"EBI-1113953","identifier":"P0A6S5","identifierLink":"https://www.uniprot.org/uniprotkb/P0A6S5/entry","name":"ftsB","description":"Cell division protein FtsB","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR37485","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1119082","identifier":"P0AEN4","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEN4/entry","name":"ftsL","description":"Cell division protein FtsL","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR37479","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1130157","identifier":"P06136","identifierLink":"https://www.uniprot.org/uniprotkb/P06136/entry","name":"ftsQ","description":"Cell division protein FtsQ","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR35851","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1922","complexName":"Fibrinogen complex","organismName":"Homo sapiens; 9606","description":"Glycoprotein complex that forms fibrin clots as the last step of the coagulation pathway. Fibrinogen heterohexamers (this complex) are activated by minor proteolysis of alpha and beta chains by alpha-thrombin complex (CPX-6222) to form so-called fibrin monomers (CPX-6225). Fibrin clot (CPX-6230) formation is catalysed by factor XIIIa (CPX-6231). Clots are dissolved mainly by the proteolytic action of plasmin (P00747).","predictedComplex":false,"interactors":[{"ac":"EBI-26361764","identifier":"P02679-PRO_0000009099","identifierLink":"https://www.uniprot.org/uniprotkb/P02679-PRO_0000009099/entry","name":"FGG","description":"Fibrinogen gamma chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-26361770","identifier":"P02671-PRO_0000009021","identifierLink":"https://www.uniprot.org/uniprotkb/P02671-PRO_0000009021/entry","name":"FGA","description":"Fibrinopeptide A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-26361775","identifier":"P02675-PRO_0000009070","identifierLink":"https://www.uniprot.org/uniprotkb/P02675-PRO_0000009070/entry","name":"FGB","description":"Fibrinopeptide B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-1923","complexName":"BAM complex","organismName":"Escherichia coli (strain K12); 83333","description":"Outer membrane protein assembly complex involved in assembly and insertion of beta-barrel proteins into the outer membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-1128087","identifier":"P0AC02","identifierLink":"https://www.uniprot.org/uniprotkb/P0AC02/entry","name":"bamD","description":"Outer membrane protein assembly factor BamD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR37423","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1129043","identifier":"P0A903","identifierLink":"https://www.uniprot.org/uniprotkb/P0A903/entry","name":"bamC","description":"Outer membrane protein assembly factor BamC","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-6391574","identifier":"P0A937","identifierLink":"https://www.uniprot.org/uniprotkb/P0A937/entry","name":"bamE","description":"Outer membrane protein assembly factor BamE","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR37482","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-907297","identifier":"P77774","identifierLink":"https://www.uniprot.org/uniprotkb/P77774/entry","name":"bamB","description":"Outer membrane protein assembly factor BamB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32303","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-907371","identifier":"P0A940","identifierLink":"https://www.uniprot.org/uniprotkb/P0A940/entry","name":"bamA","description":"Outer membrane protein assembly factor BamA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR12815","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1924","complexName":"DNA polymerase III holoenzyme complex","organismName":"Escherichia coli (strain K12); 83333","description":"Responsible for primer-initiated 5' to 3' polymerization of DNA on a single-stranded DNA template as part of chromosomal replication. Copying of the template strands is performed by the DNA polymerase III core complex (CPX-1925) within the holoenzyme. To achieve the processivity needed to synthesize the entire chromosome, the Pol III core associates with the dimeric beta sliding clamp (CPX-1927), which is assembled around DNA by the pentameric clamp loader complex (CPX-1926).","predictedComplex":false,"interactors":[{"ac":"EBI-6467979","identifier":"CPX-1925","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-1925","name":"DNA polymerase III core complex","description":null,"stochiometry":"minValue: 3, maxValue: 3","interactorType":"stable complex","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-6467993","identifier":"CPX-1926","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-1926","name":"DNA polymerase III clamp loader complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-6468862","identifier":"CPX-1927","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-1927","name":"DNA polymerase III, beta sliding clamp processivity factor complex","description":null,"stochiometry":"minValue: 2, maxValue: 2","interactorType":"stable complex","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]}]},{"complexAC":"CPX-1925","complexName":"DNA polymerase III core complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalytic complex with both 5'-3' DNA polymerase and 3'-5' proofreading exonuclease activity. Active as a proofreading DNA polymerase in addition to forming the catalytic core of the DNA polymerase III (Pol III) holoenzyme which functions as the leading- and lagging-strand replicase in DNA replication.","predictedComplex":false,"interactors":[{"ac":"EBI-549111","identifier":"P10443","identifierLink":"https://www.uniprot.org/uniprotkb/P10443/entry","name":"dnaE","description":"DNA polymerase III subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549131","identifier":"P03007","identifierLink":"https://www.uniprot.org/uniprotkb/P03007/entry","name":"dnaQ","description":"DNA polymerase III subunit epsilon","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30231","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549182","identifier":"P0ABS8","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABS8/entry","name":"holE","description":"DNA polymerase III subunit theta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]}]},{"complexAC":"CPX-1926","complexName":"DNA polymerase III clamp loader complex","organismName":"Escherichia coli (strain K12); 83333","description":"A member of the AAA+ family of ATPases which utilizes ATP hydrolysis to load the sliding clamp onto the DNA at the primer template junction. The holA/delta subunit is responsible for clamp binding and opening. holB/delta' acts as a stator and stabilizes the interaction of holA with the sliding clamp. The tau (P06710-1) and gamma (P06710-2) subunits are active ATPases. The clamp loading function of the tau and gamma subunits is interchangeable but only tau oligomerizes Pol III. Each dnaX subunit binds one molecule of ATP, and the clamp loader binds and hydrolyses three ATP molecules for each loading cycle.The holD/psi and holC/chi subunits bridge the clamp loader complex with the SSB complex (CPX-1928).","predictedComplex":false,"interactors":[{"ac":"EBI-549140","identifier":"P06710","identifierLink":"https://www.uniprot.org/uniprotkb/P06710/entry","name":"dnaX","description":"DNA polymerase III subunit tau","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549153","identifier":"P28630","identifierLink":"https://www.uniprot.org/uniprotkb/P28630/entry","name":"holA","description":"DNA polymerase III subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34388","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549161","identifier":"P28631","identifierLink":"https://www.uniprot.org/uniprotkb/P28631/entry","name":"holB","description":"DNA polymerase III subunit delta'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549169","identifier":"P28905","identifierLink":"https://www.uniprot.org/uniprotkb/P28905/entry","name":"holC","description":"DNA polymerase III subunit chi","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR38767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549176","identifier":"P28632","identifierLink":"https://www.uniprot.org/uniprotkb/P28632/entry","name":"holD","description":"DNA polymerase III subunit psi","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]}]},{"complexAC":"CPX-1927","complexName":"DNA polymerase III, beta sliding clamp processivity factor complex","organismName":"Escherichia coli (strain K12); 83333","description":"Loaded onto DNA at the replication fork by the clamp loader complex (CPX-1926) and tethers the DNA polymerase III (CPX-1925) to DNA. At least 3 beta homodimers seem to be present at each replications folk; two are tethered to the two active polymerase core subcomplexes while a third appears to be a little further away, possibly still attached to the end of an Okasaki fragment prior to primer removal and ligation of the gap.","predictedComplex":false,"interactors":[{"ac":"EBI-542385","identifier":"P0A988","identifierLink":"https://www.uniprot.org/uniprotkb/P0A988/entry","name":"dnaN","description":"Beta sliding clamp","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30478","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1946","complexName":"dnaB helicase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Homohexameric helicase which participates in initiation and elongation during DNA replication, using the energy of ATP hydrolysis to translocate down the lagging-strand template, splitting two strands apart in advance of the leading-strand replicase, Pol III (CPX-1925). Exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with dnaA, dnaC, dnaG (primase), and other prepriming proteins. Two DnaB helicase hexamers are recruited and loaded onto each of the separated single-stranded (ss)DNA strands and unwind DNA bi-directionally away from the replication fork by translocating along and encircling the ssDNA.","predictedComplex":false,"interactors":[{"ac":"EBI-548978","identifier":"P0ACB0","identifierLink":"https://www.uniprot.org/uniprotkb/P0ACB0/entry","name":"dnaB","description":"Replicative DNA helicase DnaB","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30153","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1928","complexName":"SSB single-stranded DNA binding complex","organismName":"Escherichia coli (strain K12); 83333","description":"Forms homotetramers on single-stranded DNA at the replication fork, removing DNA secondary structure and protecting against nucleases, and is displaced by the DNA Polymerase III complex (CPX-1925) during lagging strand synthesis. \r\nIt interacts with the ssDNA cooperatively via either 2 or all 4 subunits.\r\ndnaG primase binds the SSB tetramer and synthesises RNA primers on ssDNA until it is displaced by the chi subunit of the clamp loader complex (CPX-1926).","predictedComplex":false,"interactors":[{"ac":"EBI-1118620","identifier":"P0AGE0","identifierLink":"https://www.uniprot.org/uniprotkb/P0AGE0/entry","name":"ssb","description":"Single-stranded DNA-binding protein","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10302","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1929","complexName":"PhnGHIJKL complex","organismName":"Escherichia coli (strain K12); 83333","description":"Formed from components of the phn operon in gram-negative bacteria that facilitates the internalization and degradation of organophosphonates. Carbon-phosphorous lyase (CP lyase) and alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase activites have been attributed to at least the PhnG, PhnH, PhnI, PhnJ, PhnK and PhnL components of the Phn operon. It is unclear which of the subunits are absolutely necessary for each activity. PhnG, PhnH, PhnI and PhnL have alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase activity and PhnJ has alpha-D-ribose 1-methylphosphonate 5-phosphate C-P-lyase activity in vitro. However, PhnJ can only be isolated in a complex of at least PhnG, PhnH, PhnI, PhnJ and PhnK but this complex is catalytically inactive, possibly because it lacks PhnL.","predictedComplex":false,"interactors":[{"ac":"EBI-1125776","identifier":"P16679","identifierLink":"https://www.uniprot.org/uniprotkb/P16679/entry","name":"phnL","description":"Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42798","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1127704","identifier":"P16687","identifierLink":"https://www.uniprot.org/uniprotkb/P16687/entry","name":"phnI","description":"Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnI","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-1131434","identifier":"P16688","identifierLink":"https://www.uniprot.org/uniprotkb/P16688/entry","name":"phnJ","description":"Alpha-D-ribose 1-methylphosphonate 5-phosphate C-P lyase","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-6401276","identifier":"P16686","identifierLink":"https://www.uniprot.org/uniprotkb/P16686/entry","name":"phnH","description":"Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnH","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-9126715","identifier":"P16685","identifierLink":"https://www.uniprot.org/uniprotkb/P16685/entry","name":"phnG","description":"Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-9144395","identifier":"P16678","identifierLink":"https://www.uniprot.org/uniprotkb/P16678/entry","name":"phnK","description":"Putative phosphonates utilization ATP-binding protein PhnK","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42764","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1930","complexName":"DXP reductoisomerase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Enzyme involved in the 2-C-methyl-D-erythritol 4-phosphate pathway of  isopentenyl diphosphate biosynthesis. It catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).\r\n\r\nDXR is a promising target for the design of herbicidal, antibacterial, and antimalarial substances.","predictedComplex":false,"interactors":[{"ac":"EBI-1114368","identifier":"P45568","identifierLink":"https://www.uniprot.org/uniprotkb/P45568/entry","name":"dxr","description":"1-deoxy-D-xylulose 5-phosphate reductoisomerase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30525","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1931","complexName":"Respiratory chain complex II","organismName":"Escherichia coli (strain K12); 83333","description":"Key enzyme linking the Krebs cycle with the respiratory chain in aerobic respiration: Catalyzes the oxidation of succinate to fumarate and the reduction of quinone to quinol. Electrons flow from the FAD-bound succinate through the Fe-S clusters to a b556 heme. Electrons ultimately reduce quinone to quinol in the membrane bound part of the enzyme. Under most conditions the electrons are used to reduce oxygen, allowing ATP synthesis. \r\n\r\nMember of the Complex II family. The functionally inverse complex found in anaerobic respiration is the QFR complex (CPX-1967).","predictedComplex":false,"interactors":[{"ac":"EBI-1035514","identifier":"P07014","identifierLink":"https://www.uniprot.org/uniprotkb/P07014/entry","name":"sdhB","description":"Succinate dehydrogenase iron-sulfur subunit","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11921","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1035526","identifier":"P69054","identifierLink":"https://www.uniprot.org/uniprotkb/P69054/entry","name":"sdhC","description":"Succinate dehydrogenase cytochrome b556 subunit","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10978","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1035534","identifier":"P0AC44","identifierLink":"https://www.uniprot.org/uniprotkb/P0AC44/entry","name":"sdhD","description":"Succinate dehydrogenase hydrophobic membrane anchor subunit","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR38689","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1225105","identifier":"CHEBI:16238","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16238","name":"fad","description":"FAD - Flavin adenine dinucleotide","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-371263","identifier":"P0AC41","identifierLink":"https://www.uniprot.org/uniprotkb/P0AC41/entry","name":"sdhA","description":"Succinate dehydrogenase flavoprotein subunit","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11632","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-6880484","identifier":"CHEBI:33725","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:33725","name":"fe4-s4","description":"tetra-μ3-sulfido-tetrairon","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-6880488","identifier":"CHEBI:47402","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:47402","name":"fe3-s4","description":"tri-μ-sulfido-μ3-sulfido-triiron","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-6880987","identifier":"CHEBI:33739","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:33739","name":"fe2-s2","description":"di-μ-sulfido-diiron(0)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-6881029","identifier":"CHEBI:36141","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:36141","name":"quinone","description":"quinone","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-6895748","identifier":"CHEBI:51381","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:51381","name":"succinate salt","description":"succinate salt","stochiometry":"minValue: 3, maxValue: 3","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1978","complexName":"Enzyme IIA-maltose transport inhibitory complex","organismName":"Escherichia coli (strain K12); 83333","description":"Binding of enzyme IIA (EIIA-Glc), a component of the glucose-specific phosphotransferase system, inhibits maltose transport from the periplasm to the cytoplasm. Two molecules of EIIA-Glc each bind allosterically to both subunits of MalK thereby fastening the maltose transporter in the open, inward-facing conformation which prevents the binding of maltose-loaded maltose binding protein MBP (MalE) (CPX-1932).\r\n\r\nOnly the non-phosphorylated form of enzyme IIA functions as a maltose uptake inhibitor.","predictedComplex":false,"interactors":[{"ac":"EBI-1118919","identifier":"P02916","identifierLink":"https://www.uniprot.org/uniprotkb/P02916/entry","name":"malF","description":"Maltose/maltodextrin transport system permease protein MalF","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR47314","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-369856","identifier":"P69783","identifierLink":"https://www.uniprot.org/uniprotkb/P69783/entry","name":"crr","description":"PTS system glucose-specific EIIA component","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR45008","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-550803","identifier":"P68187","identifierLink":"https://www.uniprot.org/uniprotkb/P68187/entry","name":"malK","description":"Maltose/maltodextrin import ATP-binding protein MalK","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43875","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6400985","identifier":"P68183","identifierLink":"https://www.uniprot.org/uniprotkb/P68183/entry","name":"malG","description":"Maltose/maltodextrin transport system permease protein MalG","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32243","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1933","complexName":"DnaB-DnaG primase-helicase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Involved in the synthesis of RNA primer sequences used in DNA replication.  dnaG binding to dnaB displaces dnaC from dnaB (CPX-1934), activates the helicase and transposition activity of dnaB and thereby moves replication from the initiation to the priming phase. The interaction of the dnaB helicase and dnaG primase at the replication folk stimulates each others activities: As the helicase unwinds the parental DNA, the primase synthesises Okasaki RNA primers. Finally, DNA Polymerase III holoenzyme docks onto the primer-ssDNA duplex and initiates DNA synthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-548978","identifier":"P0ACB0","identifierLink":"https://www.uniprot.org/uniprotkb/P0ACB0/entry","name":"dnaB","description":"Replicative DNA helicase DnaB","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30153","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549259","identifier":"P0ABS5","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABS5/entry","name":"dnaG","description":"DNA primase","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30313","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1934","complexName":"dnaB-dnaC complex","organismName":"Escherichia coli (strain K12); 83333","description":"After the formation of a DNA bubble, two dnaB helicase hexamers are recruited and loaded onto each of the separated single-stranded DNA strands as dnaB-dnaC complexes. Binding of the helicase loader dnaC inhibits the ATPase and helicase activities of dnaB. dnaC needs to be displaced by the binding of primase dnaG to dnaB before dnaB can initiate its helicase function. Upon binding DNA, dnaC hydrolyzes ATP, allowing dnaB to isomerize into a topologically closed, pre-translocation state competent to bind primase","predictedComplex":false,"interactors":[{"ac":"EBI-548978","identifier":"P0ACB0","identifierLink":"https://www.uniprot.org/uniprotkb/P0ACB0/entry","name":"dnaB","description":"Replicative DNA helicase DnaB","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30153","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549012","identifier":"P0AEF0","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEF0/entry","name":"dnaC","description":"Replicative helicase loader DnaC","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1936","complexName":"Divisome complex","organismName":"Escherichia coli (strain K12); 83333","description":"Mediates the process of cell division, forming a tightly regulated peptidoglycan (PG) synthesis machine that builds a septum between the segregated chromosomes to separate the cell into two daughter cells. ftsZ forms a ring-like structure (Z-ring) at the midcell which establishes the division plane and enables the assembly of the divisome. Arrival of ftsN at the Z ring signals the completion of divisome core assembly and activates septal PG synthesis by activating the enzymatic activities of the two PG synthases, ftsW and ftsI. Additional proteins are known to transiently associate with this core complex but are not essential or conditionally essential for division.","predictedComplex":false,"interactors":[{"ac":"EBI-1029213","identifier":"P77173","identifierLink":"https://www.uniprot.org/uniprotkb/P77173/entry","name":"zipA","description":"Cell division protein ZipA","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR38685","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1134233","identifier":"P29131","identifierLink":"https://www.uniprot.org/uniprotkb/P29131/entry","name":"ftsN","description":"Cell division protein FtsN","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR38687","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1214767","identifier":"P0ABG4","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABG4/entry","name":"ftsW","description":"Probable peptidoglycan glycosyltransferase FtsW","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30474","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21981596","identifier":"CPX-4602","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-4602","name":"FtsEX ABC cell division complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-370963","identifier":"P0A9A6","identifierLink":"https://www.uniprot.org/uniprotkb/P0A9A6/entry","name":"ftsZ","description":"Cell division protein FtsZ","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30314","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-548564","identifier":"P0AD68","identifierLink":"https://www.uniprot.org/uniprotkb/P0AD68/entry","name":"ftsI","description":"Peptidoglycan D,D-transpeptidase FtsI","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30627","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-550562","identifier":"P0ABH0","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABH0/entry","name":"ftsA","description":"Cell division protein FtsA","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32432","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-550795","identifier":"P46889","identifierLink":"https://www.uniprot.org/uniprotkb/P46889/entry","name":"ftsK","description":"DNA translocase FtsK","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR22683","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9547109","identifier":"CPX-3099","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-3099","name":"FtsQBL complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]}]},{"complexAC":"CPX-2698","complexName":"pre-mRNA cleavage and polyadenylation specificity factor complex","organismName":"Homo sapiens; 9606","description":"Endonuclease required for the 3' end processing of most mRNAs. Endonucleolytic cleavage of the nascent pre-mRNA defines the 3' end of the mature transcript and a poly(A) tail is added to the resultant free 3' end, marking the mRNA for nuclear export and controlling mRNA stability and translational efficiency in the cytoplasm. CPSF is an inherently inactive endonuclease, which is activated by accessory factors cleavage stimulatory factor (CPX-2701), cleavage factor IIm (CPX-2692) and RBBP6 (Q7Z6E9). The poly(A) polymerase enzyme (P51003) is not a stable subunit of this complex but is recruited to cleaved transcripts by FIP1L1. RBBP6 is transiently recruited in an RNA-dependent manner.","predictedComplex":false,"interactors":[{"ac":"EBI-1021914","identifier":"Q6UN15","identifierLink":"https://www.uniprot.org/uniprotkb/Q6UN15/entry","name":"FIP1L1","description":"Pre-mRNA 3'-end-processing factor FIP1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13484","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1043224","identifier":"Q9P2I0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P2I0/entry","name":"CPSF2","description":"Cleavage and polyadenylation specificity factor subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45922","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1044699","identifier":"Q9UKF6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UKF6/entry","name":"CPSF3","description":"Cleavage and polyadenylation specificity factor subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11203","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1051992","identifier":"Q92797","identifierLink":"https://www.uniprot.org/uniprotkb/Q92797/entry","name":"SYMPK","description":"Symplekin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15245","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347859","identifier":"Q10570","identifierLink":"https://www.uniprot.org/uniprotkb/Q10570/entry","name":"CPSF1","description":"Cleavage and polyadenylation specificity factor subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712637","identifier":"Q9C0J8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9C0J8/entry","name":"WDR33","description":"pre-mRNA 3' end processing protein WDR33","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22836","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-725860","identifier":"O95639","identifierLink":"https://www.uniprot.org/uniprotkb/O95639/entry","name":"CPSF4","description":"Cleavage and polyadenylation specificity factor subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2699","complexName":"TLR1-TLR10 toll-like receptor complex","organismName":"Homo sapiens; 9606","description":"Type I membrane receptor that plays a crucial role in innate immunity by recognizing conserved patterns in diverse microbial molecules including lipoproteins, lipopeptides, lipopolysaccharide, flagellin, and nucleic acids","predictedComplex":false,"interactors":[{"ac":"EBI-16825459","identifier":"Q9BXR5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BXR5/entry","name":"TLR10","description":"Toll-like receptor 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24365","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9009517","identifier":"Q15399","identifierLink":"https://www.uniprot.org/uniprotkb/Q15399/entry","name":"TLR1","description":"Toll-like receptor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24365","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2700","complexName":"Hedgehog signalling complex","organismName":"Drosophila melanogaster; 7227","description":"Transcriptional repressor complex involved in hedgehog signaling pathway. In the absence of hh (Q02936), the complex promotes the proteolytic processing of the Ci transcription factor to a truncated repressor protein (PRO_0000406217). hh activation of the pathway blocks the processing of ci, allowing the accumulation of the full-length activator protein (PRO_0000046917). The complex associates with microtubules in the absence of Hh stimulation.","predictedComplex":false,"interactors":[{"ac":"EBI-102069","identifier":"O16844","identifierLink":"https://www.uniprot.org/uniprotkb/O16844/entry","name":"cos","description":"Kinesin-like protein costa","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-165536","identifier":"P23647","identifierLink":"https://www.uniprot.org/uniprotkb/P23647/entry","name":"fu","description":"Serine/threonine-protein kinase fused","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22983","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-94976","identifier":"P19538","identifierLink":"https://www.uniprot.org/uniprotkb/P19538/entry","name":"ci","description":"Transcriptional activator cubitus interruptus","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45718","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2701","complexName":"Cleavage stimulation factor complex, CSTF2 variant","organismName":"Homo sapiens; 9606","description":"Binds a G/U-rich region downstream from the cleavage site on pre-mRNAs and provides specificity for poly(A) site selection as part of the pre-mRNA 3' end processing machinery. Required to activate the CPSF complex (CPX-2698).","predictedComplex":false,"interactors":[{"ac":"EBI-1056775","identifier":"Q12996","identifierLink":"https://www.uniprot.org/uniprotkb/Q12996/entry","name":"CSTF3","description":"Cleavage stimulation factor subunit 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19980","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1789619","identifier":"Q05048","identifierLink":"https://www.uniprot.org/uniprotkb/Q05048/entry","name":"CSTF1","description":"Cleavage stimulation factor subunit 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44133","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-711360","identifier":"P33240","identifierLink":"https://www.uniprot.org/uniprotkb/P33240/entry","name":"CSTF2","description":"Cleavage stimulation factor subunit 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45735","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2702","complexName":"Intraflagellar transport complex A","organismName":"Drosophila melanogaster; 7227","description":"IFT particles, composed of the IFT-A and IFT-B (CPX-2704) complexes, enable bidirectional motility along axoneme microtubules essential for the formation (ciliogenesis) and maintenance of cilia that assemble within a membrane projection from the cell surface. Outward or anterograde movement from the cell body to the ciliary tip  is powered by kinesin-2 while the inward or retrograde movement back to the cell body is powered by cytoplasmic Dynein-2 motor.","predictedComplex":false,"interactors":[{"ac":"EBI-128310","identifier":"Q9W097","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W097/entry","name":"Oseg4","description":"WD repeat-containing protein 35","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12764","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-154394","identifier":"Q9VK67","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VK67/entry","name":"IFT43","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR33724","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-176454","identifier":"Q9VSJ6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VSJ6/entry","name":"Oseg1","description":"Intraflagellar transport protein 122 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12764","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32710760","identifier":"Q7KTZ4","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KTZ4/entry","name":"rempA","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15722","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3404357","identifier":"A1ZBM3","identifierLink":"https://www.uniprot.org/uniprotkb/A1ZBM3/entry","name":"Oseg6","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14920","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2703","complexName":"Cleavage stimulation factor complex, CSTF2T variant","organismName":"Homo sapiens; 9606","description":"Binds a G/U-rich region downstream from the cleavage site on pre-mRNAs and provides specificity for poly(A) site selection as part of the pre-mRNA 3' end processing machinery. Required to activate the CPSF complex (CPX-2698).CSTF2T is expressed in testis and brain and is required for spermatogenesis.","predictedComplex":false,"interactors":[{"ac":"EBI-1056775","identifier":"Q12996","identifierLink":"https://www.uniprot.org/uniprotkb/Q12996/entry","name":"CSTF3","description":"Cleavage stimulation factor subunit 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19980","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1789619","identifier":"Q05048","identifierLink":"https://www.uniprot.org/uniprotkb/Q05048/entry","name":"CSTF1","description":"Cleavage stimulation factor subunit 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44133","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-747012","identifier":"Q9H0L4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H0L4/entry","name":"CSTF2T","description":"Cleavage stimulation factor subunit 2 tau variant","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45735","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2704","complexName":"Intraflagellar transport complex B","organismName":"Drosophila melanogaster; 7227","description":"IFT particles, composed of the IFT-A (CPX-2702) and IFT-B complexes, enable bidirectional motility along axoneme microtubules essential for the formation (ciliogenesis) and maintenance of cilia that assemble within a membrane projection from the cell surface. Outward or anterograde movement from the cell body to the ciliary tip  is powered by kinesin-2 while the inward or retrograde movement back to the cell body is powered by cytoplasmic Dynein-2 motor.","predictedComplex":false,"interactors":[{"ac":"EBI-100152","identifier":"Q9VMC0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VMC0/entry","name":"IFT52","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12969","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-146474","identifier":"Q9VR64","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VR64/entry","name":"Cluap1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21547","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-174058","identifier":"Q9VFL0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VFL0/entry","name":"IFT54","description":"TRAF3-interacting protein 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR31363","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2507884","identifier":"Q9W040","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W040/entry","name":"Oseg2","description":"Intraflagellar transport protein 172 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15722","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26759611","identifier":"Q9VF41","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VF41/entry","name":"Ttc26","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14781","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32710901","identifier":"Q7KRS6","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KRS6/entry","name":"nompB","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR44117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32710939","identifier":"Q9VII8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VII8/entry","name":"Oseg5","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR24098","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32710968","identifier":"Q9VK41","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VK41/entry","name":"Ttc30","description":"Tetratricopeptide repeat protein 30 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR20931","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-92466","identifier":"Q9VQS5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VQS5/entry","name":"IFT57","description":"Intraflagellar transport protein 57 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR16011","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-95499","identifier":"Q9VJ72","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VJ72/entry","name":"IFT46","description":"Intraflagellar transport protein 46 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13376","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9922164","identifier":"A1Z6F0","identifierLink":"https://www.uniprot.org/uniprotkb/A1Z6F0/entry","name":"IFT20","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR31978","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2705","complexName":"U7 small nuclear ribonucleoprotein complex","organismName":"Homo sapiens; 9606","description":"Essential role in histone pre-mRNA splicing. The heteroheptameric complex forms on binding to a conserved Sm site [consensus AU(4-6)G] found in single-stranded regions of U7 snRNA.U7 snRNA is produced in the nucleus by RNA polymerase II and exported to the cytoplasm, where the Sm proteins bind and promote the hypermethylation of the N7-monomethyl guanosine cap at their 5'-ends, to produce the 2,2,7-trimethyl guanosine cap structure.","predictedComplex":false,"interactors":[{"ac":"EBI-2626024","identifier":"P83369","identifierLink":"https://www.uniprot.org/uniprotkb/P83369/entry","name":"LSM11","description":"U7 snRNA-associated Sm-like protein LSm11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21415","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2696446","identifier":"URS0000659914_9606","identifierLink":"http://rnacentral.org/rna/URS0000659914_9606","name":"u7_human_snrna","description":"RNA, U7 small nuclear","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small nuclear rna","organismName":"Homo sapiens; 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Ligation of the two exons is then performed by the tRNA-splicing ligase complex (CPX-6411). CLP1 has been observed to influence the level of premature and mature tRNA gene products but the mechanism for this is not yet understood.","predictedComplex":false,"interactors":[{"ac":"EBI-11017932","identifier":"Q9BSV6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BSV6/entry","name":"TSEN34","description":"tRNA-splicing endonuclease subunit Sen34","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13070","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2559818","identifier":"Q8NCE0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NCE0/entry","name":"TSEN2","description":"tRNA-splicing endonuclease subunit Sen2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21227","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2559824","identifier":"Q7Z6J9","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z6J9/entry","name":"TSEN54","description":"tRNA-splicing endonuclease subunit Sen54","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21027","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2559831","identifier":"Q92989","identifierLink":"https://www.uniprot.org/uniprotkb/Q92989/entry","name":"CLP1","description":"Polyribonucleotide 5'-hydroxyl-kinase Clp1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12755","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372432","identifier":"Q8WW01","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WW01/entry","name":"TSEN15","description":"tRNA-splicing endonuclease subunit Sen15","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28582","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2708","complexName":"KIP1 E3 ubiquitin ligase complex","organismName":"Drosophila melanogaster; 7227","description":"E3 ubiquitin ligase complex which is found only in males. Highly enriched in testis where it plays a role in sperm storage. Required for the polycystin-2 protein, Amo (Q9VK95), to reach the tip of the sperm tail.","predictedComplex":false,"interactors":[{"ac":"EBI-32711491","identifier":"Q9VFC4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VFC4/entry","name":"Kpc1","description":"RING-type E3 ubiquitin transferase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13363","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32711518","identifier":"A0A0B4KFW5","identifierLink":"https://www.uniprot.org/uniprotkb/A0A0B4KFW5/entry","name":"Kpc2","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46738","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2709","complexName":"Ragulator complex","organismName":"Drosophila melanogaster; 7227","description":"Involved in amino acid sensing and activation of Tor (Q9VK45) promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPases which couples amino acid transport to activation of complex, Ragulator functions as a guanine nucleotide exchange factor activating the small Rag GTPases. Activated Ragulator and Rag GTPases function as a scaffold recruiting Tor to lysosomes where it is in turn activated. LAMTOR1 is directly responsible for anchoring the Ragulator complex to membranes. Also required for late endosomes/lysosomes biogenesis, it may regulate both the recycling of receptors through endosomes and the MAPK signaling pathway through recruitment of some of its components to late endosomes.","predictedComplex":false,"interactors":[{"ac":"EBI-111967","identifier":"Q9VJD2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VJD2/entry","name":"Lamtor3","description":"Ragulator complex protein LAMTOR3 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13378","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-165902","identifier":"Q9VW73","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VW73/entry","name":"Lamtor1","description":"Ragulator complex protein LAMTOR1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13401","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-175452","identifier":"O96824","identifierLink":"https://www.uniprot.org/uniprotkb/O96824/entry","name":"Lamtor5","description":"Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 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Recruited by Mediator complex (CPX-3227) subunit MED26 (O95402) to regulate transcription termination at replication-dependent histone and snRNA genes and 3′-processing of mRNAs encoding replication-dependent histones and snRNA precursors into mature, non-polyadenylated transcripts.","predictedComplex":false,"interactors":[{"ac":"EBI-1245868","identifier":"P55199","identifierLink":"https://www.uniprot.org/uniprotkb/P55199/entry","name":"ELL","description":"RNA polymerase II elongation factor ELL","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23288","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2513919","identifier":"Q9Y2F5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2F5/entry","name":"ICE1","description":"Little elongation complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11852","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4322746","identifier":"Q659A1","identifierLink":"https://www.uniprot.org/uniprotkb/Q659A1/entry","name":"ICE2","description":"Little elongation complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5280267","identifier":"Q8N5P1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N5P1/entry","name":"ZC3H8","description":"Zinc finger CCCH domain-containing protein 8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2713","complexName":"Little elongation complex, ELL2 variant","organismName":"Homo sapiens; 9606","description":"Regulates the initiation and elongation of RNA polymerase II (Pol II)-transcribed genes encoding small nuclear RNAs (snRNAs). 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AP-2 is involved in plasma membrane to endosome traffic.","predictedComplex":false,"interactors":[{"ac":"EBI-102705","identifier":"O62530","identifierLink":"https://www.uniprot.org/uniprotkb/O62530/entry","name":"AP-2mu","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-133110","identifier":"Q9VDC3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VDC3/entry","name":"AP-2sigma","description":"AP complex subunit sigma","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-183420","identifier":"P91926","identifierLink":"https://www.uniprot.org/uniprotkb/P91926/entry","name":"AP-2alpha","description":"AP-2 complex subunit alpha","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-85346","identifier":"Q24253","identifierLink":"https://www.uniprot.org/uniprotkb/Q24253/entry","name":"AP-1-2beta","description":"AP complex subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2727","complexName":"Adaptor complex AP-3","organismName":"Drosophila melanogaster; 7227","description":"Adaptor complex that orchestrates the formation of membrane coats that mediate cargo selection and vesicle budding, for example by linking clathrin to the membrane surface of trans-Golgi network vesicles. 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Drosophila AP-3 genes were first linked to defects in the biogenesis of visual pigment granules.","predictedComplex":false,"interactors":[{"ac":"EBI-115159","identifier":"P54362","identifierLink":"https://www.uniprot.org/uniprotkb/P54362/entry","name":"g","description":"AP-3 complex subunit delta","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22781","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-115466","identifier":"O76928","identifierLink":"https://www.uniprot.org/uniprotkb/O76928/entry","name":"cm","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30858894","identifier":"Q9W1E8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W1E8/entry","name":"or","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-94191","identifier":"Q9W4K1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W4K1/entry","name":"rb","description":"AP-3 complex subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2728","complexName":"Anaphase-promoting complex","organismName":"Drosophila melanogaster; 7227","description":"APC, a key regulator of cell cycle progression, is a conserved E3 ubiqutin ligase which facilitates multiubiqutination of cell cycle proteins, including cyclins, so marking them for proteasomal destruction. Generally believed that APC acts as a scaffold that brings E2 enzymes and substrates into close proximity. APC activity is required for metaphase-anaphase transition, mitotic exit, G1 phase and DNA replication. Acts by mediating the ubiquitination and subsequent degradation of target proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-114295","identifier":"Q9V831","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V831/entry","name":"APC10","description":"Anaphase-promoting complex subunit 10","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12936","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-124356","identifier":"Q9W4H9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W4H9/entry","name":"fzr","description":"Fizzy-related protein homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19918","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15121143","identifier":"Q7KA43","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KA43/entry","name":"lmgA","description":"Anaphase-promoting complex subunit 11","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16074030","identifier":"Q9VCN6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VCN6/entry","name":"Cdc16","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16074062","identifier":"Q9I7L8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9I7L8/entry","name":"Cdc23","description":"Cyclosome subunit 8","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-164066","identifier":"Q9W1E5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W1E5/entry","name":"mr","description":"Anaphase-promoting complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-175583","identifier":"Q9VS37","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VS37/entry","name":"Cdc27","description":"Cell division cycle protein 27 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-176696","identifier":"Q24044","identifierLink":"https://www.uniprot.org/uniprotkb/Q24044/entry","name":"fzy","description":"Cell division cycle protein 20 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19918","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-187290","identifier":"Q9W3Y6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W3Y6/entry","name":"APC7","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30858940","identifier":"Q9W395","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W395/entry","name":"APC4","description":"Anaphase-promoting complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13260","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3418000","identifier":"Q9VZL2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VZL2/entry","name":"ida","description":"Anaphase-promoting complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12830","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-99850","identifier":"Q9VXV3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VXV3/entry","name":"shtd","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12827","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2729","complexName":"Apoptosome","organismName":"Drosophila melanogaster; 7227","description":"A protease complex that cleaves loops in DrICE (O01382), the executioner procaspase to create the active caspase.","predictedComplex":false,"interactors":[{"ac":"EBI-108311","identifier":"Q9XYF4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XYF4/entry","name":"Dronc","description":"Caspase Dronc","stochiometry":"minValue: 8, maxValue: 8","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15034","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-93302","identifier":"Q7KLI1","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KLI1/entry","name":"Dark","description":"Apoptosome protein Dark","stochiometry":"minValue: 8, maxValue: 8","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22845","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2730","complexName":"siRNA RISC-loading complex, R2D2 variant","organismName":"Drosophila melanogaster; 7227","description":"Endoribonclease complex that has dicing, slicing, guide-strand selection, and AGO2-loading activities.The complex binds asymmetrically to duplex siRNAs, selecting one strand of exogenous siRNAs according to the relative thermodynamic stability of base-pairing at either end and loading it onto AGO2 to form RNA-induced silencing complexes (RISCs). The siRNA is processed into 21 nucleotide siRNA duplexes with 2 nucleotide 3′-overhangs by the RNase III family enzyme Dcr-1 (Q9VCU9).","predictedComplex":false,"interactors":[{"ac":"EBI-156415","identifier":"Q9VLW8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VLW8/entry","name":"r2d2","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46205","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-442476","identifier":"Q9VUQ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VUQ5/entry","name":"AGO2","description":"Protein argonaute-2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22891","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-84244","identifier":"A1ZAW0","identifierLink":"https://www.uniprot.org/uniprotkb/A1ZAW0/entry","name":"Dcr-2","description":"Endoribonuclease Dcr-2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14950","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2731","complexName":"Mitochondrial electron transfer flavoprotein complex","organismName":"Homo sapiens; 9606","description":"Functions as a specific electron acceptor for primary dehydrogenases involved in mitochondrial fatty acid and amino acid catabolism, transferring the electrons to terminal respiratory systems  the electron transfer flavoprotein-ubiquinone oxidoreductase protein (Q16134) which then transfers the electron to the ubiquinone pool in the inner mitochondrial membrane. Located on the matrix face of the inner mitochondrial membrane and docks onto the surface of partner proteins via a recognition peptide element located within an anchor domain.","predictedComplex":false,"interactors":[{"ac":"EBI-1052886","identifier":"P13804","identifierLink":"https://www.uniprot.org/uniprotkb/P13804/entry","name":"ETFA","description":"Electron transfer flavoprotein subunit alpha, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43153","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1056543","identifier":"P38117","identifierLink":"https://www.uniprot.org/uniprotkb/P38117/entry","name":"ETFB","description":"Electron transfer flavoprotein subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12508985","identifier":"CHEBI:456215","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:456215","name":"amp(2-)","description":"AMP(2-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2732","complexName":"siRNA RISC-loading complex, loqs variant","organismName":"Drosophila melanogaster; 7227","description":"Endoribonclease complex that has dicing, slicing, guide-strand selection, and AGO2-loading activities.The complex binds asymmetrically to duplex siRNAs, selecting one strand of exogenous siRNAs according to the relative thermodynamic stability of base-pairing at either end and loading it onto AGO2 to form RNA-induced silencing complexes (RISCs). The siRNA is processed into 21 nucleotide siRNA duplexes with 2 nucleotide 3′-overhangs by the RNase III family enzyme Dicer.","predictedComplex":false,"interactors":[{"ac":"EBI-162836","identifier":"Q9VJY9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VJY9/entry","name":"loqs","description":"Protein Loquacious","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46205","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-442476","identifier":"Q9VUQ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VUQ5/entry","name":"AGO2","description":"Protein argonaute-2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22891","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-84244","identifier":"A1ZAW0","identifierLink":"https://www.uniprot.org/uniprotkb/A1ZAW0/entry","name":"Dcr-2","description":"Endoribonuclease Dcr-2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14950","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2733","complexName":"miRNA RISC complex","organismName":"Drosophila melanogaster; 7227","description":"Incorporates one strand of a micro RNA (miRNA) and uses this  as a template for recognizing complementary mRNA. Once bound to a complementary strand, it activates RNase and cleaves the RNA.","predictedComplex":false,"interactors":[{"ac":"EBI-105513","identifier":"Q32KD4","identifierLink":"https://www.uniprot.org/uniprotkb/Q32KD4/entry","name":"AGO1","description":"Protein argonaute-1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22891","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-160693","identifier":"Q8SY33","identifierLink":"https://www.uniprot.org/uniprotkb/Q8SY33/entry","name":"gw","description":"Protein Gawky","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2735","complexName":"Nuclear exosome targeting complex","organismName":"Homo sapiens; 9606","description":"Promotes the exosomal degradation of a subset of non-coding promoter-upstream transcripts, enhancer RNAs and 3′-extended products of histone and small nuclear RNA transcription. It also targets intronic RNA for decay and/or processing of embedded small nucleolar RNAs. Most probably acts by disentangling ribonucleoprotein complexes and threading unwound RNAs into the nuclear exosome channel (CPX-476, CPX-591).","predictedComplex":false,"interactors":[{"ac":"EBI-1263058","identifier":"Q6NZY4","identifierLink":"https://www.uniprot.org/uniprotkb/Q6NZY4/entry","name":"ZCCHC8","description":"Zinc finger CCHC domain-containing protein 8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13316","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347612","identifier":"P42285","identifierLink":"https://www.uniprot.org/uniprotkb/P42285/entry","name":"MTREX","description":"Exosome RNA helicase MTR4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-746903","identifier":"Q9Y580","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y580/entry","name":"RBM7","description":"RNA-binding protein 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13798","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2736","complexName":"SKI complex","organismName":"Homo sapiens; 9606","description":"Central component of the 3'-5' cytoplasmic mRNA degradation pathway which mediates degradation by the exosome (CPX-592,CPX-600). The SKI complex appears to thread RNAs directly to the exosome, coupling the SKIV2L helicase and the exoribonuclease of the exosome  through a continuous RNA channel.","predictedComplex":false,"interactors":[{"ac":"EBI-358545","identifier":"Q9GZS3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9GZS3/entry","name":"SKIC8","description":"Superkiller complex protein 8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44090","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373226","identifier":"Q15477","identifierLink":"https://www.uniprot.org/uniprotkb/Q15477/entry","name":"SKIC2","description":"Superkiller complex protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6083436","identifier":"Q6PGP7","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PGP7/entry","name":"SKIC3","description":"Superkiller complex protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15704","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2737","complexName":"miRNA RISC-loading complex","organismName":"Drosophila melanogaster; 7227","description":"Endoribonuclease required for the formation of a mature RNA induced silencing complex (RISC, CPX-2733). Processes precursor miRNAs (pre-miRNAs) to mature miRNAs and then loads them onto AGO1 (Q32KD4). The primary transcripts, pri-miRNAs, are processed to pre-miRNAs in the nucleus by an RNase III enzyme, drosha (Q7KNF1). Upon export to the cytoplasm, pre-miRNAs are further processed by DCR-1.","predictedComplex":false,"interactors":[{"ac":"EBI-105513","identifier":"Q32KD4","identifierLink":"https://www.uniprot.org/uniprotkb/Q32KD4/entry","name":"AGO1","description":"Protein argonaute-1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22891","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-112170","identifier":"Q9VCU9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VCU9/entry","name":"Dcr-1","description":"Endoribonuclease Dcr-1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14950","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2740","complexName":"TRAMP complex, TENT4B-ZCCHC7 variant","organismName":"Homo sapiens; 9606","description":"Recognises and binds to splicing-defective pre-mRNAs and spliced-out introns leading to their rapid degradation by the nuclear exosome (CPX-476, CPX-591). Adds a short oligo(A) tail to the RNA which is assumed to make it a better substrate for 3'-end degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-2803971","identifier":"Q8NDF8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NDF8/entry","name":"TENT4B","description":"Terminal nucleotidyltransferase 4B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347612","identifier":"P42285","identifierLink":"https://www.uniprot.org/uniprotkb/P42285/entry","name":"MTREX","description":"Exosome RNA helicase MTR4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7265024","identifier":"Q8N3Z6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N3Z6/entry","name":"ZCCHC7","description":"Zinc finger CCHC domain-containing protein 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46543","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2742","complexName":"ATAC histone acetyltransferase complex","organismName":"Drosophila melanogaster; 7227","description":"Histone acetyltransferase complex with two separate acetyltransferase enzymes with distinct preferences for histone substrates.  It positively regulates gene transcription and, although it does not have any intrinsic remodeling activity, facilitates nucleosome sliding of ISWI and SWI-SNF families of chromatin-remodeling complexes.","predictedComplex":false,"interactors":[{"ac":"EBI-133915","identifier":"Q7KSD8","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KSD8/entry","name":"Ada2a","description":"Transcriptional adapter 2A","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12374","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-138718","identifier":"Q9V444","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V444/entry","name":"Chrac-14","description":"DNA polymerase epsilon subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46172","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-139086","identifier":"Q9VTZ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VTZ1/entry","name":"Gcn5","description":"histone acetyltransferase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45750","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-157363","identifier":"Q9VM59","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VM59/entry","name":"Atac1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22705","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-157691","identifier":"Q9VJ73","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VJ73/entry","name":"Atac2","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR20916","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-176193","identifier":"Q9VJQ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VJQ5/entry","name":"NC2beta","description":"Protein Dr1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46138","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-186463","identifier":"Q9VBX2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VBX2/entry","name":"Mocs2B","description":"Molybdopterin synthase catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23404","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2912837","identifier":"Q9W2I4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W2I4/entry","name":"Sgf29","description":"SAGA-associated factor 29kDa","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21539","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2912878","identifier":"Q9V4C8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V4C8/entry","name":"Hcf","description":"Host cell factor","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46003","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30858590","identifier":"M9PHZ1","identifierLink":"https://www.uniprot.org/uniprotkb/M9PHZ1/entry","name":"Ada3","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13556","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30860224","identifier":"M9NFF9","identifierLink":"https://www.uniprot.org/uniprotkb/M9NFF9/entry","name":"Atac3","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR24193","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-90899","identifier":"Q9V3J8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V3J8/entry","name":"wds","description":"Protein will die slowly","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 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May promote autophagosome formation.","predictedComplex":false,"interactors":[{"ac":"EBI-109649","identifier":"Q9W3R7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W3R7/entry","name":"Atg5","description":"Autophagy protein 5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26825021","identifier":"Q9VTU1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VTU1/entry","name":"Atg12","description":"Autophagy protein 12-like","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13385","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30860270","identifier":"B7Z0R7","identifierLink":"https://www.uniprot.org/uniprotkb/B7Z0R7/entry","name":"Atg16","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19878","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2744","complexName":"Phosphatidylinositol 3-kinase complex, class III, ATG14 variant","organismName":"Drosophila melanogaster; 7227","description":"A phosphatidylinositol 3-kinase complex that specifically phosphorylates 1-phosphatidyl-1D-myo-inositol(1-) (CHEBI:57880) in an ATP- and Mn(2+)-dependent manner. Plays a key role in initiation and maturation of autophagosomes, involved in the transport of lysosomal enzyme precursors to lysosomes, required for transport from early to late endosomes.","predictedComplex":false,"interactors":[{"ac":"EBI-134130","identifier":"Q9VCE1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VCE1/entry","name":"Atg6","description":"Beclin-1-like protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12768","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-144670","identifier":"Q9W1M7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W1M7/entry","name":"Pi3K59F","description":"Phosphatidylinositol 3-kinase catalytic subunit type 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3406245","identifier":"Q9VHH2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VHH2/entry","name":"Vps15","description":"non-specific serine/threonine protein kinase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR17583","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3415310","identifier":"Q9VAP6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VAP6/entry","name":"Atg14","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13664","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2745","complexName":"ATG1 protein kinase complex","organismName":"Drosophila melanogaster; 7227","description":"Central regulator of autophagy initiation. Essential for recruitment of Atg proteins to the pre-autophagosomal structure, the putative site for autophagosome formation, under starvation condition, resulting in the sequestration of cytoplasmic proteins and organelles for bulk degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-109195","identifier":"Q9VWQ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VWQ1/entry","name":"Atg101","description":"Autophagy-related protein 101","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13292","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-166647","identifier":"Q7KTS2","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KTS2/entry","name":"Atg17","description":"RB1-inducible coiled-coil protein 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-179591","identifier":"Q9VHR6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VHR6/entry","name":"Atg13","description":"Autophagy-related protein 13 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13430","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-466412","identifier":"Q8MQJ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8MQJ7/entry","name":"Atg1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR24348","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2746","complexName":"Brahma SWI/SNF ATP-dependent chromatin remodeling complex","organismName":"Drosophila melanogaster; 7227","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC).","predictedComplex":false,"interactors":[{"ac":"EBI-115993","identifier":"Q8IN94","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IN94/entry","name":"osa","description":"Trithorax group protein osa","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-123863","identifier":"Q7K012","identifierLink":"https://www.uniprot.org/uniprotkb/Q7K012/entry","name":"Bap55","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-130188","identifier":"P10987","identifierLink":"https://www.uniprot.org/uniprotkb/P10987/entry","name":"Act5C","description":"Actin-5C","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-132623","identifier":"Q9VF03","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VF03/entry","name":"mor","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-136550","identifier":"Q7K3G5","identifierLink":"https://www.uniprot.org/uniprotkb/Q7K3G5/entry","name":"d4","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-151570","identifier":"Q24090","identifierLink":"https://www.uniprot.org/uniprotkb/Q24090/entry","name":"Snr1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-163765","identifier":"Q9W384","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W384/entry","name":"Bap111","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31428598","identifier":"Q9W3G1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W3G1/entry","name":"Dmel\\CG10555","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23107","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3413604","identifier":"O76857","identifierLink":"https://www.uniprot.org/uniprotkb/O76857/entry","name":"BCL7-like","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-75169","identifier":"Q9VYG2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VYG2/entry","name":"Bap60","description":"Brahma-associated protein of 60 kDa","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-868480","identifier":"P25439","identifierLink":"https://www.uniprot.org/uniprotkb/P25439/entry","name":"brm","description":"ATP-dependent helicase brm","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2747","complexName":"BBSome complex","organismName":"Drosophila melanogaster; 7227","description":"The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. It is involved in the trafficking of membrane proteins to primary cilia and interacts with IFT-A and IFT-B complexes in the intraflagella transport system.","predictedComplex":false,"interactors":[{"ac":"EBI-179095","identifier":"Q9I7P3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9I7P3/entry","name":"BBS5","description":"BBSome complex member BBS5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30860924","identifier":"E1JIG6","identifierLink":"https://www.uniprot.org/uniprotkb/E1JIG6/entry","name":"BBIP1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR28596","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30860944","identifier":"A1Z8E9","identifierLink":"https://www.uniprot.org/uniprotkb/A1Z8E9/entry","name":"BBS4","description":"BBSome complex member BBS4 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR44186","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30860964","identifier":"Q9VPP9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VPP9/entry","name":"BBS8","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR44177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30860987","identifier":"B7YZM8","identifierLink":"https://www.uniprot.org/uniprotkb/B7YZM8/entry","name":"BBS9","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR20991","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30861033","identifier":"A1ZBK9","identifierLink":"https://www.uniprot.org/uniprotkb/A1ZBK9/entry","name":"Arl6","description":"ADP-ribosylation factor-like protein 6","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11711","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3412121","identifier":"Q9VS19","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VS19/entry","name":"BBS1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR20870","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2748","complexName":"SCF E3 ubiquitin ligase complex, FBXL21 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXL21 target proteins include CRY1 (Q16526)/CRY2 (Q49AN0) to which it binds with a higher affinity than does SCF-FBXL3 (CPX-3291). In the nucleus, where both FBXL21 and FBXL3 are present, FBXL21 sequesters CRY proteins from FBXL3 and protects them from FBXL3-induced proteasomal degradation. In the cytosol, where FBXL3 is absent, FBXL21 triggers the slow degradation of CRY1/2 thus playing a role in maintaining circadian clock oscillations.","predictedComplex":false,"interactors":[{"ac":"EBI-21842236","identifier":"Q9UKT6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UKT6/entry","name":"FBXL21P","description":"Putative F-box/LRR-repeat protein 21","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2749","complexName":"TRAMP complex, TENT4A-ZCCHC7 variant","organismName":"Homo sapiens; 9606","description":"Recognises and binds to splicing-defective pre-mRNAs and spliced-out introns leading to their rapid degradation by the nuclear exosome (CPX-476, CPX-591). Adds a short oligo(A) tail to the RNA which is assumed to make it a better substrate for 3'-end degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-347612","identifier":"P42285","identifierLink":"https://www.uniprot.org/uniprotkb/P42285/entry","name":"MTREX","description":"Exosome RNA helicase MTR4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7265024","identifier":"Q8N3Z6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N3Z6/entry","name":"ZCCHC7","description":"Zinc finger CCHC domain-containing protein 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46543","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7851084","identifier":"Q5XG87","identifierLink":"https://www.uniprot.org/uniprotkb/Q5XG87/entry","name":"TENT4A","description":"Terminal nucleotidyltransferase 4A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2750","complexName":"Poly(A) tail exosome targeting complex, RBM26 variant","organismName":"Homo sapiens; 9606","description":"Present in the nucleoplasm where it recognises and directs a subset of long and polyadenylated poly(A) RNAs for exosomal degradation.  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The neurotoxin causes paralysis by both pre- and postsynaptic blocking of acetylcholine signalling. The CA subunit increases the lethal potency of the uncomplexed CB subunit by enabling the toxin to reach the specific protein crotoxin receptor at the neuromuscular junction.","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-28965060","identifier":"P08878-PRO_0000022854","identifierLink":"https://www.uniprot.org/uniprotkb/P08878-PRO_0000022854/entry","name":"p08878-pro","description":"Crotoxin chain alpha CA1, CA2 and CA4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Crotalus durissus terrificus; 8732","xrefs":[]},{"ac":"EBI-28965064","identifier":"P08878-PRO_0000022856","identifierLink":"https://www.uniprot.org/uniprotkb/P08878-PRO_0000022856/entry","name":"p08878-pro","description":"Crotoxin chain beta CA2, CA3 and CA4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Crotalus durissus terrificus; 8732","xrefs":[]},{"ac":"EBI-28965072","identifier":"P08878-PRO_0000022858","identifierLink":"https://www.uniprot.org/uniprotkb/P08878-PRO_0000022858/entry","name":"p08878-pro","description":"Crotoxin chain gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Crotalus durissus terrificus; 8732","xrefs":[]},{"ac":"EBI-28965081","identifier":"P0CG56","identifierLink":"https://www.uniprot.org/uniprotkb/P0CG56/entry","name":"pa2bb","description":"Phospholipase A2 crotoxin basic subunit CBb","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Crotalus durissus terrificus; 8732","xrefs":[]}]},{"complexAC":"CPX-2752","complexName":"Poly(A) tail exosome targeting complex, RBM27 variant","organismName":"Homo sapiens; 9606","description":"Recognises and binds to splicing-defective pre-mRNAs and spliced-out introns leading to their rapid degradation by the nuclear exosome (CPX-476, CPX-591). 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Involved in pigment granule biogenesis.","predictedComplex":false,"interactors":[{"ac":"EBI-122095","identifier":"Q9VTC2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VTC2/entry","name":"Blos4","description":"Biogenesis of lysosome-related organelles complex 1 subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR16230","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-168264","identifier":"Q9VTM0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VTM0/entry","name":"Pldn","description":"Biogenesis of lysosome-related organelles complex 1 subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR31328","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-179987","identifier":"Q9VVT5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVT5/entry","name":"Dysb","description":"Dysbindin protein homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-2108282","identifier":"A1Z9S1","identifierLink":"https://www.uniprot.org/uniprotkb/A1Z9S1/entry","name":"Blos1","description":"Biogenesis of lysosome-related organelles complex 1 subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30861077","identifier":"A8JNV4","identifierLink":"https://www.uniprot.org/uniprotkb/A8JNV4/entry","name":"Blos3","description":"Biogenesis of lysosome-related organelles complex 1 subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR31974","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30861089","identifier":"Q0KI28","identifierLink":"https://www.uniprot.org/uniprotkb/Q0KI28/entry","name":"Muted","description":"Biogenesis of lysosome-related organelles complex 1 subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR31784","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-87041","identifier":"Q9VTE0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VTE0/entry","name":"Blos2","description":"Biogenesis of lysosome-related organelles complex 1 subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46479","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-88022","identifier":"Q9VQF9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VQF9/entry","name":"Snapin","description":"SNAPIN protein homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR31305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2755","complexName":"BLOC-2 complex","organismName":"Drosophila melanogaster; 7227","description":"Adaptor complex required for the biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules. Involved in eye pigmentation.","predictedComplex":false,"interactors":[{"ac":"EBI-123285","identifier":"Q9VHN9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VHN9/entry","name":"p","description":"BLOC-2 complex member HPS5 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23287","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3409831","identifier":"Q9VNX0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VNX0/entry","name":"NP_649372","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR28633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2756","complexName":"BLOC-3 complex","organismName":"Drosophila melanogaster; 7227","description":"A probable guanine exchange factor (GEF) complex required for the biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules. BLOC-3 is proposed to regulate protein trafficking and organelle dynamics.","predictedComplex":false,"interactors":[{"ac":"EBI-30861133","identifier":"Q7K3N1","identifierLink":"https://www.uniprot.org/uniprotkb/Q7K3N1/entry","name":"HPS1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3424142","identifier":"A1ZAX8","identifierLink":"https://www.uniprot.org/uniprotkb/A1ZAX8/entry","name":"HPS4","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14407","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2757","complexName":"CRL4-ERCC8 E3 ubiquitin ligase complex, CUL4A variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor ERCC8. The complex is active in the transcription coupled branch of nucleotide excision repair through the ubiquitination and subsequent proteasomal degradation of ERCC6 (Q03468) in a UV-dependent manner. This enables the recovery of RNA synthesis after transcription-coupled repair. ERRC6 is a component of the B-WICH chromatin remodelling complex (CPX-1099).","predictedComplex":false,"interactors":[{"ac":"EBI-295260","identifier":"Q13216","identifierLink":"https://www.uniprot.org/uniprotkb/Q13216/entry","name":"ERCC8","description":"DNA excision repair protein ERCC-8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46202","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456106","identifier":"Q13619","identifierLink":"https://www.uniprot.org/uniprotkb/Q13619/entry","name":"CUL4A","description":"Cullin-4A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2758","complexName":"CRL4-ERCC8 E3 ubiquitin ligase complex, CUL4B variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor ERCC8. The complex is is active in the transcription coupled branch of nucleotide excision repair through the ubiquitination and subsequent proteasomal degradation of ERCC6 (Q03468) in a UV-dependent manner. This enables the recovery of RNA synthesis after transcription-coupled repair. ERRC6 is a component of the B-WICH chromatin remodelling complex (CPX-1099).","predictedComplex":false,"interactors":[{"ac":"EBI-295260","identifier":"Q13216","identifierLink":"https://www.uniprot.org/uniprotkb/Q13216/entry","name":"ERCC8","description":"DNA excision repair protein ERCC-8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46202","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456067","identifier":"Q13620","identifierLink":"https://www.uniprot.org/uniprotkb/Q13620/entry","name":"CUL4B","description":"Cullin-4B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2759","complexName":"CRL4-CRBN E3 ubiquitin ligase complex, CUL4A variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor CRBN. The complex is active in a wide range of biological functions, including ion channel regulation, cancer development and biological regulation, immune regulation, energy metabolism regulation through the ubiquitination and subsequent proteasomal degradation of a range of target proteins. Target of thalidomide, lenalidomide and pomalidomide, therapeutically important drugs for multiple myeloma and other B-cell malignancies.","predictedComplex":false,"interactors":[{"ac":"EBI-2510250","identifier":"Q96SW2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96SW2/entry","name":"CRBN","description":"Protein cereblon","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456106","identifier":"Q13619","identifierLink":"https://www.uniprot.org/uniprotkb/Q13619/entry","name":"CUL4A","description":"Cullin-4A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2760","complexName":"BORC complex","organismName":"Drosophila melanogaster; 7227","description":"Lysosome associated multi-subunit protein complex that promotes lysosome positioning through coupling to the small GTPase Arl8. This initiates a chain of interactions that promotes the kinesin-dependent movement of lysosomes toward the plus ends of microtubules in the peripheral cytoplasm.","predictedComplex":false,"interactors":[{"ac":"EBI-103162","identifier":"Q9VYT1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VYT1/entry","name":"BORCS5","description":"BLOC-1-related complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR31634","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15108681","identifier":"Q9W0Q3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W0Q3/entry","name":"BORCS6","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13440","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-195214","identifier":"Q9VTY4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VTY4/entry","name":"kxdl1","description":"KxDL motif-containing protein CG10681","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13511","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2108282","identifier":"A1Z9S1","identifierLink":"https://www.uniprot.org/uniprotkb/A1Z9S1/entry","name":"Blos1","description":"Biogenesis of lysosome-related organelles complex 1 subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30861229","identifier":"A1ZBV5","identifierLink":"https://www.uniprot.org/uniprotkb/A1ZBV5/entry","name":"BORCS7","description":"BLOC-1-related complex subunit 7","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR31397","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30861243","identifier":"Q8IR45","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IR45/entry","name":"borc8","description":"BLOC-1-related complex subunit 8 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21146","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-87041","identifier":"Q9VTE0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VTE0/entry","name":"Blos2","description":"Biogenesis of lysosome-related organelles complex 1 subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46479","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-88022","identifier":"Q9VQF9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VQF9/entry","name":"Snapin","description":"SNAPIN protein homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR31305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2761","complexName":"C/D small nucleolar ribonuclear protein complex","organismName":"Drosophila melanogaster; 7227","description":"S-adenosyl-L-methionine-dependent methyltransferase complex that catalyzes the site-specific 2'-O-methylation of ribosomal RNAs using box C/D snoRNAs as guides thus assisting the assembly of ribosomes. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA.","predictedComplex":false,"interactors":[{"ac":"EBI-155336","identifier":"Q9VM69","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VM69/entry","name":"nop5","description":"Nucleolar protein 58","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-185305","identifier":"Q9W1V3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W1V3/entry","name":"Fib","description":"rRNA 2'-O-methyltransferase fibrillarin","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10335","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30813205","identifier":"CHEBI:59789","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:59789","name":"s-adenosyl-l-methionine zwitterion","description":"S-adenosyl-L-methionine zwitterion","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-30861259","identifier":"Q8MSW9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8MSW9/entry","name":"U3-55K","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19865","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3402783","identifier":"Q95WY3","identifierLink":"https://www.uniprot.org/uniprotkb/Q95WY3/entry","name":"Nop56","description":"Nucleolar protein 56","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2762","complexName":"CRL4-CRBN E3 ubiquitin ligase complex, CUL4B variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor CRBN. The complex is active in a wide range of biological functions, including ion channel regulation, cancer development and biological regulation, immune regulation, energy metabolism regulation through the ubiquitination and subsequent proteasomal degradation of a range of target proteins. Target of thalidomide, lenalidomide and pomalidomide, therapeutically important drugs for multiple myeloma and other B-cell malignancies.","predictedComplex":false,"interactors":[{"ac":"EBI-2510250","identifier":"Q96SW2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96SW2/entry","name":"CRBN","description":"Protein cereblon","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456067","identifier":"Q13620","identifierLink":"https://www.uniprot.org/uniprotkb/Q13620/entry","name":"CUL4B","description":"Cullin-4B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2763","complexName":"Chromatin assembly factor 1 complex","organismName":"Drosophila melanogaster; 7227","description":"Catalyzes de novo assembly of nucleosomes onto newly synthesized DNA, involved in chromatin assembly following both DNA replication and some forms of DNA repair. Binds modified histones H3 and H4 and deposits them as a tetramer, preferentially onto replicating DNA, in a step coupled to the replication process. This is followed by deposition of a pair of dimers of histones H2A and H2B mediated by other factor(s) in a process not necessarily coupled to DNA replication. The histone core of nucleosomes consists of two copies of each of histones H2A, H2B, H3 and H4. CAF-1 nucleosome deposition is thought to be involved in heterochromatic silencing and is  also implicated in epigenetic regulation.","predictedComplex":false,"interactors":[{"ac":"EBI-128685","identifier":"A1Z898","identifierLink":"https://www.uniprot.org/uniprotkb/A1Z898/entry","name":"Caf1-105","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15271","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-130352","identifier":"Q9W3D1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W3D1/entry","name":"Caf1-180","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15272","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-75924","identifier":"Q24572","identifierLink":"https://www.uniprot.org/uniprotkb/Q24572/entry","name":"Caf1-55","description":"Chromatin assembly factor 1 p55 subunit","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2764","complexName":"Cyclin-dependent protein kinase-activating kinase complex","organismName":"Drosophila melanogaster; 7227","description":"Cyclin-dependent kinase (CDK) activation minimally depends on two events: binding to a cyclin and phosphorylation of a conserved Thr residue in the activation (T) loop. CAK activates cyclin-associated kinases by threonine phosphorylation, thus regulating cell cycle progression. 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The complex selectively binds and ubiquitylates dimers of proteins containing a BTB/POZ domain of aberrant composition and triggers their clearance by proteasomal degradation. SCF-FBXL17 target proteins include KBTBD8 (Q8NFY9), the substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that acts as a regulator of neural crest specification and also SPAST (Q9UBP0) an ATP-dependent polyglutamylated microtubule severing protein.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8835653","identifier":"Q9UF56","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UF56/entry","name":"FBXL17","description":"F-box/LRR-repeat protein 17","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2774","complexName":"CHAT histone acetyltransferase complex","organismName":"Drosophila melanogaster; 7227","description":"Histone acetyltransferase required for histone H3 acetylation.","predictedComplex":false,"interactors":[{"ac":"EBI-139086","identifier":"Q9VTZ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VTZ1/entry","name":"Gcn5","description":"histone acetyltransferase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45750","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2912837","identifier":"Q9W2I4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W2I4/entry","name":"Sgf29","description":"SAGA-associated factor 29kDa","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21539","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30858590","identifier":"M9PHZ1","identifierLink":"https://www.uniprot.org/uniprotkb/M9PHZ1/entry","name":"Ada3","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13556","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30863004","identifier":"Q8I8V0-2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8I8V0-2/entry","name":"Ada2b","description":"Transcriptional adapter 2b","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-3415429","identifier":"Q9NK54","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NK54/entry","name":"chif","description":"Protein chiffon","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2775","complexName":"CHRAC chromatin remodeling complex","organismName":"Drosophila melanogaster; 7227","description":"ATP-dependent chromatin remodeling complex required for efficient DNA replication through highly condensed chromatin. It facilitates this process by mediating the sliding of nucleosomes from an end position to the center of a 248 base pair rDNA without causing major trans displacement of histones.","predictedComplex":false,"interactors":[{"ac":"EBI-138718","identifier":"Q9V444","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V444/entry","name":"Chrac-14","description":"DNA polymerase epsilon subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46172","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-193917","identifier":"Q9V452","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V452/entry","name":"Chrac-16","description":"Chromatin accessibility complex 16kD protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10252","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-196350","identifier":"Q9V9T4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V9T4/entry","name":"Acf","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46510","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-367628","identifier":"Q24368","identifierLink":"https://www.uniprot.org/uniprotkb/Q24368/entry","name":"Iswi","description":"Chromatin-remodeling complex ATPase chain Iswi","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2776","complexName":"Gamma-tubulin small complex","organismName":"Drosophila melanogaster; 7227","description":"Required for the nucleation of microtubules, the process in which several tubulin molecules interact to form a microtubule seed. Essential at each developmental stage.","predictedComplex":false,"interactors":[{"ac":"EBI-165241","identifier":"P42271","identifierLink":"https://www.uniprot.org/uniprotkb/P42271/entry","name":"gammaTub37C","description":"Tubulin gamma-2 chain","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-176976","identifier":"Q9XYP8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XYP8/entry","name":"Grip91","description":"Gamma-tubulin complex component 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19302","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-178952","identifier":"P23257","identifierLink":"https://www.uniprot.org/uniprotkb/P23257/entry","name":"gammaTub23C","description":"Tubulin gamma-1 chain","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-252093","identifier":"Q9XYP7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XYP7/entry","name":"Grip84","description":"Gamma-tubulin complex component 2 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19302","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2777","complexName":"CRL4-CDT2 E3 ubiquitin ligase complex, CUL4B variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor DTL/CDT2. The complex is active in regulating cell cycle control, DNA damage response and translesion DNA synthesis. Responsible for the S phase-dependent proteolysis of CDT1 (Q9H211), an essential replication protein for licensing DNA replication origins. The binding of CDT1 and DTL/CDT2 to the same trimeric PCNA clamp (CPX-538) during DNA synthesis promotes the ubiquitination of CDT1, resulting in its ubiquitin-dependent proteolysis and prevents DNA re-replication and genome instability. Responsible for the degradation of CDKN1A/p21Cip1 (P38936) both during S-phase and following UV damage thus inhibiting p53-dependent G1 arrest that occurs following DNA damage. This again is mediated by PCNA binding.","predictedComplex":false,"interactors":[{"ac":"EBI-1176075","identifier":"Q9NZJ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZJ0/entry","name":"DTL","description":"Denticleless protein homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22852","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456067","identifier":"Q13620","identifierLink":"https://www.uniprot.org/uniprotkb/Q13620/entry","name":"CUL4B","description":"Cullin-4B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2778","complexName":"CRL4-AMBRA1 E3 ubiquitin ligase complex, CUL4B variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor AMBRA1. The complex is active in the regulation of the transition from G1 to S cell phase, binding and ubiquitinating phosphorylated Cyclin-D (CCND1 (P24385), CCND2 (P30279) and CCND3 (P30281)),","predictedComplex":false,"interactors":[{"ac":"EBI-2512975","identifier":"Q9C0C7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9C0C7/entry","name":"AMBRA1","description":"Activating molecule in BECN1-regulated autophagy protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22874","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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In response to amino acid depletion,  the complex strongly increases GTP hydrolysis by RagA-B within the heterodimeric Rag complex converting the protein to its inactive GDP-bound form. This releases TORC1 (CPX-2265) from the lysosomal surface and inhibits TORC1 signaling The GATOR1 complex is negatively regulated by GATOR2 (CPX-2664).","predictedComplex":false,"interactors":[{"ac":"EBI-113252","identifier":"Q9VUB4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VUB4/entry","name":"Nprl3","description":"GATOR complex protein NPRL3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13153","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30879678","identifier":"Q9VXA0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VXA0/entry","name":"Nprl2","description":"GATOR complex protein NPRL2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12991","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3407605","identifier":"Q9W0E3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W0E3/entry","name":"Iml1","description":"GATOR complex protein Iml1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13179","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2782","complexName":"CRL4-DCAF5 E3 ubiquitin ligase complex, CUL4A variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor DCAF5. The complex is active in the ubiquitination and degradation of lysine-methylated non-histone proteins. Regulates the self-renewal and pluripotency or multipotency of embryonic and many adult stem cells.","predictedComplex":false,"interactors":[{"ac":"EBI-3253159","identifier":"Q96JK2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96JK2/entry","name":"DCAF5","description":"DDB1- and CUL4-associated factor 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15574","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456106","identifier":"Q13619","identifierLink":"https://www.uniprot.org/uniprotkb/Q13619/entry","name":"CUL4A","description":"Cullin-4A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2783","complexName":"CRL4-DCAF5 E3 ubiquitin ligase complex, CUL4B variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor DCAF5. 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The complex is active in nuclear receptor homeostasis.","predictedComplex":false,"interactors":[{"ac":"EBI-2559044","identifier":"Q58WW2","identifierLink":"https://www.uniprot.org/uniprotkb/Q58WW2/entry","name":"DCAF6","description":"DDB1- and CUL4-associated factor 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15574","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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The complex is active in controlling cell proliferation, ubiquitinating and targetting the tumour suppressor ST7 (Q9NRC1) for degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-2559135","identifier":"Q8WV16","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WV16/entry","name":"DCAF4","description":"DDB1- and CUL4-associated factor 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44472","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456106","identifier":"Q13619","identifierLink":"https://www.uniprot.org/uniprotkb/Q13619/entry","name":"CUL4A","description":"Cullin-4A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2800","complexName":"Snf1 protein kinase complex variant SIP2","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Energy sensor protein kinase complex, activated by glucose depletion. Regulates cellular energy metabolism by activating energy-producing pathways and inhibiting energy-consuming processes via derepression of glucose-repressed genes. Required for the diauxic shift, in which genes required for mitochondrial oxidative metabolism (normally repressed by glucose) are switched on; growth then resumes at a lower rate. Role in filamentous invasive growth, on glucose depletion, in haploid cells. \r\nThe activity of this complex is modulated by reversible phosphorylation of SNF1 Thr-210 which increases in response to glucose starvation and correlates with large increases in cellular ADP-to-ATP and AMP-to-ATP ratios. Binding of ADP, but not AMP, to the complex protects against dephosphorylation of Thr-210, suggesting that ADP, rather than AMP, may be the critical activating signal. When glucose levels are high, the complex is cytoplasmic. Upon glucose depletion, SIP2-containing SNF1 remain in the cytosol.","predictedComplex":false,"interactors":[{"ac":"EBI-17187","identifier":"P34164","identifierLink":"https://www.uniprot.org/uniprotkb/P34164/entry","name":"SIP2","description":"SNF1 protein kinase subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17516","identifier":"P06782","identifierLink":"https://www.uniprot.org/uniprotkb/P06782/entry","name":"SNF1","description":"Carbon catabolite-derepressing protein kinase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17537","identifier":"P12904","identifierLink":"https://www.uniprot.org/uniprotkb/P12904/entry","name":"SNF4","description":"5'-AMP-activated protein kinase subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2801","complexName":"Gamma-tubulin ring complex","organismName":"Drosophila melanogaster; 7227","description":"Required for the nucleation of microtubules, the process in which several tubulin molecules interact to form a microtubule seed. Localised on the centromere.","predictedComplex":false,"interactors":[{"ac":"EBI-115452","identifier":"Q9VJ57","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VJ57/entry","name":"Grip71","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR44414","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-165241","identifier":"P42271","identifierLink":"https://www.uniprot.org/uniprotkb/P42271/entry","name":"gammaTub37C","description":"Tubulin gamma-2 chain","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-176976","identifier":"Q9XYP8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XYP8/entry","name":"Grip91","description":"Gamma-tubulin complex component 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19302","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-178952","identifier":"P23257","identifierLink":"https://www.uniprot.org/uniprotkb/P23257/entry","name":"gammaTub23C","description":"Tubulin gamma-1 chain","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-188191","identifier":"Q9VXU8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VXU8/entry","name":"Grip128","description":"Gamma-tubulin complex component","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19302","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2508540","identifier":"Q9VTS3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VTS3/entry","name":"Grip163","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19302","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-252093","identifier":"Q9XYP7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XYP7/entry","name":"Grip84","description":"Gamma-tubulin complex component 2 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19302","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3411704","identifier":"Q9VKU7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VKU7/entry","name":"Grip75","description":"Gamma-tubulin complex component 4 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19302","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2804","complexName":"CRL4-DCAF6 E3 ubiquitin ligase complex, CUL4B variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor DCAF6. The complex is active in nuclear receptor homeostasis.","predictedComplex":false,"interactors":[{"ac":"EBI-2559044","identifier":"Q58WW2","identifierLink":"https://www.uniprot.org/uniprotkb/Q58WW2/entry","name":"DCAF6","description":"DDB1- and CUL4-associated factor 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15574","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456067","identifier":"Q13620","identifierLink":"https://www.uniprot.org/uniprotkb/Q13620/entry","name":"CUL4B","description":"Cullin-4B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2806","complexName":"NPHP transition zone complex","organismName":"Homo sapiens; 9606","description":"Part of  the transition zone, a barrier located at the base of cilia which separates the interior and exterior of cilia. The transition zone is characterized by Y-shaped structures that span from the axoneme to the ciliary membrane and comprises of the MKS and NPHP modules.","predictedComplex":false,"interactors":[{"ac":"EBI-4281852","identifier":"O75161","identifierLink":"https://www.uniprot.org/uniprotkb/O75161/entry","name":"NPHP4","description":"Nephrocystin-4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31043","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5235485","identifier":"Q68CZ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q68CZ1/entry","name":"RPGRIP1L","description":"Protein fantom","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14240","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-953828","identifier":"O15259","identifierLink":"https://www.uniprot.org/uniprotkb/O15259/entry","name":"NPHP1","description":"Nephrocystin-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15176","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2808","complexName":"Coagulation factor VIIa - tissue factor complex","organismName":"Homo sapiens; 9606","description":"A serine-type endopeptidase complex of the extrinsic blood coagulation pathway (tissue factor pathway) whose formation in the plasma membrane initiates the blood coagulation process by initiating the cell-surface assembly and propagation of the coagulation protease cascade. Activates coagulation factors IX (P00740) and X (P00742) by limited proteolysis to form active factors IXa (CPX-4945) and Xa (CPX-6215). Selectively cleavages of Arg-|-Ile bonds in factor X to form factor Xa. The coagulation pathway is terminated when fibrinogen is cleaved to fibrin which in turn polymerizes to produce a clot. \r\n\r\nIts zymogen form of factor VII is activated by selective cleavage of Arg-|-Ile bonds to form active factor VIIa. Activation is triggered by trauma and minor proteolysis by thrombin (FIIa, P00734), factor Xa (P00742), factor XIa (P03951) and factor XIIa (P00748). Also constitutively activated at very low levels. Inhibited by complex formation with TFPI (P10646/P48307) and factor Xa.","predictedComplex":false,"interactors":[{"ac":"EBI-11295611","identifier":"P13726-PRO_0000033638","identifierLink":"https://www.uniprot.org/uniprotkb/P13726-PRO_0000033638/entry","name":"F3","description":"Tissue factor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-11295626","identifier":"P08709-PRO_0000027730","identifierLink":"https://www.uniprot.org/uniprotkb/P08709-PRO_0000027730/entry","name":"F7","description":"Factor VII light chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-11295631","identifier":"P08709-PRO_0000027731","identifierLink":"https://www.uniprot.org/uniprotkb/P08709-PRO_0000027731/entry","name":"F7","description":"Factor VII heavy chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 9, maxValue: 9","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2809","complexName":"CRL4-DCAF9 E3 ubiquitin ligase complex, CUL4B variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor DCAF8. The complex is active in the negative regulation of adipogenesis and fat formation.","predictedComplex":false,"interactors":[{"ac":"EBI-311222","identifier":"Q8N5D0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N5D0/entry","name":"WDTC1","description":"WD and tetratricopeptide repeats protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15574","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456067","identifier":"Q13620","identifierLink":"https://www.uniprot.org/uniprotkb/Q13620/entry","name":"CUL4B","description":"Cullin-4B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2810","complexName":"Convulxin venom toxin complex","organismName":"Crotalus durissus terrificus; 8732","description":"C-type lectin-related protein complex that is a potent platelet agonist acting on glycoprotein VI collagen receptor (GPVI) to induce platelet aggregation. May also activate the NLRP3 inflammasome complex (CPX-4141) in peripheral blood mononuclear cells.","predictedComplex":false,"interactors":[{"ac":"EBI-9026162","identifier":"O93427","identifierLink":"https://www.uniprot.org/uniprotkb/O93427/entry","name":"slb","description":"Snaclec convulxin subunit beta","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Crotalus durissus terrificus; 8732","xrefs":[]},{"ac":"EBI-9026165","identifier":"O93426","identifierLink":"https://www.uniprot.org/uniprotkb/O93426/entry","name":"sla","description":"Snaclec convulxin subunit alpha","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Crotalus durissus terrificus; 8732","xrefs":[]}]},{"complexAC":"CPX-2811","complexName":"Lactose synthase complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the production of lactose, the primary carbohydrate in milk, in the lactating mammary gland. The complex forms in the Golgi apparatus and transfers D-galactose (derived from UDP-galactose) to the OH-4 position of glucose forming a  beta-1-4 glycosidic bond to create lactose.","predictedComplex":false,"interactors":[{"ac":"EBI-11019039","identifier":"P15291-2","identifierLink":"https://www.uniprot.org/uniprotkb/P15291-2/entry","name":"B4GALT1","description":"Beta-1,4-galactosyltransferase 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-50437486","identifier":"P00709","identifierLink":"https://www.uniprot.org/uniprotkb/P00709/entry","name":"LALBA","description":"Alpha-lactalbumin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11407","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2812","complexName":"DNA-directed RNA polymerase III complex","organismName":"Caenorhabditis elegans; 6239","description":"Catalyzes the transcription of RNA from an DNA template by acting as a nucleotidyl transferase that polymerizes ribonucleotides at the 3-prime end of an RNA transcript. Responsible for the transcription of genes encoding small structured RNAs such as tRNAs, the 7 SL lncRNA, spliceosomal U6 snRNA and ribosomal 5S RNA. Pol III machinery recognizes conserved promoter elements located within the transcribed region, generally the box A and box B sequences, which contribute to the D- and T-loops in the tRNA structure.","predictedComplex":false,"interactors":[{"ac":"EBI-2414203","identifier":"Q9N5K2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9N5K2/entry","name":"rpb-5","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10535","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2415434","identifier":"Q9N4B7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9N4B7/entry","name":"rpc-11","description":"DNA-directed RNA polymerase subunit","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-320556","identifier":"Q19826","identifierLink":"https://www.uniprot.org/uniprotkb/Q19826/entry","name":"rpb-8","description":"Probable DNA-directed RNA polymerases I, II, and III subunit RPABC3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 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6239","xrefs":[{"identifier":"PTHR13946","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50437156","identifier":"Q8IG67","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IG67/entry","name":"let-611","description":"DNA-directed RNA polymerase III subunit RPC3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12949","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50437177","identifier":"Q27492","identifierLink":"https://www.uniprot.org/uniprotkb/Q27492/entry","name":"rpc-2","description":"DNA-directed RNA polymerase subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR20856","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50437204","identifier":"Q18566","identifierLink":"https://www.uniprot.org/uniprotkb/Q18566/entry","name":"rpc-1","description":"DNA-directed RNA polymerase subunit","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR19376","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50437230","identifier":"Q9U3I0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9U3I0/entry","name":"rpb-12","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50437272","identifier":"Q9N3T3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9N3T3/entry","name":"q9n3t3","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR15367","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50437287","identifier":"Q23206","identifierLink":"https://www.uniprot.org/uniprotkb/Q23206/entry","name":"q23206","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12069","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50437297","identifier":"Q23645","identifierLink":"https://www.uniprot.org/uniprotkb/Q23645/entry","name":"rpc-25","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12709","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50437312","identifier":"P90847","identifierLink":"https://www.uniprot.org/uniprotkb/P90847/entry","name":"p90847","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13408","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50437323","identifier":"Q0G841","identifierLink":"https://www.uniprot.org/uniprotkb/Q0G841/entry","name":"q0g841","description":"DNA-directed RNA polymerase III subunit RPC9","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR15561","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50437342","identifier":"Q9UAY9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UAY9/entry","name":"rpac-40","description":"DNA-directed RNA polymerases I and III subunit RPAC1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6546038","identifier":"P91529","identifierLink":"https://www.uniprot.org/uniprotkb/P91529/entry","name":"rpc6","description":"Probable DNA-directed RNA polymerase III subunit RPC6","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2813","complexName":"Condensin I complex","organismName":"Drosophila melanogaster; 7227","description":"Involved in chromosome condensation and segregation, both in meiosis and mitosis. Assembles in alternating pattern with Condensin II (CPX-2814) complex along metaphase chromosomes with fully resolved sister chromatids. Also affects nuclear architecture and chromosome stability during interphase. Defects in Condensin complexes lead to anaphase bridges and apoptosis. In meiosis, only stably associates with chromosomes after anaphase I.","predictedComplex":false,"interactors":[{"ac":"EBI-142992","identifier":"Q7KK96","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KK96/entry","name":"SMC2","description":"Structural maintenance of chromosomes protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR43941","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-147085","identifier":"Q9VIP9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VIP9/entry","name":"barr","description":"Condensin complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13108","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-196316","identifier":"Q9V3A7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V3A7/entry","name":"glu","description":"Structural maintenance of chromosomes protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR18937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30872419","identifier":"A1Z987","identifierLink":"https://www.uniprot.org/uniprotkb/A1Z987/entry","name":"Cap-G","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14418","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-96549","identifier":"Q9VAJ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VAJ1/entry","name":"Cap-D2","description":"Condensin complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2814","complexName":"Condensin II complex","organismName":"Drosophila melanogaster; 7227","description":"Involved in chromosome condensation and segregation, both in meiosis and mitosis. Assembles in alternating pattern with Condensin I (CPX-2813) complex along metaphase chromosomes with fully resolved sister chromatids. Also affects nuclear architecture and chromosome stability during interphase. Defects in Condensin complexes lead to anaphase bridges and apoptosis. In meiosis, only stably associates with chromosomes after anaphase I.","predictedComplex":false,"interactors":[{"ac":"EBI-142992","identifier":"Q7KK96","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KK96/entry","name":"SMC2","description":"Structural maintenance of chromosomes protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR43941","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-196316","identifier":"Q9V3A7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V3A7/entry","name":"glu","description":"Structural maintenance of chromosomes protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR18937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30872477","identifier":"Q8INL2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8INL2/entry","name":"Cap-H2","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14324","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3406282","identifier":"Q9VMQ4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VMQ4/entry","name":"Cap-D3","description":"Condensin-2 complex subunit","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2951","complexName":"GABA-A receptor, alpha-6/beta-3/delta","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-6258252","identifier":"P28472","identifierLink":"https://www.uniprot.org/uniprotkb/P28472/entry","name":"GABRB3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744352","identifier":"O14764","identifierLink":"https://www.uniprot.org/uniprotkb/O14764/entry","name":"GABRD","description":"Gamma-aminobutyric acid receptor subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008507","identifier":"Q16445","identifierLink":"https://www.uniprot.org/uniprotkb/Q16445/entry","name":"GABRA6","description":"Gamma-aminobutyric acid receptor subunit alpha-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2952","complexName":"GABA-A receptor, alpha6-beta2-delta","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-6949072","identifier":"P47870","identifierLink":"https://www.uniprot.org/uniprotkb/P47870/entry","name":"GABRB2","description":"Gamma-aminobutyric acid receptor subunit beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744352","identifier":"O14764","identifierLink":"https://www.uniprot.org/uniprotkb/O14764/entry","name":"GABRD","description":"Gamma-aminobutyric acid receptor subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008507","identifier":"Q16445","identifierLink":"https://www.uniprot.org/uniprotkb/Q16445/entry","name":"GABRA6","description":"Gamma-aminobutyric acid receptor subunit alpha-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2953","complexName":"GABA-A receptor, alpha4-beta2-delta","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-3909227","identifier":"P48169","identifierLink":"https://www.uniprot.org/uniprotkb/P48169/entry","name":"GABRA4","description":"Gamma-aminobutyric acid receptor subunit alpha-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6949072","identifier":"P47870","identifierLink":"https://www.uniprot.org/uniprotkb/P47870/entry","name":"GABRB2","description":"Gamma-aminobutyric acid receptor subunit beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744352","identifier":"O14764","identifierLink":"https://www.uniprot.org/uniprotkb/O14764/entry","name":"GABRD","description":"Gamma-aminobutyric acid receptor subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2954","complexName":"GABA-A receptor, alpha4-beta3-delta","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptor (alpha-4/beta-3/delta) binds both GABA and histamine (CHEBI:35678), adding to the speculation that it acts as a coincidence detector in the regulation of sleep and wakefulness.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-3909227","identifier":"P48169","identifierLink":"https://www.uniprot.org/uniprotkb/P48169/entry","name":"GABRA4","description":"Gamma-aminobutyric acid receptor subunit alpha-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6258252","identifier":"P28472","identifierLink":"https://www.uniprot.org/uniprotkb/P28472/entry","name":"GABRB3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744352","identifier":"O14764","identifierLink":"https://www.uniprot.org/uniprotkb/O14764/entry","name":"GABRD","description":"Gamma-aminobutyric acid receptor subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2981","complexName":"GABA-A receptor, alpha6-beta3-gamma2","organismName":"Mus musculus; 10090","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-9215146","identifier":"P22723","identifierLink":"https://www.uniprot.org/uniprotkb/P22723/entry","name":"Gabrg2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9215266","identifier":"P16305","identifierLink":"https://www.uniprot.org/uniprotkb/P16305/entry","name":"Gabra6","description":"Gamma-aminobutyric acid receptor subunit alpha-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9215296","identifier":"P63080","identifierLink":"https://www.uniprot.org/uniprotkb/P63080/entry","name":"Gabrb3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2986","complexName":"GABA-A receptor, alpha6-beta3-delta","organismName":"Mus musculus; 10090","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-9215266","identifier":"P16305","identifierLink":"https://www.uniprot.org/uniprotkb/P16305/entry","name":"Gabra6","description":"Gamma-aminobutyric acid receptor subunit alpha-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9215296","identifier":"P63080","identifierLink":"https://www.uniprot.org/uniprotkb/P63080/entry","name":"Gabrb3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9215886","identifier":"P22933","identifierLink":"https://www.uniprot.org/uniprotkb/P22933/entry","name":"Gabrd","description":"Gamma-aminobutyric acid receptor subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2987","complexName":"GABA-A receptor, alpha6-beta2-delta","organismName":"Mus musculus; 10090","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-9215199","identifier":"P63137","identifierLink":"https://www.uniprot.org/uniprotkb/P63137/entry","name":"Gabrb2","description":"Gamma-aminobutyric acid receptor subunit beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9215266","identifier":"P16305","identifierLink":"https://www.uniprot.org/uniprotkb/P16305/entry","name":"Gabra6","description":"Gamma-aminobutyric acid receptor subunit alpha-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9215886","identifier":"P22933","identifierLink":"https://www.uniprot.org/uniprotkb/P22933/entry","name":"Gabrd","description":"Gamma-aminobutyric acid receptor subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2988","complexName":"GABA-A receptor, alpha4-beta2-delta","organismName":"Mus musculus; 10090","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-9215199","identifier":"P63137","identifierLink":"https://www.uniprot.org/uniprotkb/P63137/entry","name":"Gabrb2","description":"Gamma-aminobutyric acid receptor subunit beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9215886","identifier":"P22933","identifierLink":"https://www.uniprot.org/uniprotkb/P22933/entry","name":"Gabrd","description":"Gamma-aminobutyric acid receptor subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9216027","identifier":"Q9D6F4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D6F4/entry","name":"Gabra4","description":"Gamma-aminobutyric acid receptor subunit alpha-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2989","complexName":"GABA-A receptor, alpha4-beta3-delta","organismName":"Mus musculus; 10090","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-9215296","identifier":"P63080","identifierLink":"https://www.uniprot.org/uniprotkb/P63080/entry","name":"Gabrb3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9215886","identifier":"P22933","identifierLink":"https://www.uniprot.org/uniprotkb/P22933/entry","name":"Gabrd","description":"Gamma-aminobutyric acid receptor subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9216027","identifier":"Q9D6F4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D6F4/entry","name":"Gabra4","description":"Gamma-aminobutyric acid receptor subunit alpha-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2165","complexName":"Protein farnesyltransferase complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the transfer of a 15-carbon lipid, the farnesyl moiety, from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X (CaaX box).\r\n\r\nThe hydrophobic farnesyl moiety aids membrane attachment of the target proteins which include many essential signal transduction proteins, including members of the Ras superfamily. Farnesylation is essential both for normal functioning of these proteins, and for the transforming activity of oncogenic mutants.","predictedComplex":false,"interactors":[{"ac":"EBI-602336","identifier":"P49354","identifierLink":"https://www.uniprot.org/uniprotkb/P49354/entry","name":"FNTA","description":"Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-602349","identifier":"P49356","identifierLink":"https://www.uniprot.org/uniprotkb/P49356/entry","name":"FNTB","description":"Protein farnesyltransferase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11774","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2166","complexName":"GABA-A receptor, alpha3-beta3-gamma2","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.The alpha3-beta3-gamma2 receptor is implicated in mediating the anxiolytic and muscle relaxant activities of diazepam, in anticonvulsant action and in the antiabsence effects of clonazepam.","predictedComplex":false,"interactors":[{"ac":"EBI-1763805","identifier":"P34903","identifierLink":"https://www.uniprot.org/uniprotkb/P34903/entry","name":"GABRA3","description":"Gamma-aminobutyric acid receptor subunit alpha-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6258252","identifier":"P28472","identifierLink":"https://www.uniprot.org/uniprotkb/P28472/entry","name":"GABRB3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008430","identifier":"P18507","identifierLink":"https://www.uniprot.org/uniprotkb/P18507/entry","name":"GABRG2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2167","complexName":"GABA-A receptor, alpha1-beta3-gamma2","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-6258252","identifier":"P28472","identifierLink":"https://www.uniprot.org/uniprotkb/P28472/entry","name":"GABRB3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6258308","identifier":"P14867","identifierLink":"https://www.uniprot.org/uniprotkb/P14867/entry","name":"GABRA1","description":"Gamma-aminobutyric acid receptor subunit alpha-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008430","identifier":"P18507","identifierLink":"https://www.uniprot.org/uniprotkb/P18507/entry","name":"GABRG2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2168","complexName":"GABA-A receptor, alpha5-beta3-gamma2","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptor assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nPredominantly expressed in the cerebral cortex, the GABA-A, alpha-5 receptor subtypes constitute less than 5% of the entire receptor population but up to 25% of the receptor subtype are located in the crucial learning and memory-associated area of the brain; the hippocampus.\r\n \r\nLargely absent at GABAergic synapses, exhibit little synaptic phasic inhibition, but abundant in the dendritic regions of extrasynaptic sites, and mediate tonic inhibition with continuously occurring smaller amplitude.\r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets:\r\n\r\n1) Positive allosteric modulation of GABA-A alpha-5 receptor subtypes can selectively decrease hippocampal activity and reverse psychosis-like physiological and behavioural changes in rats; may potentially help treat patients with post-traumatic stress disorder (PTSD) and comorbid psychosis; allopregnanolone (CHEBI:50169), a naturally occurring progesterone derivative, is a PAM referred to as brexanolone when used for the medical treatment of moderate to severe postpartum depression.\r\n\r\n2) Negative-allosteric modulators for reducing their tonic inhibition have been shown to enhance learning and memory in neurological disorders such as schizophrenia, Down syndrome, and autism with a possible alternative benzodiazepine binding site.","predictedComplex":false,"interactors":[{"ac":"EBI-6258252","identifier":"P28472","identifierLink":"https://www.uniprot.org/uniprotkb/P28472/entry","name":"GABRB3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008430","identifier":"P18507","identifierLink":"https://www.uniprot.org/uniprotkb/P18507/entry","name":"GABRG2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008566","identifier":"P31644","identifierLink":"https://www.uniprot.org/uniprotkb/P31644/entry","name":"GABRA5","description":"Gamma-aminobutyric acid receptor subunit alpha-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2982","complexName":"GABA-A receptor, alpha-3/beta-3/gamma-2","organismName":"Mus musculus; 10090","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-9215146","identifier":"P22723","identifierLink":"https://www.uniprot.org/uniprotkb/P22723/entry","name":"Gabrg2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9215296","identifier":"P63080","identifierLink":"https://www.uniprot.org/uniprotkb/P63080/entry","name":"Gabrb3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9215388","identifier":"P26049","identifierLink":"https://www.uniprot.org/uniprotkb/P26049/entry","name":"Gabra3","description":"Gamma-aminobutyric acid receptor subunit alpha-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2983","complexName":"GABA-A receptor, alpha1-beta3-gamma2","organismName":"Mus musculus; 10090","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-770691","identifier":"P62812","identifierLink":"https://www.uniprot.org/uniprotkb/P62812/entry","name":"Gabra1","description":"Gamma-aminobutyric acid receptor subunit alpha-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9215146","identifier":"P22723","identifierLink":"https://www.uniprot.org/uniprotkb/P22723/entry","name":"Gabrg2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9215296","identifier":"P63080","identifierLink":"https://www.uniprot.org/uniprotkb/P63080/entry","name":"Gabrb3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2984","complexName":"GABA-A receptor, alpha5-beta3-gamma2","organismName":"Mus musculus; 10090","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-8069233","identifier":"Q8BHJ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BHJ7/entry","name":"Gabra5","description":"Gamma-aminobutyric acid receptor subunit alpha-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9215146","identifier":"P22723","identifierLink":"https://www.uniprot.org/uniprotkb/P22723/entry","name":"Gabrg2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9215296","identifier":"P63080","identifierLink":"https://www.uniprot.org/uniprotkb/P63080/entry","name":"Gabrb3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2985","complexName":"GABA-A receptor, alpha2-beta3-gamma2","organismName":"Mus musculus; 10090","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-9215146","identifier":"P22723","identifierLink":"https://www.uniprot.org/uniprotkb/P22723/entry","name":"Gabrg2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9215296","identifier":"P63080","identifierLink":"https://www.uniprot.org/uniprotkb/P63080/entry","name":"Gabrb3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9215553","identifier":"P26048","identifierLink":"https://www.uniprot.org/uniprotkb/P26048/entry","name":"Gabra2","description":"Gamma-aminobutyric acid receptor subunit alpha-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2169","complexName":"Protein geranylgeranyl transferase type I complex","organismName":"Bos taurus; 9913","description":"Catalyzes the transfer of a 20-carbon lipid, the geranyl-geranyl moiety, from geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X (CaaX box). The Zn2+ is required for peptide, but not for isoprenoid, substrate binding.\r\n\r\nThe hydrophobic geranyl-geranyl moiety aids membrane attachment of the target proteins which include many essential signal transduction proteins, including members of the Ras superfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-9008459","identifier":"P29702","identifierLink":"https://www.uniprot.org/uniprotkb/P29702/entry","name":"FNTA","description":"Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR11129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008606","identifier":"Q5EAD5","identifierLink":"https://www.uniprot.org/uniprotkb/Q5EAD5/entry","name":"PGGT1B","description":"Geranylgeranyl transferase type-1 subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR11774","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2170","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha2-beta2","organismName":"Homo sapiens; 9606","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. Mainly found in optic lobe. Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10899404","identifier":"P17787-PRO_0000000379","identifierLink":"https://www.uniprot.org/uniprotkb/P17787-PRO_0000000379/entry","name":"CHRNB2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-10950423","identifier":"Q15822-PRO_0000000340","identifierLink":"https://www.uniprot.org/uniprotkb/Q15822-PRO_0000000340/entry","name":"CHRNA2","description":"Neuronal acetylcholine receptor subunit alpha-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-2171","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha9-alpha10","organismName":"Homo sapiens; 9606","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous antagonists such as alpha-bungarotoxin. Unlike classic nicotinic acetylcholine receptors, nicotine blocks acetylcholine-evoked currents in alpha9-alpha10 receptors giving these receptors a pharmacological profile unknown for any other nicotinic or muscarinic cholinergic receptor subtype. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Upregulated by pro-inflammatory cytokines, for example TNF-alpha. Mediates fast, short-lived synaptic transmission of neurotransmitters and is more active than the alpha9 homopentamer (CPX-226). Mainly found in peripheral nervous system and non-neuronal cells, especially in the auditory system (mechanosensory hair, inner-ear tissue, the cochlea) but also in tonsils, immortalized B-cells, cultured T-cells and PBMCs, keratinocytes and in the pituitary gland. In the auditory system the subunits assemble to form the receptor that mediates synaptic transmission between efferent olivocochlear cholinergic fibers which descend from the brainstem and hair cells of the cochlea.","predictedComplex":false,"interactors":[{"ac":"EBI-11164927","identifier":"Q9UGM1-PRO_0000000371","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UGM1-PRO_0000000371/entry","name":"CHRNA9","description":"Neuronal acetylcholine receptor subunit alpha-9","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-11164935","identifier":"Q9GZZ6-PRO_0000000376","identifierLink":"https://www.uniprot.org/uniprotkb/Q9GZZ6-PRO_0000000376/entry","name":"CHRNA10","description":"Neuronal acetylcholine receptor subunit alpha-10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-2173","complexName":"Amylin receptor 1 complex","organismName":"Homo sapiens; 9606","description":"A transmembrane, G-protein-coupled signalling receptor complex that serves as receptor for amylin polypeptide (Amy). \r\n\r\nAmylin is produced in beta-islet cells of the pancreas. It is implicated in selective inhibition of insulin-stimulated glucose utilization and glycogen deposition in muscle, gastric emptying, gastric acid secretion, postprandial glucagon secretion and food intake and aids weight loss. \r\n\r\nCALCR only acts as amylin receptor when bound by RAMP proteins. In the absence of RAMP proteins, CALCR functions as calcitonin receptor. Contrary to the calcitonin receptor-like receptors (CPX-2189, CPX-2191, CPX-3148), the calcitonin receptor can migrate to the plasma membrane without guidance from RAMP proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-2615663","identifier":"P30988","identifierLink":"https://www.uniprot.org/uniprotkb/P30988/entry","name":"CALCR","description":"Calcitonin receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45620","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-962893","identifier":"O60894","identifierLink":"https://www.uniprot.org/uniprotkb/O60894/entry","name":"RAMP1","description":"Receptor activity-modifying protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3186","complexName":"Amylin receptor 2 complex","organismName":"Homo sapiens; 9606","description":"A transmembrane, G-protein-coupled signalling receptor complex that serves as receptor for the amylin polypeptides (Amy). \r\n\r\nAmylin is produced in beta-islet cells of the pancreas. It is implicated in selective inhibition of insulin-stimulated glucose utilization and glycogen deposition in muscle, gastric emptying, gastric acid secretion, postprandial glucagon secretion and food intake and aids weight loss. \r\n\r\nCALCR only acts as amylin receptor when bound by RAMP proteins. In the absence of RAMP proteins, CALCR functions as calcitonin receptor. Unlike the calcitonin receptor-like receptors (CPX-2189, CPX-2191, CPX-3148), the calcitonin receptor can migrate to the plasma membrane without guidance from RAMP proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-2615663","identifier":"P30988","identifierLink":"https://www.uniprot.org/uniprotkb/P30988/entry","name":"CALCR","description":"Calcitonin receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45620","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9009040","identifier":"O60895","identifierLink":"https://www.uniprot.org/uniprotkb/O60895/entry","name":"RAMP2","description":"Receptor activity-modifying protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3187","complexName":"Amylin receptor 3 complex","organismName":"Homo sapiens; 9606","description":"A transmembrane, G-protein-coupled signalling receptor complex that serves as receptor for the amylin polypeptides (Amy). \r\n\r\nAmylin is produced in beta-islet cells of the pancreas. It is implicated in selective inhibition of insulin-stimulated glucose utilization and glycogen deposition in muscle, gastric emptying, gastric acid secretion, postprandial glucagon secretion and food intake and aids weight loss. \r\n\r\nCALCR only acts as amylin receptor when bound by RAMP proteins. In the absence of RAMP proteins, CALCR functions as calcitonin receptor. Unlike the calcitonin receptor-like receptors (CPX-2189, CPX-2191, CPX-3148), the calcitonin receptor can migrate to the plasma membrane without guidance from RAMP proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-2615663","identifier":"P30988","identifierLink":"https://www.uniprot.org/uniprotkb/P30988/entry","name":"CALCR","description":"Calcitonin receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45620","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-720447","identifier":"O60896","identifierLink":"https://www.uniprot.org/uniprotkb/O60896/entry","name":"RAMP3","description":"Receptor activity-modifying protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3235","complexName":"Amylin receptor 1 complex","organismName":"Mus musculus; 10090","description":"A transmembrane, G-protein-coupled signalling receptor complex that serves as receptor for amylin polypeptide (Amy). \r\n\r\nAmylin is produced in beta-islet cells of the pancreas. It is implicated in selective inhibition of insulin-stimulated glucose utilization and glycogen deposition in muscle, gastric emptying, gastric acid secretion, postprandial glucagon secretion and food intake and aids weight loss. \r\n\r\nCALCR only acts as amylin receptor when bound by RAMP proteins. In the absence of RAMP proteins, CALCR functions as calcitonin receptor. Unlike the calcitonin receptor-like receptors (CPX-3149, CPX-3150, CPX-3151), the calcitonin receptor can migrate to the plasma membrane without guidance from RAMP proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-9661498","identifier":"Q9WTJ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WTJ5/entry","name":"Ramp1","description":"Receptor activity-modifying protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9821077","identifier":"Q60755","identifierLink":"https://www.uniprot.org/uniprotkb/Q60755/entry","name":"Calcr","description":"Calcitonin receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45620","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3236","complexName":"Amylin receptor 2 complex","organismName":"Mus musculus; 10090","description":"A transmembrane, G-protein-coupled signalling receptor complex that serves as receptor for the amylin polypeptides (Amy). \r\n\r\nAmylin is produced in beta-islet cells of the pancreas. It is implicated in selective inhibition of insulin-stimulated glucose utilization and glycogen deposition in muscle, gastric emptying, gastric acid secretion, postprandial glucagon secretion and food intake and aids weight loss. \r\n\r\nCALCR only acts as amylin receptor when bound by RAMP proteins. In the absence of RAMP proteins, CALCR functions as calcitonin receptor. Unlike the calcitonin receptor-like receptors (CPX-3149, CPX-3150, CPX-3151), the calcitonin receptor can migrate to the plasma membrane without guidance from RAMP proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-8398957","identifier":"Q9WUP0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WUP0/entry","name":"Ramp2","description":"Receptor activity-modifying protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9821077","identifier":"Q60755","identifierLink":"https://www.uniprot.org/uniprotkb/Q60755/entry","name":"Calcr","description":"Calcitonin receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45620","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3237","complexName":"Amylin receptor 3 complex","organismName":"Mus musculus; 10090","description":"A transmembrane, G-protein-coupled signalling receptor complex that serves as receptor for the amylin polypeptides (Amy). \r\n\r\nAmylin is produced in beta-islet cells of the pancreas. It is implicated in selective inhibition of insulin-stimulated glucose utilization and glycogen deposition in muscle, gastric emptying, gastric acid secretion, postprandial glucagon secretion and food intake and aids weight loss. \r\n\r\nCALCR only acts as amylin receptor when bound by RAMP proteins. In the absence of RAMP proteins, CALCR functions as calcitonin receptor. Unlike the calcitonin receptor-like receptors (CPX-3149, CPX-3150, CPX-3151), the calcitonin receptor can migrate to the plasma membrane without guidance from RAMP proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-9635424","identifier":"Q9WUP1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WUP1/entry","name":"Ramp3","description":"Receptor activity-modifying protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9821077","identifier":"Q60755","identifierLink":"https://www.uniprot.org/uniprotkb/Q60755/entry","name":"Calcr","description":"Calcitonin receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45620","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2174","complexName":"GABA-A receptor, alpha2-beta3-gamma2","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-2685723","identifier":"P47869","identifierLink":"https://www.uniprot.org/uniprotkb/P47869/entry","name":"GABRA2","description":"Gamma-aminobutyric acid receptor subunit alpha-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6258252","identifier":"P28472","identifierLink":"https://www.uniprot.org/uniprotkb/P28472/entry","name":"GABRB3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008430","identifier":"P18507","identifierLink":"https://www.uniprot.org/uniprotkb/P18507/entry","name":"GABRG2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2175","complexName":"5-hydroxytryptamine-3A receptor complex","organismName":"Homo sapiens; 9606","description":"Inward-rectifying, ligand-gated ion channel, which when activated by 5-hydroxytryptamine (5-HT, serotonin) causes fast neuronal depolarization and excitation or modulation of neurotransmitter release depending on their neuronal localisation (central and/or peripheral nervous system). A cation-specific, but otherwise relatively non-selective, ion channel with low conductance. Ca2+-permeability is related to subunit composition with 5HT3A homopentamers being more permeable than 5HT3A/B heteropentamers. \r\n\r\nFound pre- and post-synaptically but with different properties - pre-synaptic 5-HT3 receptors are predominantly calcium-permeant while post-synaptic receptors are permeant to Na+ and K+. Also Mg2+ permeant. Pre-synaptic depolarisations are generally slower than post-synaptic depolarisations. \r\n\r\n5-HT3 receptors increase the frequency of spontaneous excitatory post-synaptic currents (sEPSCs) or miniature EPSCs (mEPSCs). These may be related to 5-HT3-induced depolarisation of pre-synaptic membranes and subsequent activation of cholinergic or glutamatergic neurotransmissions or evoked excitatory post-synaptic currents (eEPSCs) or spontaneous inhibitory post-synaptic currents (sIPSCs) related to GABAergic neurotransmissions post-synaptic 5-HT3 receptor activation. \r\n\r\nDue to different residues in transmembrane domain M2 of the 5-HT3A and 5-HT3B subunits the 5-HT3A/B heteromeric receptors are more efficient conductors than 5-HT3A homomeric receptors and have increased agonist and antagonist affinity. Homomeric receptors recover faster from desensitisation but are probably less prevalent in vivo. \r\n\r\nHigh levels of expression are found in the vagal terminals of the dorsal vagal complex where it is involved in the vomiting reflex (especially post-operative and chemotherapy- and radiation-induced vomiting and nausea), in the amygdala and the hippocampi. 5-HT3 receptor antagonists therefore act as effective anti-emetic drugs. Lower levels of expression are found in the forebrain with higher relative expression in the striatum than the cortical regions. \r\n\r\nInvolved in processes associated with emotion, cognition, memory and pain perception. \r\n\r\nInvolved in ganglionic transmission in the myenteric plexus in the mucosal layer and expressed in the gastrointestinal (GI) tract where serotonin mediates control over a variety of physiological functions such as the contraction/relaxation of smooth muscle, and peristaltic and secretory reflexes, directly or indirectly through intrinsic primary afferent neurons.\r\n\r\nPlays an important role in the regulation of inflammation and immune responses in the peripheral nervous system. \r\n\r\nActivation of 5-HT3 receptors on visceral afferents in some irritable bowel syndrome (IBS) patients results in visceral hypersensitivity. \r\n\r\nChaperone proteins assist assembly, modifications and export from the ER followed by transport in vesicle-like structures along microtubules to the plasma membrane where they typically form clusters in F-actin-rich regions.","predictedComplex":false,"interactors":[{"ac":"EBI-9008743","identifier":"P46098","identifierLink":"https://www.uniprot.org/uniprotkb/P46098/entry","name":"HTR3A","description":"5-hydroxytryptamine receptor 3A","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2955","complexName":"GABA-B receptor complex","organismName":"Homo sapiens; 9606","description":"G-protein-coupled, metabotropic transmembrane receptor for gamma-aminobutyric acid (GABA), the major inhibitory neurotransmitter in the vertebrate brain. Linked via G-proteins to potassium channels.\r\n\r\nLigand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis. Calcium is required for high affinity binding to GABA. Plays a critical role in the fine-tuning of inhibitory synaptic transmission. Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials. Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception.","predictedComplex":false,"interactors":[{"ac":"EBI-715469","identifier":"O75899","identifierLink":"https://www.uniprot.org/uniprotkb/O75899/entry","name":"GABBR2","description":"Gamma-aminobutyric acid type B receptor subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10519","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724156","identifier":"Q9UBS5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UBS5/entry","name":"GABBR1","description":"Gamma-aminobutyric acid type B receptor subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10519","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2990","complexName":"GABA-B receptor complex","organismName":"Mus musculus; 10090","description":"G-protein-coupled, metabotropic transmembrane receptor for gamma-aminobutyric acid (GABA), the major inhibitory neurotransmitter in the vertebrate brain. Linked via G-proteins to potassium channels.\r\n\r\nLigand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis. Calcium is required for high affinity binding to GABA. Plays a critical role in the fine-tuning of inhibitory synaptic transmission. Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials. Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception.","predictedComplex":false,"interactors":[{"ac":"EBI-770718","identifier":"Q9WV18","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WV18/entry","name":"Gabbr1","description":"Gamma-aminobutyric acid type B receptor subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10519","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-770749","identifier":"Q80T41","identifierLink":"https://www.uniprot.org/uniprotkb/Q80T41/entry","name":"Gabbr2","description":"Gamma-aminobutyric acid type B receptor subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10519","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2176","complexName":"Gamma-secretase complex, APH1A-PSEN1 variant","organismName":"Homo sapiens; 9606","description":"Integral membrane aspartyl protease which performs the intramembrane cleavage of integral membrane proteins such as Notch receptors, clearing the anchors of type-I membrane proteins left in the membrane after shedding of their ectodomain. Cleaves proteins consisting of a single hydrophobic transmembrane helix and with a remaining ectodomain of limited length. Responsible for generating the carboxyl terminus of the amyloid beta-protein (Abeta) from the amyloid protein precursor, APP (P05067).","predictedComplex":false,"interactors":[{"ac":"EBI-21395953","identifier":"P49768-PRO_0000236055","identifierLink":"https://www.uniprot.org/uniprotkb/P49768-PRO_0000236055/entry","name":"PSEN1","description":"Presenilin-1 CTF12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2606326","identifier":"P49768-PRO_0000025591","identifierLink":"https://www.uniprot.org/uniprotkb/P49768-PRO_0000025591/entry","name":"PSEN1","description":"Presenilin-1 NTF subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2606935","identifier":"Q96BI3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96BI3/entry","name":"APH1A","description":"Gamma-secretase subunit APH-1A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12889","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-998440","identifier":"Q92542","identifierLink":"https://www.uniprot.org/uniprotkb/Q92542/entry","name":"NCSTN","description":"Nicastrin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-998468","identifier":"Q9NZ42","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZ42/entry","name":"PSENEN","description":"Gamma-secretase subunit PEN-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16318","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2177","complexName":"GyrA-GyrB DNA Gyrase complex","organismName":"Escherichia coli (strain K12); 83333","description":"A DNA gyrase of type IIA topoisomerase that negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings. It alters DNA topology by effecting a transient double-strand break in the DNA backbone, cleaving both strands and passing the double helix through 3 pairs of N-gates formed by ATPase domains of the gyrB subunit and resealing the gaps.\r\nIt facilitates DNA melting at oriC in order for replication initiation to take place. DNA Gyrase also removes the left-handed positive supercoiling generated in front of moving replication forks. \r\n\r\nStructure-guided deletion of a 170-amino acid insertion (Thr565 - Arg731) in gyrB greatly reduces the DNA binding, supercoiling and DNA-stimulated ATPase activities of gyrase.","predictedComplex":false,"interactors":[{"ac":"EBI-22179735","identifier":"CHEBI:29101","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29101","name":"sodium(1+)","description":"sodium(1+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-541911","identifier":"P0AES6","identifierLink":"https://www.uniprot.org/uniprotkb/P0AES6/entry","name":"gyrB","description":"DNA gyrase subunit B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR45866","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-547129","identifier":"P0AES4","identifierLink":"https://www.uniprot.org/uniprotkb/P0AES4/entry","name":"gyrA","description":"DNA gyrase subunit A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43493","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967750","identifier":"CHEBI:29103","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29103","name":"potassium(1+)","description":"Potassium (1+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2179","complexName":"Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-gamma","organismName":"Homo sapiens; 9606","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron and ultimately producing muscle contractions. Mediates fast, short-lived synaptic transmission of neurotransmitters at the foetal extra-junctional, non-innervated muscle but acts slower than the adult receptor.","predictedComplex":false,"interactors":[{"ac":"EBI-11172448","identifier":"P02708-PRO_0000000305","identifierLink":"https://www.uniprot.org/uniprotkb/P02708-PRO_0000000305/entry","name":"CHRNA1","description":"Acetylcholine receptor subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-11172459","identifier":"P11230-PRO_0000000315","identifierLink":"https://www.uniprot.org/uniprotkb/P11230-PRO_0000000315/entry","name":"CHRNB1","description":"Acetylcholine receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-11172474","identifier":"P07510-PRO_0000000334","identifierLink":"https://www.uniprot.org/uniprotkb/P07510-PRO_0000000334/entry","name":"CHRNG","description":"Acetylcholine receptor subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-9008829","identifier":"Q07001","identifierLink":"https://www.uniprot.org/uniprotkb/Q07001/entry","name":"CHRND","description":"Acetylcholine receptor subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2180","complexName":"Neuronal nicotinic acetylcholine receptor complex, 2xalpha4-3xbeta2","organismName":"Homo sapiens; 9606","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived, mainly pre-synaptic transmission of neurotransmitters. Major receptor in Central Nervous System and predominantly found in cerebellum, cortex, forebrain, hippocampus, mesencephalon, striatum, superior colliculus and thalamus. Up-regulated by pro-inflammatory cytokines, for example TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10899398","identifier":"P43681-PRO_0000000351","identifierLink":"https://www.uniprot.org/uniprotkb/P43681-PRO_0000000351/entry","name":"CHRNA4","description":"Neuronal acetylcholine receptor subunit alpha-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-10899404","identifier":"P17787-PRO_0000000379","identifierLink":"https://www.uniprot.org/uniprotkb/P17787-PRO_0000000379/entry","name":"CHRNB2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-2181","complexName":"Protein farnesyltransferase complex","organismName":"Rattus norvegicus; 10116","description":"Catalyzes the transfer of a 15-carbon lipid, the farnesyl moiety, from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X (CaaX box).\r\n\r\nThe hydrophobic farnesyl moiety aids membrane attachment of the target proteins which include many essential signal transduction proteins, including members of the Ras superfamily. Farnesylation is essential both for normal functioning of these proteins, and for the transforming activity of oncogenic mutants.","predictedComplex":false,"interactors":[{"ac":"EBI-602447","identifier":"Q04631","identifierLink":"https://www.uniprot.org/uniprotkb/Q04631/entry","name":"Fnta","description":"Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-602454","identifier":"Q02293","identifierLink":"https://www.uniprot.org/uniprotkb/Q02293/entry","name":"Fntb","description":"Protein farnesyltransferase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11774","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2182","complexName":"CX3 complex","organismName":"Homo sapiens; 9606","description":"Required for the efficient restart of stalled replication forks. The complex prevents degradation of stalled forks to avoid replication fork collapse and maintain genomic integrity.","predictedComplex":false,"interactors":[{"ac":"EBI-2267048","identifier":"O43502","identifierLink":"https://www.uniprot.org/uniprotkb/O43502/entry","name":"RAD51C","description":"DNA repair protein RAD51 homolog 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2849976","identifier":"O43542","identifierLink":"https://www.uniprot.org/uniprotkb/O43542/entry","name":"XRCC3","description":"DNA repair protein XRCC3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46487","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2183","complexName":"Hydrogen:potassium-exchanging ATPase complex","organismName":"Rattus norvegicus; 10116","description":"Catalyzes the hydrolysis of ATP coupled with the exchange of H+ (outwards) and K+ (inwards) ions across the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-9008893","identifier":"P18598","identifierLink":"https://www.uniprot.org/uniprotkb/P18598/entry","name":"Atp4b","description":"Potassium-transporting ATPase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11523","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008901","identifier":"P09626","identifierLink":"https://www.uniprot.org/uniprotkb/P09626/entry","name":"Atp4a","description":"Potassium-transporting ATPase alpha chain 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR43294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9514326","identifier":"CHEBI:39128","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:39128","name":"magnesium ion","description":"magnesium ion","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2184","complexName":"MIER1 histone deacetylase complex, HDAC1 variant","organismName":"Homo sapiens; 9606","description":"Class I histone deacetylase complex with a role in transcriptional repression, by acting as an epigenetic eraser removing acetyl groups from histone tails. This results in the loss of binding sites for regulatory reader proteins and causes chromatin compaction by restoring the positive charge on histone tails. May act downstream of the Polycomb repressive 2 family of complexes to expand regions of repressed chromatin and may bind and deposit histone octamers onto nucleosome-depleted regions of DNA.","predictedComplex":false,"interactors":[{"ac":"EBI-301834","identifier":"Q13547","identifierLink":"https://www.uniprot.org/uniprotkb/Q13547/entry","name":"HDAC1","description":"Histone deacetylase 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3504940","identifier":"Q8N108","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N108/entry","name":"MIER1","description":"Mesoderm induction early response protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10865","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2185","complexName":"Protein farnesyltransferase complex","organismName":"Mus musculus; 10090","description":"Catalyzes the transfer of a 15-carbon lipid, the farnesyl moiety, from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X (CaaX box).\r\n\r\nThe hydrophobic farnesyl moiety aids membrane attachment of the target proteins which include many essential signal transduction proteins, including members of the Ras superfamily. Farnesylation is essential both for normal functioning of these proteins, and for the transforming activity of oncogenic mutants.","predictedComplex":false,"interactors":[{"ac":"EBI-9008925","identifier":"Q61239","identifierLink":"https://www.uniprot.org/uniprotkb/Q61239/entry","name":"Fnta","description":"Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008934","identifier":"Q8K2I1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K2I1/entry","name":"Fntb","description":"Protein farnesyltransferase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11774","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2186","complexName":"SHU complex","organismName":"Homo sapiens; 9606","description":"Role in the homologous recombination DNA damage repair process and the restart of stalled replication forks. The complex binds to single-stranded DNA and has DNA-dependent ATPase activity.","predictedComplex":false,"interactors":[{"ac":"EBI-11318692","identifier":"Q14159","identifierLink":"https://www.uniprot.org/uniprotkb/Q14159/entry","name":"SPIDR","description":"DNA repair-scaffolding protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR34347","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1175604","identifier":"Q9NTI5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NTI5/entry","name":"PDS5B","description":"Sister chromatid cohesion protein PDS5 homolog B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12663","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5281637","identifier":"Q6NVH7","identifierLink":"https://www.uniprot.org/uniprotkb/Q6NVH7/entry","name":"SWSAP1","description":"ATPase SWSAP1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28653","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5281647","identifier":"Q19AV6","identifierLink":"https://www.uniprot.org/uniprotkb/Q19AV6/entry","name":"ZSWIM7","description":"Zinc finger SWIM domain-containing protein 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28498","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2187","complexName":"Acetylcholine receptor, alpha1-beta1-gamma-delta","organismName":"Tetronarce californica; 7787","description":"A ligand-gated ion channel receptor complex that is sensitive to achetylcholine. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron and ultimately producing muscle contractions. Mediates fast, short-lived synaptic transmission of neurotransmitters.","predictedComplex":false,"interactors":[{"ac":"EBI-11172104","identifier":"P02710-PRO_0000000310","identifierLink":"https://www.uniprot.org/uniprotkb/P02710-PRO_0000000310/entry","name":"CHRNA1","description":"Acetylcholine receptor subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Tetronarce californica; 7787","xrefs":[]},{"ac":"EBI-11172109","identifier":"P02712-PRO_0000000319","identifierLink":"https://www.uniprot.org/uniprotkb/P02712-PRO_0000000319/entry","name":"CHRNB1","description":"Acetylcholine receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Tetronarce californica; 7787","xrefs":[]},{"ac":"EBI-11172114","identifier":"P02718-PRO_0000000326","identifierLink":"https://www.uniprot.org/uniprotkb/P02718-PRO_0000000326/entry","name":"chrnd","description":"Acetylcholine receptor subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Tetronarce californica; 7787","xrefs":[]},{"ac":"EBI-11172119","identifier":"P02714-PRO_0000000338","identifierLink":"https://www.uniprot.org/uniprotkb/P02714-PRO_0000000338/entry","name":"CHRNG","description":"Acetylcholine receptor subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Tetronarce californica; 7787","xrefs":[]}]},{"complexAC":"CPX-2188","complexName":"Amiloride-sensitive sodium channel complex, alpha-beta-gamma","organismName":"Homo sapiens; 9606","description":"Inward cation channel with high sodium selectivity but also permeable to lithium. Activated under low extracellular sodium concentrations and self-inhibited by high extracellular sodium concentrations. Activation is dependent on proteolytic cleavage of alpha and gamma subunits, post-translational modifications (such as glycosylation of beta subunit and palmitoylation) and possibly cyclic nucleotides that lift self-inhibition. Regulated by hormones such as aldosterone and vasopressin and inhibited by the diuretic amiloride. Although the channel activity itself is not voltage-gated, ameloride-sensitivity may be voltage-dependent. Channel gating and conductance are comparatively slow. \r\n\r\nPlays an essential role in electrolyte and blood pressure homeostasis, but also in airway surface liquid (ASL) homeostasis, which is important for proper clearance of mucus and pathogens. Mutations leading to a loss of ASL homeostatis are a trigger for cystic fibrosis. The inward sodium transport may trigger action potentials in neurons by gradually depolarizing membrane potentials. In nephrons may also be activated by shear stress potentially changing the conformation of the bulky extracellular loop or the transmembrane domains and thereby increasing channel opening times. May also play a role in salt and sour taste perception. \r\n\r\nFound in the apical membrane of many epithelial cell types, especially in the Aldosterone Sensitive Distal Nephron (ASDN), kidney, colon, lung and sweat glands but also in heart, liver, pancreas, skeletal muscle and blood leukocytes. Also expressed in vascular endothelia where their mechanical properties and function differ from epithelial sodium channels (ENaCs) in other tissues: vascular endothelia are ‘leaky’, allowing passive sodium transport through the membrane. Here, ENaCs are activated by increased external sodium concentrations that enhances the sodium influx into the cell. May stabilize F-actin through strengthening of the inter-subunits causing swelling or stiffening of endothelia and which can ultimately lead to hypertension.","predictedComplex":false,"interactors":[{"ac":"EBI-2547187","identifier":"P51168","identifierLink":"https://www.uniprot.org/uniprotkb/P51168/entry","name":"SCNN1B","description":"Epithelial sodium channel subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11690","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2547354","identifier":"P51170","identifierLink":"https://www.uniprot.org/uniprotkb/P51170/entry","name":"SCNN1G","description":"Epithelial sodium channel subunit gamma","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11690","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7845444","identifier":"P37088","identifierLink":"https://www.uniprot.org/uniprotkb/P37088/entry","name":"SCNN1A","description":"Epithelial sodium channel subunit alpha","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11690","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2189","complexName":"CGRP receptor complex","organismName":"Homo sapiens; 9606","description":"A transmembrane, G-protein-coupled signalling receptor complex that serves as receptor for calcitonin gene-related peptides (CGRP). CGRPs are produced in both peripheral and central neurons and are one of the most potent peptide vasodilators known. Expressed at trigeminal nerve endings that innervate cerebral blood vessels. RAMP1 is responsible for transporting CALCRL to the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-962878","identifier":"Q16602","identifierLink":"https://www.uniprot.org/uniprotkb/Q16602/entry","name":"CALCRL","description":"Calcitonin gene-related peptide type 1 receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45620","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9635079","identifier":"O60894-PRO_0000030168","identifierLink":"https://www.uniprot.org/uniprotkb/O60894-PRO_0000030168/entry","name":"RAMP1","description":"Receptor activity-modifying protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-3149","complexName":"CGRP receptor complex","organismName":"Mus musculus; 10090","description":"A transmembrane, G-protein-coupled signalling receptor complex that serves as receptor for calcitonin gene-related peptides (CGRP). CGRPs are produced in both peripheral and central neurons and are one of the most potent peptide vasodilators known. They are expressed at trigeminal nerve endings that innervate cerebral blood vessels, and this localization, its vasodilatory effect, and other evidence suggest a direct role of CGRPs in migraine. RAMP1 is responsible for transporting CALCRL to the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-9635261","identifier":"Q9R1W5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R1W5/entry","name":"Calcrl","description":"Calcitonin gene-related peptide type 1 receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45620","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9635301","identifier":"Q9WTJ5-PRO_0000030169","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WTJ5-PRO_0000030169/entry","name":"Ramp1","description":"Receptor activity-modifying protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-2190","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha2-beta4","organismName":"Homo sapiens; 9606","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10950423","identifier":"Q15822-PRO_0000000340","identifierLink":"https://www.uniprot.org/uniprotkb/Q15822-PRO_0000000340/entry","name":"CHRNA2","description":"Neuronal acetylcholine receptor subunit alpha-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-10950454","identifier":"P30926-PRO_0000000389","identifierLink":"https://www.uniprot.org/uniprotkb/P30926-PRO_0000000389/entry","name":"CHRNB4","description":"Neuronal acetylcholine receptor subunit beta-4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-2191","complexName":"Adrenomedullin receptor AM1 complex","organismName":"Homo sapiens; 9606","description":"A transmembrane, G-protein-coupled signalling receptor complex that serves as the adrenomedullin (AM) receptor to control neovascularization and the stabilization of vascular integrity. AM, a polypeptide, belongs to the calcitonin family of peptides. It is produced by vascular smooth muscle cells and endothelial cells and has strong hypotensive and vasodilation activity. RAMP2 is responsible for transporting CALCRL to the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-962878","identifier":"Q16602","identifierLink":"https://www.uniprot.org/uniprotkb/Q16602/entry","name":"CALCRL","description":"Calcitonin gene-related peptide type 1 receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45620","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9635100","identifier":"O60895-PRO_0000030172","identifierLink":"https://www.uniprot.org/uniprotkb/O60895-PRO_0000030172/entry","name":"RAMP2","description":"Receptor activity-modifying protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-3148","complexName":"Adrenomedullin receptor AM2 complex","organismName":"Homo sapiens; 9606","description":"A transmembrane, G-protein-coupled signalling receptor complex that serves as the adrenomedullin (AM) receptor to control neovascularization and the stabilization of vascular integrity. AM, a polypeptide, belongs to the calcitonin family of peptides. It is produced by vascular smooth muscle cells and endothelial cells and has strong hypotensive and vasodilation activity. RAMP3 is responsible for transporting CALCRL to the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-962878","identifier":"Q16602","identifierLink":"https://www.uniprot.org/uniprotkb/Q16602/entry","name":"CALCRL","description":"Calcitonin gene-related peptide type 1 receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45620","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9635180","identifier":"O60896-PRO_0000030176","identifierLink":"https://www.uniprot.org/uniprotkb/O60896-PRO_0000030176/entry","name":"RAMP3","description":"Receptor activity-modifying protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-3150","complexName":"Adrenomedullin receptor AM1 complex","organismName":"Mus musculus; 10090","description":"A transmembrane, G-protein-coupled signalling receptor complex that serves as the adrenomedullin (AM) receptor to control neovascularization and the stabilization of vascular integrity. AM, a polypeptide, belongs to the calcitonin family of peptides. It is produced by vascular smooth muscle cells and endothelial cells and has strong hypotensive and vasodilation activity. RAMP2 is responsible for transporting CALCRL to the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-9635261","identifier":"Q9R1W5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R1W5/entry","name":"Calcrl","description":"Calcitonin gene-related peptide type 1 receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45620","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9635336","identifier":"Q9WUP0-PRO_0000030173","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WUP0-PRO_0000030173/entry","name":"Ramp2","description":"Receptor activity-modifying protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-3151","complexName":"Adrenomedullin receptor AM2 complex","organismName":"Mus musculus; 10090","description":"A transmembrane, G-protein-coupled signalling receptor complex that serves as the adrenomedullin (AM) receptor to control neovascularization and the stabilization of vascular integrity. AM, a polypeptide, belongs to the calcitonin family of peptides. It is produced by vascular smooth muscle cells and endothelial cells and has strong hypotensive and vasodilation activity. RAMP3 is responsible for transporting CALCRL to the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-9635261","identifier":"Q9R1W5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R1W5/entry","name":"Calcrl","description":"Calcitonin gene-related peptide type 1 receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45620","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9635451","identifier":"Q9WUP1-PRO_0000030177","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WUP1-PRO_0000030177/entry","name":"Ramp3","description":"Receptor activity-modifying protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-2192","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta2-beta3","organismName":"Homo sapiens; 9606","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10899404","identifier":"P17787-PRO_0000000379","identifierLink":"https://www.uniprot.org/uniprotkb/P17787-PRO_0000000379/entry","name":"CHRNB2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-10950432","identifier":"P32297-PRO_0000000346","identifierLink":"https://www.uniprot.org/uniprotkb/P32297-PRO_0000000346/entry","name":"CHRNA3","description":"Neuronal acetylcholine receptor subunit alpha-3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-10955378","identifier":"Q05901-PRO_0000000383","identifierLink":"https://www.uniprot.org/uniprotkb/Q05901-PRO_0000000383/entry","name":"CHRNB3","description":"Neuronal acetylcholine receptor subunit beta-3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-10955383","identifier":"Q15825-PRO_0000000360","identifierLink":"https://www.uniprot.org/uniprotkb/Q15825-PRO_0000000360/entry","name":"CHRNA6","description":"Neuronal acetylcholine receptor subunit alpha-6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-2193","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha3-beta2","organismName":"Homo sapiens; 9606","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. Mainly found in autonomic ganglia. Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10899404","identifier":"P17787-PRO_0000000379","identifierLink":"https://www.uniprot.org/uniprotkb/P17787-PRO_0000000379/entry","name":"CHRNB2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-10950432","identifier":"P32297-PRO_0000000346","identifierLink":"https://www.uniprot.org/uniprotkb/P32297-PRO_0000000346/entry","name":"CHRNA3","description":"Neuronal acetylcholine receptor subunit alpha-3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-2194","complexName":"Ribonucleoside-diphosphate reductase RR1 complex, RRM2 variant","organismName":"Homo sapiens; 9606","description":"Catalyzes the reduction of ribonucleotides to the corresponding deoxyribonucleotides, an essential step in the de novo synthesis of monomeric precursors for DNA replication and repair, while reducing either glutaredoxin (P35754/Q9NS18) or thioredoxin (P10599). Supplies nucleotides for DNA replication during G1/S phase. The RRM1 subunit binds 2 Mg2+ ions and RRM2 contains a ferric iron-tyrosyl free radical center. The enzyme is allosterically regulated: stimulated by ATP and inhibited by dATP binding to the activity site on the RRM1 subunit. Possibly suppressed by DNA damage which primarily activates related RRM1-RRM2B complex (CPX-369) during G0/G1 and G2/M transitions. Appears to compensate for missing RRM2B (Q7LG56) subunit.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2339245","identifier":"P31350","identifierLink":"https://www.uniprot.org/uniprotkb/P31350/entry","name":"RRM2","description":"Ribonucleoside-diphosphate reductase subunit M2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23409","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-717006","identifier":"P23921","identifierLink":"https://www.uniprot.org/uniprotkb/P23921/entry","name":"RRM1","description":"Ribonucleoside-diphosphate reductase large subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11573","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2195","complexName":"Hydrogen:potassium-exchanging ATPase complex","organismName":"Sus scrofa; 9823","description":"Catalyzes the hydrolysis of ATP coupled with the exchange of H+ (outwards) and K+ (inwards) ions across the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-8803609","identifier":"P19156","identifierLink":"https://www.uniprot.org/uniprotkb/P19156/entry","name":"ATP4A","description":"Potassium-transporting ATPase alpha chain 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Sus scrofa; 9823","xrefs":[{"identifier":"PTHR43294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9009115","identifier":"P18434","identifierLink":"https://www.uniprot.org/uniprotkb/P18434/entry","name":"ATP4B","description":"Potassium-transporting ATPase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Sus scrofa; 9823","xrefs":[{"identifier":"PTHR11523","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9514326","identifier":"CHEBI:39128","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:39128","name":"magnesium ion","description":"magnesium ion","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2196","complexName":"Polycomb repressive complex 2.1, EZH1-RBBP4-PCL3-PALI1 variant","organismName":"Homo sapiens; 9606","description":"Histone-lysine N-methyltransferase which trimethylates Lys-10  (H3K9me3)  and Lys-28 on histone H3 (H3K27me3)  leading to transcriptional silencing of genes critical for development and stem cell differentiation. Also mediates mono and dimethylation of H3K27. PRC2 is preferably targeted to CpG islands in cells. EZH1-containing PRC2 displays a high binding affinity towards nucleosomes and exhibits chromatin compaction activity.","predictedComplex":false,"interactors":[{"ac":"EBI-1264675","identifier":"Q15022","identifierLink":"https://www.uniprot.org/uniprotkb/Q15022/entry","name":"SUZ12","description":"Polycomb protein SUZ12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22597","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2339674","identifier":"Q5T6S3","identifierLink":"https://www.uniprot.org/uniprotkb/Q5T6S3/entry","name":"PHF19","description":"PHD finger protein 19","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-620823","identifier":"Q09028","identifierLink":"https://www.uniprot.org/uniprotkb/Q09028/entry","name":"RBBP4","description":"Histone-binding protein RBBP4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-746045","identifier":"Q96JN0","identifierLink":"https://www.uniprot.org/uniprotkb/Q96JN0/entry","name":"LCOR","description":"Ligand-dependent corepressor","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21545","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8830732","identifier":"Q92800","identifierLink":"https://www.uniprot.org/uniprotkb/Q92800/entry","name":"EZH1","description":"Histone-lysine N-methyltransferase EZH1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45747","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-923794","identifier":"O75530","identifierLink":"https://www.uniprot.org/uniprotkb/O75530/entry","name":"EED","description":"Polycomb protein EED","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10253","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2197","complexName":"Exodeoxyribonuclease V complex","organismName":"Escherichia coli (strain K12); 83333","description":"An exonuclease complex essential in DNA double-strand break repair by homologous recombination. It catalyzes the unwinding of double-stranded DNA at DNA damage sites and cleaves the resulting single-stranded DNA (through recB activity). This process is ATP-hydrolysis-dependent which is provided by the ATPase activity of recD. The two helicases act with opposite polarity: recB is an SF1A enzyme  with a 3'-5' polarity and recD an SF1B enzyme with a 5'-3' polarity. They cooperate to unwind DNA in a highly processive manner where the DNA gets unwound in the recB-recC interface with the 5' single-stranded (ss)DNA single-strand fed into the recD subunit and the 3'ssDNA remaining in the recB-recC dimer. The nuclease activity of the recB subunit might be regulated by the recD protein.","predictedComplex":false,"interactors":[{"ac":"EBI-556814","identifier":"P08394","identifierLink":"https://www.uniprot.org/uniprotkb/P08394/entry","name":"recB","description":"RecBCD enzyme subunit RecB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11070","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-556823","identifier":"P07648","identifierLink":"https://www.uniprot.org/uniprotkb/P07648/entry","name":"recC","description":"RecBCD enzyme subunit RecC","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30591","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-556830","identifier":"P04993","identifierLink":"https://www.uniprot.org/uniprotkb/P04993/entry","name":"recD","description":"RecBCD enzyme subunit RecD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43788","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2198","complexName":"Polycomb repressive complex 2.1,EZH2-RBBP4-PCL3-PALI1 variant","organismName":"Homo sapiens; 9606","description":"Histone-lysine N-methyltransferase which trimethylates Lys-10  (H3K9me3)  and Lys-28 on histone H3 (H3K27me3)  leading to transcriptional silencing of genes critical for development and stem cell differentiation. Also mediates mono and dimethylation of H3K27. PRC2 is preferably targeted to CpG islands in cells. EZH2, rather than EZH1, appears to be the main PRC2 methyltransferase and is responsible for the deposition of most H3K27me3 marks.","predictedComplex":false,"interactors":[{"ac":"EBI-1264675","identifier":"Q15022","identifierLink":"https://www.uniprot.org/uniprotkb/Q15022/entry","name":"SUZ12","description":"Polycomb protein SUZ12","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22597","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2339674","identifier":"Q5T6S3","identifierLink":"https://www.uniprot.org/uniprotkb/Q5T6S3/entry","name":"PHF19","description":"PHD finger protein 19","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-530054","identifier":"Q15910","identifierLink":"https://www.uniprot.org/uniprotkb/Q15910/entry","name":"EZH2","description":"Histone-lysine N-methyltransferase EZH2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45747","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-620823","identifier":"Q09028","identifierLink":"https://www.uniprot.org/uniprotkb/Q09028/entry","name":"RBBP4","description":"Histone-binding protein RBBP4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-746045","identifier":"Q96JN0","identifierLink":"https://www.uniprot.org/uniprotkb/Q96JN0/entry","name":"LCOR","description":"Ligand-dependent corepressor","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21545","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-923794","identifier":"O75530","identifierLink":"https://www.uniprot.org/uniprotkb/O75530/entry","name":"EED","description":"Polycomb protein EED","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10253","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2200","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha3-beta4","organismName":"Homo sapiens; 9606","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. Found in the central nervous systems brain (cerebellum, habenula, pineal gland, trigeminal nerve, vagus nerve), the peripheral nervous system (autonomic ganglia, ciliary ganglia) and non-neural tissues (adrenal medulla).\r\nUpregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10950432","identifier":"P32297-PRO_0000000346","identifierLink":"https://www.uniprot.org/uniprotkb/P32297-PRO_0000000346/entry","name":"CHRNA3","description":"Neuronal acetylcholine receptor subunit alpha-3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-10950454","identifier":"P30926-PRO_0000000389","identifierLink":"https://www.uniprot.org/uniprotkb/P30926-PRO_0000000389/entry","name":"CHRNB4","description":"Neuronal acetylcholine receptor subunit beta-4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-2201","complexName":"Cyclin-dependent protein kinase 5 holoenzyme complex, p35 variant","organismName":"Homo sapiens; 9606","description":"A proline-directed serine/threonine kinase complex that functions in neuronal activities unrelated to cell-cycle progression, including neuronal migration during the development of the central nervous system, dendritic spine morphogenesis, cortical lamination, fasciculation of axon fibres, synaptic activity, neuronal survival, and neuronal cell death in post-mitotic neurons. Phosphorylates cytoskeletal proteins. Participates in the regulation of the circadian clock by modulating the function of CLOCK protein (O15516). \r\n\r\nUnlike most CDKs, CDK5 is directly activated by the specific activators CDK5R1 (Q15078) and CDK5R2 (Q13319). Although cyclin I (Q14094) appears to be involved in the activation of CDK5 in the anti-apoptotic pathway (PMID:19729834) direct binding assays have yet to be published.\r\n\r\nPredominantly cytoplasmic, in association with plasma membrane. The proteolytic variant p25-CDK5 (CPX-3142) is nuclear.","predictedComplex":false,"interactors":[{"ac":"EBI-1041567","identifier":"Q00535","identifierLink":"https://www.uniprot.org/uniprotkb/Q00535/entry","name":"CDK5","description":"Cyclin-dependent kinase 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-746189","identifier":"Q15078","identifierLink":"https://www.uniprot.org/uniprotkb/Q15078/entry","name":"CDK5R1","description":"Cyclin-dependent kinase 5 activator 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23401","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3141","complexName":"Cyclin-dependent protein kinase 5 holoenzyme complex, p39 variant","organismName":"Homo sapiens; 9606","description":"A proline-directed serine/threonine kinase complex that functions in neuronal activities unrelated to cell-cycle progression, including neuronal migration during the development of the central nervous system, dendritic spine morphogenesis, cortical lamination, fasciculation of axon fibres, synaptic activity, neuronal survival, and neuronal cell death in post-mitotic neurons. Phosphorylates cytoskeletal proteins. Predominantly found at the cytoplasmic side of the plasma membrane. Closely related to CDK5-p35 complex (CPX-2201).\r\n\r\nUnlike most CDKs, CDK5 is directly activated by the specific activators CDK5R1 (Q15078) and CDK5R2 (Q13319). Although cyclin I (Q14094) appears to be involved in the activation of CDK5 in the anti-apoptotic pathway (PMID:19729834) direct binding assays have yet to be published. \r\n\r\nA proteolytic variant p29-CDK5 akin to p25-CDK5 (CPX-3142) may also exist but experimental evidence is scarce.","predictedComplex":false,"interactors":[{"ac":"EBI-1041567","identifier":"Q00535","identifierLink":"https://www.uniprot.org/uniprotkb/Q00535/entry","name":"CDK5","description":"Cyclin-dependent kinase 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7146273","identifier":"Q13319","identifierLink":"https://www.uniprot.org/uniprotkb/Q13319/entry","name":"CDK5R2","description":"Cyclin-dependent kinase 5 activator 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23401","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3142","complexName":"Cyclin-dependent protein kinase 5 holoenzyme complex, p25 variant","organismName":"Homo sapiens; 9606","description":"A proline-directed serine/threonine kinase complex that functions in neuronal activities unrelated to cell-cycle progression, including neuronal migration during the development of the central nervous system, dendritic spine morphogenesis, cortical lamination, fasciculation of axon fibres, synaptic activity, neuronal survival, and neuronal cell death in post-mitotic neurons. Phosphorylates cytoskeletal proteins. Participates in the regulation of the circadian clock by modulating the function of CLOCK protein (O15516).\r\n\r\nUnlike most CDKs, CDK5 is directly activated by the specific activators CDK5R1 (Q15078) and CDK5R2 (Q13319). Although cyclin I (Q14094) appears to be involved in the activation of CDK5 in the anti-apoptotic pathway (PMID:19729834) direct binding assays have yet to be published.\r\n\r\nPredominantly nuclear. The variant p35-CDK5 (CPX-2201) is cytoplasmic, in association with plasma membrane.\r\n\r\nWhether CDK5-p25 is over- or under-expressed in patients with Alzheimer's Disease and possibly other neurodegenerative diseases is unclear as both situations have been observed according to the literature.","predictedComplex":false,"interactors":[{"ac":"EBI-1041567","identifier":"Q00535","identifierLink":"https://www.uniprot.org/uniprotkb/Q00535/entry","name":"CDK5","description":"Cyclin-dependent kinase 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1226571","identifier":"Q15078-PRO_0000004795","identifierLink":"https://www.uniprot.org/uniprotkb/Q15078-PRO_0000004795/entry","name":"CDK5R1","description":"Cyclin-dependent kinase 5 activator 1, p25","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-3143","complexName":"Cyclin-dependent protein kinase 5 holoenzyme complex, p35 variant","organismName":"Mus musculus; 10090","description":"A proline-directed serine/threonine kinase complex that functions in neuronal activities unrelated to cell-cycle progression, including neuronal migration during the development of the central nervous system, dendritic spine morphogenesis, cortical lamination, fasciculation of axon fibres, synaptic activity, neuronal survival, and neuronal cell death in post-mitotic neurons. Phosphorylates cytoskeletal proteins. Participates in the regulation of the circadian clock by modulating the function of CLOCK protein (O08785). \r\nUnlike most CDKs, CDK5 is directly activated by the specific activators CDK5R1 (P61809) and CDK5R2 (O35926). Although cyclin I (Q9Z2V9) appears to be involved in the activation of CDK5 in the anti-apoptotic pathway (PMID:19729834) direct binding assays have yet to be published.\r\n\r\nPredominantly cytoplasmic, in association with plasma membrane. The proteolytic variant p25-CDK5 (CPX-3144) is nuclear.","predictedComplex":false,"interactors":[{"ac":"EBI-6510052","identifier":"P49615","identifierLink":"https://www.uniprot.org/uniprotkb/P49615/entry","name":"Cdk5","description":"Cyclin-dependent kinase 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7840438","identifier":"P61809","identifierLink":"https://www.uniprot.org/uniprotkb/P61809/entry","name":"Cdk5r1","description":"Cyclin-dependent kinase 5 activator 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23401","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3144","complexName":"Cyclin-dependent protein kinase 5 holoenzyme complex, p25 variant","organismName":"Mus musculus; 10090","description":"A proline-directed serine/threonine kinase complex that functions in neuronal activities unrelated to cell-cycle progression, including neuronal migration during the development of the central nervous system, dendritic spine morphogenesis, cortical lamination, fasciculation of axon fibres, synaptic activity, neuronal survival, and neuronal cell death in post-mitotic neurons. Phosphorylates cytoskeletal proteins. Participates in the regulation of the circadian clock by modulating the function of CLOCK protein (O08785).\r\n\r\nUnlike most CDKs, CDK5 is directly activated by the specific activators CDK5R1 (P61809) and CDK5R2 (O35926). Although cyclin I (Q9Z2V9) appears to be involved in the activation of CDK5 in the anti-apoptotic pathway (PMID:19729834) direct binding assays have yet to be published.\r\n\r\nPredominantly nuclear. The variant p35-CDK5 (CPX-3143) is cytoplasmic, in association with plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-6510052","identifier":"P49615","identifierLink":"https://www.uniprot.org/uniprotkb/P49615/entry","name":"Cdk5","description":"Cyclin-dependent kinase 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9633765","identifier":"P61809-PRO_0000004797","identifierLink":"https://www.uniprot.org/uniprotkb/P61809-PRO_0000004797/entry","name":"Cdk5r1","description":"Cyclin-dependent kinase 5 activator 1, p25","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-3145","complexName":"Cyclin-dependent protein kinase 5 holoenzyme complex, p39 variant","organismName":"Mus musculus; 10090","description":"A proline-directed serine/threonine kinase complex that functions in neuronal activities unrelated to cell-cycle progression, including neuronal migration during the development of the central nervous system, dendritic spine morphogenesis, cortical lamination, fasciculation of axon fibres, synaptic activity, neuronal survival, and neuronal cell death in post-mitotic neurons. Phosphorylates cytoskeletal proteins. Predominantly found at the cytoplasmic side of the plasma membrane. Closely related to CDK5-p35 complex (CPX-3143).\r\n\r\nUnlike most CDKs, CDK5 is directly activated by the specific activators CDK5R1 (P61809) and CDK5R2 (O35926). Although cyclin I (Q9Z2V9) appears to be involved in the activation of CDK5 in the anti-apoptotic pathway (PMID:19729834) direct binding assays have yet to be published.\r\n\r\nA proteolytic variant p29-CDK5 akin to p25-CDK5 (CPX-3144) may also exist but experimental evidence is scarce.","predictedComplex":false,"interactors":[{"ac":"EBI-6510052","identifier":"P49615","identifierLink":"https://www.uniprot.org/uniprotkb/P49615/entry","name":"Cdk5","description":"Cyclin-dependent kinase 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8526914","identifier":"O35926","identifierLink":"https://www.uniprot.org/uniprotkb/O35926/entry","name":"Cdk5r2","description":"Cyclin-dependent kinase 5 activator 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23401","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2202","complexName":"NMDA receptor complex, GluN1-GluN2A","organismName":"Homo sapiens; 9606","description":"Voltage-gated ion channel of the ionotrophic glutamate receptor (iGluR) family that is characterised by high calcium permeability and very slow deactivation. Activated by simultaneous binding of glycine to GluN1 and L-glutamate to GluN2. Blocked by physiological concentrations of extracellular magnesium which is released by membrane depolarization. \r\n\r\nPredominantly post-synaptic receptor that mediates mostly the late/slow phase of the majority of the fast excitatory neurotransmission in the mammalian brain where it plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. \r\n\r\nCombinations of different receptor isoforms and their splice variants result in formation of ion channels with distinct spatiotemporal expression patterns and pharmacological and electrophysiological properties. \r\n\r\nReplacement of one or more subunits with GluN3A (Q8TCU5) or GluN3B (O60391) subunits results in relatively Ca2+-impermeable cation channels that are resistant to Mg2+. \r\n\r\nDysfunctional NMDA receptors are implicated in various neurological disorders and injuries including depression, schizophrenia, Alzheimer's and Parkinson's disease, chronic and neuropathic pain, as well as neuronal loss following ischaemia or stroke.","predictedComplex":false,"interactors":[{"ac":"EBI-7249937","identifier":"Q12879","identifierLink":"https://www.uniprot.org/uniprotkb/Q12879/entry","name":"GRIN2A","description":"Glutamate receptor ionotropic, NMDA 2A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-998542","identifier":"Q05586","identifierLink":"https://www.uniprot.org/uniprotkb/Q05586/entry","name":"GRIN1","description":"Glutamate receptor ionotropic, NMDA 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2203","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha4-beta4","organismName":"Homo sapiens; 9606","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10899398","identifier":"P43681-PRO_0000000351","identifierLink":"https://www.uniprot.org/uniprotkb/P43681-PRO_0000000351/entry","name":"CHRNA4","description":"Neuronal acetylcholine receptor subunit alpha-4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-10950454","identifier":"P30926-PRO_0000000389","identifierLink":"https://www.uniprot.org/uniprotkb/P30926-PRO_0000000389/entry","name":"CHRNB4","description":"Neuronal acetylcholine receptor subunit beta-4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-2204","complexName":"Polycomb repressive complex 2.1, EZH2-RBBP4-PCL1-PALI1 variant","organismName":"Homo sapiens; 9606","description":"Histone-lysine N-methyltransferase which trimethylates Lys-10  (H3K9me3)  and Lys-28 on histone H3 (H3K27me3)  leading to transcriptional silencing of genes critical for development and stem cell differentiation. Also mediates mono and dimethylation of H3K27. PRC2 is preferably targeted to CpG islands in cells. 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The C-degron is generally a motif of fewer than ten residues ending with -Ala-Gly, -Trp-Gly or -Pro-Gly and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. Ubiquitinates incompletely synthesized nascent peptide chains from stalled ribosomes","predictedComplex":false,"interactors":[{"ac":"EBI-301231","identifier":"Q15369","identifierLink":"https://www.uniprot.org/uniprotkb/Q15369/entry","name":"ELOC","description":"Elongin-C","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301238","identifier":"Q15370","identifierLink":"https://www.uniprot.org/uniprotkb/Q15370/entry","name":"ELOB","description":"Elongin-B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13248","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3201175","identifier":"Q6PID8","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PID8/entry","name":"KLHDC10","description":"Kelch domain-containing protein 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46428","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456179","identifier":"Q13617","identifierLink":"https://www.uniprot.org/uniprotkb/Q13617/entry","name":"CUL2","description":"Cullin-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2224","complexName":"Larval serum protein complex","organismName":"Drosophila melanogaster; 7227","description":"Storage protein complex which may serve as nutrient reserves to support metamorphosis and reproduction in feeding larvae","predictedComplex":false,"interactors":[{"ac":"EBI-124104","identifier":"P11996","identifierLink":"https://www.uniprot.org/uniprotkb/P11996/entry","name":"Lsp1beta","description":"Larval serum protein 1 beta chain","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11511","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3411786","identifier":"P11995","identifierLink":"https://www.uniprot.org/uniprotkb/P11995/entry","name":"Lsp1alpha","description":"Larval serum protein 1 alpha chain","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11511","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-36945556","identifier":"P11997","identifierLink":"https://www.uniprot.org/uniprotkb/P11997/entry","name":"Lsp1gamma","description":"Larval serum protein 1 gamma chain","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11511","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2225","complexName":"Myosin class V complex, MYO2 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Building block of the class V myosin processive molecular motor involved in a range of organelle-transporting functions, including the transport of vacuoles and mRNA. The myosin heavy chain motor domain mediates the ATP-dependent interaction with the F-actin cytoskeleton. The myosin neck region with the bound light chains acts as a rigid lever arm that amplifies movements within the myosin motor domain into a large mechanical stroke that directionally propels the myosin along the actin filament. Myosin V has a high duty cycle, i.e. remains attached to actin for a large fraction of the mechanochemical cycle due to the slow rate of ADP release, the rate-limiting step in the ATPase cycle. This kinetic adaptation allows myosin V to take multiple steps without dissociating from the actin filament. Myosin V can take large steps of approximately 36nm, a distance equal to the helical repeat of the actin filament allowing Myosin V to walk in a straight line on the actin filament, in a hand-over-hand fashion.","predictedComplex":false,"interactors":[{"ac":"EBI-10988","identifier":"P53141","identifierLink":"https://www.uniprot.org/uniprotkb/P53141/entry","name":"MLC1","description":"Myosin light chain 1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11659","identifier":"P19524","identifierLink":"https://www.uniprot.org/uniprotkb/P19524/entry","name":"MYO2","description":"Myosin-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13140","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3976","identifier":"P06787","identifierLink":"https://www.uniprot.org/uniprotkb/P06787/entry","name":"CMD1","description":"Calmodulin","stochiometry":"minValue: 8, maxValue: 8","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2226","complexName":"KLHDC2-Elongin C-Elongin B E3 ubiquitin ligase complex","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase complex which targets degradation signals (degrons) within the C-termini of substrate proteins in a pathway termed destruction via C-end degrons (DesCEND). The C-degron is generally a motif of fewer than ten residues ending with -Gly-Gly and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. Substrates include early terminated selenoproteins SelK (Q9Y6D0) and SelS (Q9BQE4) and the N-terminal proteolytic product of the USP1 deubiquitinating enzyme (O94782),","predictedComplex":false,"interactors":[{"ac":"EBI-301231","identifier":"Q15369","identifierLink":"https://www.uniprot.org/uniprotkb/Q15369/entry","name":"ELOC","description":"Elongin-C","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301238","identifier":"Q15370","identifierLink":"https://www.uniprot.org/uniprotkb/Q15370/entry","name":"ELOB","description":"Elongin-B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13248","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456179","identifier":"Q13617","identifierLink":"https://www.uniprot.org/uniprotkb/Q13617/entry","name":"CUL2","description":"Cullin-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-715326","identifier":"Q9Y2U9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2U9/entry","name":"KLHDC2","description":"Kelch domain-containing protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46228","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2227","complexName":"SF3B complex","organismName":"Homo sapiens; 9606","description":"Role in pre-mRNA splicing. The SF3B complex is recruited to the 12S U2 small nuclear ribonucleoprotein (snRNP), generating the 15S U2 snRNP. The SF3A complex (CPX-2565) is then incorporated into the snRNP, forming the functional 17S U2 snRNP. As the17S snRNP enters the spliceosome, SF3b6 recognizes the branch site adenosine in pre-mRNA and facilitates an interaction between U2 and the branch point sequence. Once catalytic activation of the spliceosome is primed, the SF3B complex is removed from the branch point through the action of the ATPase DHX16 (O60231) but still binds loosely to U2 within the spliceosome until it finally disassembles from the splicing machinery. The complex may also have additional, non-splicing, roles in the cell.\r\n\r\nMutations in SF3B2 and SF3B4 are associated with Craniofacial microsomia (MIM:164210) and Nager syndrome (MIM:154400), respectively.","predictedComplex":false,"interactors":[{"ac":"EBI-1046261","identifier":"Q9Y3B4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3B4/entry","name":"SF3B6","description":"Splicing factor 3B subunit 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2555365","identifier":"Q7RTV0","identifierLink":"https://www.uniprot.org/uniprotkb/Q7RTV0/entry","name":"PHF5A","description":"PHD finger-like domain-containing protein 5A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13120","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2555428","identifier":"Q9BWJ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BWJ5/entry","name":"SF3B5","description":"Splicing factor 3B subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20978","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-346977","identifier":"Q15393","identifierLink":"https://www.uniprot.org/uniprotkb/Q15393/entry","name":"SF3B3","description":"Splicing factor 3B subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348469","identifier":"Q15427","identifierLink":"https://www.uniprot.org/uniprotkb/Q15427/entry","name":"SF3B4","description":"Splicing factor 3B subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48030","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749111","identifier":"Q13435","identifierLink":"https://www.uniprot.org/uniprotkb/Q13435/entry","name":"SF3B2","description":"Splicing factor 3B subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12785","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-876542","identifier":"O75533","identifierLink":"https://www.uniprot.org/uniprotkb/O75533/entry","name":"SF3B1","description":"Splicing factor 3B subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2228","complexName":"KLHDC3-Elongin C-Elongin B E3 ubiquitin ligase complex","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase complex which targets degradation signals (degrons) within the C-termini of substrate proteins in a pathway termed destruction via C-end degrons (DesCEND). The C-degron is generally a motif of fewer than ten residues ending with  -Arg-(Xaa)n-Arg-Gly, -Arg-(Xaa)n-Lys-Gly, or -Arg-(Xaa)n-Gln-Gly and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. Substrates include the cell cycle regulator CDKN2A (Q8N726).","predictedComplex":false,"interactors":[{"ac":"EBI-1055396","identifier":"Q9BQ90","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BQ90/entry","name":"KLHDC3","description":"Kelch domain-containing protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46461","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301231","identifier":"Q15369","identifierLink":"https://www.uniprot.org/uniprotkb/Q15369/entry","name":"ELOC","description":"Elongin-C","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301238","identifier":"Q15370","identifierLink":"https://www.uniprot.org/uniprotkb/Q15370/entry","name":"ELOB","description":"Elongin-B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13248","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456179","identifier":"Q13617","identifierLink":"https://www.uniprot.org/uniprotkb/Q13617/entry","name":"CUL2","description":"Cullin-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2229","complexName":"PRAME-Elongin C-Elongin B E3 ubiquitin ligase complex","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase complex which targets epigenetically and transcriptionally active promoter regions bound by the CCAAT-binding factor complex (CPX-1956) and probably plays a role in chromatin regulation. PRAME is upregulated by signalling pathways that are activated in response to infection/inflammation and may target bacterial proteins for destruction.","predictedComplex":false,"interactors":[{"ac":"EBI-301231","identifier":"Q15369","identifierLink":"https://www.uniprot.org/uniprotkb/Q15369/entry","name":"ELOC","description":"Elongin-C","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301238","identifier":"Q15370","identifierLink":"https://www.uniprot.org/uniprotkb/Q15370/entry","name":"ELOB","description":"Elongin-B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13248","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348325","identifier":"P78395","identifierLink":"https://www.uniprot.org/uniprotkb/P78395/entry","name":"PRAME","description":"Melanoma antigen preferentially expressed in tumors","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14224","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456179","identifier":"Q13617","identifierLink":"https://www.uniprot.org/uniprotkb/Q13617/entry","name":"CUL2","description":"Cullin-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2230","complexName":"RSF complex","organismName":"Drosophila melanogaster; 7227","description":"A nucleosome remodeling complex that participates in chromatin assembly and facilitates DNA transcription. The RSF1 subunit functions as the histone chaperone through an association with the H3/H4 tetramer and is independent of the histone tails. The histone octamer (composed of H2A, H2B, H3 and H4) is required for the RSF complex to bind DNA. The Iswi subunit provides the energy for the nucleosome spacing activity and is dependent on the histone tails. May play a role in silent chromatin formation by promoting histone H2Av (P08985) replacement.","predictedComplex":false,"interactors":[{"ac":"EBI-181187","identifier":"Q9VID9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VID9/entry","name":"BEST:LD19244","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14296","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-367628","identifier":"Q24368","identifierLink":"https://www.uniprot.org/uniprotkb/Q24368/entry","name":"Iswi","description":"Chromatin-remodeling complex ATPase chain Iswi","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2231","complexName":"MYCN-MAX transcriptional activator complex","organismName":"Homo sapiens; 9606","description":"Proto-oncogenic transcriptional activator recognizing E box hexanucleotides containing the DNA consensus sequence CACGTG within gene promoters. The MYCN-MAX heterodimer upregulates gene transcription by interaction with TATA binding protein (TBP, P20226), which in turn upregulates RNA polymerase transcription of the gene. Role in cellular proliferation and division.","predictedComplex":false,"interactors":[{"ac":"EBI-751711","identifier":"P61244","identifierLink":"https://www.uniprot.org/uniprotkb/P61244/entry","name":"MAX","description":"Protein max","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10328","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-878369","identifier":"P04198","identifierLink":"https://www.uniprot.org/uniprotkb/P04198/entry","name":"MYCN","description":"N-myc proto-oncogene protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45851","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2233","complexName":"Signal peptidase complex","organismName":"Drosophila melanogaster; 7227","description":"Catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. The complex cleaves the signal peptides of most secretory and many membrane proteins as soon as the lumenal domain of the translocating polypeptide is large enough to expose its cleavage site to the enzyme, during the translocation of the protein through the translocon pore into the endoplasmic reticulum.","predictedComplex":false,"interactors":[{"ac":"EBI-1627594","identifier":"Q9VAL0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VAL0/entry","name":"Spase12","description":"Signal peptidase complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13202","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-195856","identifier":"Q9VCA9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VCA9/entry","name":"Spase22-23","description":"Signal peptidase complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12804","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26706129","identifier":"Q9VYY2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VYY2/entry","name":"Spase25","description":"Signal peptidase complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13085","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34605782","identifier":"O97066","identifierLink":"https://www.uniprot.org/uniprotkb/O97066/entry","name":"twr","description":"Signal peptidase complex catalytic subunit SEC11","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10806","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2234","complexName":"Mannose-1-phosphate guanyltransferase complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the reaction of GTP and mannose-1-phosphate to form GDP-mannose and diphosphate. GDP-mannose is required for protein glycosylation and glycophospholipid anchor synthesis and is also the precursor of GDP-fucose, another sugar nucleotide critical for glycosylation. GMPPA acts to maintain mannose homeostasis by sensing the concentration of GDP-mannose and allosterically regulating the enzymatic activity of GMPPB.","predictedComplex":false,"interactors":[{"ac":"EBI-750945","identifier":"Q9Y5P6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5P6/entry","name":"GMPPB","description":"Mannose-1-phosphate guanylyltransferase catalytic subunit beta","stochiometry":"minValue: 8, maxValue: 8","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22572","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-750953","identifier":"Q96IJ6","identifierLink":"https://www.uniprot.org/uniprotkb/Q96IJ6/entry","name":"GMPPA","description":"Mannose-1-phosphate guanylyltransferase regulatory subunit alpha","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22572","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2235","complexName":"Signal recognition particle receptor complex","organismName":"Drosophila melanogaster; 7227","description":"Mediates the co-translational targeting of membrane and secretory proteins. The signal recognition particle (SRP, CPX-2657) binds to 9-12 large hydrophobic residues that constitute the signal sequences of nascent proteins as they emerge from the exit tunnel of the ribosome. The resulting targeting complex, composed of the SRP and the ribosome-nascent chain complex, then docks with the Signal recognition particle receptor.  This interaction catalyzes the GTP-dependent transfer of the nascent chain from SRP to the protein translocation apparatus in the ER membrane. Following GTP hydrolysis, the complex dissociates.","predictedComplex":false,"interactors":[{"ac":"EBI-121637","identifier":"Q9U5L1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9U5L1/entry","name":"SrpRalpha","description":"Signal recognition particle receptor subunit alpha homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR43134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9940803","identifier":"Q9VSN9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VSN9/entry","name":"SrpRbeta","description":"Signal recognition particle receptor subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11485","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2236","complexName":"STRIPAK complex, STRIP1-STRN3 variant","organismName":"Homo sapiens; 9606","description":"Multisubunit protein phosphatase complex which acts as a signaling hub to recruit multiple catalytic and regulatory binding partners  Key negative regulator of the Hippo pathway that controls tissue homeostasis and suppresses tumorigenesis. Recruited to auto-activated STK3/4 (Q13188/Q13043)  via the adaptor protein SLMAP (Q14BN4) to reverse T-loop phosphorylation of these Hippo kinases, limiting their activation through feedback inhibition. Inositol hexakisphosphate acts to sense the cellular phosphate balance and may regulate phosphatase activity by stabilizing STRIP1, enabling STRIPAK assembly.","predictedComplex":false,"interactors":[{"ac":"EBI-1053857","identifier":"Q13033","identifierLink":"https://www.uniprot.org/uniprotkb/Q13033/entry","name":"STRN3","description":"Striatin-3","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15653","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1251377","identifier":"CHEBI:17401","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:17401","name":"myo-inositol hexakisphosphate","description":"myo-inositol hexakisphosphate","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1773588","identifier":"Q5VSL9","identifierLink":"https://www.uniprot.org/uniprotkb/Q5VSL9/entry","name":"STRIP1","description":"Striatin-interacting protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302388","identifier":"P30153","identifierLink":"https://www.uniprot.org/uniprotkb/P30153/entry","name":"PPP2R1A","description":"Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712311","identifier":"P67775","identifierLink":"https://www.uniprot.org/uniprotkb/P67775/entry","name":"PPP2CA","description":"Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-713935","identifier":"Q9Y3A3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3A3/entry","name":"MOB4","description":"MOB-like protein phocein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2237","complexName":"STRIPAK complex","organismName":"Drosophila melanogaster; 7227","description":"Multisubunit protein phosphatase complex with striatin acting as the regulatory subunit. 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SCF-FBXL5 target proteins include the iron regulatory protein IRP2 (P48200). The stability of FBXL5 increases under iron- and oxygen-replete conditions and decreases with iron depletion. This differential stability is mediated by an iron- and oxygen-binding hemerythrin domain (IPR012312) that acts as a ligand-dependent regulatory potentially linking iron sensing via the FBXL5 hemerythrin domain, IRP2 regulation, and cellular responses to maintain mammalian iron homeostasis.","predictedComplex":false,"interactors":[{"ac":"EBI-2692340","identifier":"Q9UKA1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UKA1/entry","name":"FBXL5","description":"F-box/LRR-repeat protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13318","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2240","complexName":"Mitochondrial RNase Z complex","organismName":"Homo sapiens; 9606","description":"Responsible for the 3' endonucleolytic cleavage of precursor tRNAs (pre-tRNAs), catalyzing phosphodiester bond hydrolysis to remove approximately 12 leader nucleotides to yield mature tRNAs. This immediately follows tRNA 5′-processing by the RNase P complex (CPX-6155). Also important for nuclear RNA processing of tRNAs and other non-coding RNAs such as sno-RNAs.","predictedComplex":false,"interactors":[{"ac":"EBI-2107046","identifier":"Q7L0Y3","identifierLink":"https://www.uniprot.org/uniprotkb/Q7L0Y3/entry","name":"TRMT10C","description":"tRNA methyltransferase 10 homolog C","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13563","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25827394","identifier":"CHEBI:10668","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:10668","name":"trna precursor","description":"tRNA precursor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-718223","identifier":"Q9BQ52","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BQ52/entry","name":"ELAC2","description":"Zinc phosphodiesterase ELAC protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-79964","identifier":"Q99714","identifierLink":"https://www.uniprot.org/uniprotkb/Q99714/entry","name":"HSD17B10","description":"3-hydroxyacyl-CoA dehydrogenase type-2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43658","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2241","complexName":"SCF E3 ubiquitin ligase complex, FBXL13 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXL13 target proteins include the centrosomal protein CEP192 (Q8TEP8) which is required for mitotic centrosome maturation, microtubule nucleation and bipolar spindle assembly.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6425502","identifier":"Q8NEE6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NEE6/entry","name":"FBXL13","description":"F-box and leucine-rich repeat protein 13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13318","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2242","complexName":"mlc-EIIB transcriptional regulator complex","organismName":"Escherichia coli (strain K12); 83333","description":"Transcriptional regulation complex that acts to sequester the mlc transcriptional repressor that regulates the expression of proteins that are part of the phosphotransferase system for sugar uptake. In the absence of glucose, ptsG mainly exists in a phosphorylated form and does not bind mlc. When glucose is available, transported glucose takes the glucose-specific enzyme II complex (CPX-5943) forms and transfer the phosphate residue onto its glucose ligand. Dephosphorylated membrane-bound ptsG binds mlc and sequesters it from its target promoters. This leads to increased synthesis of ptsG and other phosphotransferase system proteins required for glucose import and metabolism.","predictedComplex":false,"interactors":[{"ac":"EBI-1116104","identifier":"P50456","identifierLink":"https://www.uniprot.org/uniprotkb/P50456/entry","name":"mlc","description":"DNA-binding transcriptional repressor Mlc","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR18964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-903497","identifier":"P69786","identifierLink":"https://www.uniprot.org/uniprotkb/P69786/entry","name":"ptsG","description":"PTS system glucose-specific EIICB component","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30009","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2243","complexName":"Testis-specific gamma-tubulin ring complex","organismName":"Drosophila melanogaster; 7227","description":"Tissue specific gamma-tubulin complex localized to the testis during spermatogenesis. Required for the nucleation of microtubules, the process in which several tubulin molecules interact to form a microtubule seed. Localised on the centromere.","predictedComplex":false,"interactors":[{"ac":"EBI-178952","identifier":"P23257","identifierLink":"https://www.uniprot.org/uniprotkb/P23257/entry","name":"gammaTub23C","description":"Tubulin gamma-1 chain","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-193456","identifier":"Q9VS91","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VS91/entry","name":"t-Grip84","description":"Gamma-tubulin complex component","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19302","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3433997","identifier":"Q4LDP4","identifierLink":"https://www.uniprot.org/uniprotkb/Q4LDP4/entry","name":"t-Grip91","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19302","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34610365","identifier":"Q8IRA1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IRA1/entry","name":"t-Grip128","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19302","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2571","complexName":"Non-canonical polycomb repressive complex 1.4, RNF2-RYBP variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin-protein ligase that acts as a transcriptional repressor by mediating the monoubiquitination of Lys-119 of histone H2A, compacting chromatin, stalling RNA polymerase II and transcriptionally silencing genes critical for development.","predictedComplex":false,"interactors":[{"ac":"EBI-2341576","identifier":"P35226","identifierLink":"https://www.uniprot.org/uniprotkb/P35226/entry","name":"BMI1","description":"Polycomb complex protein BMI-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10825","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-722416","identifier":"Q99496","identifierLink":"https://www.uniprot.org/uniprotkb/Q99496/entry","name":"RNF2","description":"E3 ubiquitin-protein ligase RING2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752324","identifier":"Q8N488","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N488/entry","name":"RYBP","description":"RING1 and YY1-binding protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12920","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2572","complexName":"Tubulin polyglutamylase complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the formation of polyglutamate side chains of variable lengths on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin.The glutamyl side chain then elongates through the successive addition of glutamate residues to the alpha-carboxyl group of the preceding glutamate. Polyglutamylated microtubules consist of different alpha- and beta-tubulin subunits with varied number of added glutamate residues and regulates the interaction of microtubules with microtubule-associated proteins and molecular motors.","predictedComplex":false,"interactors":[{"ac":"EBI-11328383","identifier":"Q6ZTW0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6ZTW0/entry","name":"TPGS1","description":"Tubulin polyglutamylase complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13324229","identifier":"Q9BSH3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BSH3/entry","name":"NICN1","description":"Nicolin-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20587965","identifier":"O95922","identifierLink":"https://www.uniprot.org/uniprotkb/O95922/entry","name":"TTLL1","description":"Polyglutamylase complex subunit TTLL1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12241","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-748091","identifier":"Q68CL5","identifierLink":"https://www.uniprot.org/uniprotkb/Q68CL5/entry","name":"TPGS2","description":"Tubulin polyglutamylase complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31854","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9477875","identifier":"Q8IUZ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IUZ0/entry","name":"LRRC49","description":"Leucine-rich repeat-containing protein 49","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45973","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2573","complexName":"Separin-securin complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Regulates the metaphase-to-anaphase transition during cell cycle progression, playing a role in control of the metaphase-anaphase transition and anaphase onset. Required for sister chromatid separation and also spindle elongation. 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Its catalytic cysteine attacks the NEDD8~adenylate, producing a covalent thioester-linkage between UBA3 catalytic cysteine and the NEDD8 C-terminus. The thioester-linked NEDD8 will be transferred directly to the E2 UBE2M NEDD8-conjugating enzyme (P61081). Before this transfer, UBA3 binds a second NEDD8 molecule at the adenylation active site. Thus, during the activation cycle, UBA3 binds two NEDD8 molecules, each at a distinct site: the catalytic cysteine via a thioester, and the adenylation active site.","predictedComplex":false,"interactors":[{"ac":"EBI-717567","identifier":"Q8TBC4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TBC4/entry","name":"UBA3","description":"NEDD8-activating enzyme E1 catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-718631","identifier":"Q13564","identifierLink":"https://www.uniprot.org/uniprotkb/Q13564/entry","name":"NAE1","description":"NEDD8-activating enzyme E1 regulatory subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2589","complexName":"Actin-related protein 2/3 complex, Arpc3B variant","organismName":"Drosophila melanogaster; 7227","description":"Assembles branched actin networks capable of generating protrusive force and resisting mechanical deformation by stimulating new filament growth from the side of existing actin filaments associated with regions of the plasma membrane. Purified Arp2/3 complex is inactive but stimulates rapid actin polymerization in the presence of activator proteins, the most potent type being the VCA (Verprolin, cofilin, acidic) domain-containing Wiskott-Aldrich syndrome protein (WASP) family members. The Arp2/3 complex appears to bind VCA and an existing actin filament in a cooperative manner. Upon activation, Arp2 and Arp3 move into the side-by-side arrangement of consecutive actin subunits along the short pitch helical axis of an actin filament, mimicking a filamentous actin dimer and creating a template for new filament assembly. The process appears to be ATP-dependent.","predictedComplex":false,"interactors":[{"ac":"EBI-138385","identifier":"P45888","identifierLink":"https://www.uniprot.org/uniprotkb/P45888/entry","name":"Arp2","description":"Actin-related protein 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-143351","identifier":"Q9VIM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VIM5/entry","name":"Arpc2","description":"Actin-related protein 2/3 complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12058","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-176768","identifier":"P32392","identifierLink":"https://www.uniprot.org/uniprotkb/P32392/entry","name":"Arp3","description":"Actin-related protein 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-177874","identifier":"Q9VX82","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VX82/entry","name":"Arpc3B","description":"Actin-related protein 2/3 complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12391","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-178420","identifier":"Q9VMH2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VMH2/entry","name":"Arpc4","description":"Actin-related protein 2/3 complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22629","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-183402","identifier":"O97182","identifierLink":"https://www.uniprot.org/uniprotkb/O97182/entry","name":"Arpc1","description":"Actin-related protein 2/3 complex subunit","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10709","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-192564","identifier":"Q9VQD8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VQD8/entry","name":"Arpc5","description":"Actin-related protein 2/3 complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2590","complexName":"Polycomb repressive complex 1, Su(Z)2 variant","organismName":"Drosophila melanogaster; 7227","description":"E3 ubiquitin-protein ligase that acts as a transcriptional repressor by mediating the monoubiquitination of Lys-119 of histone H2A (P84051), compacting chromatin, stalling  RNA polymerase II and transcriptionally silencing genes critical for development.","predictedComplex":false,"interactors":[{"ac":"EBI-122709","identifier":"Q9W523","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W523/entry","name":"ph-d","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12247","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-145507","identifier":"Q9VB08","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VB08/entry","name":"Sce","description":"E3 ubiquitin-protein ligase RING1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-177152","identifier":"P26017","identifierLink":"https://www.uniprot.org/uniprotkb/P26017/entry","name":"Pc","description":"Polycomb group protein Pc","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46389","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-300360","identifier":"P39769","identifierLink":"https://www.uniprot.org/uniprotkb/P39769/entry","name":"ph-p","description":"Polyhomeotic-proximal chromatin protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12247","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3431645","identifier":"P25172","identifierLink":"https://www.uniprot.org/uniprotkb/P25172/entry","name":"Su(z)2","description":"Protein suppressor 2 of zeste","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10825","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2591","complexName":"Polycomb repressive complex 2, Pcl variant","organismName":"Drosophila melanogaster; 7227","description":"Histone-lysine N-methyltransferase which trimethylates Lys-10  (H3K9me3)  and Lys-28 on histone H3 (H3K27me3)  leading to transcriptional silencing of genes critical for development.","predictedComplex":false,"interactors":[{"ac":"EBI-112315","identifier":"P42124","identifierLink":"https://www.uniprot.org/uniprotkb/P42124/entry","name":"E(z)","description":"Histone-lysine N-methyltransferase E(z)","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45747","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-300450","identifier":"Q9NJG9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NJG9/entry","name":"Su(z)12","description":"Polycomb protein Su(z)12","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22597","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-430086","identifier":"Q24459","identifierLink":"https://www.uniprot.org/uniprotkb/Q24459/entry","name":"Pcl","description":"Polycomb protein Pcl","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13037","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-75924","identifier":"Q24572","identifierLink":"https://www.uniprot.org/uniprotkb/Q24572/entry","name":"Caf1-55","description":"Chromatin assembly factor 1 p55 subunit","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-88911","identifier":"Q24338","identifierLink":"https://www.uniprot.org/uniprotkb/Q24338/entry","name":"esc","description":"Polycomb protein esc","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10253","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2592","complexName":"Actin-related protein 2/3 complex, ARPC1A-ACTR3-ARPC5L variant","organismName":"Homo sapiens; 9606","description":"Assembles branched actin networks capable of generating protrusive force and resisting mechanical deformation by stimulating new filament growth from the side of existing actin filaments associated with regions of the plasma membrane. Purified Arp2/3 complex is inactive but stimulates rapid actin polymerization in the presence of activator proteins, the most potent type being the VCA (Verprolin, cofilin, acidic) domain-containing Wiskott-Aldrich syndrome protein (WASP) family members. The Arp2/3 complex appears to bind VCA and an existing actin filament in a cooperative manner. Upon activation, ACTR2 and ACTR3 move into the side-by-side arrangement of consecutive actin subunits along the short pitch helical axis of an actin filament, mimicking a filamentous actin dimer and creating a template for new filament assembly.  The process appears to be ATP-dependent.","predictedComplex":false,"interactors":[{"ac":"EBI-1020827","identifier":"Q92747","identifierLink":"https://www.uniprot.org/uniprotkb/Q92747/entry","name":"ARPC1A","description":"Actin-related protein 2/3 complex subunit 1A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10709","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-351428","identifier":"P61158","identifierLink":"https://www.uniprot.org/uniprotkb/P61158/entry","name":"ACTR3","description":"Actin-related protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-351829","identifier":"O15145","identifierLink":"https://www.uniprot.org/uniprotkb/O15145/entry","name":"ARPC3","description":"Actin-related protein 2/3 complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12391","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-351872","identifier":"P59998","identifierLink":"https://www.uniprot.org/uniprotkb/P59998/entry","name":"ARPC4","description":"Actin-related protein 2/3 complex subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22629","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352356","identifier":"O15144","identifierLink":"https://www.uniprot.org/uniprotkb/O15144/entry","name":"ARPC2","description":"Actin-related protein 2/3 complex subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12058","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353580","identifier":"P61160","identifierLink":"https://www.uniprot.org/uniprotkb/P61160/entry","name":"ACTR2","description":"Actin-related protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-711189","identifier":"Q9BPX5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BPX5/entry","name":"ARPC5L","description":"Actin-related protein 2/3 complex subunit 5-like protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2594","complexName":"Polycomb repressive complex 1, RING1-PCGF2-CBX4-PHC1 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin-protein ligase that acts as a transcriptional repressor by mediating the monoubiquitination of Lys-119 of histone H2A, compacting chromatin, stalling RNA polymerase II and transcriptionally silencing genes critical for development.  CBX4 contributes to the maintenance of epithelial identity in the developing epidermis by repressing non-epidermal gene expression programs.","predictedComplex":false,"interactors":[{"ac":"EBI-2129767","identifier":"P35227","identifierLink":"https://www.uniprot.org/uniprotkb/P35227/entry","name":"PCGF2","description":"Polycomb group RING finger protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10825","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-722425","identifier":"O00257","identifierLink":"https://www.uniprot.org/uniprotkb/O00257/entry","name":"CBX4","description":"E3 SUMO-protein ligase CBX4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46727","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-725403","identifier":"P78364","identifierLink":"https://www.uniprot.org/uniprotkb/P78364/entry","name":"PHC1","description":"Polyhomeotic-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12247","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752313","identifier":"Q06587","identifierLink":"https://www.uniprot.org/uniprotkb/Q06587/entry","name":"RING1","description":"E3 ubiquitin-protein ligase RING1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2595","complexName":"Nuclear exosome","organismName":"Drosophila melanogaster; 7227","description":"3' to 5' exo- and endoribonuclease complex that is involved in RNA maturation and degradation which include the removal of unstable and aberrant transcripts and may also regulate the levels of specific transcripts in response to environmental factors. Restricted to processing linear and circular single-stranded RNAs only. RNAs with complex secondary structures, particularly at the 3' end of the molecule, may have to be unwound or pre-processed by cofactors prior to entering the complex. Although some RNAs may be targeted directly to the catalytic subunits, the majority of substrates enter the barrel-like structure of the exosome through a pore at the centre of the cap and are threaded through the central channel in a 3' to 5' orientation. The ribonuclease activity of the catalytic subunits facilitates the degradation process. \r\n\r\nTwo different exosomes exist in yeast, one found in the nucleus and nucleolus (this complex), the other form is lacking the RRP6 subunit and is found in the cytosol (CPX-603).\r\n\r\nThe nuclear/nucleolar RNA exosome is involved in a) proper maturation of most RNA species such as intron-removal from pre-mRNAs and tRNA precursors and rRNA, snRNA, snoRNA, lncRNA and enhancer RNA processing, especially the removal of their 3-prime ends, b) the elimination of RNA processing by-products and non-coding, cryptic transcripts, such as upstream antisense RNA species (uaRNA), enhancer RNAs (eRNAs), heterochromatin-forming repetitive elements (ribosomal DNA repeats and centromeres) and long non-coding RNAs, c) the elimination of mRNAs with processing defects and mRNAs that fail to undergo proper splicing or 3′ end formation and d) gene expression either by mRNA processing or coordination of intron retention leading to regulation of decay of otherwise intact mRNAs. Nuclear exosome activity therefore limits or excludes export of target RNAs to the cytoplasm. Possibly also involved in the degradation of mRNAs with defects in their co-transcriptional packaging into ribonucleoprotein particles (mRNPs), retention of aberrant transcripts on the chromatin and transcription termination or DNA damage repair processes.","predictedComplex":false,"interactors":[{"ac":"EBI-104987","identifier":"Q9VK19","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VK19/entry","name":"Ski6","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-106288","identifier":"Q8IPX7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IPX7/entry","name":"Rrp40","description":"Exosome complex component RRP40","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-115588","identifier":"Q8T4A9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8T4A9/entry","name":"Rrp45","description":"Exosome complex component RRP45","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-123608","identifier":"Q29QQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q29QQ9/entry","name":"Rrp42","description":"Ribosomal RNA-processing protein 42","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-164185","identifier":"Q9VC93","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VC93/entry","name":"Dis3","description":"Exosome complex exonuclease RRP44","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23355","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-166198","identifier":"Q9VGZ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VGZ2/entry","name":"Rrp46","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-178854","identifier":"Q9VKJ4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VKJ4/entry","name":"Csl4","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12686","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-186218","identifier":"Q9W1M9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W1M9/entry","name":"Rrp4","description":"Exosome complex component RRP4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2507849","identifier":"Q9VFF3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VFF3/entry","name":"Rrp6","description":"Exosome complex component 10 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12124","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-92844","identifier":"Q9VW53","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VW53/entry","name":"Mtr3","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2596","complexName":"Cytoplasmic exosome","organismName":"Drosophila melanogaster; 7227","description":"3' to 5' exo- and endoribonuclease complex that is involved in RNA maturation and degradation which include the removal of unstable and aberrant transcripts and may also regulate the levels of specific transcripts in response to environmental factors. Restricted to processing linear and circular single-stranded RNAs only. RNAs with complex secondary structures, particularly at the 3' end of the molecule, may have to be unwound or pre-processed by co-factors prior to entering the complex. Although some RNAs may be targeted directly to the catalytic subunits, the majority of substrates enter the barrel-like structure of the exosome through a pore at the centre of the cap and are threaded through the central channel in a 3' to 5' orientation. The ribonuclease activity of the catalytic subunits facilitates the degradation process. \r\n\r\nTwo different exosomes exist in yeast, one found in the nucleus and nucleolus (this complex), the other form is lacking the RRP6 subunit and is found in the cytosol (CPX-603).\r\n\r\nThe nuclear/nucleolar RNA exosome is involved in a) proper maturation of most RNA species such as intron-removal from pre-mRNAs and tRNA precursors and rRNA, snRNA, snoRNA, lncRNA and enhancer RNA processing, especially the removal of their 3-prime ends, b) the elimination of RNA processing by-products and non-coding, cryptic transcripts, such as upstream antisense RNA species (uaRNA), enhancer RNAs (eRNAs), heterochromatin-forming repetitive elements (ribosomal DNA repeats and centromeres) and long non-coding RNAs, c) the elimination of mRNAs with processing defects and mRNAs that fail to undergo proper splicing or 3′ end formation and d) gene expression either by mRNA processing or coordination of intron retention leading to regulation of decay of otherwise intact mRNAs. Nuclear exosome activity therefore limits or excludes export of target RNAs to the cytoplasm. Possibly also involved in the degradation of mRNAs with defects in their co-transcriptional packaging into ribonucleoprotein particles (mRNPs), retention of aberrant transcripts on the chromatin and transcription termination or DNA damage repair processes.","predictedComplex":false,"interactors":[{"ac":"EBI-104987","identifier":"Q9VK19","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VK19/entry","name":"Ski6","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-106288","identifier":"Q8IPX7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IPX7/entry","name":"Rrp40","description":"Exosome complex component RRP40","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-115588","identifier":"Q8T4A9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8T4A9/entry","name":"Rrp45","description":"Exosome complex component RRP45","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-123608","identifier":"Q29QQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q29QQ9/entry","name":"Rrp42","description":"Ribosomal RNA-processing protein 42","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-164185","identifier":"Q9VC93","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VC93/entry","name":"Dis3","description":"Exosome complex exonuclease RRP44","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23355","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-166198","identifier":"Q9VGZ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VGZ2/entry","name":"Rrp46","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-178854","identifier":"Q9VKJ4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VKJ4/entry","name":"Csl4","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12686","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-186218","identifier":"Q9W1M9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W1M9/entry","name":"Rrp4","description":"Exosome complex component RRP4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-92844","identifier":"Q9VW53","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VW53/entry","name":"Mtr3","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2598","complexName":"Polycomb repressive complex 1, RING1-PCGF2-CBX6-PHC3 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin-protein ligase that acts as a transcriptional repressor by mediating the monoubiquitination of Lys-119 of histone H2A, compacting chromatin, stalling RNA polymerase II and transcriptionally silencing genes. CBX6 is critical for development, balancing embyronic stem cell pluripotency and differentiation, and is recruited to chromatin independently of H3K27me3.","predictedComplex":false,"interactors":[{"ac":"EBI-1223801","identifier":"Q8NDX5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NDX5/entry","name":"PHC3","description":"Polyhomeotic-like protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12247","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2129767","identifier":"P35227","identifierLink":"https://www.uniprot.org/uniprotkb/P35227/entry","name":"PCGF2","description":"Polycomb group RING finger protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10825","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3951758","identifier":"O95503","identifierLink":"https://www.uniprot.org/uniprotkb/O95503/entry","name":"CBX6","description":"Chromobox protein homolog 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46389","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752313","identifier":"Q06587","identifierLink":"https://www.uniprot.org/uniprotkb/Q06587/entry","name":"RING1","description":"E3 ubiquitin-protein ligase RING1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2600","complexName":"Polycomb repressive complex 1, RING1-PCGF2-CBX7-PHC1 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin-protein ligase that acts as a transcriptional repressor by mediating the monoubiquitination of Lys-119 of histone H2A, compacting chromatin, stalling RNA polymerase II and transcriptionally silencing genes. CBX7 plays a role in stem cell self-renewal.","predictedComplex":false,"interactors":[{"ac":"EBI-2129767","identifier":"P35227","identifierLink":"https://www.uniprot.org/uniprotkb/P35227/entry","name":"PCGF2","description":"Polycomb group RING finger protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10825","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3923843","identifier":"O95931","identifierLink":"https://www.uniprot.org/uniprotkb/O95931/entry","name":"CBX7","description":"Chromobox protein homolog 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47277","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-725403","identifier":"P78364","identifierLink":"https://www.uniprot.org/uniprotkb/P78364/entry","name":"PHC1","description":"Polyhomeotic-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12247","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752313","identifier":"Q06587","identifierLink":"https://www.uniprot.org/uniprotkb/Q06587/entry","name":"RING1","description":"E3 ubiquitin-protein ligase RING1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2601","complexName":"Polycomb repressive complex 1, RING1-PCGF2-CBX7-PHC2 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin-protein ligase that acts as a transcriptional repressor by mediating the monoubiquitination of Lys-119 of histone H2A, compacting chromatin, stalling RNA polymerase II and transcriptionally silencing genes. 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9606","xrefs":[{"identifier":"PTHR12247","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752313","identifier":"Q06587","identifierLink":"https://www.uniprot.org/uniprotkb/Q06587/entry","name":"RING1","description":"E3 ubiquitin-protein ligase RING1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2602","complexName":"DNA-directed RNA polymerase I complex","organismName":"Drosophila melanogaster; 7227","description":"Catalyzes the transcription of ribosomal RNA from a DNA template by acting as a nucleotidyl transferase that polymerizes ribonucleotides at the 3' end of an RNA transcript synthesizing precursors of rRNAs.","predictedComplex":false,"interactors":[{"ac":"EBI-136073","identifier":"Q9VMX3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VMX3/entry","name":"Polr1C","description":"DNA-directed RNA polymerases I and III subunit RPAC1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 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Snx3 and Snx6 have been implicated in lysosomal enzyme trafficking in larval fat body cells.","predictedComplex":false,"interactors":[{"ac":"EBI-107274","identifier":"Q9VLQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VLQ9/entry","name":"Snx6","description":"Sorting nexin","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-123075","identifier":"Q9VPX5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VPX5/entry","name":"Vps29","description":"Vacuolar protein sorting-associated protein 29","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11124","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-138059","identifier":"Q9VQQ6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VQQ6/entry","name":"Snx1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10555","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34595473","identifier":"Q9W552","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W552/entry","name":"Vps26","description":"Vacuolar protein sorting-associated protein 26","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12233","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-82500","identifier":"Q9VG51","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VG51/entry","name":"Snx3","description":"Sorting nexin-3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45963","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-98206","identifier":"Q9W277","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W277/entry","name":"Vps35","description":"Vacuolar protein sorting-associated protein 35","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11099","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2612","complexName":"NXF3-NXT2 mRNA nuclear export factor complex","organismName":"Homo sapiens; 9606","description":"Mediates the export of bulk mRNA through direct interactions with both the mRNA cargo and nuclear pore proteins that contain characteristic phenylalanine-glycine repeating sequence motifs (FG-nucleoporins or FG-nups). 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CBX6 is critical for development, balancing embyronic stem cell pluripotency and differentiation, and is recruited to chromatin independently of H3K27me3.","predictedComplex":false,"interactors":[{"ac":"EBI-2129767","identifier":"P35227","identifierLink":"https://www.uniprot.org/uniprotkb/P35227/entry","name":"PCGF2","description":"Polycomb group RING finger protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10825","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3951758","identifier":"O95503","identifierLink":"https://www.uniprot.org/uniprotkb/O95503/entry","name":"CBX6","description":"Chromobox protein homolog 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46389","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-725403","identifier":"P78364","identifierLink":"https://www.uniprot.org/uniprotkb/P78364/entry","name":"PHC1","description":"Polyhomeotic-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12247","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752313","identifier":"Q06587","identifierLink":"https://www.uniprot.org/uniprotkb/Q06587/entry","name":"RING1","description":"E3 ubiquitin-protein ligase RING1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2617","complexName":"Polycomb repressive complex 1, RING1-PCGF2-CBX6-PHC2 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin-protein ligase that acts as a transcriptional repressor by mediating the monoubiquitination of Lys-119 of histone H2A, compacting chromatin, stalling RNA polymerase II and transcriptionally silencing genes. 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CBX7 plays a role in stem cell self-renewal.","predictedComplex":false,"interactors":[{"ac":"EBI-1223801","identifier":"Q8NDX5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NDX5/entry","name":"PHC3","description":"Polyhomeotic-like protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12247","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2129767","identifier":"P35227","identifierLink":"https://www.uniprot.org/uniprotkb/P35227/entry","name":"PCGF2","description":"Polycomb group RING finger protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10825","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3923843","identifier":"O95931","identifierLink":"https://www.uniprot.org/uniprotkb/O95931/entry","name":"CBX7","description":"Chromobox protein homolog 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47277","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752313","identifier":"Q06587","identifierLink":"https://www.uniprot.org/uniprotkb/Q06587/entry","name":"RING1","description":"E3 ubiquitin-protein ligase RING1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2621","complexName":"Polycomb repressive complex 1, RING1-PCGF2-CBX8-PHC1 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin-protein ligase that acts as a transcriptional repressor by mediating the monoubiquitination of Lys-119 of histone H2A, compacting chromatin, stalling RNA polymerase II and transcriptionally silencing genes. 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CBX8 appears to be active during mitosis and interacts with the phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN (P60484).","predictedComplex":false,"interactors":[{"ac":"EBI-2129767","identifier":"P35227","identifierLink":"https://www.uniprot.org/uniprotkb/P35227/entry","name":"PCGF2","description":"Polycomb group RING finger protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10825","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712912","identifier":"Q9HC52","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HC52/entry","name":"CBX8","description":"Chromobox protein homolog 8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46389","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-713786","identifier":"Q8IXK0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IXK0/entry","name":"PHC2","description":"Polyhomeotic-like protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12247","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752313","identifier":"Q06587","identifierLink":"https://www.uniprot.org/uniprotkb/Q06587/entry","name":"RING1","description":"E3 ubiquitin-protein ligase RING1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2623","complexName":"Polycomb repressive complex 1, RING1-PCGF2-CBX8-PHC3 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin-protein ligase that acts as a transcriptional repressor by mediating the monoubiquitination of Lys-119 of histone H2A, compacting chromatin, stalling RNA polymerase II and transcriptionally silencing genes. 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Membrane sequestration of the FLCN-FNIP complex by GABARAP family members uncouples its regulation of RRAGC/RRAGD resulting in impaired substrate-specific mTOR-dependent phosphorylation of transcription factor TFE3 (P19532) and TFEB (P19484) which act as master regulators of lysosomal biogenesis, autophagy, lysosomal exocytosis, lipid catabolism, energy metabolism and immune response.","predictedComplex":false,"interactors":[{"ac":"EBI-2946919","identifier":"Q8TF40","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TF40/entry","name":"FNIP1","description":"Folliculin-interacting protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21634","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2970160","identifier":"Q8NFG4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NFG4/entry","name":"FLCN","description":"Folliculin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31441","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2625","complexName":"DNA-directed RNA polymerase II complex","organismName":"Drosophila melanogaster; 7227","description":"Catalyzes the transcription of RNA from a DNA template by acting as a nucleotidyl transferase that polymerizes ribonucleotides at the 3' end of an RNA transcript. 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Pol II appears to oscillate between inactive and active conformations at each step of nucleotide addition.","predictedComplex":false,"interactors":[{"ac":"EBI-124475","identifier":"Q9VDY6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VDY6/entry","name":"Polr2M","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23171","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-137989","identifier":"P08266","identifierLink":"https://www.uniprot.org/uniprotkb/P08266/entry","name":"Polr2B","description":"DNA-directed RNA polymerase II subunit RPB2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR20856","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-162272","identifier":"O97183","identifierLink":"https://www.uniprot.org/uniprotkb/O97183/entry","name":"Polr2C","description":"DNA-directed RNA polymerase II subunit RPB3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 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-2","xrefs":[]}]},{"complexAC":"CPX-2626","complexName":"Outer dynein arm-docking complex","organismName":"Homo sapiens; 9606","description":"Mediates outer dynein arms (ODA) binding onto the doublet microtubule. The cilial/flagellar axoneme consists of 96nm repeat units, each of which contains four identical outer dynein arms and six unique inner dynein arms arranged in two rows along the length of the A-tubule. The dynein motors walk along the neighboring B-tubule to generate interdoublet sliding, which is transferred into bending by interdoublet linkers that resist the sliding. The Calaxin subunit may act to modulate complex activity depending on Ca2+ concentration and to stabilise its interaction with the doublet microtubule.","predictedComplex":false,"interactors":[{"ac":"EBI-10173858","identifier":"Q96M63","identifierLink":"https://www.uniprot.org/uniprotkb/Q96M63/entry","name":"ODAD1","description":"Outer dynein arm-docking complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21694","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1046387","identifier":"Q96NG3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96NG3/entry","name":"ODAD4","description":"Outer dynein arm-docking complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12200605","identifier":"Q5T2S8","identifierLink":"https://www.uniprot.org/uniprotkb/Q5T2S8/entry","name":"ODAD2","description":"Outer dynein arm-docking complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 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9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3955564","identifier":"Q8NHM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NHM5/entry","name":"KDM2B","description":"Lysine-specific demethylase 2B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23123","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-722416","identifier":"Q99496","identifierLink":"https://www.uniprot.org/uniprotkb/Q99496/entry","name":"RNF2","description":"E3 ubiquitin-protein ligase RING2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749901","identifier":"Q9BSM1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BSM1/entry","name":"PCGF1","description":"Polycomb group RING finger protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10825","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752324","identifier":"Q8N488","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N488/entry","name":"RYBP","description":"RING1 and YY1-binding protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12920","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8833946","identifier":"Q5H9F3","identifierLink":"https://www.uniprot.org/uniprotkb/Q5H9F3/entry","name":"BCORL1","description":"BCL-6 corepressor-like protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2628","complexName":"DNA-directed RNA polymerase III complex","organismName":"Drosophila melanogaster; 7227","description":"Catalyzes the transcription of RNA from an DNA template by acting as a nucleotidyl transferase that polymerizes ribonucleotides at the 3' end of an RNA transcript. Responsible for the transcription of genes encoding short non-coding RNAs, such as tRNA, 5S rRNA and U6 snRNA transcripts. \r\n\r\nPol III machinery recognizes conserved promoter elements located within the transcribed region, generally the box A and box B sequences, which contribute to the  D- and T-loops in the tRNA structure. POLR3F, POLR3G and POLR3C play a role in transcription initiation whereas the POLR3D-POLR3E heterodimer is crucial for the correct recognition of the termination signals of class III genes. POLR3K is required for RNA cleavage. Pol III initiation does not require ATP hydrolysis to open a transcription bubble to isolate and secure the template strand in the catalytic site and Pol III is capable of reinitiating transcription more rapidly on the same gene after the first transcription cycle without being released (facilitated reinitiation), resulting in a higher initiation efficiency; this appears to require an POLR3K-dependent conformational change of Pol III.","predictedComplex":false,"interactors":[{"ac":"EBI-119510","identifier":"Q9VD25","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VD25/entry","name":"Polr3F","description":"DNA-directed RNA polymerase III subunit RPC6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-127243","identifier":"Q9VP85","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VP85/entry","name":"Polr3E","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12069","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-136073","identifier":"Q9VMX3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VMX3/entry","name":"Polr1C","description":"DNA-directed RNA polymerases I and III subunit RPAC1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15135920","identifier":"Q9VX99","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VX99/entry","name":"Polr3I","description":"DNA-directed RNA polymerase III subunit RPC9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15561","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-156773","identifier":"P25167","identifierLink":"https://www.uniprot.org/uniprotkb/P25167/entry","name":"Polr3B","description":"DNA-directed RNA polymerase III subunit RPC2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR20856","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-170383","identifier":"Q8SYM9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8SYM9/entry","name":"Polr3D","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13408","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-171749","identifier":"Q9VC49","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VC49/entry","name":"Polr2L","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23431","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-181962","identifier":"A1ZBX4","identifierLink":"https://www.uniprot.org/uniprotkb/A1ZBX4/entry","name":"Polr3K","description":"DNA-directed RNA polymerase subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-196097","identifier":"Q24320","identifierLink":"https://www.uniprot.org/uniprotkb/Q24320/entry","name":"Polr2F","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR47227","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2108861","identifier":"Q9VTL6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VTL6/entry","name":"Polr3H","description":"DNA-directed RNA polymerase III subunit RPC8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12709","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3406685","identifier":"Q9VG60","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VG60/entry","name":"Polr3C","description":"DNA-directed RNA polymerase III subunit RPC3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12949","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3424132","identifier":"Q86BI8","identifierLink":"https://www.uniprot.org/uniprotkb/Q86BI8/entry","name":"Polr3G","description":"DNA-directed RNA polymerase III subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15367","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34598260","identifier":"Q7JZF5","identifierLink":"https://www.uniprot.org/uniprotkb/Q7JZF5/entry","name":"Polr2E","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10535","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34598313","identifier":"Q9VNZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VNZ3/entry","name":"Polr2H","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10917","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34598358","identifier":"Q6IGE3","identifierLink":"https://www.uniprot.org/uniprotkb/Q6IGE3/entry","name":"Polr2K","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34602429","identifier":"A8JUY3","identifierLink":"https://www.uniprot.org/uniprotkb/A8JUY3/entry","name":"Polr3A","description":"DNA-directed RNA polymerase subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19376","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-89092","identifier":"Q9VIZ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VIZ0/entry","name":"Polr1D","description":"DNA-directed RNA polymerases I and III subunit RPAC2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13946","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2629","complexName":"Ribonuclease MRP complex","organismName":"Drosophila melanogaster; 7227","description":"Essential endoribonuclease  closely related to RNAse P complex. RNAse MRP is involved in the processing of ribosomal RNAs, mitochondrial RNAs and certain messenger RNAs. Processes ribosomal RNA (rRNA) precursors at the A3 site allowing formation of the 5.8S pre-rRNA.  The RNA subunit RMRP is a catalytically active ribozyme that is capable of both recognizing and cleaving substrates.","predictedComplex":false,"interactors":[{"ac":"EBI-114899","identifier":"Q9VSC6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VSC6/entry","name":"Pop4","description":"Ribonuclease P protein subunit p29","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13348","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1151669","identifier":"Q2MGL3","identifierLink":"https://www.uniprot.org/uniprotkb/Q2MGL3/entry","name":"Rpp20","description":"Ribonuclease P protein subunit p20","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15314","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-129910","identifier":"Q9VAA7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VAA7/entry","name":"Rpp14b","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15441","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-137434","identifier":"Q0E9N4","identifierLink":"https://www.uniprot.org/uniprotkb/Q0E9N4/entry","name":"Rpp25","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13516","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-177124","identifier":"Q9VPM0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VPM0/entry","name":"Rpp30","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3403264","identifier":"Q7KVW2","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KVW2/entry","name":"Pop1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22731","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34602780","identifier":"Q9VVE0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVE0/entry","name":"Pop5","description":"Ribonuclease P/MRP protein subunit POP5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR48414","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34602801","identifier":"A8JRG8","identifierLink":"https://www.uniprot.org/uniprotkb/A8JRG8/entry","name":"Rpp14a","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15441","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34602823","identifier":"URS00005704F6_7227","identifierLink":"http://rnacentral.org/rna/URS00005704F6_7227","name":"rmrp_drome_rna","description":"RNA component of mitochondrial RNA processing endoribonuclease","stochiometry":null,"interactorType":"small nucleolar rna","organismName":"Drosophila melanogaster; 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7227","xrefs":[{"identifier":"PTHR13526","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-75557","identifier":"Q9VVR1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVR1/entry","name":"not","description":"Ubiquitin carboxyl-terminal hydrolase nonstop","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21646","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-95967","identifier":"Q9VGE2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VGE2/entry","name":"Spt3","description":"SAGA complex subunit Spt3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11380","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2645","complexName":"DBIRD complex","organismName":"Homo sapiens; 9606","description":"Acts at the interface between messenger ribonucleoprotein particles and RNA polymerase II (RNAPII), integrating transcript elongation with the regulation of alternative splicing. Binds directly to RNAPII.and regulates alternative splicing of a large set of exons embedded in A/T-rich DNA.  May act as an elongation factor, facilitating transcript elongation across A/T-rich regions.","predictedComplex":false,"interactors":[{"ac":"EBI-2560158","identifier":"Q5BKZ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q5BKZ1/entry","name":"ZNF326","description":"DBIRD complex subunit ZNF326","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12190","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355410","identifier":"Q8N163","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N163/entry","name":"CCAR2","description":"Cell cycle and apoptosis regulator protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21237","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2646","complexName":"SCF-SLMB E3 ubiquitin ligase complex","organismName":"Drosophila melanogaster; 7227","description":"E3 ubiquitin ligase that plays a critical role in the pruning of unnecessary axons/dendrites during the development of the nervous system, including both dendrite arborization neurons (ddaC dendrites) and mushroom body γ axons. The complex is believed to act primarily through inactivation of the InR/PI3K/TOR pathway. May also play a role in modulating wnt-signalling through the destruction of beta- catenin. May also regulate the levels of FERM protein Expanded (Q07436), one of the main upstream Hippo signalling regulators, by ubiquitylation which triggers downstream degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-136038","identifier":"Q24311","identifierLink":"https://www.uniprot.org/uniprotkb/Q24311/entry","name":"Cul1","description":"Cullin homolog 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-153139","identifier":"Q9W5E1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W5E1/entry","name":"Roc1a","description":"RING-box protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-180180","identifier":"O77430","identifierLink":"https://www.uniprot.org/uniprotkb/O77430/entry","name":"SkpA","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34604499","identifier":"A0A0B4KHK1","identifierLink":"https://www.uniprot.org/uniprotkb/A0A0B4KHK1/entry","name":"slmb","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR44156","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2647","complexName":"SEC61 translocon complex, SEC61G1 variant","organismName":"Drosophila melanogaster; 7227","description":"Translocates hydrophilic polypeptide segments of newly synthesized proteins across the endoplasmic reticulum membrane and integrates hydrophobic transmembrane segments into the membrane for subsequent transport to other subcellular locations via vesicular trafficking. The complex associates with several other molecular machines and enzymes, such as the ribosome, the SEC62-SEC63 complex, and oligosaccharyltransferase complex  which selectively glycosylates nascent polypeptide chains in the endoplasmic reticulum.","predictedComplex":false,"interactors":[{"ac":"EBI-111134","identifier":"Q8STG9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8STG9/entry","name":"Sec61alpha","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10906","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-165380","identifier":"Q9V668","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V668/entry","name":"SEC61G1","description":"Protein transport protein Sec61 gamma-1 subunit","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12309","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-92490","identifier":"Q7JZN0","identifierLink":"https://www.uniprot.org/uniprotkb/Q7JZN0/entry","name":"Sec61beta","description":"Protein transport protein Sec61 subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13509","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2649","complexName":"PEX2-PEX10-PEX12 E3 ubiquitin ligase complex","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin-ligase complex which forms a retrotranslocation channel required for the export of the PEX5 peroxisomal import -receptor (P50542) from peroxisomes to the cytosol, promoting PEX5 recycling. When receptor recycling is compromised, the receptor is polyubiquitylated by the complex, extracted from the ligase channel by another ATPase, and degraded by the proteasome.","predictedComplex":false,"interactors":[{"ac":"EBI-594789","identifier":"O60683","identifierLink":"https://www.uniprot.org/uniprotkb/O60683/entry","name":"PEX10","description":"Peroxisome biogenesis factor 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23350","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-594836","identifier":"O00623","identifierLink":"https://www.uniprot.org/uniprotkb/O00623/entry","name":"PEX12","description":"Peroxisome assembly protein 12","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-713978","identifier":"P28328","identifierLink":"https://www.uniprot.org/uniprotkb/P28328/entry","name":"PEX2","description":"Peroxisome biogenesis factor 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48178","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2650","complexName":"SEC61 translocon complex, SEC61G2 variant","organismName":"Drosophila melanogaster; 7227","description":"Translocates hydrophilic polypeptide segments of newly synthesized proteins across the endoplasmic reticulum membrane and integrates hydrophobic transmembrane segments into the membrane for subsequent transport to other subcellular locations via vesicular trafficking. The complex associates with several other molecular machines and enzymes, such as the ribosome, the SEC62-SEC63 complex, and oligosaccharyltransferase complex  which selectively glycosylates nascent polypeptide chains in the endoplasmic reticulum.","predictedComplex":false,"interactors":[{"ac":"EBI-111134","identifier":"Q8STG9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8STG9/entry","name":"Sec61alpha","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10906","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26701937","identifier":"Q9VWE9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VWE9/entry","name":"Sec61gamma","description":"Protein transport protein Sec61 gamma-2 subunit","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12309","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-92490","identifier":"Q7JZN0","identifierLink":"https://www.uniprot.org/uniprotkb/Q7JZN0/entry","name":"Sec61beta","description":"Protein transport protein Sec61 subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13509","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2651","complexName":"SMC5-SMC6 SUMO ligase complex, qjt variant","organismName":"Drosophila melanogaster; 7227","description":"SUMO ligase complex with a role in homologous recombination (HR) and replication. Required for chromosome segregation at repetitive sequences.  Localizes to repetitive elements such as the rDNA and telomeres  where is is thought to promote and resolve HR-dependent intermediates using ATP-hydrolysis to symmetrically reel DNA into loops. Also required for telomere maintenance during replication and telomere elongation and for  SUMOylating components of the replisome, such as MCM2 (P49735) and the POLE2 (Q9VRQ7) subunit of the DNA polymerase epsilon complex (CPX-2422), which is important for replication fork progression in the presence of DNA-damaging agents.","predictedComplex":false,"interactors":[{"ac":"EBI-107457","identifier":"Q9VCB8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VCB8/entry","name":"SMC6","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19306","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-116945","identifier":"Q9VKV4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VKV4/entry","name":"Nse4","description":"Non-structural maintenance of chromosomes element 4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR16140","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-127679","identifier":"Q9I7L4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9I7L4/entry","name":"MAGE","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11736","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26795860","identifier":"Q9VMA0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VMA0/entry","name":"Nse1","description":"Non-structural maintenance of chromosomes element 1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR20973","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34605016","identifier":"Q8IPT2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IPT2/entry","name":"SMC5","description":"Structural maintenance of chromosomes protein 5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45916","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3952248","identifier":"Q9VVH7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVH7/entry","name":"qjt","description":"E3 SUMO-protein ligase NSE2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21330","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2652","complexName":"Signal recognition particle","organismName":"Homo sapiens; 9606","description":"A conserved ribonucleoprotein particle, which includes in its structure a small cytoplasmic RNA (scRNA). In co-translational targeting of membrane and secretory proteins, SRP recognizes signal sequences as soon as they emerge from the ribosomal polypeptide exit tunnel and binds to the ribosome-nascent chain complex (RNC), leading to retardation of peptide elongation. The SRP-RNC complex is targeted to the endoplasmic reticulum (ER) membrane by interaction with the SRP receptor (SR, CPX-630). SRP54 recognizes the signal sequence and interacts with the SRP receptor in a GTP-dependent manner. After docking to the membrane, the RNC is transferred to the protein-conducting channel, the translocon, and protein synthesis continues. The SRP-SR complex dissociates from the ribosome and, as a result of GTP hydrolysis, SRP and SR dissociate from each other. The complex may also protect the mRNA transcripts of SRP-dependent proteins from degradation","predictedComplex":false,"interactors":[{"ac":"EBI-1048560","identifier":"Q9UHB9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UHB9/entry","name":"SRP68","description":"Signal recognition particle subunit SRP68","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12860","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1058850","identifier":"O76094","identifierLink":"https://www.uniprot.org/uniprotkb/O76094/entry","name":"SRP72","description":"Signal recognition particle subunit SRP72","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14094","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2680090","identifier":"P09132","identifierLink":"https://www.uniprot.org/uniprotkb/P09132/entry","name":"SRP19","description":"Signal recognition particle 19 kDa protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR17453","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2854176","identifier":"P61011","identifierLink":"https://www.uniprot.org/uniprotkb/P61011/entry","name":"SRP54","description":"Signal recognition particle subunit SRP54","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11564","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34605573","identifier":"URS00000478B7_9606","identifierLink":"http://rnacentral.org/rna/URS00000478B7_9606","name":"rn7sl1_human_rna","description":"RNA component of signal recognition particle 7SL1","stochiometry":null,"interactorType":"signal recognition particle rna","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-350743","identifier":"P49458","identifierLink":"https://www.uniprot.org/uniprotkb/P49458/entry","name":"SRP9","description":"Signal recognition particle 9 kDa protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12834","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353399","identifier":"P37108","identifierLink":"https://www.uniprot.org/uniprotkb/P37108/entry","name":"SRP14","description":"Signal recognition particle 14 kDa protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12013","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2653","complexName":"SNIP1/SkIP associated RNA-processing complex","organismName":"Homo sapiens; 9606","description":"Role in RNA processing and transcription, potentially by controlling mRNA stability. Recruited to both the 3' end of the Cyclin D1 (P24385) gene and to Cyclin D1 RNA and plays a role in Cyclin D1 expression and thus cell proliferation..","predictedComplex":false,"interactors":[{"ac":"EBI-352039","identifier":"Q9Y2W1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2W1/entry","name":"THRAP3","description":"Thyroid hormone receptor-associated protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15268","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-437804","identifier":"Q9NYF8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NYF8/entry","name":"BCLAF1","description":"Bcl-2-associated transcription factor 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15268","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-632715","identifier":"Q13573","identifierLink":"https://www.uniprot.org/uniprotkb/Q13573/entry","name":"SNW1","description":"SNW domain-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12096","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-681904","identifier":"Q9H307","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H307/entry","name":"PNN","description":"Pinin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12707","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749336","identifier":"Q8TAD8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAD8/entry","name":"SNIP1","description":"Smad nuclear-interacting protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23308","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2655","complexName":"SMC5-SMC6 SUMO ligase complex, cerv variant","organismName":"Drosophila melanogaster; 7227","description":"SUMO ligase complex with a role in homologous recombination (HR) and replication. Required for chromosome segregation at repetitive sequences.  Localizes to repetitive elements such as the rDNA and telomeres  where is is thought to promote and resolve HR-dependent intermediates using ATP-hydrolysis to symmetrically reel DNA into loops. Also required for telomere maintenance during replication and telomere elongation and for  SUMOylating components of the replisome, such as MCM2 (P49735) and the POLE2 (Q9VRQ7) subunit of the DNA polymerase epsilon complex (CPX-2422), which is important for replication fork progression in the presence of DNA-damaging agents.","predictedComplex":false,"interactors":[{"ac":"EBI-107457","identifier":"Q9VCB8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VCB8/entry","name":"SMC6","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19306","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-116945","identifier":"Q9VKV4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VKV4/entry","name":"Nse4","description":"Non-structural maintenance of chromosomes element 4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR16140","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-127679","identifier":"Q9I7L4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9I7L4/entry","name":"MAGE","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11736","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15135758","identifier":"Q9VXT3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VXT3/entry","name":"cerv","description":"E3 SUMO-protein ligase NSE2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21330","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26795860","identifier":"Q9VMA0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VMA0/entry","name":"Nse1","description":"Non-structural maintenance of chromosomes element 1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR20973","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34605016","identifier":"Q8IPT2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IPT2/entry","name":"SMC5","description":"Structural maintenance of chromosomes protein 5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45916","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2656","complexName":"Ribosome quality control complex","organismName":"Homo sapiens; 9606","description":"A 60S-ribosomal subunit-associated E3 ubiquitin ligase complex involved in proteasomal mediated degradation of  polypeptides whose translation is stalled on the ribosome. The abnormal stalled ribosome is recognized and ubiquitinated at one or more specific residues by the E3 ubiquitin ligase ZNF598 (Q86UK7) . Ribosome ubiquitination induces subunit dissociation by the RQT complex (CPX-6642). Dissociation of the 40S subunits allows binding of 60S ribosome-nascent chains to NEMF, which recruits the LTN1 E3 ubiquitin ligase. LTN1 ubiquitinates the nascent polypeptide chains, targeting them for degradation. NEMF attaches C-terminal alanyl/threonyl sequences to stalled polypeptides. The ATPase VCP and cofactors UFD1 and NPL4 unfold ubiquitinated polypeptides, then extract the peptidyl-tRNA from the 60S, thereby recruiting it to the 26S proteasome for degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-1044684","identifier":"O94822","identifierLink":"https://www.uniprot.org/uniprotkb/O94822/entry","name":"LTN1","description":"E3 ubiquitin-protein ligase listerin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12389","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10817953","identifier":"CPX-137","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-137","name":"VCP-NPL4-UFD1 AAA ATPase complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-11277056","identifier":"O60524","identifierLink":"https://www.uniprot.org/uniprotkb/O60524/entry","name":"NEMF","description":"Ribosome quality control complex subunit NEMF","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-745182","identifier":"Q9BQ70","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BQ70/entry","name":"TCF25","description":"Ribosome quality control complex subunit TCF25","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2657","complexName":"Signal recognition particle","organismName":"Drosophila melanogaster; 7227","description":"A conserved ribonucleoprotein particle, which includes in its structure a small cytoplasmic RNA (scRNA). In co-translational targeting of membrane and secretory proteins, SRP recognizes signal sequences as soon as they emerge from the ribosomal polypeptide exit tunnel and binds to the ribosome-nascent chain complex (RNC), leading to retardation of peptide elongation. The SRP-RNC complex is targeted to the endoplasmic reticulum (ER) membrane by interaction with the SRP receptor (SR). SRP54 recognizes the signal sequence and interacts with the SRP receptor in a GTP-dependent manner. After docking to the membrane, the RNC is transferred to the protein-conducting channel, the translocon, and protein synthesis continues. The SRP-SR complex dissociates from the ribosome and, as a result of GTP hydrolysis, SRP and SR dissociate from each other. The complex may also protect the mRNA transcripts of SRP-dependent proteins from degradation","predictedComplex":false,"interactors":[{"ac":"EBI-100633","identifier":"Q9VSC1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VSC1/entry","name":"Srp9","description":"Signal recognition particle 9 kDa protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12834","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-140887","identifier":"Q9V3D9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V3D9/entry","name":"Srp54k","description":"Signal recognition particle 54 kDa protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11564","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-189424","identifier":"Q9VSS2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VSS2/entry","name":"Srp68","description":"Signal recognition particle subunit SRP68","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12860","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26706929","identifier":"Q9VDL0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VDL0/entry","name":"Srp14","description":"Signal recognition particle 14 kDa protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12013","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-271530","identifier":"P49963","identifierLink":"https://www.uniprot.org/uniprotkb/P49963/entry","name":"Srp19","description":"Signal recognition particle 19 kDa protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR17453","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34605743","identifier":"URS00005977F9_7227","identifierLink":"http://rnacentral.org/rna/URS00005977F9_7227","name":"7sl_drome_rna","description":"RNA component of signal recognition particle 7SL","stochiometry":null,"interactorType":"signal recognition particle rna","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-85889","identifier":"Q9VDK7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VDK7/entry","name":"Srp72","description":"Signal recognition particle subunit SRP72","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14094","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2658","complexName":"SCF E3 ubiquitin ligase complex, FBXL12 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXL12 assembles atypical ubiquitin chains containing both Lys-48 and Lys-63 linkages. SCF-FBXL12 target proteins include calmodulin kinase I (Q14012), degradation of which triggers G1 arrest by preventing CAMKI-mediated phosphorylation of CDKN1B/p27kip (P46527) and assembly of the G1 phase kinase, Cyclin D1-CDK4 complex (CPX-2010). The complex ubiquitinates CDKN1A/p21 (P38936) which stabilizes this protein.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-719790","identifier":"Q9NXK8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NXK8/entry","name":"FBXL12","description":"F-box/LRR-repeat protein 12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2659","complexName":"POMT1-POMT2 O-mannosyltransferase complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the addition of an O-linked mannose to the hydroxyl group of serines or threonines of proteins such as  the transmembrane protein dystroglycan.(Q14118).","predictedComplex":false,"interactors":[{"ac":"EBI-21504644","identifier":"Q9UKY4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UKY4/entry","name":"POMT2","description":"Protein O-mannosyl-transferase 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2803504","identifier":"Q9Y6A1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6A1/entry","name":"POMT1","description":"Protein O-mannosyl-transferase 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2660","complexName":"DNA-directed RNA polymerase III complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the transcription of RNA from an DNA template by acting as a nucleotidyl transferase that polymerizes ribonucleotides at the 3-prime end of an RNA transcript. Responsible for the transcription of genes encoding small structured RNAs such as tRNAs, the 7 SL lncRNA, spliceosomal U6 snRNA and ribosomal 5S RNA. \r\n\r\nPol III machinery recognizes conserved promoter elements located within the transcribed region, generally the box A and box B sequences, which contribute to the  D- and T-loops in the tRNA structure. RPC34, RPC31 and RPC82 play a role in transcription initiation whereas the RPC37-RPC53 heterodimer is crucial for the correct recognition of the termination signals of class III genes. RPC11 is required for RNA cleavage. Pol III is capable of reinitiating transcription more rapidly on the same gene after the first transcription cycle without being released (facilitated reinitiation), resulting in a higher initiation efficiency; this appears to require an RPC11-dependent conformational change of Pol III. \r\n\r\nThe core complex is believed to assemble in the cytoplasm before being transported to the nucleus.","predictedComplex":false,"interactors":[{"ac":"EBI-15781","identifier":"P20434","identifierLink":"https://www.uniprot.org/uniprotkb/P20434/entry","name":"RPB5","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10535","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15786","identifier":"P20435","identifierLink":"https://www.uniprot.org/uniprotkb/P20435/entry","name":"RPO26","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47227","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15794","identifier":"P20436","identifierLink":"https://www.uniprot.org/uniprotkb/P20436/entry","name":"RPB8","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10917","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15802","identifier":"P22139","identifierLink":"https://www.uniprot.org/uniprotkb/P22139/entry","name":"RPB10","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23431","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15810","identifier":"P04051","identifierLink":"https://www.uniprot.org/uniprotkb/P04051/entry","name":"RPO31","description":"DNA-directed RNA polymerase III subunit RPC1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19376","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15815","identifier":"P22276","identifierLink":"https://www.uniprot.org/uniprotkb/P22276/entry","name":"RET1","description":"DNA-directed RNA polymerase III subunit RPC2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR20856","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15821","identifier":"P32349","identifierLink":"https://www.uniprot.org/uniprotkb/P32349/entry","name":"RPC82","description":"DNA-directed RNA polymerase III subunit RPC3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12949","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15826","identifier":"P25441","identifierLink":"https://www.uniprot.org/uniprotkb/P25441/entry","name":"RPC53","description":"DNA-directed RNA polymerase III subunit RPC4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13408","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15831","identifier":"P07703","identifierLink":"https://www.uniprot.org/uniprotkb/P07703/entry","name":"RPC40","description":"DNA-directed RNA polymerases I and III subunit RPAC1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15835","identifier":"P32910","identifierLink":"https://www.uniprot.org/uniprotkb/P32910/entry","name":"RPC34","description":"DNA-directed RNA polymerase III subunit RPC6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15841","identifier":"P17890","identifierLink":"https://www.uniprot.org/uniprotkb/P17890/entry","name":"RPC31","description":"DNA-directed RNA polymerase III subunit RPC7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15367","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15846","identifier":"P28000","identifierLink":"https://www.uniprot.org/uniprotkb/P28000/entry","name":"RPC19","description":"DNA-directed RNA polymerases I and III subunit RPAC2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13946","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15850","identifier":"P40422","identifierLink":"https://www.uniprot.org/uniprotkb/P40422/entry","name":"RPC10","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15854","identifier":"P35718","identifierLink":"https://www.uniprot.org/uniprotkb/P35718/entry","name":"RPC25","description":"DNA-directed RNA polymerase III subunit RPC8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12709","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15858","identifier":"Q04307","identifierLink":"https://www.uniprot.org/uniprotkb/Q04307/entry","name":"RPC11","description":"DNA-directed RNA polymerase III subunit RPC10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25782","identifier":"P47076","identifierLink":"https://www.uniprot.org/uniprotkb/P47076/entry","name":"RPC17","description":"DNA-directed RNA polymerase III subunit RPC9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15561","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26370","identifier":"P36121","identifierLink":"https://www.uniprot.org/uniprotkb/P36121/entry","name":"RPC37","description":"DNA-directed RNA polymerase III subunit RPC5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 5, maxValue: 5","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2661","complexName":"DNA-directed RNA polymerase II complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Catalyzes the transcription of RNA from a DNA template by acting as a nucleotidyl transferase that polymerizes ribonucleotides at the 3' end of an RNA transcript. Synthesizes precursors of mRNAs, and most snRNA and microRNAs. \r\n\r\nDuring a transcription cycle, Pol II, general transcription factors and the mediator complex assemble as the preinitiation complex (PIC) at the promoter. 11-15 base pairs of DNA surrounding the transcription start site are melted and the single-stranded DNA template strand of the promoter is positioned deeply within the central active site cleft of Pol II to form the open complex. After synthesis of about 30 bases of RNA, Pol II releases its contacts with the core promoter and the rest of the transcription machinery (promoter clearance) and enters the stage of transcription elongation in which it moves on the template as the transcript elongates. Pol II appears to oscillate between inactive and active conformations at each step of nucleotide addition.","predictedComplex":false,"interactors":[{"ac":"EBI-1533422","identifier":"Q09191","identifierLink":"https://www.uniprot.org/uniprotkb/Q09191/entry","name":"rpb5","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10535","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1533481","identifier":"Q92399","identifierLink":"https://www.uniprot.org/uniprotkb/Q92399/entry","name":"rpb8","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10917","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1533501","identifier":"P87123","identifierLink":"https://www.uniprot.org/uniprotkb/P87123/entry","name":"rpb11","description":"DNA-directed RNA polymerase II subunit RPB11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13946","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1533514","identifier":"P48011","identifierLink":"https://www.uniprot.org/uniprotkb/P48011/entry","name":"rpc10","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1533685","identifier":"P36595","identifierLink":"https://www.uniprot.org/uniprotkb/P36595/entry","name":"rpb6","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR47227","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1534105","identifier":"O13877","identifierLink":"https://www.uniprot.org/uniprotkb/O13877/entry","name":"rpb10","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23431","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-608029","identifier":"O14459","identifierLink":"https://www.uniprot.org/uniprotkb/O14459/entry","name":"rpb7","description":"DNA-directed RNA polymerase II subunit rpb7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12709","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-697198","identifier":"P37382","identifierLink":"https://www.uniprot.org/uniprotkb/P37382/entry","name":"rpb3","description":"DNA-directed RNA polymerase II subunit RPB3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-697212","identifier":"P36594","identifierLink":"https://www.uniprot.org/uniprotkb/P36594/entry","name":"rpb1","description":"DNA-directed RNA polymerase II subunit rpb1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR19376","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-697230","identifier":"Q02061","identifierLink":"https://www.uniprot.org/uniprotkb/Q02061/entry","name":"rpb2","description":"DNA-directed RNA polymerase II subunit RPB2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR20856","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-697320","identifier":"O74825","identifierLink":"https://www.uniprot.org/uniprotkb/O74825/entry","name":"rpb4","description":"DNA-directed RNA polymerase II subunit rpb4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR21297","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9022426","identifier":"O74635","identifierLink":"https://www.uniprot.org/uniprotkb/O74635/entry","name":"rpb9","description":"DNA-directed RNA polymerase II subunit RPB9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 3, maxValue: 3","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2663","complexName":"Actin-related protein 2/3 complex, ARPC1B-ACTR3-ARPC5L variant","organismName":"Homo sapiens; 9606","description":"Assembles branched actin networks capable of generating protrusive force and resisting mechanical deformation by stimulating new filament growth from the side of existing actin filaments associated with regions of the plasma membrane. Purified Arp2/3 complex is inactive but stimulates rapid actin polymerization in the presence of activator proteins, the most potent type being the VCA (Verprolin, cofilin, acidic) domain-containing Wiskott-Aldrich syndrome protein (WASP) family members. The Arp2/3 complex appears to bind VCA and an existing actin filament in a cooperative manner. Upon activation, ACTR2 and ACTR3 move into the side-by-side arrangement of consecutive actin subunits along the short pitch helical axis of an actin filament, mimicking a filamentous actin dimer and creating a template for new filament assembly. The process appears to be ATP-dependent.","predictedComplex":false,"interactors":[{"ac":"EBI-1044647","identifier":"O15143","identifierLink":"https://www.uniprot.org/uniprotkb/O15143/entry","name":"ARPC1B","description":"Actin-related protein 2/3 complex subunit 1B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10709","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-351428","identifier":"P61158","identifierLink":"https://www.uniprot.org/uniprotkb/P61158/entry","name":"ACTR3","description":"Actin-related protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-351829","identifier":"O15145","identifierLink":"https://www.uniprot.org/uniprotkb/O15145/entry","name":"ARPC3","description":"Actin-related protein 2/3 complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12391","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-351872","identifier":"P59998","identifierLink":"https://www.uniprot.org/uniprotkb/P59998/entry","name":"ARPC4","description":"Actin-related protein 2/3 complex subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22629","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352356","identifier":"O15144","identifierLink":"https://www.uniprot.org/uniprotkb/O15144/entry","name":"ARPC2","description":"Actin-related protein 2/3 complex subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12058","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353580","identifier":"P61160","identifierLink":"https://www.uniprot.org/uniprotkb/P61160/entry","name":"ACTR2","description":"Actin-related protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-711189","identifier":"Q9BPX5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BPX5/entry","name":"ARPC5L","description":"Actin-related protein 2/3 complex subunit 5-like protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2664","complexName":"GATOR2 complex","organismName":"Drosophila melanogaster; 7227","description":"Functions as an activator of the amino acid-sensing branch of the mTORC1 pathway. Indirectly activates mTORC1 through the inhibition of the Rag GTPase activating protein activity GATOR1 complex (CPX-2781).","predictedComplex":false,"interactors":[{"ac":"EBI-118041","identifier":"Q7K2X8","identifierLink":"https://www.uniprot.org/uniprotkb/Q7K2X8/entry","name":"Nup44A","description":"Nucleoporin seh1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11024","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-169056","identifier":"Q9V3J4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V3J4/entry","name":"Sec13","description":"Protein SEC13 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11024","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30879913","identifier":"Q9VKK2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VKK2/entry","name":"Wdr59","description":"GATOR2 complex protein Wdr59","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46170","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3407214","identifier":"Q9XZ25","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XZ25/entry","name":"Wdr24","description":"GATOR2 complex protein Wdr24","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46200","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3418826","identifier":"Q9VQ89","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VQ89/entry","name":"mio","description":"GATOR2 complex protein Mio","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR16453","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2665","complexName":"CASTOR1 arginine-sensing complex","organismName":"Homo sapiens; 9606","description":"Binds arginine, leading to the disruption of the interaction between CASTOR1 and the GATOR2 complex (CPX-6227), allowing GATOR2 to plays its role as a positive regulator of the mTORC1 pathway. In the absence of arginine, interacts with GATOR2 to negatively regulate mTORC1 activity.","predictedComplex":false,"interactors":[{"ac":"EBI-10276168","identifier":"Q8WTX7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WTX7/entry","name":"CASTOR1","description":"Cytosolic arginine sensor for mTORC1 subunit 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2666","complexName":"Eukaryotic translation initiation factor 4F, EIF4A1 and EIF4G1 variant","organismName":"Homo sapiens; 9606","description":"Eukaryotic translation initiation factor 4F (eIF4F) consists of three subunits, eIF4A, eIF4E, and eIF4G. Cap-dependent translation initiation commences with the binding of the cap structure (m7GTP) found at the 5 prime end of mRNA to eIF4E subunit. The eIF4F complex then loads mRNAs onto the 40S ribosomal subunit together with eIF3.\r\nSubunit eIF4A is an ATP-dependent RNA helicase involved in cap recognition and is required for mRNA binding to ribosome. eIF4G subunit serves as a scaffold for eIF4A and eIF4E subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-73440","identifier":"P06730","identifierLink":"https://www.uniprot.org/uniprotkb/P06730/entry","name":"EIF4E","description":"Eukaryotic translation initiation factor 4E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-73449","identifier":"P60842","identifierLink":"https://www.uniprot.org/uniprotkb/P60842/entry","name":"EIF4A1","description":"Eukaryotic initiation factor 4A-I","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-73711","identifier":"Q04637","identifierLink":"https://www.uniprot.org/uniprotkb/Q04637/entry","name":"EIF4G1","description":"Eukaryotic translation initiation factor 4 gamma 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23253","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2667","complexName":"CASTOR1-CASTOR2 arginine binding complex","organismName":"Homo sapiens; 9606","description":"Interacts with GATOR2 to negatively regulate mTORC1 activity. Binding of arginine to CASTOR1, leads to the disruption of the interaction between CASTOR1 and the GATOR2 complex (CPX-6227), allowing GATOR2 to plays its role as a positive regulator of the mTORC1 pathway. CASTOR2 constitutively associates with GATOR2 and does not bind arginine.","predictedComplex":false,"interactors":[{"ac":"EBI-10276168","identifier":"Q8WTX7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WTX7/entry","name":"CASTOR1","description":"Cytosolic arginine sensor for mTORC1 subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11102839","identifier":"A6NHX0","identifierLink":"https://www.uniprot.org/uniprotkb/A6NHX0/entry","name":"CASTOR2","description":"Cytosolic arginine sensor for mTORC1 subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2668","complexName":"Actin-related protein 2/3 complex, ARPC1B-ACTR3B-ARPC5L variant","organismName":"Homo sapiens; 9606","description":"Assembles branched actin networks capable of generating protrusive force and resisting mechanical deformation by stimulating new filament growth from the side of existing actin filaments associated with regions of the plasma membrane. Purified Arp2/3 complex is inactive but stimulates rapid actin polymerization in the presence of activator proteins, the most potent type being the VCA (Verprolin, cofilin, acidic) domain-containing Wiskott-Aldrich syndrome protein (WASP) family members. The Arp2/3 complex appears to bind VCA and an existing actin filament in a cooperative manner. Upon activation, ACTR2 and ACTR3B move into the side-by-side arrangement of consecutive actin subunits along the short pitch helical axis of an actin filament, mimicking a filamentous actin dimer and creating a template for new filament assembly. The process appears to be ATP-dependent.","predictedComplex":false,"interactors":[{"ac":"EBI-1020827","identifier":"Q92747","identifierLink":"https://www.uniprot.org/uniprotkb/Q92747/entry","name":"ARPC1A","description":"Actin-related protein 2/3 complex subunit 1A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10709","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1047175","identifier":"Q9P1U1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P1U1/entry","name":"ACTR3B","description":"Actin-related protein 3B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-351829","identifier":"O15145","identifierLink":"https://www.uniprot.org/uniprotkb/O15145/entry","name":"ARPC3","description":"Actin-related protein 2/3 complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12391","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-351872","identifier":"P59998","identifierLink":"https://www.uniprot.org/uniprotkb/P59998/entry","name":"ARPC4","description":"Actin-related protein 2/3 complex subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22629","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352356","identifier":"O15144","identifierLink":"https://www.uniprot.org/uniprotkb/O15144/entry","name":"ARPC2","description":"Actin-related protein 2/3 complex subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12058","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353580","identifier":"P61160","identifierLink":"https://www.uniprot.org/uniprotkb/P61160/entry","name":"ACTR2","description":"Actin-related protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-711189","identifier":"Q9BPX5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BPX5/entry","name":"ARPC5L","description":"Actin-related protein 2/3 complex subunit 5-like protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2669","complexName":"XPC complex, RAD23B variant","organismName":"Homo sapiens; 9606","description":"A nucleotide-excision repair complex that is involved in damage sensing during global genome nucleotide excision repair. Acts as a DNA-binding damage sensor which rapidly screens duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex. Recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix including single-stranded loops, mismatched bubbles or single-stranded overhangs.","predictedComplex":false,"interactors":[{"ac":"EBI-1789926","identifier":"P41208","identifierLink":"https://www.uniprot.org/uniprotkb/P41208/entry","name":"CETN2","description":"Centrin-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372610","identifier":"Q01831","identifierLink":"https://www.uniprot.org/uniprotkb/Q01831/entry","name":"XPC","description":"DNA repair protein complementing XP-C cells","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12135","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-954531","identifier":"P54727","identifierLink":"https://www.uniprot.org/uniprotkb/P54727/entry","name":"RAD23B","description":"UV excision repair protein RAD23 homolog B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10621","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2670","complexName":"GINS complex","organismName":"Drosophila melanogaster; 7227","description":"Required for the initiation of replication and for replication fork progression, mediating interactions with replication factors. Binds to and enhances the enzymatic function of the MCM helicase (CPX-2942) during the initiation and elongation stages of replication. Core component of the replicative helicase CMG complex that serves as the replicative helicase unwinding duplex DNA ahead of moving replication fork during chromosome duplication.","predictedComplex":false,"interactors":[{"ac":"EBI-124971","identifier":"Q9VBI1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VBI1/entry","name":"Sld5","description":"DNA replication complex GINS protein SLD5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21206","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-133591","identifier":"Q9VQY9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VQY9/entry","name":"Psf2","description":"Probable DNA replication complex GINS protein PSF2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12772","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15589005","identifier":"Q9W2V7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W2V7/entry","name":"Psf3","description":"DNA replication complex GINS protein PSF3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22768","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-170577","identifier":"Q9W0I7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W0I7/entry","name":"Psf1","description":"DNA replication complex GINS protein PSF1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12914","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2671","complexName":"CMG helicase complex","organismName":"Drosophila melanogaster; 7227","description":"DNA helicase that unwinds or rearranges duplex DNA during replication, recombination and repair.\r\n\r\nSurrounds the leading strand during DNA replication and recruits the DNA polymerase epsilon complex (CPX-2422) for leading-strand synthesis. CDC45 adds the GINS complex (CPX-2670) onto each MCM complex (CPX-2942) to form two active CMG helicases that surround each strand of parental DNA. CMG then translocates along single-strand DNA in the 3-prime to 5-prime direction for bidirectional replication.The complex unwinds duplex regions up to 500 bp.","predictedComplex":false,"interactors":[{"ac":"EBI-156880","identifier":"O96989","identifierLink":"https://www.uniprot.org/uniprotkb/O96989/entry","name":"Cdc45","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10507","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9022874","identifier":"CPX-2670","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-2670","name":"GINS complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-913696","identifier":"CPX-2942","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-2942","name":"MCM complex","description":"MCM2-7 heterohexomer","stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Drosophila melanogaster; 7227","xrefs":[]}]},{"complexAC":"CPX-2672","complexName":"XPC complex, RAD23A variant","organismName":"Homo sapiens; 9606","description":"A nucleotide-excision repair complex that is involved in damage sensing during global genome nucleotide excision repair. Acts as a DNA-binding damage sensor which rapidly screens duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex. Recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix including single-stranded loops, mismatched bubbles or single-stranded overhangs.","predictedComplex":false,"interactors":[{"ac":"EBI-1789926","identifier":"P41208","identifierLink":"https://www.uniprot.org/uniprotkb/P41208/entry","name":"CETN2","description":"Centrin-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372610","identifier":"Q01831","identifierLink":"https://www.uniprot.org/uniprotkb/Q01831/entry","name":"XPC","description":"DNA repair protein complementing XP-C cells","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12135","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-746453","identifier":"P54725","identifierLink":"https://www.uniprot.org/uniprotkb/P54725/entry","name":"RAD23A","description":"UV excision repair protein RAD23 homolog A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10621","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2673","complexName":"Gamma-secretase complex","organismName":"Drosophila melanogaster; 7227","description":"Integral membrane aspartyl protease which performs the intramembrane cleavage of integral membrane proteins such as Notch receptors, clearing the anchors of type-I membrane proteins left in the membrane after shedding of their ectodomain. Cleaves proteins consisting of a single hydrophobic transmembrane helix and with a remaining ectodomain of limited length.","predictedComplex":false,"interactors":[{"ac":"EBI-129812","identifier":"Q9VQG2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VQG2/entry","name":"aph-1","description":"Gamma-secretase subunit Aph-1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12889","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-154347","identifier":"Q86BE9","identifierLink":"https://www.uniprot.org/uniprotkb/Q86BE9/entry","name":"pen-2","description":"Gamma-secretase subunit pen-2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR16318","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-170442","identifier":"Q9VC27","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VC27/entry","name":"Nct","description":"Nicastrin","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-255741","identifier":"O02194","identifierLink":"https://www.uniprot.org/uniprotkb/O02194/entry","name":"Psn","description":"Presenilin homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10202","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2674","complexName":"M-Calpain complex","organismName":"Homo sapiens; 9606","description":"A calcium-dependent protease complex that processes the substrate by limited proteolysis rather than degrading it. In some cases the proteolytic action activates the substrate, for example, it cleaves CDK5R1/p35 (Q15078) into its p25 form that is associated with Alzheimer's disease. Involved in cytoskeletal remodeling, signal transduction and implicated in cell cycle regulation and apoptosis. Finely-balanced calpain homeostasis is required as both over and under-activation causes disease. Calpain complexes recognise their substrates based on a short peptide sequence. Inhibited by the intrinsically-unstructured calpastatin (P20810) by its tight binding to the calpain catalytic subunit.","predictedComplex":false,"interactors":[{"ac":"EBI-1028956","identifier":"P17655","identifierLink":"https://www.uniprot.org/uniprotkb/P17655/entry","name":"CAPN2","description":"Calpain-2 catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10183","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-711828","identifier":"P04632","identifierLink":"https://www.uniprot.org/uniprotkb/P04632/entry","name":"CAPNS1","description":"Calpain small subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46735","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2675","complexName":"Box H/ACA ribonucleoprotein complex","organismName":"Drosophila melanogaster; 7227","description":"Pseudouridine synthesis complex that converts uridine into pseudouridine at numerous specific sites within ribosomal RNAs (rRNAs) and spliceosomal small nuclear RNAs (snRNAs), isomerizing the uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine residues may serve to stabilize the conformation of rRNAs.","predictedComplex":false,"interactors":[{"ac":"EBI-181635","identifier":"Q7KVQ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KVQ0/entry","name":"Gar1","description":"H/ACA ribonucleoprotein complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23237","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-187697","identifier":"Q9V3U2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V3U2/entry","name":"NHP2","description":"H/ACA ribonucleoprotein complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-188550","identifier":"Q9V5P6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V5P6/entry","name":"Nop10","description":"H/ACA ribonucleoprotein complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-99635","identifier":"O44081","identifierLink":"https://www.uniprot.org/uniprotkb/O44081/entry","name":"Nop60B","description":"H/ACA ribonucleoprotein complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23127","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2676","complexName":"Glycosylphosphatidylinsitol ethanolamine-phosphate transferase II complex","organismName":"Drosophila melanogaster; 7227","description":"Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. Transfers ethanolamine phosphate to the 6-position of the GPI second mannose in Man-Man-Man-(EtNP)Man-GlcN-(acyl)PI, sequentially following the addition of a phosphoethanolamine moiety to the third mannose by GPI-ET-III complex (CPX-2695).","predictedComplex":false,"interactors":[{"ac":"EBI-168856","identifier":"A1Z705","identifierLink":"https://www.uniprot.org/uniprotkb/A1Z705/entry","name":"PIG-G","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23072","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31434232","identifier":"Q9VW21","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VW21/entry","name":"PIG-F","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR43157","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2677","complexName":"Glycosylphosphatidylinsitol ethanolamine-phosphate transferase II complex","organismName":"Homo sapiens; 9606","description":"Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. Transfers ethanolamine phosphate to the 6-position of the GPI second mannose in Man-Man-Man-(EtNP)Man-GlcN-(acyl)PI, sequentially following the addition of a phosphoethanolamine moiety to the third mannose by GPI-ET-III complex (CPX-2679).","predictedComplex":false,"interactors":[{"ac":"EBI-11724298","identifier":"Q5H8A4","identifierLink":"https://www.uniprot.org/uniprotkb/Q5H8A4/entry","name":"PIGG","description":"GPI ethanolamine phosphate transferase 2, catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23072","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17180304","identifier":"Q07326","identifierLink":"https://www.uniprot.org/uniprotkb/Q07326/entry","name":"PIGF","description":"GPI ethanolamine phosphate transferase, stabilizing subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43157","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2678","complexName":"Glycosylphosphatidylinsitol ethanolamine-phosphate transferase II complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. Transfers ethanolamine phosphate to the 6-position of the GPI second mannose in Man-Man-Man-(EtNP)Man-GlcN-(acyl)PI, sequentially following the addition of a phosphoethanolamine moiety to the third mannose by GPI-ET-III complex (CPX-2680).","predictedComplex":false,"interactors":[{"ac":"EBI-2061439","identifier":"Q06636","identifierLink":"https://www.uniprot.org/uniprotkb/Q06636/entry","name":"GPI11","description":"Glycosylphosphatidylinositol anchor biosynthesis protein 11","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43157","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25898","identifier":"P40367","identifierLink":"https://www.uniprot.org/uniprotkb/P40367/entry","name":"LAS21","description":"GPI ethanolamine phosphate transferase 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23072","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2679","complexName":"Glycosylphosphatidylinsitol ethanolamine-phosphate transferase III complex","organismName":"Homo sapiens; 9606","description":"Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. Transfers ethanolamine phosphate to the 6-position of the GPI third mannose in Man-Man-Man-(EtNP)Man-GlcN-(acyl)PI, sequentially followed by the addition of a phosphoethanolamine moiety to the second mannose by the GPI-ET-II (CPX-2677).","predictedComplex":false,"interactors":[{"ac":"EBI-11722765","identifier":"Q8TEQ8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TEQ8/entry","name":"PIGO","description":"GPI ethanolamine phosphate transferase 3, catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23071","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17180304","identifier":"Q07326","identifierLink":"https://www.uniprot.org/uniprotkb/Q07326/entry","name":"PIGF","description":"GPI ethanolamine phosphate transferase, stabilizing subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43157","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2680","complexName":"Glycosylphosphatidylinsitol ethanolamine-phosphate transferase III complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. Transfers ethanolamine phosphate to the 6-position of the GPI third mannose in Man-Man-Man-(EtNP)Man-GlcN-(acyl)PI, sequentially followed by the addition of a phosphoethanolamine moiety to the second mannose by the GPI-ET-II complex (CPX-2678).","predictedComplex":false,"interactors":[{"ac":"EBI-2061439","identifier":"Q06636","identifierLink":"https://www.uniprot.org/uniprotkb/Q06636/entry","name":"GPI11","description":"Glycosylphosphatidylinositol anchor biosynthesis protein 11","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43157","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32339","identifier":"Q07830","identifierLink":"https://www.uniprot.org/uniprotkb/Q07830/entry","name":"GPI13","description":"GPI ethanolamine phosphate transferase 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23071","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2683","complexName":"SCF E3 ubiquitin ligase complex, FBXL7 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXL7 target proteins include AURKA (O14965), required for normal spindle positioning during mitosis, BIRC5 (O15392), a component of the chromosome passage protein complex (CPX-116) which is essential for chromosome alignment and segregation during mitosis and cytokinesis and the SNAI1 (O95863) transcription factor. Ubiquitinates MYC (P01106) when phosphorylated at Thr-58 and Ser-62. May play a role in the regulation of apoptosis.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-914660","identifier":"Q9UJT9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UJT9/entry","name":"FBXL7","description":"F-box/LRR-repeat protein 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13318","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2685","complexName":"Glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex","organismName":"Drosophila melanogaster; 7227","description":"Monoglycosyltransferase complex that catalyses the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to the 6-position of phosphatidylinositol, the first, and committed, step of glycosylphosphatidylinositol (GPI) biosynthesis. GPI is a complex glycolipid with a core structure, phosphoethanolamine-6-mannose-alpha1,2-mannose-alpha1,6-mannose-alpha1,4-glucosamine-alpha1,6-inositol-phospholipid that functions as a membrane anchor for many cell surface proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-32710110","identifier":"A0A2U8U156","identifierLink":"https://www.uniprot.org/uniprotkb/A0A2U8U156/entry","name":"PIG-C","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12982","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32710124","identifier":"Q9VHX6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VHX6/entry","name":"PIG-H","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15231","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32710140","identifier":"Q8MSE4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8MSE4/entry","name":"PIG-P","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32710157","identifier":"Q8IR17","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IR17/entry","name":"PIG-Q","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21329","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3414229","identifier":"Q7JUM3","identifierLink":"https://www.uniprot.org/uniprotkb/Q7JUM3/entry","name":"PIG-A","description":"phosphatidylinositol N-acetylglucosaminyltransferase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45871","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2686","complexName":"Glycosylphosphatidylinositol-mannosyltransferase I complex","organismName":"Drosophila melanogaster; 7227","description":"Mannosyltransferase complex responsible for the transfer of the first mannose to the glycosylphosphatidylinositol (GPI) during GPI precursor assembly. GPI is a complex glycolipid with a core structure, phosphoethanolamine-6-mannose-alpha1,2-mannose-alpha1,6-mannose-alpha1,4-glucosamine-alpha1,6-inositol-phospholipid that functions as a membrane anchor for many cell surface proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-183668","identifier":"Q9W2E4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W2E4/entry","name":"PIG-M","description":"GPI alpha-1,4-mannosyltransferase I, catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32710198","identifier":"A0A0B4LES9","identifierLink":"https://www.uniprot.org/uniprotkb/A0A0B4LES9/entry","name":"PIG-X","description":"Phosphatidylinositol-glycan biosynthesis class X protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR28650","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2687","complexName":"GPI-anchor transamidase complex","organismName":"Drosophila melanogaster; 7227","description":"Transamidase enzyme complex that transfers the glycosylphosphatidylinositol (GPI) lipid to the newly made GPI protein in the endoplasmic reticulum, replacing the C-terminal GPI attachment signal peptide of a protein with the lipid. GPI is a complex glycolipid with a core structure, phosphoethanolamine-6-mannose-alpha1,2-mannose-alpha1,6-mannose-alpha1,4-glucosamine-alpha1,6-inositol-phospholipid that functions as a membrane anchor for many cell surface proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-184745","identifier":"Q9W3G0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W3G0/entry","name":"PIG-T","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12959","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32710331","identifier":"Q8T4E1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8T4E1/entry","name":"PIG-K","description":"Putative GPI-anchor transamidase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR48067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32710347","identifier":"Q9VC10","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VC10/entry","name":"PIG-S","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21072","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32710370","identifier":"Q9VLK0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VLK0/entry","name":"PIG-U","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13121","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3425229","identifier":"Q9W464","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W464/entry","name":"GAA1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2688","complexName":"UTP-B complex","organismName":"Homo sapiens; 9606","description":"Required for early co-transcriptional events in ribosome biogenesis, acting as an RNA chaperone to initiate ribosome assembly. May facilitate specific U3 snoRNA-5'-external transcribed spacer (ETS) base-pairing with PWP2 bridging the interaction site. A sub-unit of the small subunit (SSU) processome, a 2.2 MDa ribonucleoprotein complex involved in the processing, assembly and maturation of nascent pre-ribosomal RNA to form the small ribosomal subunit. The SSU processome is a giant particle composed of numerous ribosome assembly factors, including the UTP-A (CPX-2450), UTP-B,  and MPP10 (CPX-2478) complexes, the U3 small nucleolar ribonucleoprotein (snoRNP) and many individual proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-2512413","identifier":"Q8NI36","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NI36/entry","name":"WDR36","description":"WD repeat-containing protein 36","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22840","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-592816","identifier":"Q9Y5J1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5J1/entry","name":"UTP18","description":"U3 small nucleolar RNA-associated protein 18 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18359","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-715766","identifier":"Q12788","identifierLink":"https://www.uniprot.org/uniprotkb/Q12788/entry","name":"TBL3","description":"Transducin beta-like protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19854","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-722224","identifier":"Q15269","identifierLink":"https://www.uniprot.org/uniprotkb/Q15269/entry","name":"PWP2","description":"Periodic tryptophan protein 2 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19858","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727436","identifier":"Q9UNX4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UNX4/entry","name":"WDR3","description":"WD repeat-containing protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19853","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749211","identifier":"Q9NYH9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NYH9/entry","name":"UTP6","description":"U3 small nucleolar RNA-associated protein 6 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23271","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2691","complexName":"Hypoxia-inducible transcription factor complex","organismName":"Drosophila melanogaster; 7227","description":"A basic helix-loop-helix-PER-ARNT-SIM (bHLH-PAS) family transcription factor complex composed of a constitutively expressed HIF-beta subunit and an oxygen-regulated HIF-alpha subunit which mediates hypoxia-dependent transcription.  Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element  of target gene promoters. HIF-dependent transcription is activated by insulin and mediated by the PI3K-AKT and TOR pathways.","predictedComplex":false,"interactors":[{"ac":"EBI-151300","identifier":"Q24167","identifierLink":"https://www.uniprot.org/uniprotkb/Q24167/entry","name":"sima","description":"Protein similar","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23043","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-172695","identifier":"O15945","identifierLink":"https://www.uniprot.org/uniprotkb/O15945/entry","name":"tgo","description":"Aryl hydrocarbon receptor nuclear translocator homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23042","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2692","complexName":"pre-mRNA cleavage factor IIm complex","organismName":"Homo sapiens; 9606","description":"Required for the activation of the mRNA cleavage and polyadenylation specificity factor complex (CPX-2698), an endonuclease responsible for the 3' end processing of most mRNAs.The cleavage of PSFC additionally requires the cleavage stimulatory factor (CPX-2701/CPX-2703) and RBBP6 (Q7Z6E9),","predictedComplex":false,"interactors":[{"ac":"EBI-2559809","identifier":"O94913","identifierLink":"https://www.uniprot.org/uniprotkb/O94913/entry","name":"PCF11","description":"Pre-mRNA cleavage complex 2 protein Pcf11","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15921","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2559831","identifier":"Q92989","identifierLink":"https://www.uniprot.org/uniprotkb/Q92989/entry","name":"CLP1","description":"Polyribonucleotide 5'-hydroxyl-kinase Clp1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12755","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2693","complexName":"INO80 chromatin remodeling complex","organismName":"Drosophila melanogaster; 7227","description":"ATP-dependent nucleosome remodeling complex which slides mononucleosomes to a central position on a DNA template while tightly organizing nucleosomes within arrays. Functions in maintaining genome stability and removes H2AZ from nucleosomes. May play a largely repressive role in gene transcription, blocking H3K79 methylation and restricting transcription to gene units in euchromatin and away from silent regions, such as heterochromatin. Activates the expression of pluripotency factors by facilitating the recruitment of Mediator and Pol II at their promoters. Required for fork maintenance and progression in stalled replication forks. It is recruited to DNA damage sites.","predictedComplex":false,"interactors":[{"ac":"EBI-125201","identifier":"Q8ST83","identifierLink":"https://www.uniprot.org/uniprotkb/Q8ST83/entry","name":"pho","description":"Polycomb protein PHO","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14003","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-128490","identifier":"Q9VX09","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VX09/entry","name":"Arp8","description":"Actin-related protein 8","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-130188","identifier":"P10987","identifierLink":"https://www.uniprot.org/uniprotkb/P10987/entry","name":"Act5C","description":"Actin-5C","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-168170","identifier":"Q9VZJ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VZJ3/entry","name":"Rcd5","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13233","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-192924","identifier":"Q9V3K3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V3K3/entry","name":"rept","description":"RuvB-like helicase 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-234957","identifier":"Q9VH07","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VH07/entry","name":"pont","description":"RuvB-like helicase 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3414232","identifier":"Q9VDY1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VDY1/entry","name":"Ino80","description":"Chromatin-remodeling ATPase INO80","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45685","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-85467","identifier":"Q9VEC3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VEC3/entry","name":"Arp5","description":"Actin-related protein 5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2694","complexName":"Histone pre-RNA core cleavage complex","organismName":"Homo sapiens; 9606","description":"Endonuclease complex required for processing of mRNA precursors in a U7 snRNP (U7 machinery) for replication-dependent histone pre-mRNAs which are cleaved at the 3' end but not polyadenylated. The cleavage reaction depends on U7 snRNP complex (CPX-2705) and on CASP8AP2 (Q9UKL3). The 5' end of U7 snRNA recognizes histone pre-mRNAs by base pairing with the histone downstream element located 3' of the cleavage site.","predictedComplex":false,"interactors":[{"ac":"EBI-1043224","identifier":"Q9P2I0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P2I0/entry","name":"CPSF2","description":"Cleavage and polyadenylation specificity factor subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45922","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1044699","identifier":"Q9UKF6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UKF6/entry","name":"CPSF3","description":"Cleavage and polyadenylation specificity factor subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11203","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1051992","identifier":"Q92797","identifierLink":"https://www.uniprot.org/uniprotkb/Q92797/entry","name":"SYMPK","description":"Symplekin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15245","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-711360","identifier":"P33240","identifierLink":"https://www.uniprot.org/uniprotkb/P33240/entry","name":"CSTF2","description":"Cleavage stimulation factor subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45735","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2695","complexName":"Glycosylphosphatidylinsitol ethanolamine-phosphate transferase III complex","organismName":"Drosophila melanogaster; 7227","description":"Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol (GPI)-anchor biosynthesis. Transfers ethanolamine phosphate to the 6-position of the GPI third mannose in Man-Man-Man-(EtNP)Man-GlcN-(acyl)PI, sequentially followed by the addition of a phosphoethanolamine moiety to the second mannose by the GPI-ET-II complex (CPX-2676).","predictedComplex":false,"interactors":[{"ac":"EBI-31434232","identifier":"Q9VW21","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VW21/entry","name":"PIG-F","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR43157","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31573795","identifier":"A1ZB84","identifierLink":"https://www.uniprot.org/uniprotkb/A1ZB84/entry","name":"PIG-O","description":"GPI ethanolamine phosphate transferase 3, catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23071","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2697","complexName":"Glycosylphosphatidylinositol-mannosyltransferase I complex","organismName":"Homo sapiens; 9606","description":"Mannosyltransferase complex responsible for the transfer of the first mannose to the glycosylphosphatidylinositol (GPI) during GPI precursor assembly. GPI is a complex glycolipid with a core structure, phosphoethanolamine-6-mannose-alpha1,2-mannose-alpha1,6-mannose-alpha1,4-glucosamine-alpha1,6-inositol-phospholipid that functions as a membrane anchor for many cell surface proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-25585044","identifier":"Q8TBF5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TBF5/entry","name":"PIGX","description":"GPI alpha-1,4-mannosyltransferase I, stabilizing subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28650","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3915702","identifier":"Q9H3S5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H3S5/entry","name":"PIGM","description":"GPI alpha-1,4-mannosyltransferase I, catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1788","complexName":"Thrombospondin 2 complex","organismName":"Homo sapiens; 9606","description":"Secreted glycoprotein that functions during the tissue remodeling that is associated with development, wound healing, synaptogenesis, angiogenesis, and cancer. Through its interactions with proteins and proteoglycans, such as glycosaminoglycans, low density lipoprotein receptor-related protein-1, various integrins, calreticulin, and fibrinogen, TSP-2 functions at the interface of the cell membrane and the extracellular matrix to regulate matrix structure and cellular behaviour.","predictedComplex":false,"interactors":[{"ac":"EBI-2466249","identifier":"P35442","identifierLink":"https://www.uniprot.org/uniprotkb/P35442/entry","name":"THBS2","description":"Thrombospondin-2","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10199","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3023","complexName":"Thrombospondin 2 complex","organismName":"Mus musculus; 10090","description":"Secreted glycoprotein that functions during the tissue remodeling that is associated with development, wound healing, synaptogenesis, angiogenesis, and cancer. Through its interactions with proteins and proteoglycans, such as glycosaminoglycans, low density lipoprotein receptor-related protein-1, various integrins, calreticulin, and fibrinogen, TSP-2 functions at the interface of the cell membrane and the extracellular matrix to regulate matrix structure and cellular behaviour.","predictedComplex":false,"interactors":[{"ac":"EBI-4567830","identifier":"Q03350","identifierLink":"https://www.uniprot.org/uniprotkb/Q03350/entry","name":"Thbs2","description":"Thrombospondin-2","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10199","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1789","complexName":"Thrombospondin 3 complex","organismName":"Homo sapiens; 9606","description":"Secreted glycoprotein that functions during the tissue remodeling that is associated with development, wound healing, synaptogenesis, angiogenesis, and cancer. Through its interactions with proteins and proteoglycans, such as glycosaminoglycans, low density lipoprotein receptor-related protein-1, various integrins, calreticulin, and fibrinogen, TSP-3 functions at the interface of the cell membrane and the extracellular matrix to regulate matrix structure and cellular behaviour.","predictedComplex":false,"interactors":[{"ac":"EBI-2530931","identifier":"P49746","identifierLink":"https://www.uniprot.org/uniprotkb/P49746/entry","name":"THBS3","description":"Thrombospondin-3","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10199","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3024","complexName":"Thrombospondin 3 complex","organismName":"Mus musculus; 10090","description":"Secreted glycoprotein that functions during the tissue remodeling that is associated with development, wound healing, synaptogenesis, angiogenesis, and cancer. Through its interactions with proteins and proteoglycans, such as glycosaminoglycans, low density lipoprotein receptor-related protein-1, various integrins, calreticulin, and fibrinogen, TSP-3 functions at the interface of the cell membrane and the extracellular matrix to regulate matrix structure and cellular behaviour.","predictedComplex":false,"interactors":[{"ac":"EBI-9251426","identifier":"Q05895","identifierLink":"https://www.uniprot.org/uniprotkb/Q05895/entry","name":"Thbs3","description":"Thrombospondin-3","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10199","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1790","complexName":"Thrombospondin 4 complex","organismName":"Homo sapiens; 9606","description":"Secreted glycoprotein that functions during the tissue remodeling that is associated with development, wound healing, synaptogenesis, angiogenesis, and cancer. Through its interactions with proteins and proteoglycans, such as glycosaminoglycans, low density lipoprotein receptor-related protein-1, various integrins, calreticulin, and fibrinogen, TSP-4 functions at the interface of the cell membrane and the extracellular matrix to regulate matrix structure and cellular behaviour.","predictedComplex":false,"interactors":[{"ac":"EBI-2530989","identifier":"P35443","identifierLink":"https://www.uniprot.org/uniprotkb/P35443/entry","name":"THBS4","description":"Thrombospondin-4","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10199","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3025","complexName":"Thrombospondin 4 complex","organismName":"Mus musculus; 10090","description":"Secreted glycoprotein that functions during the tissue remodeling that is associated with development, wound healing, synaptogenesis, angiogenesis, and cancer. Through its interactions with proteins and proteoglycans, such as glycosaminoglycans, low density lipoprotein receptor-related protein-1, various integrins, calreticulin, and fibrinogen, TSP-4 functions at the interface of the cell membrane and the extracellular matrix to regulate matrix structure and cellular behaviour.","predictedComplex":false,"interactors":[{"ac":"EBI-6171531","identifier":"Q9Z1T2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z1T2/entry","name":"Thbs4","description":"Thrombospondin-4","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10199","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1791","complexName":"Thrombospondin 5 complex","organismName":"Homo sapiens; 9606","description":"Secreted glycoprotein that functions through its interactions with proteins and proteoglycans, such as collagens, various integrins and fibronectin. May play a role in the structural integrity of cartilage. Acts to stimulate collagen fibrillogenesis, interacting with free collagen I and II molecules, bringing multiple molecules into close proximity, to promote further assembly.","predictedComplex":false,"interactors":[{"ac":"EBI-2531022","identifier":"P49747","identifierLink":"https://www.uniprot.org/uniprotkb/P49747/entry","name":"COMP","description":"Cartilage oligomeric matrix protein","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10199","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3026","complexName":"Thrombospondin 5 complex","organismName":"Mus musculus; 10090","description":"Secreted glycoprotein that functions through its interactions with proteins and proteoglycans, such as collagens, various integrins and fibronectin. May play a role in the structural integrity of cartilage. Acts to stimulate collagen fibrillogenesis, interacting with free collagen I and II molecules, bringing multiple molecules into close proximity, to promote further assembly.","predictedComplex":false,"interactors":[{"ac":"EBI-9028018","identifier":"Q9R0G6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R0G6/entry","name":"Comp","description":"Cartilage oligomeric matrix protein","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10199","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1793","complexName":"TREX complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Couples transcription elongation by RNA polymerase II to mRNA export. Associates with the polymerase and travels with it along the length of the transcribed gene. TREX is composed of the THO transcription elongation complex (CPX-1792) as well as other proteins that couple THO to mRNA export proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-10841","identifier":"P33441","identifierLink":"https://www.uniprot.org/uniprotkb/P33441/entry","name":"MFT1","description":"THO complex subunit MFT1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-15475","identifier":"P53552","identifierLink":"https://www.uniprot.org/uniprotkb/P53552/entry","name":"THO2","description":"THO complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21597","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18500","identifier":"Q07478","identifierLink":"https://www.uniprot.org/uniprotkb/Q07478/entry","name":"SUB2","description":"ATP-dependent RNA helicase SUB2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47958","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29234","identifier":"P53851","identifierLink":"https://www.uniprot.org/uniprotkb/P53851/entry","name":"TEX1","description":"Protein TEX1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22839","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29516","identifier":"Q12159","identifierLink":"https://www.uniprot.org/uniprotkb/Q12159/entry","name":"YRA1","description":"RNA annealing protein YRA1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19965","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30898","identifier":"O13539","identifierLink":"https://www.uniprot.org/uniprotkb/O13539/entry","name":"THP2","description":"THO complex subunit THP2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-8526","identifier":"P17629","identifierLink":"https://www.uniprot.org/uniprotkb/P17629/entry","name":"HPR1","description":"THO complex subunit HPR1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1794","complexName":"Integrin alpha5-beta1 complex","organismName":"Homo sapiens; 9606","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for fibronectin and fibrinogen which its binds via the sequence R-G-D in the ligand.","predictedComplex":false,"interactors":[{"ac":"EBI-1382311","identifier":"P08648","identifierLink":"https://www.uniprot.org/uniprotkb/P08648/entry","name":"ITGA5","description":"Integrin alpha-5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-703066","identifier":"P05556","identifierLink":"https://www.uniprot.org/uniprotkb/P05556/entry","name":"ITGB1","description":"Integrin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3027","complexName":"Integrin alpha5-beta1 complex","organismName":"Mus musculus; 10090","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for fibronectin and fibrinogen which its binds via the sequence R-G-D in the ligand.","predictedComplex":false,"interactors":[{"ac":"EBI-644224","identifier":"P09055","identifierLink":"https://www.uniprot.org/uniprotkb/P09055/entry","name":"Itgb1","description":"Integrin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6477055","identifier":"P11688","identifierLink":"https://www.uniprot.org/uniprotkb/P11688/entry","name":"Itga5","description":"Integrin alpha-5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1795","complexName":"Integrin alphav-beta3 complex","organismName":"Homo sapiens; 9606","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and von Willebrand factor which its binds via the sequence R-G-D in the ligand.","predictedComplex":false,"interactors":[{"ac":"EBI-298282","identifier":"P06756","identifierLink":"https://www.uniprot.org/uniprotkb/P06756/entry","name":"ITGAV","description":"Integrin alpha-V","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-702847","identifier":"P05106","identifierLink":"https://www.uniprot.org/uniprotkb/P05106/entry","name":"ITGB3","description":"Integrin beta-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3035","complexName":"Integrin alphav-beta3 complex","organismName":"Mus musculus; 10090","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and von Willebrand factor which its binds via the sequence R-G-D in the ligand.","predictedComplex":false,"interactors":[{"ac":"EBI-6507153","identifier":"O54890","identifierLink":"https://www.uniprot.org/uniprotkb/O54890/entry","name":"Itgb3","description":"Integrin beta-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6598977","identifier":"P43406","identifierLink":"https://www.uniprot.org/uniprotkb/P43406/entry","name":"Itgav","description":"Integrin alpha-V","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1796","complexName":"Integrin alphav-beta5 complex","organismName":"Homo sapiens; 9606","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and von Willebrands Factor which it binds via the sequence R-G-D in the ligand.","predictedComplex":false,"interactors":[{"ac":"EBI-1223434","identifier":"P18084","identifierLink":"https://www.uniprot.org/uniprotkb/P18084/entry","name":"ITGB5","description":"Integrin beta-5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-298282","identifier":"P06756","identifierLink":"https://www.uniprot.org/uniprotkb/P06756/entry","name":"ITGAV","description":"Integrin alpha-V","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3131","complexName":"Integrin alphav-beta5 complex","organismName":"Mus musculus; 10090","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and von Willebrands Factor which it binds via the sequence R-G-D in the ligand.","predictedComplex":false,"interactors":[{"ac":"EBI-6598977","identifier":"P43406","identifierLink":"https://www.uniprot.org/uniprotkb/P43406/entry","name":"Itgav","description":"Integrin alpha-V","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8401821","identifier":"O70309","identifierLink":"https://www.uniprot.org/uniprotkb/O70309/entry","name":"Itgb5","description":"Integrin beta-5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1797","complexName":"Integrin alpha3-beta1 complex","organismName":"Homo sapiens; 9606","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for fibronectin, laminin, collagen, epiligrin, thrombospondin and CSPG4 which its binds via the sequence R-G-D in the ligand.","predictedComplex":false,"interactors":[{"ac":"EBI-2550768","identifier":"P26006","identifierLink":"https://www.uniprot.org/uniprotkb/P26006/entry","name":"ITGA3","description":"Integrin alpha-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-703066","identifier":"P05556","identifierLink":"https://www.uniprot.org/uniprotkb/P05556/entry","name":"ITGB1","description":"Integrin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3117","complexName":"Integrin alpha3-beta1 complex","organismName":"Mus musculus; 10090","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for fibronectin, laminin, collagen, epiligrin, thrombospondin and CSPG4 which its binds via the sequence R-G-D in the ligand.","predictedComplex":false,"interactors":[{"ac":"EBI-644224","identifier":"P09055","identifierLink":"https://www.uniprot.org/uniprotkb/P09055/entry","name":"Itgb1","description":"Integrin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8398907","identifier":"Q62470","identifierLink":"https://www.uniprot.org/uniprotkb/Q62470/entry","name":"Itga3","description":"Integrin alpha-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1798","complexName":"Integrin alpha1-beta1 complex","organismName":"Homo sapiens; 9606","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton.","predictedComplex":false,"interactors":[{"ac":"EBI-2554465","identifier":"P56199","identifierLink":"https://www.uniprot.org/uniprotkb/P56199/entry","name":"ITGA1","description":"Integrin alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-703066","identifier":"P05556","identifierLink":"https://www.uniprot.org/uniprotkb/P05556/entry","name":"ITGB1","description":"Integrin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3114","complexName":"Integrin alpha1-beta1 complex","organismName":"Mus musculus; 10090","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton.","predictedComplex":false,"interactors":[{"ac":"EBI-644224","identifier":"P09055","identifierLink":"https://www.uniprot.org/uniprotkb/P09055/entry","name":"Itgb1","description":"Integrin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9630306","identifier":"Q3V3R4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3V3R4/entry","name":"Itga1","description":"Integrin alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1799","complexName":"Integrin alphaIIb-beta3 complex","organismName":"Homo sapiens; 9606","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Integrin alphaIIb-beta3 is the most abundant surface-expressed integrin (40,000-80,000 copies per platelet) with another pool located in internal membranes and which can be exposed after platelet activation. Receptor for von Willebrand factor, fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. It recognizes the sequence R-G-D in a wide array of ligands or H-H-L-G-G-G-A-K-Q-A-G-D-V in the case of fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial cell surface.","predictedComplex":false,"interactors":[{"ac":"EBI-702693","identifier":"P08514","identifierLink":"https://www.uniprot.org/uniprotkb/P08514/entry","name":"ITGA2B","description":"Integrin alpha-IIb","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-702847","identifier":"P05106","identifierLink":"https://www.uniprot.org/uniprotkb/P05106/entry","name":"ITGB3","description":"Integrin beta-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3116","complexName":"Integrin alphaIIb-beta3 complex","organismName":"Mus musculus; 10090","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Integrin alphaIIb-beta3 is the most abundant surface-expressed integrin (40,000-80,000 copies per platelet) with another pool located in internal membranes and which can be exposed after platelet activation. Receptor for von Willebrand factor, fibronectin, fibrinogen, plasminogen, prothrombin, thrombospondin and vitronectin. It recognizes the sequence R-G-D in a wide array of ligands or H-H-L-G-G-G-A-K-Q-A-G-D-V in the case of fibrinogen gamma chain. Following activation integrin alpha-IIb/beta-3 brings about platelet/platelet interaction through binding of soluble fibrinogen. This step leads to rapid platelet aggregation which physically plugs ruptured endothelial cell surface.","predictedComplex":false,"interactors":[{"ac":"EBI-6507153","identifier":"O54890","identifierLink":"https://www.uniprot.org/uniprotkb/O54890/entry","name":"Itgb3","description":"Integrin beta-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8350776","identifier":"Q9QUM0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9QUM0/entry","name":"Itga2b","description":"Integrin alpha-IIb","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1800","complexName":"CCR4-NOT mRNA deadenylase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Major cellular mRNA deadenylase complex, removing polyA tails that protect transcripts from degradation and promotes translation in the cytoplasm. The complex is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation, and general transcription regulation, potentially by promoting the resumption of elongation of arrested RNAPII when it encounters transcriptional blocks in vivo.","predictedComplex":false,"interactors":[{"ac":"EBI-12139","identifier":"P25655","identifierLink":"https://www.uniprot.org/uniprotkb/P25655/entry","name":"CDC39","description":"General negative regulator of transcription subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13162","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12153","identifier":"P06100","identifierLink":"https://www.uniprot.org/uniprotkb/P06100/entry","name":"CDC36","description":"General negative regulator of transcription subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-12165","identifier":"P06102","identifierLink":"https://www.uniprot.org/uniprotkb/P06102/entry","name":"NOT3","description":"General negative regulator of transcription subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23326","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12174","identifier":"P34909","identifierLink":"https://www.uniprot.org/uniprotkb/P34909/entry","name":"MOT2","description":"General negative regulator of transcription subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12603","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12184","identifier":"Q12514","identifierLink":"https://www.uniprot.org/uniprotkb/Q12514/entry","name":"NOT5","description":"General negative regulator of transcription subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23326","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13629","identifier":"P39008","identifierLink":"https://www.uniprot.org/uniprotkb/P39008/entry","name":"POP2","description":"Poly(A) ribonuclease POP2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10797","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23322","identifier":"P53280","identifierLink":"https://www.uniprot.org/uniprotkb/P53280/entry","name":"CAF130","description":"Protein CAF130","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-28306","identifier":"P53829","identifierLink":"https://www.uniprot.org/uniprotkb/P53829/entry","name":"CAF40","description":"Protein CAF40","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12262","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4396","identifier":"P31384","identifierLink":"https://www.uniprot.org/uniprotkb/P31384/entry","name":"CCR4","description":"CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12121","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1801","complexName":"Integrin alpha2-beta1 complex","organismName":"Homo sapiens; 9606","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for laminin, collagen, collagen C-propeptides, fibronectin and E-cadherin. It recognizes the sequence G-F-P-G-E-R in a wide array of ligands. It is responsible for adhesion of platelets and other cells to collagens, modulation of collagen and collagenase gene expression, force generation and organization of newly synthesized extracellular matrix.","predictedComplex":false,"interactors":[{"ac":"EBI-702960","identifier":"P17301","identifierLink":"https://www.uniprot.org/uniprotkb/P17301/entry","name":"ITGA2","description":"Integrin alpha-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-703066","identifier":"P05556","identifierLink":"https://www.uniprot.org/uniprotkb/P05556/entry","name":"ITGB1","description":"Integrin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3115","complexName":"Integrin alpha2-beta1 complex","organismName":"Mus musculus; 10090","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for laminin, collagen, collagen C-propeptides, fibronectin and E-cadherin. It recognizes the sequence G-F-P-G-E-R in a wide array of ligands. It is responsible for adhesion of platelets and other cells to collagens, modulation of collagen and collagenase gene expression, force generation and organization of newly synthesized extracellular matrix.","predictedComplex":false,"interactors":[{"ac":"EBI-644224","identifier":"P09055","identifierLink":"https://www.uniprot.org/uniprotkb/P09055/entry","name":"Itgb1","description":"Integrin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8400688","identifier":"Q62469","identifierLink":"https://www.uniprot.org/uniprotkb/Q62469/entry","name":"Itga2","description":"Integrin alpha-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1802","complexName":"Integrin alpha4-beta1 complex","organismName":"Homo sapiens; 9606","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Mediates both  firm and rolling adhesion, causing leukocytes to slow down and begin rolling along the inner surface of a vessel wall. Receptor for fibronectin, in which it recognizes one or more domains within the alternatively spliced CS-1 and CS-5 regions, and VCAM-1, in which it recognizes the sequence Q-I-D-S. On activated endothelial cells  triggers homotypic aggregation for most VLA-4-positive leukocyte cell lines. It may also participate in cytolytic T-cell interactions with target cells.","predictedComplex":false,"interactors":[{"ac":"EBI-703044","identifier":"P13612","identifierLink":"https://www.uniprot.org/uniprotkb/P13612/entry","name":"ITGA4","description":"Integrin alpha-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-703066","identifier":"P05556","identifierLink":"https://www.uniprot.org/uniprotkb/P05556/entry","name":"ITGB1","description":"Integrin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3118","complexName":"integrin alpha4-beta1 complex","organismName":"Mus musculus; 10090","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for fibronectin, in which it recognizes one or more domains within the alternatively spliced CS-1 and CS-5 regions, and VCAM-1, in which it recognizes the sequence Q-I-D-S. On activated endothelial cells  triggers homotypic aggregation for most VLA-4-positive leukocyte cell lines. It may also participate in cytolytic T-cell interactions with target cells.","predictedComplex":false,"interactors":[{"ac":"EBI-644224","identifier":"P09055","identifierLink":"https://www.uniprot.org/uniprotkb/P09055/entry","name":"Itgb1","description":"Integrin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9516968","identifier":"Q00651","identifierLink":"https://www.uniprot.org/uniprotkb/Q00651/entry","name":"Itga4","description":"Integrin alpha-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1803","complexName":"Integrin alpha6-beta1 complex","organismName":"Homo sapiens; 9606","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for laminin on platelets.","predictedComplex":false,"interactors":[{"ac":"EBI-2436548","identifier":"P23229","identifierLink":"https://www.uniprot.org/uniprotkb/P23229/entry","name":"ITGA6","description":"Integrin alpha-6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-703066","identifier":"P05556","identifierLink":"https://www.uniprot.org/uniprotkb/P05556/entry","name":"ITGB1","description":"Integrin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3119","complexName":"Integrin alpha6-beta1 complex","organismName":"Mus musculus; 10090","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for laminin on platelets.","predictedComplex":false,"interactors":[{"ac":"EBI-644224","identifier":"P09055","identifierLink":"https://www.uniprot.org/uniprotkb/P09055/entry","name":"Itgb1","description":"Integrin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8357162","identifier":"Q61739","identifierLink":"https://www.uniprot.org/uniprotkb/Q61739/entry","name":"Itga6","description":"Integrin alpha-6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1804","complexName":"Integrin alpha7-beta1 complex","organismName":"Homo sapiens; 9606","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Primary laminin receptor on skeletal myoblasts and adult myofibers. During myogenic differentiation, it may induce changes in the shape and mobility of myoblasts, and facilitate their localization at laminin-rich sites of secondary fiber formation. It is involved in the maintenance of the myofibers cytoarchitecture as well as for their anchorage, viability and functional integrity.","predictedComplex":false,"interactors":[{"ac":"EBI-2565284","identifier":"Q13683","identifierLink":"https://www.uniprot.org/uniprotkb/Q13683/entry","name":"ITGA7","description":"Integrin alpha-7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-703066","identifier":"P05556","identifierLink":"https://www.uniprot.org/uniprotkb/P05556/entry","name":"ITGB1","description":"Integrin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3121","complexName":"Integrin alpha7-beta1 complex","organismName":"Mus musculus; 10090","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Primary laminin receptor on skeletal myoblasts and adult myofibers. During myogenic differentiation, it may induce changes in the shape and mobility of myoblasts, and facilitate their localization at laminin-rich sites of secondary fiber formation. It is involved in the maintenance of the myofibers cytoarchitecture as well as for their anchorage, viability and functional integrity.","predictedComplex":false,"interactors":[{"ac":"EBI-1786299","identifier":"Q61738","identifierLink":"https://www.uniprot.org/uniprotkb/Q61738/entry","name":"Itga7","description":"Integrin alpha-7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-644224","identifier":"P09055","identifierLink":"https://www.uniprot.org/uniprotkb/P09055/entry","name":"Itgb1","description":"Integrin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1805","complexName":"Dynactin complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Recruited to autoinhibited dynein, a retrograde microtubule motor complex to  activate the processive, unidirectional movement of dynein. Required for intracellular transport by dynein by localizing cytoplasmic dynein to its proper intracellular cargo and modulating dynein motor activity. Dynactin increases the run length of single dynein motors, but does not alter the directionality of dynein movement. Required for the spindle translocation late in anaphase and is involved in a cell wall synthesis checkpoint.","predictedComplex":false,"interactors":[{"ac":"EBI-12049","identifier":"P33420","identifierLink":"https://www.uniprot.org/uniprotkb/P33420/entry","name":"NIP100","description":"Protein NIP100","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR18916","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2920","identifier":"P38696","identifierLink":"https://www.uniprot.org/uniprotkb/P38696/entry","name":"ARP1","description":"Centractin","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2977","identifier":"Q04549","identifierLink":"https://www.uniprot.org/uniprotkb/Q04549/entry","name":"ARP10","description":"Actin-like protein ARP10","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-33243","identifier":"Q07887","identifierLink":"https://www.uniprot.org/uniprotkb/Q07887/entry","name":"LDB18","description":"Protein LDB18","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-9415","identifier":"P36224","identifierLink":"https://www.uniprot.org/uniprotkb/P36224/entry","name":"JNM1","description":"Nuclear migration protein JNM1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1806","complexName":"Rad17-Mec3-Ddc1 checkpoint clamp complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Enables the DNA repair pathways to restore the integrity of the DNA prior to DNA synthesis or separation of the replicated chromosomes. Associates with sites of DNA damage and modulates the MEC1 signaling pathway and the activation of RAD53 in response to DNA damage at phase G1. Loads onto DNA in an ATP-dependent manner through its interaction with the RAD24-RFC checkpoint clamp loader complex (CPX-1807). The comples is reported as showing no detectable exonuclease activity. The complex also physically regulates DNA polymerase zeta-dependent mutagenesis by controlling the access of polymerase zeta to damaged DNA.","predictedComplex":false,"interactors":[{"ac":"EBI-10658","identifier":"Q02574","identifierLink":"https://www.uniprot.org/uniprotkb/Q02574/entry","name":"MEC3","description":"DNA damage checkpoint control protein MEC3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12900","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14652","identifier":"P48581","identifierLink":"https://www.uniprot.org/uniprotkb/P48581/entry","name":"RAD17","description":"DNA damage checkpoint control protein RAD17","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10870","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30769","identifier":"Q08949","identifierLink":"https://www.uniprot.org/uniprotkb/Q08949/entry","name":"DDC1","description":"DNA damage checkpoint protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15237","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1807","complexName":"DNA replication factor C complex, RAD24 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"DNA-dependent ATPase clamp-loader complex for the Rad17-Mec3-Ddc1 checkpoint clamp complex (CPX-1806). During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighbouring subunit.","predictedComplex":false,"interactors":[{"ac":"EBI-14675","identifier":"P32641","identifierLink":"https://www.uniprot.org/uniprotkb/P32641/entry","name":"RAD24","description":"Checkpoint protein RAD24","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12172","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14992","identifier":"P40348","identifierLink":"https://www.uniprot.org/uniprotkb/P40348/entry","name":"RFC2","description":"Replication factor C subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15000","identifier":"P38629","identifierLink":"https://www.uniprot.org/uniprotkb/P38629/entry","name":"RFC3","description":"Replication factor C subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15009","identifier":"P40339","identifierLink":"https://www.uniprot.org/uniprotkb/P40339/entry","name":"RFC4","description":"Replication factor C subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15016","identifier":"P38251","identifierLink":"https://www.uniprot.org/uniprotkb/P38251/entry","name":"RFC5","description":"Replication factor C subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1808","complexName":"GCN1-GCN20 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Functions on translating ribosomes to promote binding of uncharged tRNA  to the A-site or in the transfer of uncharged tRNA from the A-site to the histidyl-tRNA synthetase (HisRS)-like domain in GCN2 for kinase activation. It is thus required for activation of GCN2 and the consequent induction of GCN4 translation in amino acid-starved cells.","predictedComplex":false,"interactors":[{"ac":"EBI-7423","identifier":"P43535","identifierLink":"https://www.uniprot.org/uniprotkb/P43535/entry","name":"GCN20","description":"Protein GCN20","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19211","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7442","identifier":"P33892","identifierLink":"https://www.uniprot.org/uniprotkb/P33892/entry","name":"GCN1","description":"eIF-2-alpha kinase activator GCN1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1809","complexName":"MER2-MEI4-REC114 meiotic recombination initiation complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Appears to act as a regulatory subunit for the Spo11 loading onto potential double strand break sites, as an essential part of the initiation of meiotic recombination.","predictedComplex":false,"interactors":[{"ac":"EBI-10742","identifier":"P21651","identifierLink":"https://www.uniprot.org/uniprotkb/P21651/entry","name":"REC107","description":"Recombination protein 107","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-14447","identifier":"P32841","identifierLink":"https://www.uniprot.org/uniprotkb/P32841/entry","name":"REC114","description":"Meiotic recombination protein REC114","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-2566907","identifier":"P29467","identifierLink":"https://www.uniprot.org/uniprotkb/P29467/entry","name":"MEI4","description":"Meiosis-specific protein MEI4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1810","complexName":"NuA3 histone acetyltransferase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Acetylates Histone H3 on Lys-14 of the mature histone protein, resulting in transcription elongation. Histone H3 methylation leads to the recruitment of NuA3 to nucleosomes, via binding of the Yng1 subunit.","predictedComplex":false,"interactors":[{"ac":"EBI-16484","identifier":"P34218","identifierLink":"https://www.uniprot.org/uniprotkb/P34218/entry","name":"SAS3","description":"Histone acetyltransferase SAS3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18920","identifier":"P35189","identifierLink":"https://www.uniprot.org/uniprotkb/P35189/entry","name":"TAF14","description":"Transcription initiation factor TFIID subunit 14","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23195","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25552","identifier":"P47128","identifierLink":"https://www.uniprot.org/uniprotkb/P47128/entry","name":"EAF6","description":"Chromatin modification-related protein EAF6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-31890","identifier":"Q08465","identifierLink":"https://www.uniprot.org/uniprotkb/Q08465/entry","name":"YNG1","description":"Protein YNG1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-33358","identifier":"Q12311","identifierLink":"https://www.uniprot.org/uniprotkb/Q12311/entry","name":"NTO1","description":"NuA3 HAT complex component NTO1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13793","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1811","complexName":"Sir2-3-4 silent chromatin complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for transcriptional repression of the silent mating type loci, HML and HMR. Spreads from sites of nucleation by first  deacetylating the H3 and H4 histone tails, and then binding stably to nucleosomes to silence promoters up to 3 kb from the telomeric repeat.","predictedComplex":false,"interactors":[{"ac":"EBI-17219","identifier":"P06700","identifierLink":"https://www.uniprot.org/uniprotkb/P06700/entry","name":"SIR2","description":"NAD-dependent histone deacetylase SIR2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11085","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17230","identifier":"P06701","identifierLink":"https://www.uniprot.org/uniprotkb/P06701/entry","name":"SIR3","description":"Regulatory protein SIR3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10763","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17237","identifier":"P11978","identifierLink":"https://www.uniprot.org/uniprotkb/P11978/entry","name":"SIR4","description":"Regulatory protein SIR4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1812","complexName":"1,3-beta-D-glucan synthase complex, FKS1-RHO1 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Synthesizes 1,3-beta-glucan, a major structural component of the yeast cell wall and of the yeast spore wall. FKS1 variant is responsible for cell wall and spore wall assembly.","predictedComplex":false,"interactors":[{"ac":"EBI-15121","identifier":"P06780","identifierLink":"https://www.uniprot.org/uniprotkb/P06780/entry","name":"RHO1","description":"GTP-binding protein RHO1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24072","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7708","identifier":"P38631","identifierLink":"https://www.uniprot.org/uniprotkb/P38631/entry","name":"FKS1","description":"1,3-beta-glucan synthase component FKS1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12741","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1813","complexName":"1,3-beta-D-glucan synthase complex, FKS2-RHO1 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Synthesizes 1,3-beta-glucan, a major structural component of the yeast cell wall and of the yeast spore wall. GSC2/FKS2 variant is active during sporulation.","predictedComplex":false,"interactors":[{"ac":"EBI-15121","identifier":"P06780","identifierLink":"https://www.uniprot.org/uniprotkb/P06780/entry","name":"RHO1","description":"GTP-binding protein RHO1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24072","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7715","identifier":"P40989","identifierLink":"https://www.uniprot.org/uniprotkb/P40989/entry","name":"GSC2","description":"1,3-beta-glucan synthase component GSC2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12741","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3028","complexName":"1,3-beta-D-glucan synthase complex, FKS3-RHO1 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Synthesizes 1,3-beta-glucan, a major structural component of the yeast cell wall and of the yeast spore wall. FKS3 variant is responsible for normal spore wall assembly.","predictedComplex":false,"interactors":[{"ac":"EBI-15121","identifier":"P06780","identifierLink":"https://www.uniprot.org/uniprotkb/P06780/entry","name":"RHO1","description":"GTP-binding protein RHO1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24072","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7722","identifier":"Q04952","identifierLink":"https://www.uniprot.org/uniprotkb/Q04952/entry","name":"FKS3","description":"1,3-beta-glucan synthase component FKS3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12741","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1814","complexName":"R2TP co-chaperone complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Co-chaperone that plays a role in box C/D snoRNP assembly/maintenance, especially under stress conditions. Also involved in the proper accumulation of box H/ACA small nucleolar RNAs.\r\nRegulates the stability of phosphatidylinositol 3-kinase-related protein kinases (PIKKs) such as TEL1 (P38110) and MEC1 (P38111), which are required for checkpoint signaling. Newly synthesized PIKK interacts with TEL2, in the \r\nTEL2–TTI1–TTI2 complex (CPX-1422), assisted by HSP90 (P02829). Phosphorylated TEl2 then mediates the interaction between PIKK and R2TP complex to eventually lead to the proper assembly of PIKK.","predictedComplex":false,"interactors":[{"ac":"EBI-21956","identifier":"P25638","identifierLink":"https://www.uniprot.org/uniprotkb/P25638/entry","name":"TAH1","description":"TPR repeat-containing protein associated with Hsp90","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-24499","identifier":"P38768","identifierLink":"https://www.uniprot.org/uniprotkb/P38768/entry","name":"PIH1","description":"Protein interacting with Hsp90 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22997","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30712","identifier":"Q03940","identifierLink":"https://www.uniprot.org/uniprotkb/Q03940/entry","name":"RVB1","description":"RuvB-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31814","identifier":"Q12464","identifierLink":"https://www.uniprot.org/uniprotkb/Q12464/entry","name":"RVB2","description":"RuvB-like protein 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1815","complexName":"Integrin alpha8-beta1 complex","organismName":"Homo sapiens; 9606","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Functions in the genesis of kidney and probably of other organs by regulating the recruitment of mesenchymal cells into epithelial structures. Recognizes the sequence R-G-D in a wide array of ligands including Tenascin, Fibronectin, Osteopontin, Transforming growth factor beta-1, Transforming growth factor beta-3 and Vitronectin. Nephronectin is probably its functional ligand in kidney genesis. Neuronal receptor for Tenascin, it mediates cell-cell interactions and regulates neurite outgrowth of sensory and motor neurons.","predictedComplex":false,"interactors":[{"ac":"EBI-2567895","identifier":"P53708","identifierLink":"https://www.uniprot.org/uniprotkb/P53708/entry","name":"ITGA8","description":"Integrin alpha-8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-703066","identifier":"P05556","identifierLink":"https://www.uniprot.org/uniprotkb/P05556/entry","name":"ITGB1","description":"Integrin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3122","complexName":"Integrin alpha8-beta1 complex","organismName":"Mus musculus; 10090","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Functions in the genesis of kidney and probably of other organs by regulating the recruitment of mesenchymal cells into epithelial structures. Recognizes the sequence R-G-D in a wide array of ligands including Tenascin, Fibronectin, Osteopontin, Transforming growth factor beta-1, Transforming growth factor beta-3 and Vitronectin. Nephronectin is probably its functional ligand in kidney genesis. Neuronal receptor for Tenascin, it mediates cell-cell interactions and regulates neurite outgrowth of sensory and motor neurons.","predictedComplex":false,"interactors":[{"ac":"EBI-644224","identifier":"P09055","identifierLink":"https://www.uniprot.org/uniprotkb/P09055/entry","name":"Itgb1","description":"Integrin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8402892","identifier":"A2ARA8","identifierLink":"https://www.uniprot.org/uniprotkb/A2ARA8/entry","name":"Itga8","description":"Integrin alpha-8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1816","complexName":"Integrin alpha9-beta1 complex","organismName":"Homo sapiens; 9606","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin.","predictedComplex":false,"interactors":[{"ac":"EBI-2567935","identifier":"Q13797","identifierLink":"https://www.uniprot.org/uniprotkb/Q13797/entry","name":"ITGA9","description":"Integrin alpha-9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-703066","identifier":"P05556","identifierLink":"https://www.uniprot.org/uniprotkb/P05556/entry","name":"ITGB1","description":"Integrin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3123","complexName":"Integrin alpha9-beta1 complex","organismName":"Mus musculus; 10090","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin.","predictedComplex":false,"interactors":[{"ac":"EBI-644224","identifier":"P09055","identifierLink":"https://www.uniprot.org/uniprotkb/P09055/entry","name":"Itgb1","description":"Integrin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8400556","identifier":"Q91YD5","identifierLink":"https://www.uniprot.org/uniprotkb/Q91YD5/entry","name":"Itga9","description":"Integrin alpha-9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-1817","complexName":"Integrin alpha10-beta1 complex","organismName":"Homo sapiens; 9606","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for collagen.","predictedComplex":false,"interactors":[{"ac":"EBI-2567971","identifier":"O75578","identifierLink":"https://www.uniprot.org/uniprotkb/O75578/entry","name":"ITGA10","description":"Integrin alpha-10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-703066","identifier":"P05556","identifierLink":"https://www.uniprot.org/uniprotkb/P05556/entry","name":"ITGB1","description":"Integrin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3124","complexName":"Integrin alpha10-beta1 complex","organismName":"Mus musculus; 10090","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for collagen.","predictedComplex":false,"interactors":[{"ac":"EBI-644224","identifier":"P09055","identifierLink":"https://www.uniprot.org/uniprotkb/P09055/entry","name":"Itgb1","description":"Integrin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9630661","identifier":"Q14BL5","identifierLink":"https://www.uniprot.org/uniprotkb/Q14BL5/entry","name":"Itga10","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-1818","complexName":"Integrin alpha11-beta1 complex","organismName":"Homo sapiens; 9606","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for collagen.","predictedComplex":false,"interactors":[{"ac":"EBI-2568019","identifier":"Q9UKX5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UKX5/entry","name":"ITGA11","description":"Integrin alpha-11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-703066","identifier":"P05556","identifierLink":"https://www.uniprot.org/uniprotkb/P05556/entry","name":"ITGB1","description":"Integrin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3125","complexName":"Integrin alpha11-beta1 complex","organismName":"Mus musculus; 10090","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for collagen.","predictedComplex":false,"interactors":[{"ac":"EBI-644224","identifier":"P09055","identifierLink":"https://www.uniprot.org/uniprotkb/P09055/entry","name":"Itgb1","description":"Integrin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9630696","identifier":"P61622","identifierLink":"https://www.uniprot.org/uniprotkb/P61622/entry","name":"Itga11","description":"Integrin alpha-11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1819","complexName":"Integrin alphav-beta1 complex","organismName":"Homo sapiens; 9606","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and von Willibrand Factor. Recognize the sequence R-G-D in a wide array of ligands.","predictedComplex":false,"interactors":[{"ac":"EBI-298282","identifier":"P06756","identifierLink":"https://www.uniprot.org/uniprotkb/P06756/entry","name":"ITGAV","description":"Integrin alpha-V","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-703066","identifier":"P05556","identifierLink":"https://www.uniprot.org/uniprotkb/P05556/entry","name":"ITGB1","description":"Integrin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3130","complexName":"Integrin alphav-beta1 complex","organismName":"Mus musculus; 10090","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for vitronectin, cytotactin, fibronectin, fibrinogen, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin and von Willibrand Factor. Recognize the sequence R-G-D in a wide array of ligands.","predictedComplex":false,"interactors":[{"ac":"EBI-644224","identifier":"P09055","identifierLink":"https://www.uniprot.org/uniprotkb/P09055/entry","name":"Itgb1","description":"Integrin beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6598977","identifier":"P43406","identifierLink":"https://www.uniprot.org/uniprotkb/P43406/entry","name":"Itgav","description":"Integrin alpha-V","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1820","complexName":"Integrin alphav-beta6 complex","organismName":"Homo sapiens; 9606","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for fibronectin and cytotactin. It recognizes the sequence R-G-D in its ligands. Internalisation of integrin alpha-V/beta-6 via clathrin-mediated endocytosis promotes carcinoma cell invasion.","predictedComplex":false,"interactors":[{"ac":"EBI-2568070","identifier":"P18564","identifierLink":"https://www.uniprot.org/uniprotkb/P18564/entry","name":"ITGB6","description":"Integrin beta-6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-298282","identifier":"P06756","identifierLink":"https://www.uniprot.org/uniprotkb/P06756/entry","name":"ITGAV","description":"Integrin alpha-V","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3132","complexName":"Integrin alphav-beta6 complex","organismName":"Mus musculus; 10090","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for fibronectin and cytotactin. It recognizes the sequence R-G-D in its ligands. Internalisation of integrin alpha-V/beta-6 via clathrin-mediated endocytosis promotes carcinoma cell invasion.","predictedComplex":false,"interactors":[{"ac":"EBI-6598977","identifier":"P43406","identifierLink":"https://www.uniprot.org/uniprotkb/P43406/entry","name":"Itgav","description":"Integrin alpha-V","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9631351","identifier":"Q9Z0T9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0T9/entry","name":"Itgb6","description":"Integrin beta-6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1821","complexName":"Integrin alphav-beta8 complex","organismName":"Homo sapiens; 9606","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Recognizes pro-TGFB1 (P01137) and pro-TGFB3 (P10600) and activates these growth factors by releasing them from the latency imposed by their surrounding prodomains. Receptor for fibronectin.","predictedComplex":false,"interactors":[{"ac":"EBI-2436381","identifier":"P26012","identifierLink":"https://www.uniprot.org/uniprotkb/P26012/entry","name":"ITGB8","description":"Integrin beta-8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-298282","identifier":"P06756","identifierLink":"https://www.uniprot.org/uniprotkb/P06756/entry","name":"ITGAV","description":"Integrin alpha-V","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3133","complexName":"Integrin alphav-beta8 complex","organismName":"Mus musculus; 10090","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Recognizes pro-Tgfb1 (P04202) and pro-Tgfb3 (P17125) and activates these growth factors by releasing them from the latency imposed by their surrounding prodomains. Receptor for fibronectin.","predictedComplex":false,"interactors":[{"ac":"EBI-6598977","identifier":"P43406","identifierLink":"https://www.uniprot.org/uniprotkb/P43406/entry","name":"Itgav","description":"Integrin alpha-V","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9631401","identifier":"Q0VBD0","identifierLink":"https://www.uniprot.org/uniprotkb/Q0VBD0/entry","name":"Itgb8","description":"Integrin beta-8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1822","complexName":"Integrin alpha6-beta4 complex","organismName":"Homo sapiens; 9606","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for laminin. It plays a critical structural role in the hemidesmosome of epithelial cells.","predictedComplex":false,"interactors":[{"ac":"EBI-2436548","identifier":"P23229","identifierLink":"https://www.uniprot.org/uniprotkb/P23229/entry","name":"ITGA6","description":"Integrin alpha-6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-948678","identifier":"P16144","identifierLink":"https://www.uniprot.org/uniprotkb/P16144/entry","name":"ITGB4","description":"Integrin beta-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3120","complexName":"integrin alpha6-beta4 complex","organismName":"Mus musculus; 10090","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for laminin. It plays a critical structural role in the hemidesmosome of epithelial cells.","predictedComplex":false,"interactors":[{"ac":"EBI-8357162","identifier":"Q61739","identifierLink":"https://www.uniprot.org/uniprotkb/Q61739/entry","name":"Itga6","description":"Integrin alpha-6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9630531","identifier":"A2A863","identifierLink":"https://www.uniprot.org/uniprotkb/A2A863/entry","name":"Itgb4","description":"Integrin beta-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1823","complexName":"Integrin alpha4-beta7 complex","organismName":"Homo sapiens; 9606","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for the cell surface adhesion molecules MADCAM1, expressed by the vascular endothelium of the gastrointestinal tract, VCAM1 and fibronectin. It recognizes one or more domains within the alternatively spliced CS-1 region of fibronectin. Interactions involves the tripeptide L-D-T in MADCAM1, and L-D-V in fibronectin. Mediates lymphocyte migration and homing to gut-associated lymphoid tissue (GALT). Binds to a tripeptide L-D-I in HIV-1 gp120, thereby allowing the virus to enter GALT, which is thought to be the major trigger of AIDS disease.","predictedComplex":false,"interactors":[{"ac":"EBI-702932","identifier":"P26010","identifierLink":"https://www.uniprot.org/uniprotkb/P26010/entry","name":"ITGB7","description":"Integrin beta-7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-703044","identifier":"P13612","identifierLink":"https://www.uniprot.org/uniprotkb/P13612/entry","name":"ITGA4","description":"Integrin alpha-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1824","complexName":"Integrin alphaE-beta7 complex","organismName":"Homo sapiens; 9606","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for E-cadherin. It mediates adhesion of intra-epithelial T-lymphocytes to epithelial cell monolayers.","predictedComplex":false,"interactors":[{"ac":"EBI-702932","identifier":"P26010","identifierLink":"https://www.uniprot.org/uniprotkb/P26010/entry","name":"ITGB7","description":"Integrin beta-7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724198","identifier":"P38570","identifierLink":"https://www.uniprot.org/uniprotkb/P38570/entry","name":"ITGAE","description":"Integrin alpha-E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3127","complexName":"Integrin alphaE-beta7 complex","organismName":"Mus musculus; 10090","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for E-cadherin. It mediates adhesion of intra-epithelial T-lymphocytes to epithelial cell monolayers.","predictedComplex":false,"interactors":[{"ac":"EBI-9517003","identifier":"P26011","identifierLink":"https://www.uniprot.org/uniprotkb/P26011/entry","name":"Itgb7","description":"Integrin beta-7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9631120","identifier":"Q60677","identifierLink":"https://www.uniprot.org/uniprotkb/Q60677/entry","name":"Itgae","description":"Integrin alpha-E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1825","complexName":"Integrin alphaL-beta2 complex","organismName":"Homo sapiens; 9606","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for ICAM1, ICAM2, ICAM3 and ICAM4.","predictedComplex":false,"interactors":[{"ac":"EBI-300173","identifier":"P05107","identifierLink":"https://www.uniprot.org/uniprotkb/P05107/entry","name":"ITGB2","description":"Integrin beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-961214","identifier":"P20701","identifierLink":"https://www.uniprot.org/uniprotkb/P20701/entry","name":"ITGAL","description":"Integrin alpha-L","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3128","complexName":"Integrin alphaL-beta2 complex","organismName":"Mus musculus; 10090","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for ICAM1, ICAM2, ICAM3 and ICAM4.","predictedComplex":false,"interactors":[{"ac":"EBI-644501","identifier":"P11835","identifierLink":"https://www.uniprot.org/uniprotkb/P11835/entry","name":"Itgb2","description":"Integrin beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-983966","identifier":"P24063","identifierLink":"https://www.uniprot.org/uniprotkb/P24063/entry","name":"Itgal","description":"Integrin alpha-L","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1826","complexName":"Integrin alphaM-beta2 complex","organismName":"Homo sapiens; 9606","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for iC3b fragment of the third complement component, in which it probably recognizes the R-G-D peptide in C3b, for fibrinogen, factor X and ICAM1. It recognizes the P1 and P2 peptides of fibrinogen gamma chain.","predictedComplex":false,"interactors":[{"ac":"EBI-2568251","identifier":"P11215","identifierLink":"https://www.uniprot.org/uniprotkb/P11215/entry","name":"ITGAM","description":"Integrin alpha-M","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-300173","identifier":"P05107","identifierLink":"https://www.uniprot.org/uniprotkb/P05107/entry","name":"ITGB2","description":"Integrin beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3129","complexName":"Integrin alphaM-beta2 complex","organismName":"Mus musculus; 10090","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for iC3b fragment of the third complement component, in which it probably recognizes the R-G-D peptide in C3b, for fibrinogen, factor X and ICAM1. It recognizes the P1 and P2 peptides of fibrinogen gamma chain.","predictedComplex":false,"interactors":[{"ac":"EBI-3649232","identifier":"P05555","identifierLink":"https://www.uniprot.org/uniprotkb/P05555/entry","name":"Itgam","description":"Integrin alpha-M","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-644501","identifier":"P11835","identifierLink":"https://www.uniprot.org/uniprotkb/P11835/entry","name":"Itgb2","description":"Integrin beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1827","complexName":"Integrin alphaX-beta2 complex","organismName":"Homo sapiens; 9606","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for fibrinogen in which it recognizes the sequence G-P-R. It mediates cell-cell interaction during inflammatory responses, in particular monocyte adhesion and chemotaxis.","predictedComplex":false,"interactors":[{"ac":"EBI-2568308","identifier":"P20702","identifierLink":"https://www.uniprot.org/uniprotkb/P20702/entry","name":"ITGAX","description":"Integrin alpha-X","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-300173","identifier":"P05107","identifierLink":"https://www.uniprot.org/uniprotkb/P05107/entry","name":"ITGB2","description":"Integrin beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3134","complexName":"Integrin alphaX-beta2 complex","organismName":"Mus musculus; 10090","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for fibrinogen in which it recognizes the sequence G-P-R. It mediates cell-cell interaction during inflammatory responses, in particular monocyte adhesion and chemotaxis.","predictedComplex":false,"interactors":[{"ac":"EBI-644501","identifier":"P11835","identifierLink":"https://www.uniprot.org/uniprotkb/P11835/entry","name":"Itgb2","description":"Integrin beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8400515","identifier":"Q9QXH4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9QXH4/entry","name":"Itgax","description":"Integrin alpha-X","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1828","complexName":"Integrin alphaD-beta2 complex","organismName":"Homo sapiens; 9606","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for ICAM3 and VCAM1. May play a role in the atherosclerotic process such as clearing lipoproteins from plaques and in phagocytosis of blood-borne pathogens, particulate matter, and senescent erythrocytes from the blood.","predictedComplex":false,"interactors":[{"ac":"EBI-2568373","identifier":"Q13349","identifierLink":"https://www.uniprot.org/uniprotkb/Q13349/entry","name":"ITGAD","description":"Integrin alpha-D","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-300173","identifier":"P05107","identifierLink":"https://www.uniprot.org/uniprotkb/P05107/entry","name":"ITGB2","description":"Integrin beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3126","complexName":"Integrin alphaD-beta2 complex","organismName":"Mus musculus; 10090","description":"Cell adhesion, bi-directional signaling receptor which functions as a link between the extra-cellular matrix and the cytoskeleton. Receptor for ICAM3 and VCAM1. May play a role in the atherosclerotic process such as clearing lipoproteins from plaques and in phagocytosis of blood-borne pathogens, particulate matter, and senescent erythrocytes from the blood.","predictedComplex":false,"interactors":[{"ac":"EBI-644501","identifier":"P11835","identifierLink":"https://www.uniprot.org/uniprotkb/P11835/entry","name":"Itgb2","description":"Integrin beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9631080","identifier":"Q3V0T4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3V0T4/entry","name":"Itgad","description":"Integrin alpha-D","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1829","complexName":"Checkpoint clamp complex","organismName":"Homo sapiens; 9606","description":"Enables the DNA repair pathways to restore the integrity of the DNA prior to DNA synthesis or separation of the replicated chromosomes. In response to genotoxic damage, the 9-1-1 complex is loaded around DNA by the Rad17-containing clamp loader. The DNA-bound 9-1-1 complex then facilitates ATR-mediated phosphorylation and activation of Chk1, a protein kinase that regulates S-phase progression, G2/M arrest, and replication fork stabilization. Stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates.","predictedComplex":false,"interactors":[{"ac":"EBI-1056174","identifier":"O60921","identifierLink":"https://www.uniprot.org/uniprotkb/O60921/entry","name":"HUS1","description":"Checkpoint protein HUS1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12900","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2606224","identifier":"Q99638","identifierLink":"https://www.uniprot.org/uniprotkb/Q99638/entry","name":"RAD9A","description":"Cell cycle checkpoint control protein RAD9A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15237","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-721835","identifier":"O60671","identifierLink":"https://www.uniprot.org/uniprotkb/O60671/entry","name":"RAD1","description":"Cell cycle checkpoint protein RAD1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10870","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1830","complexName":"CCAAT-binding factor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Transcriptional activator that binds to the 5'-CCAAT-3' consensus elements within promoters required for yeast to grow on nonermentable carbon sources such as cytochrome genes, thus acting as a global regulator of respiration. The Hap2/Hap3/Hap5 trimer is sufficient for CCAAT-specific binding at target promoters. Hap4, is necessary for transcriptional activation and is subject to glucose repression.","predictedComplex":false,"interactors":[{"ac":"EBI-8152","identifier":"P06774","identifierLink":"https://www.uniprot.org/uniprotkb/P06774/entry","name":"HAP2","description":"Transcriptional activator HAP2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12632","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8157","identifier":"P13434","identifierLink":"https://www.uniprot.org/uniprotkb/P13434/entry","name":"HAP3","description":"Transcriptional activator HAP3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11064","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8161","identifier":"P14064","identifierLink":"https://www.uniprot.org/uniprotkb/P14064/entry","name":"HAP4","description":"Transcriptional activator HAP4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-8165","identifier":"Q02516","identifierLink":"https://www.uniprot.org/uniprotkb/Q02516/entry","name":"HAP5","description":"Transcriptional activator HAP5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10252","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1831","complexName":"Eukaryotic translation initiation factor 3 core complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Orchestrates several crucial steps in the translation initiation pathway. eIF3, eIF2 (CPX-427), eIF5, and eIF1 bind to each other to form a multifactor complex (MFC) which then binds to the 40S ribosome to form the 43S preinitiation complex. Thus formed, 43S preinitiation complex binds to mRNA to form 48S PIC and scans the mRNA leader region for the start codon. In addition to the five core subunits, yeast eIF3 complex has a loosely associated subunit, namely, Hcr1 (eIF3j/Q05775). This protein promotes the binding of eIF3 to the ribosome and is involved in ribosomal biogenesis as well as proper selection of the AUG start site.","predictedComplex":false,"interactors":[{"ac":"EBI-8951","identifier":"P40217","identifierLink":"https://www.uniprot.org/uniprotkb/P40217/entry","name":"TIF34","description":"Eukaryotic translation initiation factor 3 subunit I","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19877","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8958","identifier":"Q04067","identifierLink":"https://www.uniprot.org/uniprotkb/Q04067/entry","name":"TIF35","description":"Eukaryotic translation initiation factor 3 subunit G","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10352","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8965","identifier":"P32497","identifierLink":"https://www.uniprot.org/uniprotkb/P32497/entry","name":"NIP1","description":"Eukaryotic translation initiation factor 3 subunit C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8973","identifier":"P06103","identifierLink":"https://www.uniprot.org/uniprotkb/P06103/entry","name":"PRT1","description":"Eukaryotic translation initiation factor 3 subunit B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8981","identifier":"P38249","identifierLink":"https://www.uniprot.org/uniprotkb/P38249/entry","name":"RPG1","description":"Eukaryotic translation initiation factor 3 subunit A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14005","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1832","complexName":"tRNA-intron endonuclease complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the first step of tRNA splicing, cleaving the splice sites of all the intron-containing pre-tRNAs, either in the nucleus or on the mitochondrial surface after their export out of the nucleus. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body.","predictedComplex":false,"interactors":[{"ac":"EBI-16817","identifier":"Q04675","identifierLink":"https://www.uniprot.org/uniprotkb/Q04675/entry","name":"SEN15","description":"tRNA-splicing endonuclease subunit SEN15","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28518","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16825","identifier":"P39707","identifierLink":"https://www.uniprot.org/uniprotkb/P39707/entry","name":"SEN34","description":"tRNA-splicing endonuclease subunit SEN34","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13070","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16829","identifier":"Q02825","identifierLink":"https://www.uniprot.org/uniprotkb/Q02825/entry","name":"SEN54","description":"tRNA-splicing endonuclease subunit SEN54","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21027","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16953","identifier":"P16658","identifierLink":"https://www.uniprot.org/uniprotkb/P16658/entry","name":"SEN2","description":"tRNA-splicing endonuclease subunit SEN2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21227","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1833","complexName":"SEC61 protein-conducting channel complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Cotranslational protein conducting channel (PCC) that also assembles with the Sec62-Sec63 complex (CPX-3056) to form the post-translational translocon complex (CPX-3055). Transports secretory proteins across, and inserts integral membrane proteins into, the membrane of the endoplasmic reticulum. The ribosome with an emerging signal sequence is targeted to the membrane by the signal recognition particle (CPX-609) and its receptor. The Sec61 complex acts as a receptor for the ribosome via its cytosolic loops. The alignment of the ribosomal tunnel with a central pore of the PCC allows direct movement of the nascent chain from the ribosomal tunnel exit across or into the membrane. The SEC61 channel appears to be responsible for the transport of glycoproteins. Binds to the oligosaccharyl transferase complex variant 2 (CPX-1639) which selectively glycosylates nascent polypeptide chains in the endoplasmic reticulum.","predictedComplex":false,"interactors":[{"ac":"EBI-16400","identifier":"P32915","identifierLink":"https://www.uniprot.org/uniprotkb/P32915/entry","name":"SEC61","description":"Protein transport protein SEC61","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10906","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16406","identifier":"P35179","identifierLink":"https://www.uniprot.org/uniprotkb/P35179/entry","name":"SSS1","description":"Protein transport protein SSS1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12309","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16410","identifier":"P52870","identifierLink":"https://www.uniprot.org/uniprotkb/P52870/entry","name":"SBH1","description":"Protein transport protein SBH1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13509","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1834","complexName":"SSH1 translocon complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Forms the protein-conducting channel (PCC) for secretory and membrane proteins which engages in the post- and cotranslational translocation of secretory proteins across and the insertion of integral membrane proteins into the membrane of the endoplasmic reticulum. The ribosome with an emerging signal sequence is targeted to the membrane by the signal recognition particle (SRP) and its receptor. The Ssh1 complex acts as a receptor for the ribosome via its cytosolic loops. The alignment of the ribosomal tunnel with a central pore of the PCC allows direct movement of the nascent chain from the ribosomal tunnel exit across or into the membrane. The SSH1 translocon complex does not appear to be required for the transport of glycoproteins (see SEC61 translocon complex, CPX-1833). Recognizes proteins bearing strongly hydrophobic signal sequences. Binds to the oligosaccharyl transferase complex variant 1 (CPX-1638) which selectively glycosylates nascent polypeptide chains in the endoplasmic reticulum.","predictedComplex":false,"interactors":[{"ac":"EBI-16406","identifier":"P35179","identifierLink":"https://www.uniprot.org/uniprotkb/P35179/entry","name":"SSS1","description":"Protein transport protein SSS1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12309","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16414","identifier":"P52871","identifierLink":"https://www.uniprot.org/uniprotkb/P52871/entry","name":"SBH2","description":"Protein transport protein SBH2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13509","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18175","identifier":"P38353","identifierLink":"https://www.uniprot.org/uniprotkb/P38353/entry","name":"SSH1","description":"Sec sixty-one protein homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10906","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1835","complexName":"Signal peptidase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. The complex cleaves the signal peptides of most secretory and many membrane proteins as soon as the lumenal domain of the translocating polypeptide is large enough to expose its cleavage site to the enzyme, during the translocation of the protein through the translocon pore into the endoplasmic reticulum.","predictedComplex":false,"interactors":[{"ac":"EBI-16513","identifier":"P15367","identifierLink":"https://www.uniprot.org/uniprotkb/P15367/entry","name":"SEC11","description":"Signal peptidase complex catalytic subunit SEC11","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10806","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17823","identifier":"P46965","identifierLink":"https://www.uniprot.org/uniprotkb/P46965/entry","name":"SPC1","description":"Signal peptidase complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13202","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17829","identifier":"Q12133","identifierLink":"https://www.uniprot.org/uniprotkb/Q12133/entry","name":"SPC3","description":"Signal peptidase complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12804","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27827","identifier":"Q04969","identifierLink":"https://www.uniprot.org/uniprotkb/Q04969/entry","name":"SPC2","description":"Signal peptidase complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13085","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1836","complexName":"RNA polymerase I core factor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Transcription preinitiation complex which binds tightly to the upstream element of the RNA Polymerase I (RNAP-I, CPX-1664) promoter of 35S rRNA genes. Initiation of transcription requires the assembly of the upstream activating factor (UAF, CPX-1101), the core factor (CF), the TATA binding protein SPT15, and RNAP-I with RRN3 on the upstream element and core promoter. Upon transcription initiation, UAF, RRN3 and CF dissociate from the promoter.","predictedComplex":false,"interactors":[{"ac":"EBI-15986","identifier":"P32786","identifierLink":"https://www.uniprot.org/uniprotkb/P32786/entry","name":"RRN6","description":"RNA polymerase I-specific transcription initiation factor RRN6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28221","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15990","identifier":"P40992","identifierLink":"https://www.uniprot.org/uniprotkb/P40992/entry","name":"RRN7","description":"RNA polymerase I-specific transcription initiation factor RRN7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31576","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27790","identifier":"Q04712","identifierLink":"https://www.uniprot.org/uniprotkb/Q04712/entry","name":"RRN11","description":"RNA polymerase I-specific transcription initiation factor RRN11","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28244","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1837","complexName":"CUL3-HRT1-ELC1-ELA1 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Ubiquitin ligase complex. Required for lysine 48-linked polyubiquitylation of Rpb1, the largest subunit of RNA polymerase II, which targets Pol II for proteasomal degradation, removing stalled RNA polymerase II from a DNA lesion site enabling the repair machinery to bind.","predictedComplex":false,"interactors":[{"ac":"EBI-23065","identifier":"P53202","identifierLink":"https://www.uniprot.org/uniprotkb/P53202/entry","name":"CUL3","description":"Cullin-3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29191","identifier":"P53861","identifierLink":"https://www.uniprot.org/uniprotkb/P53861/entry","name":"ELA1","description":"Elongin-A","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15141","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30154","identifier":"Q03071","identifierLink":"https://www.uniprot.org/uniprotkb/Q03071/entry","name":"ELC1","description":"Elongin-C","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR20648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31686","identifier":"Q08273","identifierLink":"https://www.uniprot.org/uniprotkb/Q08273/entry","name":"HRT1","description":"RING-box protein HRT1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1838","complexName":"a-agglutinin","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Cell surface mannoproteins that mediate cell-cell adhesion of haploid cells during mating. The a- and alpha-agglutinins, expressed by MATa and MATalpha cells, respectively, interact directly with 1:1 stoichiometry. Exposure to the pheromone expressed by the opposite mating type induces agglutinin expression and thus facilitates the agglutination reaction.","predictedComplex":false,"interactors":[{"ac":"EBI-2340","identifier":"P32323","identifierLink":"https://www.uniprot.org/uniprotkb/P32323/entry","name":"AGA1","description":"A-agglutinin anchorage subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-2347","identifier":"P32781","identifierLink":"https://www.uniprot.org/uniprotkb/P32781/entry","name":"AGA2","description":"A-agglutinin-binding subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1840","complexName":"COG Golgi transport complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Peripheral membrane oligomeric protein complex which acts as a retrograde vesicle tethering factor in intra-Golgi protein trafficking, bringing cargo vesicles in close proximity to their target compartment. May play a role in protein glycosylation by directly or indirectly effecting transport, retention, or retrieval to appropriate cisternae of resident Golgi glycosylation enzymes.","predictedComplex":false,"interactors":[{"ac":"EBI-16605","identifier":"P40094","identifierLink":"https://www.uniprot.org/uniprotkb/P40094/entry","name":"COG3","description":"Conserved oligomeric Golgi complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13302","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16614","identifier":"P53271","identifierLink":"https://www.uniprot.org/uniprotkb/P53271/entry","name":"COG2","description":"Conserved oligomeric Golgi complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-4823","identifier":"Q06096","identifierLink":"https://www.uniprot.org/uniprotkb/Q06096/entry","name":"COG4","description":"Conserved oligomeric Golgi complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24016","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4829","identifier":"P53959","identifierLink":"https://www.uniprot.org/uniprotkb/P53959/entry","name":"COG6","description":"Conserved oligomeric Golgi complex subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21506","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4835","identifier":"P53079","identifierLink":"https://www.uniprot.org/uniprotkb/P53079/entry","name":"COG1","description":"Conserved oligomeric Golgi complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-4841","identifier":"P53951","identifierLink":"https://www.uniprot.org/uniprotkb/P53951/entry","name":"COG5","description":"Conserved oligomeric Golgi complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13228","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4847","identifier":"P53195","identifierLink":"https://www.uniprot.org/uniprotkb/P53195/entry","name":"COG7","description":"Conserved oligomeric Golgi complex subunit 7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-6035","identifier":"Q04632","identifierLink":"https://www.uniprot.org/uniprotkb/Q04632/entry","name":"COG8","description":"Conserved oligomeric Golgi complex subunit 8","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21311","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1841","complexName":"PPP4C-PPP4R1 protein phosphatase 4 complex","organismName":"Bos taurus; 9913","description":"PP2A-type phosphatase implicated in a variety of critical biological processes including regulation of histone deacetylase 3 activity and microtubule growth at the centrosome via dephosphorylation of NDEL1.","predictedComplex":false,"interactors":[{"ac":"EBI-2638538","identifier":"F1MRS1","identifierLink":"https://www.uniprot.org/uniprotkb/F1MRS1/entry","name":"PPP4R1","description":"Serine/threonine-protein phosphatase 4 regulatory subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2638542","identifier":"A6H772","identifierLink":"https://www.uniprot.org/uniprotkb/A6H772/entry","name":"PPP4C","description":"Serine/threonine-protein phosphatase 4 catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1842","complexName":"PPP4C-PPP4R1 protein phosphatase 4 complex","organismName":"Homo sapiens; 9606","description":"PP2A-type phosphatase implicated in a variety of critical biological processes including regulation of histone deacetylase 3 activity and microtubule growth at the centrosome via dephosphorylation of NDEL1 (Q9GZM8).","predictedComplex":false,"interactors":[{"ac":"EBI-1046072","identifier":"P60510","identifierLink":"https://www.uniprot.org/uniprotkb/P60510/entry","name":"PPP4C","description":"Serine/threonine-protein phosphatase 4 catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1056262","identifier":"Q8TF05","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TF05/entry","name":"PPP4R1","description":"Serine/threonine-protein phosphatase 4 regulatory subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1843","complexName":"PPP4C-PPP4R2-PPP4R3A protein phosphatase 4 complex","organismName":"Homo sapiens; 9606","description":"PP2A-type phosphatase implicated in a variety of critical biological processes. Specifically dephosphorylates H2AFX phosphorylated on 'Ser-140' (gamma-H2AFX) generated during DNA replication and required for DNA DSB repair.","predictedComplex":false,"interactors":[{"ac":"EBI-1046072","identifier":"P60510","identifierLink":"https://www.uniprot.org/uniprotkb/P60510/entry","name":"PPP4C","description":"Serine/threonine-protein phosphatase 4 catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1048740","identifier":"Q9NY27","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NY27/entry","name":"PPP4R2","description":"Serine/threonine-protein phosphatase 4 regulatory subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16487","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1055598","identifier":"Q6IN85","identifierLink":"https://www.uniprot.org/uniprotkb/Q6IN85/entry","name":"PPP4R3A","description":"Serine/threonine-protein phosphatase 4 regulatory subunit 3A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23318","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1844","complexName":"PPP4C-PPP4R2-PPP4R3B protein phosphatase 4 complex","organismName":"Homo sapiens; 9606","description":"PP2A-type phosphatase implicated in a variety of critical biological processes.  Specifically dephosphorylates ATR-mediated gamma-H2AX generated during DNA replication.","predictedComplex":false,"interactors":[{"ac":"EBI-1046072","identifier":"P60510","identifierLink":"https://www.uniprot.org/uniprotkb/P60510/entry","name":"PPP4C","description":"Serine/threonine-protein phosphatase 4 catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1048740","identifier":"Q9NY27","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NY27/entry","name":"PPP4R2","description":"Serine/threonine-protein phosphatase 4 regulatory subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16487","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-720732","identifier":"Q5MIZ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q5MIZ7/entry","name":"PPP4R3B","description":"Serine/threonine-protein phosphatase 4 regulatory subunit 3B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23318","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1845","complexName":"PPP4C-PPP4R4 protein phosphatase 4 complex","organismName":"Homo sapiens; 9606","description":"PP2A-type phosphatase implicated in a variety of critical biological processes.","predictedComplex":false,"interactors":[{"ac":"EBI-1046072","identifier":"P60510","identifierLink":"https://www.uniprot.org/uniprotkb/P60510/entry","name":"PPP4C","description":"Serine/threonine-protein phosphatase 4 catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1774189","identifier":"Q6NUP7","identifierLink":"https://www.uniprot.org/uniprotkb/Q6NUP7/entry","name":"PPP4R4","description":"Serine/threonine-protein phosphatase 4 regulatory subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21467","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1846","complexName":"Histone H2A phosphatase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Dephosphorylates gammaH2AX, a required step in efficient recovery from the DNA damage checkpoint following a double-strand break repair. The phosphatase appears to target gammaH2AX after its displacement from DNA.","predictedComplex":false,"interactors":[{"ac":"EBI-12759","identifier":"P32345","identifierLink":"https://www.uniprot.org/uniprotkb/P32345/entry","name":"PPH3","description":"Serine/threonine-protein phosphatase 4 catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21239","identifier":"P38193","identifierLink":"https://www.uniprot.org/uniprotkb/P38193/entry","name":"PSY4","description":"Serine/threonine-protein phosphatase 4 regulatory subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR16487","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29107","identifier":"P40164","identifierLink":"https://www.uniprot.org/uniprotkb/P40164/entry","name":"PSY2","description":"Serine/threonine-protein phosphatase 4 regulatory subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23318","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1847","complexName":"HAUS complex","organismName":"Homo sapiens; 9606","description":"Regulates mitotic spindle assembly and centrosome integrity and is required for completion of cytokinesis. The complex interacts with the gamma-tubulin ring complex and this interaction is required for spindle assembly. May regulate microtubule nucleation events to control neuronal development.","predictedComplex":false,"interactors":[{"ac":"EBI-2514791","identifier":"Q96CS2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96CS2/entry","name":"HAUS1","description":"HAUS augmin-like complex subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31570","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2558143","identifier":"Q9BT25","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BT25/entry","name":"HAUS8","description":"HAUS augmin-like complex subunit 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31807","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2558168","identifier":"Q9H6D7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H6D7/entry","name":"HAUS4","description":"HAUS augmin-like complex subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16219","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2558196","identifier":"Q7Z4H7","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z4H7/entry","name":"HAUS6","description":"HAUS augmin-like complex subunit 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16151","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2558217","identifier":"Q68CZ6","identifierLink":"https://www.uniprot.org/uniprotkb/Q68CZ6/entry","name":"HAUS3","description":"HAUS augmin-like complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19378","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2558224","identifier":"O94927","identifierLink":"https://www.uniprot.org/uniprotkb/O94927/entry","name":"HAUS5","description":"HAUS augmin-like complex subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395719","identifier":"Q99871","identifierLink":"https://www.uniprot.org/uniprotkb/Q99871/entry","name":"HAUS7","description":"HAUS augmin-like complex subunit 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14352","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-720080","identifier":"Q9NVX0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NVX0/entry","name":"HAUS2","description":"HAUS augmin-like complex subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16039","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1848","complexName":"ATG12-ATG5 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Essential for autophagy during nutrient deprivation, a catabolic process that sequesters undesired cellular material into autophagosomes for delivery to lysosomes for degradation. Contributes to nutrition homeostasis and damage control in eukaryotic cells. \r\n\r\nActs as an E3-like ligase. This activity is dependent on ATP and two enzymes, ATG7 (P38862)  an E1-like activating enzyme and ATG10 (Q07879) an E2-like conjugating enzyme. Required for lipidation of ATG8 (P38182) (e.g. to phosphatidylethanolamine) and associates with the vesicle membranes once bound to ATG16 (CPX-1849).","predictedComplex":false,"interactors":[{"ac":"EBI-2664","identifier":"Q12380","identifierLink":"https://www.uniprot.org/uniprotkb/Q12380/entry","name":"ATG5","description":"Autophagy protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2692","identifier":"P38316","identifierLink":"https://www.uniprot.org/uniprotkb/P38316/entry","name":"ATG12","description":"Ubiquitin-like protein ATG12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13385","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1849","complexName":"ATG12-ATG5-ATG16 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Essential for autophagy during nutrient deprivation, a catabolic process that sequesters undesired cellular material into autophagosomes for delivery to lysosomes for degradation. \r\n\r\nFunctions as an E3-like enzyme in the ATG8 conjugation system. The ATG12-ATG5-ATG16 complex targets the autophagic membrane via the ATG5-ATG16 complex moiety and then recruits an ATG3:ATG8 thioester intermediate via the interaction between ATG3 and ATG12. The ATG12-ATG5 (CPX-1848) conjugate facilitates the transfer reaction of ATG8 from ATG3 to phosphatidylethanolamine (PE) through a reorganization of the catalytic centre of the E2-like enzyme ATG3. The C-terminal glycine of ATG8 is then conjugated to the amine moiety of PE. The role of ATG16, which has no E3-like activity appears to be to target the ATG12-ATG5 conjugate to the autophagic membranes. ATG8-PE/ATG12-ATG5 complexes form homogeneous oligomers, comprising two to four subunits. ATG16 may then act to reorganize ATG8-PE/ATG12-ATG5 oligomers to form a continuous, flat protein layer with meshwork-like architecture on membranes.","predictedComplex":false,"interactors":[{"ac":"EBI-2664","identifier":"Q12380","identifierLink":"https://www.uniprot.org/uniprotkb/Q12380/entry","name":"ATG5","description":"Autophagy protein 5","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2692","identifier":"P38316","identifierLink":"https://www.uniprot.org/uniprotkb/P38316/entry","name":"ATG12","description":"Ubiquitin-like protein ATG12","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13385","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27344","identifier":"Q03818","identifierLink":"https://www.uniprot.org/uniprotkb/Q03818/entry","name":"ATG16","description":"Autophagy protein 16","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1850","complexName":"Anthranilate synthase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyses the conversion of chorismic acid to anthranilic acid in the first step in the tryptophan branch of aromatic amino acid biosynthesis. Tryptophan-specific regulation of enzyme activity level occurs through feedback regulation by the end product of the pathway, regulated by a tryptophan regulatory element (62LLESAKTNNELDRYS76) within Trp2. Component I (Trp2) and Component II (Trp3) are required for   glutamine-dependent ASase activity while component I can use ammonia as cosubstrate without need of complex formation. . The C-terminal half of Trp3 also has indole-3-glycerol phosphate synthase activity.","predictedComplex":false,"interactors":[{"ac":"EBI-19575","identifier":"P00899","identifierLink":"https://www.uniprot.org/uniprotkb/P00899/entry","name":"TRP2","description":"Anthranilate synthase component 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11236","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19585","identifier":"P00937","identifierLink":"https://www.uniprot.org/uniprotkb/P00937/entry","name":"TRP3","description":"Multifunctional tryptophan biosynthesis protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43418","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1851","complexName":"RPD3S histone deacetylase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Histone deacetylase which functions by deacetylating chromatin, thereby limiting accessibility of the transcriptional machinery to the underlying DNA. RPD3S recognizes the SET2 methylated histones and deacetylates histones within transcribed sequences. This erases transcription elongation-associated histone acetylation and serves to repress the occurrence of spurious transcription initiation from cryptic start sites within open reading frames. May also act to promote nucleosome assembly like a histone chaperone and prevent RSC-dependent histone eviction from nucleosomes","predictedComplex":false,"interactors":[{"ac":"EBI-15864","identifier":"P32561","identifierLink":"https://www.uniprot.org/uniprotkb/P32561/entry","name":"RPD3","description":"Histone deacetylase RPD3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17160","identifier":"P22579","identifierLink":"https://www.uniprot.org/uniprotkb/P22579/entry","name":"SIN3","description":"Transcriptional regulatory protein SIN3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20070","identifier":"Q03010","identifierLink":"https://www.uniprot.org/uniprotkb/Q03010/entry","name":"UME1","description":"Transcriptional regulatory protein UME1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28153","identifier":"Q04779","identifierLink":"https://www.uniprot.org/uniprotkb/Q04779/entry","name":"RCO1","description":"Transcriptional regulatory protein RCO1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47636","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6281","identifier":"Q12432","identifierLink":"https://www.uniprot.org/uniprotkb/Q12432/entry","name":"EAF3","description":"Chromatin modification-related protein EAF3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10880","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1852","complexName":"RPD3L histone deacetylase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Histone deacetylase recruited to promoters in association with specific transcription factors such as UME6 (P39001), ASH1 (P34233), IME1 (P21190), WHI5 (Q12416), and STB1 (P42845) where it acts as a promoter targeted regulator of transcription.. At the promoter region, RPD3 deacetylates specific lysine residues on histones H3 and H4 in a localized region spanning about two nucleosomes. May also act to promote nucleosome assembly like a histone chaperone and prevent RSC-dependent histone eviction from nucleosomes. During vegetative growth, the complex functions as a negative regulator for all genes, whereas upon nitrogen depletion it functions as a positive regulator early during meiosis.","predictedComplex":false,"interactors":[{"ac":"EBI-15864","identifier":"P32561","identifierLink":"https://www.uniprot.org/uniprotkb/P32561/entry","name":"RPD3","description":"Histone deacetylase RPD3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16809","identifier":"P40505","identifierLink":"https://www.uniprot.org/uniprotkb/P40505/entry","name":"SDS3","description":"Transcriptional regulatory protein SDS3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17160","identifier":"P22579","identifierLink":"https://www.uniprot.org/uniprotkb/P22579/entry","name":"SIN3","description":"Transcriptional regulatory protein SIN3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20070","identifier":"Q03010","identifierLink":"https://www.uniprot.org/uniprotkb/Q03010/entry","name":"UME1","description":"Transcriptional regulatory protein UME1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21537","identifier":"P38255","identifierLink":"https://www.uniprot.org/uniprotkb/P38255/entry","name":"RXT2","description":"Transcriptional regulatory protein RXT2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27570","identifier":"P38429","identifierLink":"https://www.uniprot.org/uniprotkb/P38429/entry","name":"SAP30","description":"Transcriptional regulatory protein SAP30","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13286","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28808","identifier":"P50947","identifierLink":"https://www.uniprot.org/uniprotkb/P50947/entry","name":"PHO23","description":"Transcriptional regulatory protein PHO23","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-33349","identifier":"Q08923","identifierLink":"https://www.uniprot.org/uniprotkb/Q08923/entry","name":"CTI6","description":"Histone deacetylase complex subunit CTI6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47793","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-33895","identifier":"Q07458","identifierLink":"https://www.uniprot.org/uniprotkb/Q07458/entry","name":"RXT3","description":"Transcriptional regulatory protein RXT3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-5755","identifier":"P31385","identifierLink":"https://www.uniprot.org/uniprotkb/P31385/entry","name":"DEP1","description":"Transcriptional regulatory protein DEP1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1853","complexName":"CKM complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Cyclin-dependent kinase complex which reversibly associates with the Mediator complex (CPX-3226). The mediator complex lacking the CKM complex has a stimulatory effect on basal transcription. In contrast, the mediator complex containing the sub-complex represses basal transcription. This effect is independent of kinase activity but binding of the complex to the Mediator may interfere with RNAPII recruitment and repress transcription re-initiation.","predictedComplex":false,"interactors":[{"ac":"EBI-18053","identifier":"P25648","identifierLink":"https://www.uniprot.org/uniprotkb/P25648/entry","name":"SRB8","description":"Mediator of RNA polymerase II transcription subunit 12","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-18059","identifier":"P38931","identifierLink":"https://www.uniprot.org/uniprotkb/P38931/entry","name":"SSN2","description":"Mediator of RNA polymerase II transcription subunit 13","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR48249","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20078","identifier":"P47821","identifierLink":"https://www.uniprot.org/uniprotkb/P47821/entry","name":"SSN8","description":"RNA polymerase II holoenzyme cyclin-like subunit","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20082","identifier":"P39073","identifierLink":"https://www.uniprot.org/uniprotkb/P39073/entry","name":"SSN3","description":"Meiotic mRNA stability protein kinase SSN3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1854","complexName":"Golgi SNARE complex SED5-BOS1-BET1-SEC22","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SNARE complex required for fusion of endoplasmic reticulum-derived vesicles at the cis-Golgi cisternae. Mediates membrane fusion through the spontaneous assembly of four complementary SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) motifs. SNAREs bind to each other in-trans, that is, with SNAREs anchored in each apposed tethered membrane. The assembly process leads to a tight connection between the linked membranes and initiates membrane fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-16577","identifier":"P22214","identifierLink":"https://www.uniprot.org/uniprotkb/P22214/entry","name":"SEC22","description":"Protein transport protein SEC22","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45837","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16930","identifier":"Q01590","identifierLink":"https://www.uniprot.org/uniprotkb/Q01590/entry","name":"SED5","description":"Integral membrane protein SED5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3550","identifier":"P22804","identifierLink":"https://www.uniprot.org/uniprotkb/P22804/entry","name":"BET1","description":"Protein transport protein BET1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12791","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3735","identifier":"P25385","identifierLink":"https://www.uniprot.org/uniprotkb/P25385/entry","name":"BOS1","description":"Protein transport protein BOS1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21230","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1855","complexName":"Golgi SNARE complex SED5-GOS1-SFT1-YKT6","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SNARE complex required for fusion of endoplasmic reticulum-derived vesicles at the cis-Golgi cisternae. Mediates membrane fusion through the spontaneous assembly of four complementary SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) motifs. SNAREs bind to each other in-trans, that is, with SNAREs anchored in each apposed tethered membrane. The assembly process leads to a tight connection between the linked membranes and initiates membrane fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-16930","identifier":"Q01590","identifierLink":"https://www.uniprot.org/uniprotkb/Q01590/entry","name":"SED5","description":"Integral membrane protein SED5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17040","identifier":"P43682","identifierLink":"https://www.uniprot.org/uniprotkb/P43682/entry","name":"SFT1","description":"Protein transport protein SFT1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12791","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-24365","identifier":"P38736","identifierLink":"https://www.uniprot.org/uniprotkb/P38736/entry","name":"GOS1","description":"Golgi SNAP receptor complex member 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21094","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26982","identifier":"P36015","identifierLink":"https://www.uniprot.org/uniprotkb/P36015/entry","name":"YKT6","description":"Synaptobrevin homolog YKT6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45806","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1856","complexName":"Serine/threonine-protein phosphatase PP2A variant 1","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A serine/threonine phosphatase, the activity of the catalytic subunit of which is highly regulated by members of a family of regulatory subunits, which determine the substrate specificity, (sub)cellular localization and catalytic activity of the PP2A holoenzymes. The catalytic subunits are subject to two types of post-translational modification, phosphorylation and methylation, which are also thought to be important regulatory devices.","predictedComplex":false,"interactors":[{"ac":"EBI-12745","identifier":"P23594","identifierLink":"https://www.uniprot.org/uniprotkb/P23594/entry","name":"PPH21","description":"Serine/threonine-protein phosphatase PP2A-1 catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1936","identifier":"P31383","identifierLink":"https://www.uniprot.org/uniprotkb/P31383/entry","name":"TPD3","description":"Protein phosphatase PP2A regulatory subunit A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1942","identifier":"Q00362","identifierLink":"https://www.uniprot.org/uniprotkb/Q00362/entry","name":"CDC55","description":"Protein phosphatase PP2A regulatory subunit B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11871","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1857","complexName":"Serine/threonine-protein phosphatase PP2A variant 2","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A serine/threonine phosphatase, the activity of the catalytic subunit of which is highly regulated by members of a family of regulatory subunits, which determine the substrate specificity, (sub)cellular localization and catalytic activity of the PP2A holoenzymes. The catalytic subunits are subject to two types of post-translational modification, phosphorylation and methylation, which are also thought to be important regulatory devices.","predictedComplex":false,"interactors":[{"ac":"EBI-12745","identifier":"P23594","identifierLink":"https://www.uniprot.org/uniprotkb/P23594/entry","name":"PPH21","description":"Serine/threonine-protein phosphatase PP2A-1 catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1931","identifier":"P38903","identifierLink":"https://www.uniprot.org/uniprotkb/P38903/entry","name":"RTS1","description":"Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10257","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1936","identifier":"P31383","identifierLink":"https://www.uniprot.org/uniprotkb/P31383/entry","name":"TPD3","description":"Protein phosphatase PP2A regulatory subunit A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1858","complexName":"Serine/threonine-protein phosphatase PP2A variant 4","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A serine/threonine phosphatase, the activity of the catalytic subunit of which is highly regulated by members of a family of regulatory subunits, which determine the substrate specificity, (sub)cellular localization and catalytic activity of the PP2A holoenzymes. The catalytic subunits are subject to two types of post-translational modification, phosphorylation and methylation, which are also thought to be important regulatory devices.","predictedComplex":false,"interactors":[{"ac":"EBI-12752","identifier":"P23595","identifierLink":"https://www.uniprot.org/uniprotkb/P23595/entry","name":"PPH22","description":"Serine/threonine-protein phosphatase PP2A-2 catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1931","identifier":"P38903","identifierLink":"https://www.uniprot.org/uniprotkb/P38903/entry","name":"RTS1","description":"Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10257","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1936","identifier":"P31383","identifierLink":"https://www.uniprot.org/uniprotkb/P31383/entry","name":"TPD3","description":"Protein phosphatase PP2A regulatory subunit A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1859","complexName":"Serine/threonine-protein phosphatase PP2A variant 3","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A serine/threonine phosphatase, the activity of the catalytic subunit of which is highly regulated by members of a family of regulatory subunits, which determine the substrate specificity, (sub)cellular localization and catalytic activity of the PP2A holoenzymes. The catalytic subunits are subject to two types of post-translational modification, phosphorylation and methylation, which are also thought to be important regulatory devices.","predictedComplex":false,"interactors":[{"ac":"EBI-12752","identifier":"P23595","identifierLink":"https://www.uniprot.org/uniprotkb/P23595/entry","name":"PPH22","description":"Serine/threonine-protein phosphatase PP2A-2 catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1936","identifier":"P31383","identifierLink":"https://www.uniprot.org/uniprotkb/P31383/entry","name":"TPD3","description":"Protein phosphatase PP2A regulatory subunit A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1942","identifier":"Q00362","identifierLink":"https://www.uniprot.org/uniprotkb/Q00362/entry","name":"CDC55","description":"Protein phosphatase PP2A regulatory subunit B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11871","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1860","complexName":"Anaphase-promoting core complex","organismName":"Homo sapiens; 9606","description":"APC, a key regulator of cell cycle progression, is a conserved cullin-RING E3 ubiqutin ligase which facilitates multiubiqutination of cell cycle proteins, including cyclins, so marking them for proteasomal destruction. Generally believed that APC acts as a scaffold that brings E2 enzymes and substrates into close proximity. APC activity is required for metaphase-anaphase transition, mitotic exit, G1 phase and DNA replication. Targets securin for destruction, which is necessary for chromosome segregation. APC seems to have similar function in meiosis. Co-activators, CDC20 (Q12834) and FRZ1/CDH1 (Q9UM11), associate with APC core complex  at specific stages of cell cycle, and are thought to be involved in substrate specificity. APC-CDC20 (CPX-6087) is active in presence of high cyclin-cdk activity in M phase but after metaphase when cyclin-cdk activity decreases, FRZ1 is dephosphorylated, CDC20 is degraded and APC-FRZ1 (CPX-6088) activated.","predictedComplex":false,"interactors":[{"ac":"EBI-1266437","identifier":"Q9UM13","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UM13/entry","name":"ANAPC10","description":"Anaphase-promoting complex subunit 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12936","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1384164","identifier":"Q9UJX3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UJX3/entry","name":"ANAPC7","description":"Anaphase-promoting complex subunit 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2130187","identifier":"Q9NYG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NYG5/entry","name":"ANAPC11","description":"Anaphase-promoting complex subunit 11","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2554854","identifier":"Q9UJX5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UJX5/entry","name":"ANAPC4","description":"Anaphase-promoting complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13260","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2555937","identifier":"Q96DE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96DE5/entry","name":"ANAPC16","description":"Anaphase-promoting complex subunit 16","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31564","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2555941","identifier":"Q8NHZ8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NHZ8/entry","name":"CDC26","description":"Anaphase-promoting complex subunit CDC26","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28579","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2555953","identifier":"Q9BS18","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BS18/entry","name":"ANAPC13","description":"Anaphase-promoting complex subunit 13","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28672","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395918","identifier":"Q9H1A4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H1A4/entry","name":"ANAPC1","description":"Anaphase-promoting complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12827","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395994","identifier":"Q9UJX4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UJX4/entry","name":"ANAPC5","description":"Anaphase-promoting complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12830","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-396137","identifier":"Q9UJX2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UJX2/entry","name":"CDC23","description":"Cell division cycle protein 23 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-396211","identifier":"Q9UJX6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UJX6/entry","name":"ANAPC2","description":"Anaphase-promoting complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8787535","identifier":"P60006","identifierLink":"https://www.uniprot.org/uniprotkb/P60006/entry","name":"ANAPC15","description":"Anaphase-promoting complex subunit 15","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22526","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-994813","identifier":"P30260","identifierLink":"https://www.uniprot.org/uniprotkb/P30260/entry","name":"CDC27","description":"Cell division cycle protein 27 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-994830","identifier":"Q13042","identifierLink":"https://www.uniprot.org/uniprotkb/Q13042/entry","name":"CDC16","description":"Cell division cycle protein 16 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1861","complexName":"GET4-GET5 transmembrane domain recognition complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Escorts newly-synthesised tail-anchored proteins to GET3 (Q12154) for insertion into the endoplasmic reticulum membrane through the GET complex (CPX-956). The complex acts both as an active tethering device that brings GET3 into proximity with its substrates and enzymatically activates GET3 for transmembrane domain recognition. The complex may contain additional heat-shock domain proteins, and it is unclear how many of these are bound at any one time.","predictedComplex":false,"interactors":[{"ac":"EBI-21630","identifier":"P38276","identifierLink":"https://www.uniprot.org/uniprotkb/P38276/entry","name":"yby7","description":"UPF0303 protein YBR137W","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31784","identifier":"Q12118","identifierLink":"https://www.uniprot.org/uniprotkb/Q12118/entry","name":"SGT2","description":"Small glutamine-rich tetratricopeptide repeat-containing protein 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45831","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34904","identifier":"Q12285","identifierLink":"https://www.uniprot.org/uniprotkb/Q12285/entry","name":"MDY2","description":"Ubiquitin-like protein MDY2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-36940","identifier":"Q12125","identifierLink":"https://www.uniprot.org/uniprotkb/Q12125/entry","name":"GET4","description":"Golgi to ER traffic protein 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12875","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8050","identifier":"P31539","identifierLink":"https://www.uniprot.org/uniprotkb/P31539/entry","name":"HSP104","description":"Heat shock protein 104","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11638","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3100","complexName":"mago-y14 exon-exon junction subcomplex","organismName":"Drosophila melanogaster; 7227","description":"A nucleocytoplasmic transport complex that transports proteins and RNAs in and out of the nucleus. Shuttles between the nucleus, where it is loaded onto specific mRNAs, and the cytoplasm and functions in translational regulation. Component of the core exon-exon-junction complex (EJC), an assembly that endows the mature messenger ribonucleoprotein (mRNP) complexes with architectural information on the pre-mRNA intron structure and is important for coupling nuclear and cytoplasmic events in gene expression. Inhibits the ATPase activity of eIF4AIII (Q9VHS8) to ensure a stable association of the EJC core with the mRNA. Binds mRNA in the nucleus and is exported into the cytoplasm where it is dissociated from the mRNA by formation of Pym-mago-Y14 complex (CPX-3147). Following dissociation of Pym, mago-Y14 binds cdm (Imp13, Q9VEC5) to form nuclear import complex cdm-Mago-Y14 (CPX-3171). Released from cdm by Ran-GTP (Q9VZ23) forming cdm-Ran-GTP complex (CPX-3170) to enable mago-Y14 to act in next round of mRNP incorporation. Involved in regulation of pole plasma oskar mRNA localization.","predictedComplex":false,"interactors":[{"ac":"EBI-159609","identifier":"P49028","identifierLink":"https://www.uniprot.org/uniprotkb/P49028/entry","name":"mago","description":"Protein mago nashi","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12638","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-172458","identifier":"Q9V535","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V535/entry","name":"tsu","description":"RNA-binding protein 8A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3037","complexName":"PMT1-PMT3 dolichyl-phosphate-mannose-protein mannosyltransferase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Initiates protein O-mannosylation by catalyzing the transfer of a mannosyl residue from dolichol-phosphate-beta-D-Mannose to Ser and Thr residues of proteins in an alpha-D-mannosidic linkage. Some proteins with moderate Ser/Thr content are O-mannosylated when they are not properly folded. In the endoplasmic reticulum this removes them from folding cycles by reducing engagement with the KAR2 chaperone (P164740). O-mannosyl glycans are important for the stability, localization and/or function of various secretory and membrane proteins and hence cell wall integrity. Acts on both soluble and membrane proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-13567","identifier":"P33775","identifierLink":"https://www.uniprot.org/uniprotkb/P33775/entry","name":"PMT1","description":"Dolichyl-phosphate-mannose--protein mannosyltransferase 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13579","identifier":"P47190","identifierLink":"https://www.uniprot.org/uniprotkb/P47190/entry","name":"PMT3","description":"Dolichyl-phosphate-mannose--protein mannosyltransferase 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3040","complexName":"PMT5-PMT3 dolichyl-phosphate-mannose-protein mannosyltransferase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Initiates protein O-mannosylation by catalyzing the transfer of a mannosyl residue from dolichol-phosphate-beta-D-Mannose to Ser and Thr residues of proteins in an alpha-D-mannosidic linkage. Some proteins with moderate Ser/Thr content are O-mannosylated when they are not properly folded. In the endoplasmic reticulum this removes them from folding cycles by reducing engagement with the KAR2 chaperone (P164740). O-mannosyl glycans are important for the stability, localization and/or function of various secretory and membrane proteins and hence cell wall integrity. Acts on both soluble and membrane proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-13579","identifier":"P47190","identifierLink":"https://www.uniprot.org/uniprotkb/P47190/entry","name":"PMT3","description":"Dolichyl-phosphate-mannose--protein mannosyltransferase 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13591","identifier":"P52867","identifierLink":"https://www.uniprot.org/uniprotkb/P52867/entry","name":"PMT5","description":"Dolichyl-phosphate-mannose--protein mannosyltransferase 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3036","complexName":"PMT1-PMT2 dolichyl-phosphate-mannose-protein mannosyltransferase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Initiates protein O-mannosylation by catalyzing the transfer of a mannosyl residue from dolichol-phosphate-beta-D-Mannose to Ser and Thr residues of proteins in an alpha-D-mannosidic linkage. Some proteins with moderate Ser/Thr content are O-mannosylated when they are not properly folded. In the endoplasmic reticulum this removes them from folding cycles by reducing engagement with the KAR2 chaperone (P164740). O-mannosyl glycans are important for the stability, localization and/or function of various secretory and membrane proteins and hence cell wall integrity. Acts on both soluble and membrane proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-13567","identifier":"P33775","identifierLink":"https://www.uniprot.org/uniprotkb/P33775/entry","name":"PMT1","description":"Dolichyl-phosphate-mannose--protein mannosyltransferase 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13573","identifier":"P31382","identifierLink":"https://www.uniprot.org/uniprotkb/P31382/entry","name":"PMT2","description":"Dolichyl-phosphate-mannose--protein mannosyltransferase 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3038","complexName":"PMT5-PMT2 dolichyl-phosphate-mannose-protein mannosyltransferase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Initiates protein O-mannosylation by catalyzing the transfer of a mannosyl residue from dolichol-phosphate-beta-D-Mannose to Ser and Thr residues of proteins in an alpha-D-mannosidic linkage. Some proteins with moderate Ser/Thr content are O-mannosylated when they are not properly folded. In the endoplasmic reticulum this removes them from folding cycles by reducing engagement with the KAR2 chaperone (P164740). O-mannosyl glycans are important for the stability, localization and/or function of various secretory and membrane proteins and hence cell wall integrity. Acts on both soluble and membrane proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-13573","identifier":"P31382","identifierLink":"https://www.uniprot.org/uniprotkb/P31382/entry","name":"PMT2","description":"Dolichyl-phosphate-mannose--protein mannosyltransferase 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13591","identifier":"P52867","identifierLink":"https://www.uniprot.org/uniprotkb/P52867/entry","name":"PMT5","description":"Dolichyl-phosphate-mannose--protein mannosyltransferase 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3039","complexName":"PMT4 dolichyl-phosphate-mannose-protein mannosyltransferase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Initiates protein O-mannosylation by catalyzing the transfer of a mannosyl residue from dolichol-phosphate-beta-D-Mannose to Ser and Thr residues of proteins in an alpha-D-mannosidic linkage.  O-mannosyl glycans are important for the stability, localization and/or function of various secretory and membrane proteins and hence cell wall integrity. Acts on membrane-bound proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-13585","identifier":"P46971","identifierLink":"https://www.uniprot.org/uniprotkb/P46971/entry","name":"PMT4","description":"Dolichyl-phosphate-mannose--protein mannosyltransferase 4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1981","complexName":"BCL-2 dimer","organismName":"Homo sapiens; 9606","description":"Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1).","predictedComplex":false,"interactors":[{"ac":"EBI-77694","identifier":"P10415","identifierLink":"https://www.uniprot.org/uniprotkb/P10415/entry","name":"BCL2","description":"Apoptosis regulator Bcl-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11256","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1982","complexName":"BAD:BCL-2 complex","organismName":"Homo sapiens; 9606","description":"BH3 domain-containing BAD interacts with and inhibits anti-apoptotic BCL-2. Acts to prevent BCl-2 from sequestering BID and other pro-apoptotic molecules.","predictedComplex":false,"interactors":[{"ac":"EBI-700771","identifier":"Q92934","identifierLink":"https://www.uniprot.org/uniprotkb/Q92934/entry","name":"BAD","description":"Bcl2-associated agonist of cell death","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28540","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-77694","identifier":"P10415","identifierLink":"https://www.uniprot.org/uniprotkb/P10415/entry","name":"BCL2","description":"Apoptosis regulator Bcl-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11256","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1983","complexName":"BAD:BCL-XL complex","organismName":"Homo sapiens; 9606","description":"BH3 domain-containing BAD interacts with and inhibits anti-apoptotic BCL-XL.","predictedComplex":false,"interactors":[{"ac":"EBI-287195","identifier":"Q07817-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q07817-1/entry","name":"BCL2L1","description":"Bcl-2-like protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-700771","identifier":"Q92934","identifierLink":"https://www.uniprot.org/uniprotkb/Q92934/entry","name":"BAD","description":"Bcl2-associated agonist of cell death","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28540","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1984","complexName":"BID:BCL-2 complex","organismName":"Homo sapiens; 9606","description":"BH3 domain-containing BID interacts with BCL-2. BCL-2 inhibits BID-induced cytochrome c leakage from mitochondria without ameliorating BID processing or tBID translocation to mitochondria.","predictedComplex":false,"interactors":[{"ac":"EBI-519672","identifier":"P55957","identifierLink":"https://www.uniprot.org/uniprotkb/P55957/entry","name":"BID","description":"BH3-interacting domain death agonist","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR35447","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-77694","identifier":"P10415","identifierLink":"https://www.uniprot.org/uniprotkb/P10415/entry","name":"BCL2","description":"Apoptosis regulator Bcl-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11256","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1985","complexName":"BIM:BCL-XL complex","organismName":"Homo sapiens; 9606","description":"BH3 domain-containing BIM interacts with and inhibits anti-apoptotic BCL-XL.","predictedComplex":false,"interactors":[{"ac":"EBI-287195","identifier":"Q07817-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q07817-1/entry","name":"BCL2L1","description":"Bcl-2-like protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-526406","identifier":"O43521","identifierLink":"https://www.uniprot.org/uniprotkb/O43521/entry","name":"BCL2L11","description":"Bcl-2-like protein 11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1986","complexName":"PUMA:BCL-2 complex","organismName":"Homo sapiens; 9606","description":"BH3 domain-containing PUMA interacts with and inhibits anti-apoptotic BCL-2. May act to prevent BCL-2 from sequestering BID and other pro-apoptotic molecules.","predictedComplex":false,"interactors":[{"ac":"EBI-519884","identifier":"Q9BXH1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BXH1/entry","name":"BBC3","description":"Bcl-2-binding component 3, isoforms 1/2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-77694","identifier":"P10415","identifierLink":"https://www.uniprot.org/uniprotkb/P10415/entry","name":"BCL2","description":"Apoptosis regulator Bcl-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11256","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1987","complexName":"PUMA:BCL-XL complex","organismName":"Homo sapiens; 9606","description":"BH3 domain-containing PUMA interacts with and inhibits anti-apoptotic BCL-XL.","predictedComplex":false,"interactors":[{"ac":"EBI-287195","identifier":"Q07817-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q07817-1/entry","name":"BCL2L1","description":"Bcl-2-like protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-519884","identifier":"Q9BXH1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BXH1/entry","name":"BBC3","description":"Bcl-2-binding component 3, isoforms 1/2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-1988","complexName":"BAX oligomer","organismName":"Homo sapiens; 9606","description":"Form membrane associated oligomers, in response to cytotoxic signals, which cause membrane damage and release of apoptotic mediators such as cytochrome C.","predictedComplex":false,"interactors":[{"ac":"EBI-516580","identifier":"Q07812","identifierLink":"https://www.uniprot.org/uniprotkb/Q07812/entry","name":"BAX","description":"Apoptosis regulator BAX","stochiometry":"minValue: 8, maxValue: 8","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11256","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1989","complexName":"BAK1 oligomer","organismName":"Homo sapiens; 9606","description":"Form membrane associated oligomers which create pore-like structures in the mittochondrial outer membrane, in response to cytotoxic signals, resulting in membrane damage and release of apoptotic mediators such as cytochrome C.","predictedComplex":false,"interactors":[{"ac":"EBI-519866","identifier":"Q16611","identifierLink":"https://www.uniprot.org/uniprotkb/Q16611/entry","name":"BAK1","description":"Bcl-2 homologous antagonist/killer","stochiometry":"minValue: 8, maxValue: 8","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11256","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1990","complexName":"BIM:BCL-2 complex","organismName":"Homo sapiens; 9606","description":"Pro-apoptotic complex. BH3 domain-containing BIM interacts with and inhibits anti-apoptotic BCL-2.","predictedComplex":false,"interactors":[{"ac":"EBI-526406","identifier":"O43521","identifierLink":"https://www.uniprot.org/uniprotkb/O43521/entry","name":"BCL2L11","description":"Bcl-2-like protein 11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-77694","identifier":"P10415","identifierLink":"https://www.uniprot.org/uniprotkb/P10415/entry","name":"BCL2","description":"Apoptosis regulator Bcl-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11256","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1991","complexName":"BID:BCL-XL complex","organismName":"Homo sapiens; 9606","description":"BH3 domain-containing BID interacts with BCL-XL. BCL-XL inhibits BID-induced cytochrome C leakage from mitochondria without ameliorating BID processing or tBID translocation to mitochondria.","predictedComplex":false,"interactors":[{"ac":"EBI-287195","identifier":"Q07817-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q07817-1/entry","name":"BCL2L1","description":"Bcl-2-like protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-519672","identifier":"P55957","identifierLink":"https://www.uniprot.org/uniprotkb/P55957/entry","name":"BID","description":"BH3-interacting domain death agonist","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR35447","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1992","complexName":"6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 1 complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the synthesis and degradation of fructose 2,6-bisphosphate, therefore required for both glycolysis and gluconeogenesis. Regulated in the long term at the transcriptional level but the acute response is controlled by the phosphorylation state of Ser-32.","predictedComplex":false,"interactors":[{"ac":"EBI-709807","identifier":"P16118","identifierLink":"https://www.uniprot.org/uniprotkb/P16118/entry","name":"PFKFB1","description":"6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10606","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1993","complexName":"Ku70:Ku80 complex","organismName":"Homo sapiens; 9606","description":"Single-stranded DNA-dependent 3-prime to 5-prime ATP-dependent helicase complex which binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. Also has 5-prime-deoxyribose-5-phosphate lyase activity, nicking DNA 3-prime of an a basic site by a mechanism involving a Schiff base covalent intermediate with the a basic site. However, its main function appears to be the recruitment of several factors with enzymatic activities to DNA double stranded breaks (DSBs). Required for DSB repair, chromosome maintenance, transcription regulation, V(D)J recombination, and activating DNA-PK.","predictedComplex":false,"interactors":[{"ac":"EBI-353208","identifier":"P12956","identifierLink":"https://www.uniprot.org/uniprotkb/P12956/entry","name":"XRCC6","description":"X-ray repair cross-complementing protein 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12604","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357997","identifier":"P13010","identifierLink":"https://www.uniprot.org/uniprotkb/P13010/entry","name":"XRCC5","description":"X-ray repair cross-complementing protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12604","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1994","complexName":"6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2 complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the synthesis and degradation of fructose 2,6-bisphosphate, therefore required for both glycolysis and gluconeogenesis. 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Regulated in the long term at the transcriptional level but the acute response may be controlled by phosphorylation.","predictedComplex":false,"interactors":[{"ac":"EBI-764464","identifier":"Q16875","identifierLink":"https://www.uniprot.org/uniprotkb/Q16875/entry","name":"PFKFB3","description":"6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10606","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1996","complexName":"6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 4 complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the synthesis and degradation of fructose 2,6-bisphosphate, therefore required for both glycolysis and gluconeogenesis. Regulated in the long term at the transcriptional level but the acute response may be controlled by phosphorylation.","predictedComplex":false,"interactors":[{"ac":"EBI-764534","identifier":"Q16877","identifierLink":"https://www.uniprot.org/uniprotkb/Q16877/entry","name":"PFKFB4","description":"6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10606","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1997","complexName":"6-phosphofructokinase, M4 homotetramer","organismName":"Homo sapiens; 9606","description":"Catalyzes the phosphorylation of fructose 6-phosphate to fructose 1,6-bisphosphate in the presence of MgATP, the first irreversible step for glycolysis. 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Complex formation enables substrate binding to the kinase, leads to a rearrangement of the catalytic site and exposes Thr-172 of CDK4 for phosphorylation and subsequent activation.","predictedComplex":false,"interactors":[{"ac":"EBI-295644","identifier":"P11802","identifierLink":"https://www.uniprot.org/uniprotkb/P11802/entry","name":"CDK4","description":"Cyclin-dependent kinase 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-375001","identifier":"P24385","identifierLink":"https://www.uniprot.org/uniprotkb/P24385/entry","name":"CCND1","description":"G1/S-specific cyclin-D1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2011","complexName":"Cyclin D2-CDK4 complex","organismName":"Homo sapiens; 9606","description":"Cyclin-dependent protein kinase complex. 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Complex formation enables substrate binding to the kinase, leads to a rearrangement of the catalytic site and exposes Thr-172 of CDK4 for phosphorylation and subsequent activation.","predictedComplex":false,"interactors":[{"ac":"EBI-295644","identifier":"P11802","identifierLink":"https://www.uniprot.org/uniprotkb/P11802/entry","name":"CDK4","description":"Cyclin-dependent kinase 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-375013","identifier":"P30281","identifierLink":"https://www.uniprot.org/uniprotkb/P30281/entry","name":"CCND3","description":"G1/S-specific cyclin-D3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2013","complexName":"Cyclin D3-CDK6 complex","organismName":"Homo sapiens; 9606","description":"Cyclin-dependent protein kinase complex. Required for G1 to S phase transition of the mitotic cell cycle. Phosphorylation of Rb proteins by cyclin D:CDK6 complexes leads to their partial inactivation which allows transcription of E2F-controlled genes such as cyclin E1, which activates the downstream Cdk2 kinase. 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Overexpression enhances S phase entry consistent with an oncogenic function. Complex formation enables substrate binding to the kinase, leads to a rearrangement of the catalytic site and exposes Thr-160 of CDK2 for phosphorylation and subsequent activation.","predictedComplex":false,"interactors":[{"ac":"EBI-846963","identifier":"Q61456","identifierLink":"https://www.uniprot.org/uniprotkb/Q61456/entry","name":"Ccna1","description":"Cyclin-A1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-847048","identifier":"P97377","identifierLink":"https://www.uniprot.org/uniprotkb/P97377/entry","name":"Cdk2","description":"Cyclin-dependent kinase 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2066","complexName":"Cyclin A2-CDK2 complex","organismName":"Mus musculus; 10090","description":"Required in G1 phase of cell cycle. Complex formation enables substrate binding to the kinase, leads to a rearrangement of the catalytic site and exposes Thr-160 of CDK2 for phosphorylation and subsequent activation.","predictedComplex":false,"interactors":[{"ac":"EBI-846980","identifier":"P51943","identifierLink":"https://www.uniprot.org/uniprotkb/P51943/entry","name":"Ccna2","description":"Cyclin-A2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-847048","identifier":"P97377","identifierLink":"https://www.uniprot.org/uniprotkb/P97377/entry","name":"Cdk2","description":"Cyclin-dependent kinase 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2067","complexName":"Cyclin A1-CDK2 complex","organismName":"Rattus norvegicus; 10116","description":"Essential for spermatogenesis, essential for passage of spermatocytes into meiosis I. Overexpression enhances S phase entry consistent with an oncogenic function. Complex formation enables substrate binding to the kinase, leads to a rearrangement of the catalytic site and exposes Thr-160 of CDK2 for phosphorylation and subsequent activation.","predictedComplex":false,"interactors":[{"ac":"EBI-847009","identifier":"Q6AY13","identifierLink":"https://www.uniprot.org/uniprotkb/Q6AY13/entry","name":"Ccna1","description":"Cyclin-A1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-847090","identifier":"Q63699","identifierLink":"https://www.uniprot.org/uniprotkb/Q63699/entry","name":"Cdk2","description":"Cyclin-dependent kinase 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2068","complexName":"Cyclin A2-CDK2 complex","organismName":"Rattus norvegicus; 10116","description":"Required in G1 phase of cell cycle. Complex formation enables substrate binding to the kinase, leads to a rearrangement of the catalytic site and exposes Thr-160 of CDK2 for phosphorylation and subsequent activation.","predictedComplex":false,"interactors":[{"ac":"EBI-847029","identifier":"Q6GX89","identifierLink":"https://www.uniprot.org/uniprotkb/Q6GX89/entry","name":"q6gx89","description":"Cyclin-A2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-847090","identifier":"Q63699","identifierLink":"https://www.uniprot.org/uniprotkb/Q63699/entry","name":"Cdk2","description":"Cyclin-dependent kinase 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2069","complexName":"Cyclin B1-CDK1 complex","organismName":"Mus musculus; 10090","description":"Required for G2 to M phase transition of the mitotic cell cycle. Complex formation enables substrate binding to the kinase, leads to a rearrangement of the catalytic site and exposes Thr-161 of CDK1 for phosphorylation and subsequent activation.","predictedComplex":false,"interactors":[{"ac":"EBI-846949","identifier":"P11440","identifierLink":"https://www.uniprot.org/uniprotkb/P11440/entry","name":"Cdk1","description":"Cyclin-dependent kinase 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-847125","identifier":"P24860","identifierLink":"https://www.uniprot.org/uniprotkb/P24860/entry","name":"Ccnb1","description":"G2/mitotic-specific cyclin-B1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2070","complexName":"Cyclin B2-CDK1 complex","organismName":"Mus musculus; 10090","description":"Required for G2 to M phase transition of the mitotic cell cycle. Complex formation enables substrate binding to the kinase, leads to a rearrangement of the catalytic site and exposes Thr-161 of CDK1 for phosphorylation and subsequent activation.","predictedComplex":false,"interactors":[{"ac":"EBI-846949","identifier":"P11440","identifierLink":"https://www.uniprot.org/uniprotkb/P11440/entry","name":"Cdk1","description":"Cyclin-dependent kinase 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-847150","identifier":"P30276","identifierLink":"https://www.uniprot.org/uniprotkb/P30276/entry","name":"Ccnb2","description":"G2/mitotic-specific cyclin-B2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2071","complexName":"Cyclin B3-CDK2 complex","organismName":"Mus musculus; 10090","description":"Required for G2 to M phase transition of the mitotic cell cycle. Complex formation enables substrate binding to the kinase, leads to a rearrangement of the catalytic site and exposes Thr-161 of CDK2 for phosphorylation and subsequent activation.","predictedComplex":false,"interactors":[{"ac":"EBI-847048","identifier":"P97377","identifierLink":"https://www.uniprot.org/uniprotkb/P97377/entry","name":"Cdk2","description":"Cyclin-dependent kinase 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-847168","identifier":"Q810T2","identifierLink":"https://www.uniprot.org/uniprotkb/Q810T2/entry","name":"Ccnb3","description":"G2/mitotic-specific cyclin-B3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2072","complexName":"Cyclin B1-CDK1 complex","organismName":"Rattus norvegicus; 10116","description":"Required for G2 to M phase transition of the mitotic cell cycle. Complex formation enables substrate binding to the kinase, leads to a rearrangement of the catalytic site and exposes Thr-161 of CDK1 for phosphorylation and subsequent activation.","predictedComplex":false,"interactors":[{"ac":"EBI-847001","identifier":"P39951","identifierLink":"https://www.uniprot.org/uniprotkb/P39951/entry","name":"Cdk1","description":"Cyclin-dependent kinase 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-847197","identifier":"P30277","identifierLink":"https://www.uniprot.org/uniprotkb/P30277/entry","name":"Ccnb1","description":"G2/mitotic-specific cyclin-B1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2073","complexName":"Cyclin D1-CDK4 complex","organismName":"Mus musculus; 10090","description":"Required for G1 to S phase transition of the mitotic cell cycle. Phosphorylation of Rb proteins by cyclin D:CDK4 complexes leads to their partial inactivation which allows transcription of E2F-controlled genes such as cyclin E1, which activates the downstream Cdk2 kinase. Complex formation enables substrate binding to the kinase, leads to a rearrangement of the catalytic site and exposes Thr-172 of CDK4 for phosphorylation and subsequent activation.","predictedComplex":false,"interactors":[{"ac":"EBI-847225","identifier":"P30285","identifierLink":"https://www.uniprot.org/uniprotkb/P30285/entry","name":"Cdk4","description":"Cyclin-dependent kinase 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-847243","identifier":"P25322","identifierLink":"https://www.uniprot.org/uniprotkb/P25322/entry","name":"Ccnd1","description":"G1/S-specific cyclin-D1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2074","complexName":"Cyclin D2-CDK4 complex","organismName":"Mus musculus; 10090","description":"Required for G1 to S phase transition of the mitotic cell cycle. Phosphorylation of Rb proteins by cyclin D:CDK4 complexes leads to their partial inactivation which allows transcription of E2F-controlled genes such as cyclin E1, which activates the downstream Cdk2 kinase. Complex formation enables substrate binding to the kinase, leads to a rearrangement of the catalytic site and exposes Thr-172 of CDK4 for phosphorylation and subsequent activation.","predictedComplex":false,"interactors":[{"ac":"EBI-847225","identifier":"P30285","identifierLink":"https://www.uniprot.org/uniprotkb/P30285/entry","name":"Cdk4","description":"Cyclin-dependent kinase 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-847269","identifier":"P30280","identifierLink":"https://www.uniprot.org/uniprotkb/P30280/entry","name":"Ccnd2","description":"G1/S-specific cyclin-D2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2816","complexName":"CRL4-DCAF8 E3 ubiquitin ligase complex, CUL4B variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor DCAF8. The complex is active in epigenetic regulation through the ubiquitination and subsequent destruction of the HELLS lymphoid-specific helicase (Q9NRZ9) and DNMT3A cysteine methyltransferase DNMT3A (Q9Y6K1).","predictedComplex":false,"interactors":[{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456067","identifier":"Q13620","identifierLink":"https://www.uniprot.org/uniprotkb/Q13620/entry","name":"CUL4B","description":"Cullin-4B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-740686","identifier":"Q5TAQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q5TAQ9/entry","name":"DCAF8","description":"DDB1- and CUL4-associated factor 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15574","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2817","complexName":"CRL4-DCAF10 E3 ubiquitin ligase complex, CUL4A variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor DCAF10. The complex is active in the activation of the caspase‐dependent apoptosis pathway through the ubiquitination and subsequent degradation of BCL-2 family member MCL1 (Q07820).","predictedComplex":false,"interactors":[{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456106","identifier":"Q13619","identifierLink":"https://www.uniprot.org/uniprotkb/Q13619/entry","name":"CUL4A","description":"Cullin-4A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-723230","identifier":"Q5QP82","identifierLink":"https://www.uniprot.org/uniprotkb/Q5QP82/entry","name":"DCAF10","description":"DDB1- and CUL4-associated factor 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2818","complexName":"CRL4-DCAF8 E3 ubiquitin ligase complex, CUL4A variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor DCAF8. The complex is active in epigenetic regulation through the ubiquitination and subsequent destruction of the HELLS lymphoid-specific helicase (Q9NRZ9) and DNMT3A cysteine methyltransferase DNMT3A (Q9Y6K1).","predictedComplex":false,"interactors":[{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456106","identifier":"Q13619","identifierLink":"https://www.uniprot.org/uniprotkb/Q13619/entry","name":"CUL4A","description":"Cullin-4A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-740686","identifier":"Q5TAQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q5TAQ9/entry","name":"DCAF8","description":"DDB1- and CUL4-associated factor 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15574","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2819","complexName":"CRL4-DCAF10 E3 ubiquitin ligase complex, CUL4B variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor DCAF10. The complex is active in the activation of the caspase‐dependent apoptosis pathway through the ubiquitination and subsequent degradation of BCL-2 family member MCL1 (Q07820).","predictedComplex":false,"interactors":[{"ac":"EBI-350322","identifier":"Q16531","identifierLink":"https://www.uniprot.org/uniprotkb/Q16531/entry","name":"DDB1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456067","identifier":"Q13620","identifierLink":"https://www.uniprot.org/uniprotkb/Q13620/entry","name":"CUL4B","description":"Cullin-4B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-723230","identifier":"Q5QP82","identifierLink":"https://www.uniprot.org/uniprotkb/Q5QP82/entry","name":"DCAF10","description":"DDB1- and CUL4-associated factor 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2820","complexName":"COPI vesicle coat complex","organismName":"Drosophila melanogaster; 7227","description":"Coats vesicles which bud from the Golgi membrane and subsequently transport proteins from the cis end of the Golgi complex back to the rough endoplasmic reticulum (ER), where they were originally synthesized (retrograde transport), and between Golgi compartments. The complex binds to di-lysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi to the trans Golgi network. Cargo containing the sorting motifs KKXX and KXKXX interact with COPI to form carriers.","predictedComplex":false,"interactors":[{"ac":"EBI-122274","identifier":"P45437","identifierLink":"https://www.uniprot.org/uniprotkb/P45437/entry","name":"betaCOP","description":"Coatomer subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10635","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-123053","identifier":"P61209","identifierLink":"https://www.uniprot.org/uniprotkb/P61209/entry","name":"Arf1","description":"ADP-ribosylation factor 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11711","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-132855","identifier":"O62621","identifierLink":"https://www.uniprot.org/uniprotkb/O62621/entry","name":"beta'COP","description":"Coatomer subunit beta'","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19876","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-146110","identifier":"Q8I0G5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8I0G5/entry","name":"gammaCOP","description":"Coatomer subunit gamma","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10261","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-171121","identifier":"Q9W0B8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W0B8/entry","name":"alphaCOP","description":"Coatomer subunit alpha","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19876","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-185365","identifier":"Q9VV89","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VV89/entry","name":"zetaCOP","description":"Coatomer subunit zeta","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11043","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-85593","identifier":"Q9Y0Y5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y0Y5/entry","name":"epsilonCOP","description":"Coatomer subunit epsilon","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10805","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-90398","identifier":"Q9W555","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W555/entry","name":"deltaCOP","description":"Coatomer subunit delta","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10121","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2821","complexName":"USH2 complex","organismName":"Homo sapiens; 9606","description":"Required for cochlear stereociliary bundle development. essential for stereociliary diameter and differentiation in inner ear hair cells and for stereociliary rigidity and V-shaped three-row organization in outer ear hair cells. Form ankle links, thin fibers that connect the bases of neighboring stereocilia and only exist during development. Defects in the complex result in disorganization of the stereocilia bundle. The complex may also form in photo receptors although the presence of PDZD7 has not been proven in that location.","predictedComplex":false,"interactors":[{"ac":"EBI-20859318","identifier":"Q9H5P4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H5P4/entry","name":"PDZD7","description":"PDZ domain-containing protein 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23116","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-310886","identifier":"Q9P202","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P202/entry","name":"WHRN","description":"Whirlin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23116","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7851128","identifier":"Q8WXG9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WXG9/entry","name":"ADGRV1","description":"Adhesion G-protein coupled receptor V1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46682","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9996372","identifier":"O75445","identifierLink":"https://www.uniprot.org/uniprotkb/O75445/entry","name":"USH2A","description":"Usherin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2823","complexName":"NUBP1-NUBP2 iron-sulfur cluster assembly scaffold complex","organismName":"Homo sapiens; 9606","description":"Scaffold complex that assembles nascent FeS clusters as part of the iron-sulfur cluster (ISC)/cytosolic iron–sulfur protein assembly (CIA) assembly system, which generates and inserts [4Fe-4S] (CHEBI:49883) clusters to both cytosolic and nuclear Fe/S proteins.  Assembly of a [4Fe-4S] cluster requires interaction with the BOLA2-GLRX3 iron-sulfur cluster assembly complex (CPX-6861).","predictedComplex":false,"interactors":[{"ac":"EBI-1048886","identifier":"Q9Y5Y2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5Y2/entry","name":"NUBP2","description":"Cytosolic Fe-S cluster assembly factor NUBP2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-7391727","identifier":"P53384","identifierLink":"https://www.uniprot.org/uniprotkb/P53384/entry","name":"NUBP1","description":"Cytosolic Fe-S cluster assembly factor NUBP1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2824","complexName":"ADA complex","organismName":"Drosophila melanogaster; 7227","description":"Chromatin remodelling complex that primarily acetylates nucleosomal  histones, preferentially histone H3 and nucleosomal substrates, thus regulating transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-139086","identifier":"Q9VTZ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VTZ1/entry","name":"Gcn5","description":"histone acetyltransferase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45750","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2912837","identifier":"Q9W2I4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W2I4/entry","name":"Sgf29","description":"SAGA-associated factor 29kDa","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21539","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30858590","identifier":"M9PHZ1","identifierLink":"https://www.uniprot.org/uniprotkb/M9PHZ1/entry","name":"Ada3","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13556","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30876449","identifier":"Q8I8V0-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8I8V0-1/entry","name":"Ada2b","description":"Transcriptional adapter 2b","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]}]},{"complexAC":"CPX-2825","complexName":"ESCRT-0 complex, STAM variant","organismName":"Homo sapiens; 9606","description":"The ESCRT machinery, consisting of ESCRT-0  (this complex), -I, -II (CPX-2506), -III (CPX-329) and -IV (VPS4A/B complex, CPX-338)  has been implicated in membrane scission steps, transforming a single, continuous bilayer into two distinct bilayers, either from within the neck of a vesicle budding away from the cytoplasm or from within a membrane tubule, while segregating cargo throughout the process. Membrane fission processes include: a) the sorting of multivesicular bodies (MVB) in the endocytic pathway; cargoes destined for inclusion into the MVB pathway are covalently modified with ubiquitin, recognized by ubiquitin-binding domains in the early ESCRTs (ESCRT-0, -I, and -II) and sequestered into endosomal microdomains that bud into the endosome as intralumenal vesicles aided by ESCRT-III, b) downregulation of cell-surface receptors, c) repair of plasma membrane wounds, d) abscission of the cellular bridge during cytokineses, d) nuclear envelope sealing by annular fusion and e) budding of virions (especially HIV-1) from the plasma membrane. The ESCRT machinery seems to play an indirect role in the proper functioning of cellular polarity and migration, the miRNA machinery and gene expression regulation. ESCRT-0 binds to and clusters ubiquitinated cargo for delivery into MVBs, and recruits clathrin, ubiquitin ligases, and deubiquitinating enzymes. ESCRT-0 recruits ESCRT-I which engages ESCRT-II to nucleate ESCRT-III polymerization. VPS4A/B complex, also known as ESCRT-IV, disassembles ESCRT-III to recycle its subunits. The ESCRT-III complex facilitates changes in membrane architecture by oligomerizing to form spiral, filament-like tubules, accumulation of which is associated with membrane constriction and fission. Disassembly of ESCRT-III by VPS4A/B may be a required step for fission.","predictedComplex":false,"interactors":[{"ac":"EBI-740220","identifier":"O14964","identifierLink":"https://www.uniprot.org/uniprotkb/O14964/entry","name":"HGS","description":"Hepatocyte growth factor-regulated tyrosine kinase substrate","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46275","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752333","identifier":"Q92783","identifierLink":"https://www.uniprot.org/uniprotkb/Q92783/entry","name":"STAM","description":"Signal transducing adapter molecule 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45929","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2827","complexName":"SMG1C protein kinase complex","organismName":"Homo sapiens; 9606","description":"Forms to modulate the protein kinase activity of SMG1. When active, SMG1 mediates phosphorylation of the RNA helicase UPF1 (Q92900), a key player in the nonsense-mediated decay pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-1049832","identifier":"Q96Q15","identifierLink":"https://www.uniprot.org/uniprotkb/Q96Q15/entry","name":"SMG1","description":"Serine/threonine-protein kinase SMG1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2872322","identifier":"Q9H0W8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H0W8/entry","name":"SMG9","description":"Nonsense-mediated mRNA decay factor SMG9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14270","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3903643","identifier":"Q8ND04","identifierLink":"https://www.uniprot.org/uniprotkb/Q8ND04/entry","name":"SMG8","description":"Nonsense-mediated mRNA decay factor SMG8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13091","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2828","complexName":"F-actin capping protein complex","organismName":"Drosophila melanogaster; 7227","description":"Caps the barbed end of the actin filament  in a Ca(2+)-independent manner thereby blocking the exchange of subunits at these ends. The complex is an essential component for the reconstitution of movement powered by actin polymerization and is important for actin assembly and cell motility.","predictedComplex":false,"interactors":[{"ac":"EBI-173404","identifier":"Q9W2N0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W2N0/entry","name":"cpa","description":"F-actin-capping protein subunit alpha","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10653","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-95160","identifier":"P48603","identifierLink":"https://www.uniprot.org/uniprotkb/P48603/entry","name":"cpb","description":"F-actin-capping protein subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2829","complexName":"ACF chromatin remodeling complex","organismName":"Drosophila melanogaster; 7227","description":"An ATP-dependent chromatin remodeling complex, that regulates the even spacing of nucleosomes along the chromatin thus promoting chromatin assembly and the repression of transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-196350","identifier":"Q9V9T4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V9T4/entry","name":"Acf","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46510","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-367628","identifier":"Q24368","identifierLink":"https://www.uniprot.org/uniprotkb/Q24368/entry","name":"Iswi","description":"Chromatin-remodeling complex ATPase chain Iswi","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2830","complexName":"7SK small nuclear ribonuclearprotein","organismName":"Drosophila melanogaster; 7227","description":"Plays a central role in RNA polymerase II elongation control by sequestering positive transcription elongation factor complex b (P-TEFb, CPX-2432) and therefore regulating the availability of active P-TEFb.","predictedComplex":false,"interactors":[{"ac":"EBI-180984","identifier":"Q7K480","identifierLink":"https://www.uniprot.org/uniprotkb/Q7K480/entry","name":"bin3","description":"7SK snRNA methylphosphate capping enzyme bin3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12315","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2508506","identifier":"Q9W362","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W362/entry","name":"Larp7","description":"La-related protein 7","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22792","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30858244","identifier":"Q8INF6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8INF6/entry","name":"Hexim","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13469","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30858272","identifier":"URS00007F2EC7_7227","identifierLink":"http://rnacentral.org/rna/URS00007F2EC7_7227","name":"7sk_drome_snrna","description":"7SK small nuclear RNA","stochiometry":null,"interactorType":"nucleic acid","organismName":"Drosophila melanogaster; 7227","xrefs":[]}]},{"complexAC":"CPX-2831","complexName":"ISCA1-ISCA2 mitochondrial iron-sulfur protein assembly complex","organismName":"Homo sapiens; 9606","description":"Assembles [4Fe-4S] clusters from reductive coupling of two [2Fe-2S] clusters received from GLRX5 complexes (CPX-6862, CPX-6863). The [4Fe-4S] clusters can then be inserted into mitochondrial [4Fe-4S]-requiring proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-10258659","identifier":"Q86U28","identifierLink":"https://www.uniprot.org/uniprotkb/Q86U28/entry","name":"ISCA2","description":"Iron-sulfur cluster assembly 2 homolog, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43011","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2866528","identifier":"Q9BUE6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BUE6/entry","name":"ISCA1","description":"Iron-sulfur cluster assembly 1 homolog, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10072","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2832","complexName":"SCF E3 ubiquitin ligase complex, KDM2B variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3955564","identifier":"Q8NHM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NHM5/entry","name":"KDM2B","description":"Lysine-specific demethylase 2B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23123","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2833","complexName":"Camalexin biosynthetic metabolon complex","organismName":"Arabidopsis thaliana; 3702","description":"Required for the biosynthesis of camalexin (3-thiazol-2-yl-indole, CHEBI:22990), a phytoalexin defense compound, from tryptophan. CYP79B2 converts tryptophan to indole-3-acetaldoxime, CYP71A13 then catalyzes the conversion of indole-3-acetaldoxime to indole-3-acetonitrile (IAN). The  glutathionylation of IAN (GS-IAN) is driven by GSTU4, GS-IAN is converted to Cys(IAN), a process involving GPP1 (F4JTE7) which is recruited to this complex. CYP71B15 catalyzes two reactions, the formation of dihydrocamalexate from a indole-3-acetonitrile-cysteine conjugate and the oxidative decarboxylation of dihydrocamalexate which is the final step in camalexin biosynthesis. ATR  is required for electron transfer from NADP to cytochrome P450. Camalexin has anti bacterial and anti-fungal pathogen properties.","predictedComplex":false,"interactors":[{"ac":"EBI-1239078","identifier":"O81346","identifierLink":"https://www.uniprot.org/uniprotkb/O81346/entry","name":"CYP79B2","description":"Tryptophan N-monooxygenase 1","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR24298","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16915951","identifier":"Q9LW27","identifierLink":"https://www.uniprot.org/uniprotkb/Q9LW27/entry","name":"CYP71B15","description":"Bifunctional dihydrocamalexate synthase/camalexin synthase","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR47956","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2356153","identifier":"O49342","identifierLink":"https://www.uniprot.org/uniprotkb/O49342/entry","name":"CYP71A13","description":"Indoleacetaldoxime dehydratase","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR47956","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30855500","identifier":"O49340","identifierLink":"https://www.uniprot.org/uniprotkb/O49340/entry","name":"CYP71A12","description":"Cytochrome P450 71A12","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR47956","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30856456","identifier":"Q9ZW27","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ZW27/entry","name":"GSTU4","description":"Glutathione S-transferase U4","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11260","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30856493","identifier":"Q9SB48","identifierLink":"https://www.uniprot.org/uniprotkb/Q9SB48/entry","name":"ATR1","description":"NADPH--cytochrome P450 reductase 1","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR19384","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9663515","identifier":"CHEBI:58210","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58210","name":"fmn(3-)","description":"FMN(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2837","complexName":"CIAO1-CIAO2B-CIAO3-MMS19 cytosolic iron-sulfur protein assembly complex","organismName":"Homo sapiens; 9606","description":"Transfers [4Fe-4S] clusters assembled on the NUBP1-NUBP2 Fe-S cluster assembly scaffold complex (CPX-2823) on to cytosolic and/ or nuclear Fe/S proteins. CIAO3 receives the [4Fe-4S] cluster from the scaffold complex and then binds to the CIAO2B-CIAO1-MMS19 heterotrimer. Responsible for the maturation of many cytosolic proteins, such as DPYD (Q12882) and also transfers the Fe-S clusters to nuclear Fe-S proteins, such as POLD1 (P28340), the DNA helicase XPD (P18074) and RTEL1 (Q9NZ71)","predictedComplex":false,"interactors":[{"ac":"EBI-1044169","identifier":"Q96T76","identifierLink":"https://www.uniprot.org/uniprotkb/Q96T76/entry","name":"MMS19","description":"MMS19 nucleotide excision repair protein homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12891","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10977788","identifier":"Q9H6Q4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H6Q4/entry","name":"CIAO3","description":"Cytosolic iron-sulfur assembly component 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-725145","identifier":"O76071","identifierLink":"https://www.uniprot.org/uniprotkb/O76071/entry","name":"CIAO1","description":"Probable cytosolic iron-sulfur protein assembly protein CIAO1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19920","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744045","identifier":"Q9Y3D0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3D0/entry","name":"CIAO2B","description":"Cytosolic iron-sulfur assembly component 2B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12377","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2838","complexName":"3M complex","organismName":"Homo sapiens; 9606","description":"Core component of one of more ubiquitin ligases which play a role in maintaining microtubule and genome integrity. Known substrates include PHLDB2 (Q86SQ0) which is involved in the regulation of focal adhesion. The core complex binds additional proteins, including RBX1 (P62877) which confers E3 ubiquitin ligase activity, and also FBXW8 (Q8N3Y1) and ANKRA2 (Q9H9E1) which may give substrate specificity or themselves be substrates.","predictedComplex":false,"interactors":[{"ac":"EBI-1223896","identifier":"O75147","identifierLink":"https://www.uniprot.org/uniprotkb/O75147/entry","name":"OBSL1","description":"Obscurin-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR35971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-308606","identifier":"Q14999","identifierLink":"https://www.uniprot.org/uniprotkb/Q14999/entry","name":"CUL7","description":"Cullin-7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22771","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5236005","identifier":"Q9H0W5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H0W5/entry","name":"CCDC8","description":"Coiled-coil domain-containing protein 8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47741","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2840","complexName":"CIAO1-CIAO2A-CIAO3 cytosolic iron-sulfur protein assembly complex","organismName":"Homo sapiens; 9606","description":"Transfers [4Fe-4S] clusters assembled on the NUBP1-NUBP2 Fe-S cluster assembly scaffold complex (CPX-2823) on to cytosolic and/ or nuclear Fe/S proteins. CIAO3 receives the [4Fe-4S] cluster from the scaffold complex and then binds to the CIAO2A-CIAO1 heterodimer. May act to regulate ACO1 (P21399), a bifunctional iron sensor.","predictedComplex":false,"interactors":[{"ac":"EBI-10977788","identifier":"Q9H6Q4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H6Q4/entry","name":"CIAO3","description":"Cytosolic iron-sulfur assembly component 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-725145","identifier":"O76071","identifierLink":"https://www.uniprot.org/uniprotkb/O76071/entry","name":"CIAO1","description":"Probable cytosolic iron-sulfur protein assembly protein CIAO1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19920","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752069","identifier":"Q9H5X1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H5X1/entry","name":"CIAO2A","description":"Cytosolic iron-sulfur assembly component 2A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12377","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2841","complexName":"GRX6 iron-sulfur cluster assembly homodimer complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Reversibly binds [2Fe-2S] clusters and appears to play a role in Fe-S cluster assembly and trafficking, and in transferring an intact [2Fe-2S] cluster to an apo acceptor protein.","predictedComplex":false,"interactors":[{"ac":"EBI-10824516","identifier":"CHEBI:16856","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16856","name":"glutathione","description":"glutathione","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-25647592","identifier":"CHEBI:33737","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:33737","name":"di-mu-sulfido-diiron(2+)","description":"di-mu-sulfido-diiron(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-27068373","identifier":"Q12438","identifierLink":"https://www.uniprot.org/uniprotkb/Q12438/entry","name":"GRX6","description":"Monothiol glutaredoxin-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45694","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2842","complexName":"Mitochondrial degradosome complex","organismName":"Homo sapiens; 9606","description":"Plays an essential role in mitochondrial RNA turnover, degrading structured RNA  in an ATP-dependent manner. SUPV3L1 unwind double-stranded RNA, DNA-RNA, or  double-stranded DNA, and PNPT1 then promotes 3′-5′ degradation of the RNA molecules. Also counteracts deleterious R loops at specific hybrid-prone regions in the mitochondrial genome.","predictedComplex":false,"interactors":[{"ac":"EBI-1052020","identifier":"Q8TCS8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TCS8/entry","name":"PNPT1","description":"Polyribonucleotide nucleotidyltransferase 1, mitochondrial","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11252","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2876787","identifier":"Q8IYB8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IYB8/entry","name":"SUPV3L1","description":"ATP-dependent RNA helicase SUPV3L1, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2843","complexName":"Ferrichrome outer membrane transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"A member of the TonB-dependent transporter family (TBDTs) which binds and then transports hydroxamate siderophore ferrichrome (a ferric ion chelator) across the outer membrane. Sideraphore transport requires an outer membrane receptor (fhuA), which is relatively specific for its ligand. The ligand-bound receptor then physically interacts with the TonB protein. TBDTs are energy-dependent gated channels that usually transport large metal complexes which cannot fit through porins, and are too scarce to enter by mass-action-driven transport. Energy-dependent uptake through TBDTs requires interaction with tonB in complex with exbB and exbD in the inner membrane, ExbBD. TonB undergoes rapid energized movement driven by ExbBD which harvests the electrochemical force from the electrochemical proton gradient created by the proton gradient across the inner membrane and convert it into rotational motion. Hence, TonB may pull or twist the N-termini of TBDTs to promote transport of substrates into the periplasm. ATP-binding-cassette (ABC) transporters subsequently move the ferrichrome (Fe3+) through the periplasm and inner membrane. Also transports the antibiotic albomycin, a structural analog of ferrichrome, and acts as a receptor for colicin M, microcin J25 and bacteriophages T1, T5, phi80 and UC-1","predictedComplex":false,"interactors":[{"ac":"EBI-1116714","identifier":"P06971","identifierLink":"https://www.uniprot.org/uniprotkb/P06971/entry","name":"fhuA","description":"Ferrichrome outer membrane transporter/phage receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32552","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6399986","identifier":"P0ABU7","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABU7/entry","name":"exbB","description":"Biopolymer transport protein ExbB","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6399993","identifier":"P02929","identifierLink":"https://www.uniprot.org/uniprotkb/P02929/entry","name":"tonB","description":"Protein TonB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33446","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6417016","identifier":"P0ABV2","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABV2/entry","name":"exbD","description":"Biopolymer transport protein ExbD","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2844","complexName":"paaABCE phenylacetyl-CoA monooxygenase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Mono-oxygenase which converts phenylacetate (PA)-CoA to its 1,2-epoxide derivative, ring 1,2-epoxyphenylacetyl-CoA, as part of the PA utilization pathway, the main mechanism for degradation of a variety of organic compounds. Also catalyzes the reverse deoxygenation reaction (distinguish from dioxygenation), in which 2H+ equivalents are used to yield phenylacetyl-CoA and water when toxic epoxides accumulates due to inadequate processing by the downstream enzymes paaG (P77467) and paaZ (P77455).","predictedComplex":false,"interactors":[{"ac":"EBI-11172266","identifier":"CHEBI:49601","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49601","name":"fe2s2 iron-sulfur cluster","description":"Fe2S2 iron-sulfur cluster","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1119536","identifier":"P76077","identifierLink":"https://www.uniprot.org/uniprotkb/P76077/entry","name":"paaA","description":"1,2-phenylacetyl-CoA epoxidase, subunit A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30458","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1123811","identifier":"P76078","identifierLink":"https://www.uniprot.org/uniprotkb/P76078/entry","name":"paaB","description":"1,2-phenylacetyl-CoA epoxidase, subunit B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-1130833","identifier":"P76081","identifierLink":"https://www.uniprot.org/uniprotkb/P76081/entry","name":"paaE","description":"1,2-phenylacetyl-CoA epoxidase, subunit E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR47354","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1131666","identifier":"P76079","identifierLink":"https://www.uniprot.org/uniprotkb/P76079/entry","name":"paaC","description":"1,2-phenylacetyl-CoA epoxidase, subunit C","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30458","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11472102","identifier":"CHEBI:24875","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:24875","name":"iron cation","description":"iron cation","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2845","complexName":"LKB1-STRAD-MO25 serine/threonine protein kinase complex, CAB39-STRADA variant","organismName":"Homo sapiens; 9606","description":"Directly phosphorylates adenosine monophosphate-activated protein kinase (AMPK) family members on the T-loop thereby activating them.  Couples cellular growth and division to the availability of cellular energy. by activating the AMP kinases when energy levels are low, inhibiting signalling pathways that promote proliferation","predictedComplex":false,"interactors":[{"ac":"EBI-1109114","identifier":"Q7RTN6","identifierLink":"https://www.uniprot.org/uniprotkb/Q7RTN6/entry","name":"STRADA","description":"STE20-related kinase adapter protein alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48014","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-306838","identifier":"Q15831","identifierLink":"https://www.uniprot.org/uniprotkb/Q15831/entry","name":"STK11","description":"Serine/threonine-protein kinase STK11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43895","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-306905","identifier":"Q9Y376","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y376/entry","name":"CAB39","description":"Calcium-binding protein 39","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10182","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2846","complexName":"PeBoW complex","organismName":"Homo sapiens; 9606","description":"Role in coordinating ribosome biogenesis with cell cycle progression, required for pre-rRNA processing  and the maturation of the 60S ribosomal subunit. Forms an extensive protein-protein and protein-RNA interaction network within early ribosome assembly intermediates in the nucleolus, thereby potentially serving as a hub for stabilizing or remodeling ribonucleoprotein neighborhoods during 60S subunit biogenesis","predictedComplex":false,"interactors":[{"ac":"EBI-1050828","identifier":"Q14137","identifierLink":"https://www.uniprot.org/uniprotkb/Q14137/entry","name":"BOP1","description":"Ribosome biogenesis protein BOP1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR17605","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1053271","identifier":"O00541","identifierLink":"https://www.uniprot.org/uniprotkb/O00541/entry","name":"PES1","description":"Pescadillo homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12221","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2490660","identifier":"Q9GZL7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9GZL7/entry","name":"WDR12","description":"Ribosome biogenesis protein WDR12","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19855","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2847","complexName":"Signal peptidase complex, SEC11A variant","organismName":"Homo sapiens; 9606","description":"Catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. The complex cleaves the signal peptides of most secretory and many membrane proteins as soon as the lumenal domain of the translocating polypeptide is large enough to expose its cleavage site to the enzyme, during the translocation of the protein through the translocon pore into the endoplasmic reticulum. The complex specifically cleaves N- terminal signal peptides that contain a hydrophobic alpha-helix (h-region) shorter than 18-20 amino acids","predictedComplex":false,"interactors":[{"ac":"EBI-1042500","identifier":"P67812","identifierLink":"https://www.uniprot.org/uniprotkb/P67812/entry","name":"SEC11A","description":"Signal peptidase complex catalytic subunit SEC11A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10806","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1043352","identifier":"Q15005","identifierLink":"https://www.uniprot.org/uniprotkb/Q15005/entry","name":"SPCS2","description":"Signal peptidase complex subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13085","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6166040","identifier":"P61009","identifierLink":"https://www.uniprot.org/uniprotkb/P61009/entry","name":"SPCS3","description":"Signal peptidase complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12804","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8852196","identifier":"Q9Y6A9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6A9/entry","name":"SPCS1","description":"Signal peptidase complex subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13202","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2848","complexName":"TRMT11-TRM112 methyltransferase complex","organismName":"Homo sapiens; 9606","description":"Probable S-adenosyl-L-methionine-dependent tRNA methyltransferase complex.","predictedComplex":false,"interactors":[{"ac":"EBI-2515608","identifier":"Q7Z4G4","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z4G4/entry","name":"TRMT11","description":"tRNA (guanine(10)-N(2))-methyltransferase TRMT11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13370","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30813205","identifier":"CHEBI:59789","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:59789","name":"s-adenosyl-l-methionine zwitterion","description":"S-adenosyl-L-methionine zwitterion","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-373326","identifier":"Q9UI30","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UI30/entry","name":"TRMT112","description":"Multifunctional methyltransferase subunit TRM112-like protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12773","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2849","complexName":"CCR4-NOT mRNA deadenylase complex, CNOT6-CNOT8 variant","organismName":"Homo sapiens; 9606","description":"Major cellular mRNA deadenylase complex at least in part by  removing polyA tails that protect mRNA transcripts from degradation. Involved in the regulation of the cell cycle, chromatin modification, activation and inhibition of transcription initiation, control of transcription elongation, RNA export, nuclear RNA surveillance, and DNA damage repair in the nucleus. The CNOT4 ubiquitin ligase only weakly associates with the complex but is required for optimal deadenylation activity by the full CCR4-NOT complex.","predictedComplex":false,"interactors":[{"ac":"EBI-1054261","identifier":"Q9H9A5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H9A5/entry","name":"CNOT10","description":"CCR4-NOT transcription complex subunit 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12979","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1222758","identifier":"A5YKK6","identifierLink":"https://www.uniprot.org/uniprotkb/A5YKK6/entry","name":"CNOT1","description":"CCR4-NOT transcription complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13162","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2104458","identifier":"Q9C0C2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9C0C2/entry","name":"TNKS1BP1","description":"182 kDa tankyrase-1-binding protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22042","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2104530","identifier":"Q9ULM6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ULM6/entry","name":"CNOT6","description":"CCR4-NOT transcription complex subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12121","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2129291","identifier":"O95628","identifierLink":"https://www.uniprot.org/uniprotkb/O95628/entry","name":"CNOT4","description":"CCR4-NOT transcription complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12603","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2562014","identifier":"Q9UKZ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UKZ1/entry","name":"CNOT11","description":"CCR4-NOT transcription complex subunit 11","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15975","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357079","identifier":"Q92600","identifierLink":"https://www.uniprot.org/uniprotkb/Q92600/entry","name":"CNOT9","description":"CCR4-NOT transcription complex subunit 9","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12262","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742299","identifier":"Q9UFF9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UFF9/entry","name":"CNOT8","description":"CCR4-NOT transcription complex subunit 8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10797","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743033","identifier":"Q9NZN8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZN8/entry","name":"CNOT2","description":"CCR4-NOT transcription complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 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-2","xrefs":[]}]},{"complexAC":"CPX-2850","complexName":"METTL5-TRM112 methyltransferase complex","organismName":"Homo sapiens; 9606","description":"S-adenosylmethionine-dependent methyltransferase which catalyzes the N6-methyl-adenine (m6A) modification at position 1832 of 18S rRNA m6A modification thus playing a role in translation and embryonic stem cells  pluripotency and differentiation","predictedComplex":false,"interactors":[{"ac":"EBI-12360031","identifier":"Q9NRN9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NRN9/entry","name":"METTL5","description":"rRNA N(6)-adenosine-methyltransferase METTL5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23290","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30813205","identifier":"CHEBI:59789","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:59789","name":"s-adenosyl-l-methionine zwitterion","description":"S-adenosyl-L-methionine zwitterion","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; 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This enables EF-Tu to bind to a new GTP molecule, release EF-Ts and promote the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-301164","identifier":"P0A6P1","identifierLink":"https://www.uniprot.org/uniprotkb/P0A6P1/entry","name":"tsf","description":"Elongation factor Ts","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11741","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9010251","identifier":"P0CE48","identifierLink":"https://www.uniprot.org/uniprotkb/P0CE48/entry","name":"tufB","description":"Elongation factor Tu 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43721","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2854","complexName":"Elongation Factor eEF1 complex, variant CAM1","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Transports an aminoacylated-tRNA (aa-tRNA) to the ribosomal A-site during the elongation phase of protein synthesis. GTP bound to eEF1A (TEF1/2) is hydrolyzed upon codon-anticodon match between an aa-tRNA in the ribosomal RNA A-site and mRNA bound to the ribosome. Inactive eEF1A-GDP leaves the ribosome and must be recycled to eEF1A-GTP before binding another molecule of aa-tRNA. The guanine nucleotide exchange factor eEF1B catalyzes the exchange of GDP for GTP.","predictedComplex":false,"interactors":[{"ac":"EBI-6314","identifier":"P02994","identifierLink":"https://www.uniprot.org/uniprotkb/P02994/entry","name":"TEF1","description":"Elongation factor 1-alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6319","identifier":"P32471","identifierLink":"https://www.uniprot.org/uniprotkb/P32471/entry","name":"EFB1","description":"Elongation factor 1-beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11595","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6323","identifier":"P29547","identifierLink":"https://www.uniprot.org/uniprotkb/P29547/entry","name":"CAM1","description":"Elongation factor 1-gamma 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43986","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2855","complexName":"Fimbrial Tip Complex FimFGH","organismName":"Escherichia coli (strain K12); 83333","description":"Forms the linear tip of the Type1 fimbria, a macromolecular cell surface structure required for cellular adhesion. The fimbria consists of a 1-2 um long fimbrial rod, built by thousands of copies of the non-adhesive major subunit, FimA (P04128). The tip is optimized to have a dual functionality: flexible exploration and force sensing. The  FimFGH subunits interact through donor strand complementation where a beta-strand from one subunit completes the beta-sandwich structure of the neighboring subunit. FimH contains a lectin domain which binds mannose derivatives on the surface of neighboring cells.","predictedComplex":false,"interactors":[{"ac":"EBI-1028015","identifier":"P08191","identifierLink":"https://www.uniprot.org/uniprotkb/P08191/entry","name":"fimH","description":"Type 1 fimbrin D-mannose specific adhesin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33420","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1785833","identifier":"P08189","identifierLink":"https://www.uniprot.org/uniprotkb/P08189/entry","name":"fimF","description":"Protein FimF","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33420","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1785843","identifier":"P08190","identifierLink":"https://www.uniprot.org/uniprotkb/P08190/entry","name":"fimG","description":"Protein FimG","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33420","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2859","complexName":"CRL4-DCAF4 E3 ubiquitin ligase complex, CUL4B variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor DCAF4. 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Proteolytically cleaves poly[ADP-ribose] polymerase 1 (PARP1, P09874) at a '216-Asp-|-Gly-217' bond. \r\n\r\nIncreased Caspase-7 expression correlates with excessive neuronal cell death in neurodegenerative disorders such as Alzheimer's disease and Huntington disease. \r\n\r\nSingle nucleotide polymorphisms (SNPs) in the Caspase-7 gene have been linked with rheumatoid arthritis (K249R mutation) and Insulin-Dependent Diabetes Mellitus (D251E mutation).","predictedComplex":false,"interactors":[{"ac":"EBI-12735963","identifier":"P55210-PRO_0000004619","identifierLink":"https://www.uniprot.org/uniprotkb/P55210-PRO_0000004619/entry","name":"CASP7","description":"Caspase-7 subunit p11","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-12735969","identifier":"P55210-PRO_0000004617","identifierLink":"https://www.uniprot.org/uniprotkb/P55210-PRO_0000004617/entry","name":"CASP7","description":"Caspase-7 subunit p20","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-2865","complexName":"Glutamate-cysteine ligase complex","organismName":"Homo sapiens; 9606","description":"Catalyses the rate-limiting step in glutathione biosynthesis, the formation of L-gamma-glutamyl-L-cysteine (CHEBI:58173) from  L-cysteine (CHEBI:35235) and L-glutamate.(CHEBI:29985).","predictedComplex":false,"interactors":[{"ac":"EBI-1051387","identifier":"P48507","identifierLink":"https://www.uniprot.org/uniprotkb/P48507/entry","name":"GCLM","description":"Glutamate--cysteine ligase regulatory subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13295","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2832840","identifier":"P48506","identifierLink":"https://www.uniprot.org/uniprotkb/P48506/entry","name":"GCLC","description":"Glutamate--cysteine ligase catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11164","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2866","complexName":"N6AMT1-TRM112 methyltransferase complex","organismName":"Homo sapiens; 9606","description":"S-adenosylmethionine-dependent methyltransferase which catalyzes the monomethylation of histone H4 lysine-12 thus controlling the expression of genes encoding molecules involved in the cell cycle. 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This results in the loss of binding sites for regulatory reader proteins and causes chromatin compaction by restoring the positive charge on histone tails. Plays a role in cell division, specifically in  chromosome alignment during mitosis. Appears to be required for embryonic development. Nuclear localised throughout interphase, but is excluded from chromatin as chromosomes condense during early mitosis (prophase),  The proteins are recruited back into nuclei as the chromatin decondenses during late mitosis (telophase).","predictedComplex":false,"interactors":[{"ac":"EBI-2795449","identifier":"Q9H147","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H147/entry","name":"DNTTIP1","description":"Deoxynucleotidyltransferase terminal-interacting protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23399","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2795569","identifier":"Q6PJG2","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PJG2/entry","name":"MIDEAS","description":"Mitotic deacetylase-associated SANT domain protein","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16089","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301821","identifier":"Q92769","identifierLink":"https://www.uniprot.org/uniprotkb/Q92769/entry","name":"HDAC2","description":"Histone deacetylase 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2868","complexName":"LKB1-STRAD-MO25 serine/threonine protein kinase complex, CAB39-STRADB variant","organismName":"Homo sapiens; 9606","description":"Directly phosphorylates adenosine monophosphate-activated protein kinase (AMPK) family members on the T-loop thereby activating them.  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Couples cellular growth and division to the availability of cellular energy. by activating the AMP kinases when energy levels are low, inhibiting signalling pathways that promote proliferation.","predictedComplex":false,"interactors":[{"ac":"EBI-1047244","identifier":"Q9H9S4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H9S4/entry","name":"CAB39L","description":"Calcium-binding protein 39-like","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10182","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-306838","identifier":"Q15831","identifierLink":"https://www.uniprot.org/uniprotkb/Q15831/entry","name":"STK11","description":"Serine/threonine-protein kinase STK11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43895","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-306893","identifier":"Q9C0K7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9C0K7/entry","name":"STRADB","description":"STE20-related kinase adapter protein beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48014","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2870","complexName":"RNA decapping and exonuclease complex, DCP1A variant","organismName":"Homo sapiens; 9606","description":"Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. This is a critical step in bulk mRNA turnover and also in specific mRNA decay pathways triggered by the presence of AU-rich elements, a nonsense codon or miRNA-binding sites. Decapping inhibits translation initiation and commits the mRNA to full degradation by the 5'-to-3' exonuclease XRN1. Additional proteins, for example the microprotein NBDY (A0A0U1RRE5) may bind to the protein and regulate target specificity and also subcellular location of the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-1006038","identifier":"Q6P2E9","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P2E9/entry","name":"EDC4","description":"Enhancer of mRNA-decapping protein 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15598","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-351257","identifier":"P26196","identifierLink":"https://www.uniprot.org/uniprotkb/P26196/entry","name":"DDX6","description":"Probable ATP-dependent RNA helicase DDX6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372406","identifier":"Q8IZH2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IZH2/entry","name":"XRN1","description":"5'-3' exoribonuclease 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12341","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-374238","identifier":"Q9NPI6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPI6/entry","name":"DCP1A","description":"mRNA-decapping enzyme 1A","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16290","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-521577","identifier":"Q8IU60","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IU60/entry","name":"DCP2","description":"m7GpppN-mRNA hydrolase","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23114","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-997311","identifier":"Q96F86","identifierLink":"https://www.uniprot.org/uniprotkb/Q96F86/entry","name":"EDC3","description":"Enhancer of mRNA-decapping protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13612","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2871","complexName":"BUD23-TRM112 methyltransferase complex","organismName":"Homo sapiens; 9606","description":"S-adenosylmethionine-dependent methyltransferase which plays a role in the synthesis of the small ribosomal subunit by catalyzing the N7-methylation of a specific guanosine residue (G1639) of 18S rRNA at the 20S pre-rRNA stage.","predictedComplex":false,"interactors":[{"ac":"EBI-1044726","identifier":"O43709","identifierLink":"https://www.uniprot.org/uniprotkb/O43709/entry","name":"BUD23","description":"18S rRNA (guanine-N(7))-methyltransferase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12734","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30813205","identifier":"CHEBI:59789","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:59789","name":"s-adenosyl-l-methionine zwitterion","description":"S-adenosyl-L-methionine zwitterion","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-373326","identifier":"Q9UI30","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UI30/entry","name":"TRMT112","description":"Multifunctional methyltransferase subunit TRM112-like protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12773","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2872","complexName":"bZIP transcription factor complex, BACH1-MAFG","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site. Acts as a transcriptional repressor binding to the MARE (Maf recognition element) site in gene promoters, thus repressing the expression of NFE2L2 (Q16236) target genes which play a key role in the response to oxidative stress. Represses the transcription of heme oxygenase 1 (P09601) under low heme conditions. When free heme levels rise, activated NFE2L2 partners with MAF proteins to enable transactivation of HMOX1. Heme binds to BACH1 and heme-bound BACH1 undergoes nuclear export and ubiquitin-dependent degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-1263541","identifier":"O14867","identifierLink":"https://www.uniprot.org/uniprotkb/O14867/entry","name":"BACH1","description":"Transcription regulator protein BACH1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-713514","identifier":"O15525","identifierLink":"https://www.uniprot.org/uniprotkb/O15525/entry","name":"MAFG","description":"Transcription factor MafG","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2873","complexName":"SCF E3 ubiquitin ligase complex, FBXL20 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXL20 target proteins include the serine/threonine-protein phosphatase 2A regulatory subunit PPP2R2A (P63151) which suggests a role for the complex in cell signalling and cell cycle regulation.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8835647","identifier":"Q96IG2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96IG2/entry","name":"FBXL20","description":"F-box/LRR-repeat protein 20","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13318","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2874","complexName":"MiDAC histone deacetylase complex, HDAC1 variant","organismName":"Homo sapiens; 9606","description":"Class I histone deacetylase complex with a role in transcriptional regulation by acting as an epigenetic eraser removing acetyl groups from histone tails. This results in the loss of binding sites for regulatory reader proteins and causes chromatin compaction by restoring the positive charge on histone tails. Plays a role in cell division, specifically in  chromosome alignment during mitosis. Appears to be required for embryonic development. Nuclear localised throughout interphase, but is excluded from chromatin as chromosomes condense during early mitosis (prophase),  The proteins are recruited back into nuclei as the chromatin decondenses during late mitosis (telophase).","predictedComplex":false,"interactors":[{"ac":"EBI-2795449","identifier":"Q9H147","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H147/entry","name":"DNTTIP1","description":"Deoxynucleotidyltransferase terminal-interacting protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23399","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2795569","identifier":"Q6PJG2","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PJG2/entry","name":"MIDEAS","description":"Mitotic deacetylase-associated SANT domain protein","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16089","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301834","identifier":"Q13547","identifierLink":"https://www.uniprot.org/uniprotkb/Q13547/entry","name":"HDAC1","description":"Histone deacetylase 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2875","complexName":"RNase H2 complex","organismName":"Mus musculus; 10090","description":"Specifically degrades the RNA species of RNA:DNA duplexes and removal of ribonucleotides misincorporated in genomic DNA, thus, preventing genomic instability and the accumulation of aberrant nucleic acid. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication.","predictedComplex":false,"interactors":[{"ac":"EBI-9027324","identifier":"Q9CWY8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CWY8/entry","name":"Rnaseh2a","description":"Ribonuclease H2 subunit A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10954","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9027340","identifier":"Q80ZV0","identifierLink":"https://www.uniprot.org/uniprotkb/Q80ZV0/entry","name":"Rnaseh2b","description":"Ribonuclease H2 subunit B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13383","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9027358","identifier":"Q9CQ18","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQ18/entry","name":"Rnaseh2c","description":"Ribonuclease H2 subunit C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR47063","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2877","complexName":"Nucleolar ribonuclease P complex","organismName":"Homo sapiens; 9606","description":"Responsible for the 5' endonucleolytic cleavage of precursor tRNAs (pre-tRNAs), catalyzing phosphodiester bond hydrolysis to remove approximately 12 leader nucleotides to yield mature tRNAs. The RNA subunit of the nucleolar RNase P is a catalytically active ribozyme that is capable of both recognizing and cleaving substrates efficiently and accurately.","predictedComplex":false,"interactors":[{"ac":"EBI-28957446","identifier":"URS000013F331_9606","identifierLink":"http://rnacentral.org/rna/URS000013F331_9606","name":"h1_human_rna","description":"Ribonuclease P RNA component H1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"nucleic acid","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-366477","identifier":"O95707","identifierLink":"https://www.uniprot.org/uniprotkb/O95707/entry","name":"POP4","description":"Ribonuclease P protein subunit p29","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13348","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366493","identifier":"P78345","identifierLink":"https://www.uniprot.org/uniprotkb/P78345/entry","name":"RPP38","description":"Ribonuclease P protein subunit p38","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46948","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366505","identifier":"O75818","identifierLink":"https://www.uniprot.org/uniprotkb/O75818/entry","name":"RPP40","description":"Ribonuclease P protein subunit p40","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15396","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366525","identifier":"Q969H6","identifierLink":"https://www.uniprot.org/uniprotkb/Q969H6/entry","name":"POP5","description":"Ribonuclease P/MRP protein subunit POP5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15441","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366542","identifier":"O95059","identifierLink":"https://www.uniprot.org/uniprotkb/O95059/entry","name":"RPP14","description":"Ribonuclease P protein subunit p14","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15441","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366553","identifier":"P78346","identifierLink":"https://www.uniprot.org/uniprotkb/P78346/entry","name":"RPP30","description":"Ribonuclease P protein subunit p30","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366570","identifier":"Q9BUL9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BUL9/entry","name":"RPP25","description":"Ribonuclease P protein subunit p25","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13516","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366574","identifier":"O75817","identifierLink":"https://www.uniprot.org/uniprotkb/O75817/entry","name":"POP7","description":"Ribonuclease P protein subunit p20","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15314","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366586","identifier":"Q9H633","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H633/entry","name":"RPP21","description":"Ribonuclease P protein subunit p21","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366741","identifier":"Q99575","identifierLink":"https://www.uniprot.org/uniprotkb/Q99575/entry","name":"POP1","description":"Ribonucleases P/MRP protein subunit POP1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22731","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2878","complexName":"Crotoxin complex, aCA3-bCA1-CBb variant","organismName":"Crotalus durissus terrificus; 8732","description":"Class I, beta-neurotoxin, composed of an acidic, non-toxic and non-enzymatic subunit (CA), and a basic, weakly toxic, phospholipase A2 protein (CB). The neurotoxin causes paralysis by both pre- and postsynaptic blocking of acetylcholine signalling. The CA subunit increases the lethal potency of the uncomplexed CB subunit by enabling the toxin to reach the specific protein crotoxin receptor at the neuromuscular junction.","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-28965072","identifier":"P08878-PRO_0000022858","identifierLink":"https://www.uniprot.org/uniprotkb/P08878-PRO_0000022858/entry","name":"p08878-pro","description":"Crotoxin chain gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Crotalus durissus terrificus; 8732","xrefs":[]},{"ac":"EBI-28965081","identifier":"P0CG56","identifierLink":"https://www.uniprot.org/uniprotkb/P0CG56/entry","name":"pa2bb","description":"Phospholipase A2 crotoxin basic subunit CBb","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Crotalus durissus terrificus; 8732","xrefs":[]},{"ac":"EBI-28966157","identifier":"P08878-PRO_0000420454","identifierLink":"https://www.uniprot.org/uniprotkb/P08878-PRO_0000420454/entry","name":"p08878-pro","description":"Crotoxin chain beta CA1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Crotalus durissus terrificus; 8732","xrefs":[]},{"ac":"EBI-28997066","identifier":"P08878-PRO_0000420453","identifierLink":"https://www.uniprot.org/uniprotkb/P08878-PRO_0000420453/entry","name":"p08878-pro","description":"Crotoxin chain alpha CA3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Crotalus durissus terrificus; 8732","xrefs":[]}]},{"complexAC":"CPX-2894","complexName":"Inositol phosphorylceramide synthase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the addition of a phosphorylinositol group onto the 1-OH position of ceramide to form inositol phosphorylceramide, an essential step in forming the inositol-phosphate head group of sphingolipids. Sphingolipids are a structurally diverse class of membrane lipids implicated in a number of cell signaling functions.","predictedComplex":false,"interactors":[{"ac":"EBI-2046036","identifier":"P36107","identifierLink":"https://www.uniprot.org/uniprotkb/P36107/entry","name":"AUR1","description":"Inositol phosphorylceramide synthase catalytic subunit AUR1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31310","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-38431","identifier":"Q06346","identifierLink":"https://www.uniprot.org/uniprotkb/Q06346/entry","name":"KEI1","description":"Inositol phosphorylceramide synthase regulatory subunit KEI1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2896","complexName":"[Cu-Zn] Superoxide dismutase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the breakdown of two superoxide molecules into dioxygen and hydrogen peroxide in two asymmetrical steps using an essential copper atom in the active site of the enzyme. Reduction of the oxidized Cu(II) form of the enzyme by superoxide, releasing dioxygen (reaction 1), alternates with oxidation of the reduced Cu(I) form by another superoxide anion and two protons, generating hydrogen peroxide (reaction 2). Protects the cell guard against free radical species produced during cellular metabolism. SOD1 acquires its copper by forming a heterodimer with the  copper chaperone, CCS (CPX-2267), which also is responsible for formation of an intramolecular disulfide bond  required to increase the enzymatic activity from approximately 10 % in disulfide-reduced SOD1 to 100 % in disulfide-oxidized SOD1. The copper chaperone, CCS1 (CPX-2895), both delivers the copper and oxidises the disulfide bond. There is also evidence of CCS-independent activation of SOD1.","predictedComplex":false,"interactors":[{"ac":"EBI-17635","identifier":"P00445","identifierLink":"https://www.uniprot.org/uniprotkb/P00445/entry","name":"SOD1","description":"Superoxide dismutase [Cu-Zn]","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10003","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2008294","identifier":"CHEBI:29036","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29036","name":"copper(2+)","description":"Copper (Cu2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2897","complexName":"[Cu-Zn] Superoxide dismutase complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the breakdown of two superoxide molecules into dioxygen and hydrogen peroxide, detoxifying superoxide radicals, a by-product of oxidative phosphorylation.","predictedComplex":false,"interactors":[{"ac":"EBI-2008294","identifier":"CHEBI:29036","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29036","name":"copper(2+)","description":"Copper (Cu2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-990792","identifier":"P00441","identifierLink":"https://www.uniprot.org/uniprotkb/P00441/entry","name":"SOD1","description":"Superoxide dismutase [Cu-Zn]","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10003","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2898","complexName":"[Cu-Zn] Superoxide dismutase complex","organismName":"Mus musculus; 10090","description":"Catalyzes the breakdown of two superoxide molecules into dioxygen and hydrogen peroxide, detoxifying superoxide radicals, a by-product of oxidative phosphorylation.","predictedComplex":false,"interactors":[{"ac":"EBI-1635090","identifier":"P08228","identifierLink":"https://www.uniprot.org/uniprotkb/P08228/entry","name":"Sod1","description":"Superoxide dismutase [Cu-Zn]","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10003","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2008294","identifier":"CHEBI:29036","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29036","name":"copper(2+)","description":"Copper (Cu2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2895","complexName":"Superoxide dismutase 1 copper chaperone","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Copper chaperone for superoxide dismutase  which delivers copper to the [Cu-Zn] superoxide dismutase I (SOD1, CPX-2896) forming heterodimer (CPX-2267). Insertion of copper is required for SOD1 enzymatic activity. Oxidation of an intramolecular disulfide bond is required to increase the enzymatic activity from approximately 10 % in disulfide-reduced SOD1 to 100 % in disulfide-oxidized SOD1. The copper chaperone, CCS1, both delivers the copper and oxidises the disulfide bond.","predictedComplex":false,"interactors":[{"ac":"EBI-10287","identifier":"P40202","identifierLink":"https://www.uniprot.org/uniprotkb/P40202/entry","name":"CCS1","description":"Superoxide dismutase 1 copper chaperone","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10003","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2008294","identifier":"CHEBI:29036","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29036","name":"copper(2+)","description":"Copper (Cu2+)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2902","complexName":"RAD6-RAD18 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Ubiquitin ligase complex invovled in post-replicative repair of damaged DNA. Mono-ubiquitinates PCNA at a highly conserved lysine, lys-164, in response to replication-stalling DNA damage. This promotes the recruitment of a class of specialized polymerases capable of using damaged DNA as a template for trans-lesion synthesis. Also plays a role in the prevention of spontaneous mutations caused by oxidation of guanine to 7,8-dihydo-8-oxoguanine, caused by free radicals and reactive oxygen species.","predictedComplex":false,"interactors":[{"ac":"EBI-14659","identifier":"P10862","identifierLink":"https://www.uniprot.org/uniprotkb/P10862/entry","name":"RAD18","description":"Postreplication repair E3 ubiquitin-protein ligase RAD18","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19722","identifier":"P06104","identifierLink":"https://www.uniprot.org/uniprotkb/P06104/entry","name":"RAD6","description":"Ubiquitin-conjugating enzyme E2 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2910","complexName":"BRE1-RAD6 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Ubiquitin ligase complex. Mono-ubiquitinates the histone H2B residue lysine-123. This provides a specific tag for epigenetic transcriptional activation in addition to modulating the formation of double-strand breaks during meiosis and being a prerequisite for DNA-damage checkpoint activation. Ubiquitination of lys-123 is a prerequisite for the subsequent di- and trimethylation of histone H3 on K4 and K79 which is important for telomeric gene silencing. A BRE1-associated protein, LGE1, is also required for H2B monoubiquitination and may be part of a larger complex.","predictedComplex":false,"interactors":[{"ac":"EBI-19722","identifier":"P06104","identifierLink":"https://www.uniprot.org/uniprotkb/P06104/entry","name":"RAD6","description":"Ubiquitin-conjugating enzyme E2 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31563","identifier":"Q07457","identifierLink":"https://www.uniprot.org/uniprotkb/Q07457/entry","name":"BRE1","description":"E3 ubiquitin-protein ligase BRE1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23163","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2918","complexName":"UBR1-RAD6 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Ubiquitin ligase complex. Polyubiquitinates proteins containing unacetylated N-terminal residues causing their subsequent degradation by the proteasome as part of the Ac/N-End Rule pathway. Recognizes unacetylated N-terminal methionine if it is followed by a hydrophobic residue. Additionally, acts in an N-end rule independent manner as a component of a novel quality control pathway for proteins synthesized on cytosolic ribosomes","predictedComplex":false,"interactors":[{"ac":"EBI-19722","identifier":"P06104","identifierLink":"https://www.uniprot.org/uniprotkb/P06104/entry","name":"RAD6","description":"Ubiquitin-conjugating enzyme E2 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19909","identifier":"P19812","identifierLink":"https://www.uniprot.org/uniprotkb/P19812/entry","name":"UBR1","description":"E3 ubiquitin-protein ligase UBR1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21497","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2935","complexName":"RAD6-UBR2 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Ubiquitin ligase complex. May act in a quality control pathway for proteins synthesized on cytosolic ribosomes.\r\n\r\nUBR2 is a paralog of UBR1 (P19812) but lacks the conserved sequence motifs required for N-end rule degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-19722","identifier":"P06104","identifierLink":"https://www.uniprot.org/uniprotkb/P06104/entry","name":"RAD6","description":"Ubiquitin-conjugating enzyme E2 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34338","identifier":"Q07963","identifierLink":"https://www.uniprot.org/uniprotkb/Q07963/entry","name":"UBR2","description":"E3 ubiquitin-protein ligase UBR2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21497","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2937","complexName":"MUB1-RAD6-UBR2 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Ubiquitin ligase complex. Ubiquitylates, and targets for destruction, the RPN4 (Q03465) transcription factor, which upregulates the proteasome genes. The binding of MUB1 may position the RPN4 ubiquitylation site proximal to the Ub∼RAD6 thioester and allowing the transfer of Ubiquitin from RAD6 to RPN4. MUB1 is a short-lived protein and is ubiquitinated by the UBR2-RAD6 ubiquitin conjugating enzyme (CPX-2935).","predictedComplex":false,"interactors":[{"ac":"EBI-19722","identifier":"P06104","identifierLink":"https://www.uniprot.org/uniprotkb/P06104/entry","name":"RAD6","description":"Ubiquitin-conjugating enzyme E2 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28207","identifier":"Q03162","identifierLink":"https://www.uniprot.org/uniprotkb/Q03162/entry","name":"MUB1","description":"MYND-type zinc finger protein MUB1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34338","identifier":"Q07963","identifierLink":"https://www.uniprot.org/uniprotkb/Q07963/entry","name":"UBR2","description":"E3 ubiquitin-protein ligase UBR2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21497","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2911","complexName":"BRE1 E3 ubiquitin-protein ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"E3 ubiquitin-protein ligase. Plays a required role in regulation of RNA polymerase II association with active genes.","predictedComplex":false,"interactors":[{"ac":"EBI-31563","identifier":"Q07457","identifierLink":"https://www.uniprot.org/uniprotkb/Q07457/entry","name":"BRE1","description":"E3 ubiquitin-protein ligase BRE1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23163","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2921","complexName":"RSP5-BUL1 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Ubiquitin ligase complex. Polyubiquinates plasma membrane transporters and permeases, required for their endocytosis and subsequent degradation in the vacuole. BUL1 binds to the target protein, enabling ubiquitylation by RSP5.  Phosphorylation of BUL1 results in binding to 14-3-3 proteins proteins, protecting the permeases from down-regulation. Appears to be redundant with the RSP5-BUL2 ubiquitin ligase complex (CPX-2923).","predictedComplex":false,"interactors":[{"ac":"EBI-16219","identifier":"P39940","identifierLink":"https://www.uniprot.org/uniprotkb/P39940/entry","name":"RSP5","description":"E3 ubiquitin-protein ligase RSP5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11254","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3881","identifier":"P48524","identifierLink":"https://www.uniprot.org/uniprotkb/P48524/entry","name":"BUL1","description":"Ubiquitin ligase-binding protein BUL1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31904","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2923","complexName":"RSP5-BUL2 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Ubiquitin ligase complex. Polyubiquinates plasma membrane transporters and permeases, required for their endocytosis and subsequent degradation in the vacuole. BUL2 binds to the target protein, enabling ubiquitylation by RSP5.  Phosphorylation of BUL2 results in binding to 14-3-3 proteins, protecting the permeases from down-regulation. Appears to be redundant with the BUL1:RSP5 complex (CPX-2921).","predictedComplex":false,"interactors":[{"ac":"EBI-16219","identifier":"P39940","identifierLink":"https://www.uniprot.org/uniprotkb/P39940/entry","name":"RSP5","description":"E3 ubiquitin-protein ligase RSP5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11254","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27941","identifier":"Q03758","identifierLink":"https://www.uniprot.org/uniprotkb/Q03758/entry","name":"BUL2","description":"Ubiquitin ligase-binding protein BUL2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31904","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2972","complexName":"WAVE regulatory complex","organismName":"Drosophila melanogaster; 7227","description":"Coordinates Arp2/3-mediated actin polymerization by controlling the activity of the WAVE/SCAR protein.  In response to upstream signals, the WAVE Regulatory complex is both recruited to the membrane and concomitantly triggered to release its inhibition of WAVE.","predictedComplex":false,"interactors":[{"ac":"EBI-116862","identifier":"Q9VF87","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VF87/entry","name":"Cyfip","description":"Cytoplasmic FMR1-interacting protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12195","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-150577","identifier":"P55162","identifierLink":"https://www.uniprot.org/uniprotkb/P55162/entry","name":"Hem","description":"Membrane-associated protein Hem","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15107337","identifier":"M9PCP4","identifierLink":"https://www.uniprot.org/uniprotkb/M9PCP4/entry","name":"SCAR","description":"Wiskott-Aldrich syndrome protein family member","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-167860","identifier":"Q9Y0S9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y0S9/entry","name":"Abi","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-9206607","identifier":"Q8MLQ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8MLQ0/entry","name":"HSPC300","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR33668","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2946","complexName":"CDC48-NPL4-UFD1 AAA ATPase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A type II AAA ATPase that is involved in the dislocation/extraction step of its substrate proteins from cellular structures or multiprotein complexes into the cytosol where they are largely degraded by the proteasome. Recruited by the integral membrane protein UBX2 (Q04228) and interacts with ubiquitin ligase complexes involved in the endoplasmic reticulum-associated degradation (ERAD) pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-12193","identifier":"P33755","identifierLink":"https://www.uniprot.org/uniprotkb/P33755/entry","name":"NPL4","description":"Nuclear protein localization protein 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12710","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19997","identifier":"P53044","identifierLink":"https://www.uniprot.org/uniprotkb/P53044/entry","name":"UFD1","description":"Ubiquitin fusion degradation protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12555","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4308","identifier":"P25694","identifierLink":"https://www.uniprot.org/uniprotkb/P25694/entry","name":"CDC48","description":"Cell division control protein 48","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3069","complexName":"CDC48-NPL4-VMS1 AAA ATPase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A type II AAA ATPase that is involved in the dislocation/extraction step of its substrate proteins from cellular structures or multiprotein complexes into the cytosol where they are largely degraded by the proteasome. Required for the destruction of damaged, misfolded and ubiquitinated proteins in the mitochondrion. Under conditions of mitochondrial stress, VMS1 (Q04311) recruits CDC48 and NPL4 and extracts ubiquitinated proteins for proteasomal degradation. May also play a role in endoplasmic reticulum-associated protein degradation (ERAD).","predictedComplex":false,"interactors":[{"ac":"EBI-12193","identifier":"P33755","identifierLink":"https://www.uniprot.org/uniprotkb/P33755/entry","name":"NPL4","description":"Nuclear protein localization protein 4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12710","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4308","identifier":"P25694","identifierLink":"https://www.uniprot.org/uniprotkb/P25694/entry","name":"CDC48","description":"Cell division control protein 48","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-784329","identifier":"Q04311","identifierLink":"https://www.uniprot.org/uniprotkb/Q04311/entry","name":"VMS1","description":"tRNA endonuclease VMS1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR16036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2948","complexName":"CUE1-UBC7 ubiquitin-conjugating enzyme complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Component of the endoplasmic reticulum-associated protein degradation (ERAD) pathway. UBC7 is a ubiquitin-conjugating enzyme (E2) that functions with endoplasmic reticulum resident ubiquitin ligases (E3s) only if bound to the ER surface by CUE1. UBC7 may also be activated by CUE1.","predictedComplex":false,"interactors":[{"ac":"EBI-19749","identifier":"Q02159","identifierLink":"https://www.uniprot.org/uniprotkb/Q02159/entry","name":"UBC7","description":"Ubiquitin-conjugating enzyme E2 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27580","identifier":"P38428","identifierLink":"https://www.uniprot.org/uniprotkb/P38428/entry","name":"CUE1","description":"Coupling of ubiquitin conjugation to ER degradation protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-2973","complexName":"syg-1-syg-2 cell adhesion complex","organismName":"Caenorhabditis elegans; 6239","description":"Multi-purpose cell adhesion molecule (CAM) complex. Role in synaptogenesis in mediating adhesion between guidepost vulval epithelial cells and the axon of the hermaphrodite-specific neurons.","predictedComplex":false,"interactors":[{"ac":"EBI-321771","identifier":"B1Q236","identifierLink":"https://www.uniprot.org/uniprotkb/B1Q236/entry","name":"syg-1","description":"Synaptogenesis protein syg-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11640","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9211201","identifier":"Q9U3P2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9U3P2/entry","name":"syg-2","description":"Synaptogenesis protein syg-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11640","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2974","complexName":"rst cell adhesion complex","organismName":"Drosophila melanogaster; 7227","description":"Multi-purpose cell adhesion molecule (CAM) complex. Expressed in inter-ommatidial cells and is required for correct axonal pathway formation in the optic lobe and for programmed cell death in the developing retina. Expressed on myoblast founder cells and play a role in myoblast fusion during muscle development.","predictedComplex":false,"interactors":[{"ac":"EBI-82110","identifier":"Q08180","identifierLink":"https://www.uniprot.org/uniprotkb/Q08180/entry","name":"rst","description":"Irregular chiasm C-roughest protein","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11640","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2997","complexName":"rst-sns cell adhesion complex","organismName":"Drosophila melanogaster; 7227","description":"Multi-purpose cell adhesion molecule (CAM) complex. Probable role in epithelial remodeling process in the developing eye. Role in myoblast fusion during muscle development, may be required for the recognition of founder cells and myotubes by fusion-competent myoblasts.","predictedComplex":false,"interactors":[{"ac":"EBI-6895883","identifier":"Q0E9F2","identifierLink":"https://www.uniprot.org/uniprotkb/Q0E9F2/entry","name":"sns","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11640","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-82110","identifier":"Q08180","identifierLink":"https://www.uniprot.org/uniprotkb/Q08180/entry","name":"rst","description":"Irregular chiasm C-roughest protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11640","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2998","complexName":"hbs-rst cell adhesion complex","organismName":"Drosophila melanogaster; 7227","description":"Multi-purpose cell adhesion molecule (CAM) complex. Probable roles in epithelial remodeling process in the developing eye and myoblast fusion during muscle development.","predictedComplex":false,"interactors":[{"ac":"EBI-6894883","identifier":"Q9V787","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V787/entry","name":"hbs","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-82110","identifier":"Q08180","identifierLink":"https://www.uniprot.org/uniprotkb/Q08180/entry","name":"rst","description":"Irregular chiasm C-roughest protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11640","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2999","complexName":"hbs-kirre cell adhesion complex","organismName":"Drosophila melanogaster; 7227","description":"Multi-purpose cell adhesion molecule (CAM) complex. Probable roles in epithelial remodeling process in the developing eye and myoblast fusion during muscle development.","predictedComplex":false,"interactors":[{"ac":"EBI-3423947","identifier":"Q9W4T9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W4T9/entry","name":"kirre","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11640","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6894883","identifier":"Q9V787","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V787/entry","name":"hbs","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]}]},{"complexAC":"CPX-3000","complexName":"sns-kirre cell adhesion complex","organismName":"Drosophila melanogaster; 7227","description":"Multi-purpose cell adhesion molecule (CAM) complex. Probable roles in epithelial remodeling process in the developing eye and myoblast fusion during muscle development.","predictedComplex":false,"interactors":[{"ac":"EBI-3423947","identifier":"Q9W4T9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W4T9/entry","name":"kirre","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11640","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6895883","identifier":"Q0E9F2","identifierLink":"https://www.uniprot.org/uniprotkb/Q0E9F2/entry","name":"sns","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11640","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2991","complexName":"kirre cell adhesion complex","organismName":"Drosophila melanogaster; 7227","description":"Multi-purpose cell adhesion molecule (CAM) complex. Expressed in inter-ommatidial cells and is required for correct axonal pathway formation in the optic lobe and for programmed cell death in the developing retina. Expressed on myoblast founder cells and play a role in myoblast fusion during muscle development.","predictedComplex":false,"interactors":[{"ac":"EBI-3423947","identifier":"Q9W4T9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W4T9/entry","name":"kirre","description":null,"stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11640","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3032","complexName":"Glutamate decarboxylase 1 complex","organismName":"Homo sapiens; 9606","description":"An essential enzyme that catalyzes the production of the inhibitory neurotransmitter GABA (gamma-aminobutyric acid, CHEBI:16865) from glutamate (CHEBI:16015) and controls fundamental processes such as neurogenesis, synaptogenesis, movement and tissue development, and protection against neural injury. Involved in intermediary metabolism, participating in the GABA shunt, which bypasses two steps of the TCA cycle. \r\n\r\nApproximately 80% of GAD1 exists in the active holo form (bound to the PLP cofactor) and is responsible for production of a basal pool of GABA.","predictedComplex":false,"interactors":[{"ac":"EBI-743184","identifier":"Q99259","identifierLink":"https://www.uniprot.org/uniprotkb/Q99259/entry","name":"GAD1","description":"Glutamate decarboxylase 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45677","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8851905","identifier":"CHEBI:18405","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18405","name":"pyridoxal 5'-phosphate","description":"pyridoxal 5'-phosphate","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3033","complexName":"Glutamate decarboxylase 2 complex","organismName":"Homo sapiens; 9606","description":"An essential enzyme that catalyzes the production of the inhibitory neurotransmitter GABA (gamma-aminobutyric acid, CHEBI:16865) from glutamate (CHEBI:16015) and controls fundamental processes such as neurogenesis, synaptogenesis, movement and tissue development and protection against neural injury.  and is used as energy source through GABA shunt. Involved in intermediary metabolism, participating in the GABA shunt, which bypasses two steps of the TCA cycle. \r\n\r\nApproximately 80% of GAD2 exists in the inactive apo form and is activated to produce extra GABA when required.","predictedComplex":false,"interactors":[{"ac":"EBI-8851905","identifier":"CHEBI:18405","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18405","name":"pyridoxal 5'-phosphate","description":"pyridoxal 5'-phosphate","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9304251","identifier":"Q05329","identifierLink":"https://www.uniprot.org/uniprotkb/Q05329/entry","name":"GAD2","description":"Glutamate decarboxylase 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45677","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3061","complexName":"Glutamate decarboxylase 1 complex","organismName":"Mus musculus; 10090","description":"An essential enzyme that catalyzes the production of the inhibitory neurotransmitter GABA (gamma-aminobutyric acid, CHEBI:16865) from glutamate (CHEBI:16015) and controls fundamental processes such as neurogenesis, synaptogenesis, movement and tissue development, and protection against neural injury. Involved in intermediary metabolism, participating in the GABA shunt, which bypasses two steps of the TCA cycle. \r\n\r\nApproximately 80% of GAD1 exists in the active holo form (bound to the PLP cofactor) and is responsible for production of a basal pool of GABA.","predictedComplex":false,"interactors":[{"ac":"EBI-773498","identifier":"P48318","identifierLink":"https://www.uniprot.org/uniprotkb/P48318/entry","name":"Gad1","description":"Glutamate decarboxylase 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45677","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8851905","identifier":"CHEBI:18405","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18405","name":"pyridoxal 5'-phosphate","description":"pyridoxal 5'-phosphate","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3062","complexName":"Glutamate decarboxylase 2 complex","organismName":"Mus musculus; 10090","description":"An essential enzyme that catalyzes the production of the inhibitory neurotransmitter GABA (gamma-aminobutyric acid, CHEBI:16865) from glutamate (CHEBI:16015) and controls fundamental processes such as neurogenesis, synaptogenesis, movement and tissue development and protection against neural injury.  and is used as energy source through GABA shunt. Involved in intermediary metabolism, participating in the GABA shunt, which bypasses two steps of the TCA cycle. \r\n\r\nApproximately 80% of GAD2 exists in the inactive apo form and is activated to produce extra GABA when required.","predictedComplex":false,"interactors":[{"ac":"EBI-8313192","identifier":"P48320","identifierLink":"https://www.uniprot.org/uniprotkb/P48320/entry","name":"Gad2","description":"Glutamate decarboxylase 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45677","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8851905","identifier":"CHEBI:18405","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18405","name":"pyridoxal 5'-phosphate","description":"pyridoxal 5'-phosphate","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3066","complexName":"Glutamate decarboxylase 1 complex","organismName":"Rattus norvegicus; 10116","description":"An essential enzyme that catalyzes the production of the inhibitory neurotransmitter GABA (gamma-aminobutyric acid, CHEBI:16865) from glutamate (CHEBI:16015) and controls fundamental processes such as neurogenesis, synaptogenesis, movement and tissue development, and protection against neural injury. Involved in intermediary metabolism, participating in the GABA shunt, which bypasses two steps of the TCA cycle. \r\n\r\nApproximately 80% of GAD1 exists in the active holo form (bound to the PLP cofactor) and is responsible for production of a basal pool of GABA.","predictedComplex":false,"interactors":[{"ac":"EBI-8851905","identifier":"CHEBI:18405","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18405","name":"pyridoxal 5'-phosphate","description":"pyridoxal 5'-phosphate","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9397328","identifier":"P18088","identifierLink":"https://www.uniprot.org/uniprotkb/P18088/entry","name":"Gad1","description":"Glutamate decarboxylase 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR45677","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3067","complexName":"Glutamate decarboxylase 2 complex","organismName":"Rattus norvegicus; 10116","description":"An essential enzyme that catalyzes the production of the inhibitory neurotransmitter GABA (gamma-aminobutyric acid, CHEBI:16865) from glutamate (CHEBI:16015) and controls fundamental processes such as neurogenesis, synaptogenesis, movement and tissue development and protection against neural injury.  and is used as energy source through GABA shunt. Involved in intermediary metabolism, participating in the GABA shunt, which bypasses two steps of the TCA cycle. \r\n\r\nApproximately 80% of GAD2 exists in the inactive apo form and is activated to produce extra GABA when required.","predictedComplex":false,"interactors":[{"ac":"EBI-8851905","identifier":"CHEBI:18405","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18405","name":"pyridoxal 5'-phosphate","description":"pyridoxal 5'-phosphate","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9397355","identifier":"Q05683","identifierLink":"https://www.uniprot.org/uniprotkb/Q05683/entry","name":"Gad2","description":"Glutamate decarboxylase 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR45677","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3034","complexName":"Acetolactate synthase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the first step that is common to the biosynthesis of  branched-chain amino acids. The reaction involves the irreversible decarboxylation of pyruvate to a bound hydroxyethyl group that then condenses with either a second pyruvate molecule to form 2-acetolactate as the first step in the biosynthesis of valine and leucine. or with 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate as  the  initial  step  in  the biosynthesis of isoleucine.","predictedComplex":false,"interactors":[{"ac":"EBI-1225105","identifier":"CHEBI:16238","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16238","name":"fad","description":"FAD - Flavin adenine dinucleotide","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9087","identifier":"P25605","identifierLink":"https://www.uniprot.org/uniprotkb/P25605/entry","name":"ILV6","description":"Acetolactate synthase small subunit, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31242","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9096","identifier":"P07342","identifierLink":"https://www.uniprot.org/uniprotkb/P07342/entry","name":"ILV2","description":"Acetolactate synthase catalytic subunit, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR18968","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9301856","identifier":"CHEBI:9532","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:9532","name":"thiamine(1+) diphosphate","description":"thiamine(1+) diphosphate","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3055","complexName":"Translocon complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Post-translationally translocates nascent proteins into the endoplasmic reticulum. The complex is composed of the SEC61 translocon complex protein-conducting channel (CPX-1833) and the tetrameric SEC62-63 complex (CPX-3056). The SEC62-63 complex plays a crucial role in targeting of the signal recognition particle-independent protein substrate to the protein-conducting channel and also in the assembly of the post-translocon complex.","predictedComplex":false,"interactors":[{"ac":"EBI-16400","identifier":"P32915","identifierLink":"https://www.uniprot.org/uniprotkb/P32915/entry","name":"SEC61","description":"Protein transport protein SEC61","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10906","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16406","identifier":"P35179","identifierLink":"https://www.uniprot.org/uniprotkb/P35179/entry","name":"SSS1","description":"Protein transport protein SSS1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12309","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16410","identifier":"P52870","identifierLink":"https://www.uniprot.org/uniprotkb/P52870/entry","name":"SBH1","description":"Protein transport protein SBH1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13509","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16632","identifier":"P21825","identifierLink":"https://www.uniprot.org/uniprotkb/P21825/entry","name":"SEC62","description":"Translocation protein SEC62","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12443","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16636","identifier":"P14906","identifierLink":"https://www.uniprot.org/uniprotkb/P14906/entry","name":"SEC63","description":"Protein translocation protein SEC63","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24075","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16647","identifier":"P33754","identifierLink":"https://www.uniprot.org/uniprotkb/P33754/entry","name":"SEC66","description":"Translocation protein SEC66","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28229","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16651","identifier":"P39742","identifierLink":"https://www.uniprot.org/uniprotkb/P39742/entry","name":"SEC72","description":"Translocation protein SEC72","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-3056","complexName":"SEC62-SEC63 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for post-translational translocation of nascent proteins into the endoplasmic reticulum. Plays a crucial role in targeting of the signal recognition particle-independent protein substrate to the protein-conducting channel and also in the assembly of the post-translocon complex (CPX-3055).","predictedComplex":false,"interactors":[{"ac":"EBI-16632","identifier":"P21825","identifierLink":"https://www.uniprot.org/uniprotkb/P21825/entry","name":"SEC62","description":"Translocation protein SEC62","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12443","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16636","identifier":"P14906","identifierLink":"https://www.uniprot.org/uniprotkb/P14906/entry","name":"SEC63","description":"Protein translocation protein SEC63","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24075","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16647","identifier":"P33754","identifierLink":"https://www.uniprot.org/uniprotkb/P33754/entry","name":"SEC66","description":"Translocation protein SEC66","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28229","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16651","identifier":"P39742","identifierLink":"https://www.uniprot.org/uniprotkb/P39742/entry","name":"SEC72","description":"Translocation protein SEC72","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-3057","complexName":"PKM2 pyruvate kinase complex (dimer)","organismName":"Homo sapiens; 9606","description":"A protein kinase promoting aerobic glycolysis under glucose starvation conditions when it switches from the highly active tetrameric pyruvate kinase (CPX-3058) to the less active dimeric protein kinase. Regulates gene expression and cell proliferation by binding transcription factors such as Histone pThr12-H3, Oct-4 (Q01860), Stat3 (P40763), pTyr333-β-catenin (P35222). Often, but not always, phosphorylates the transcription factor using beta-d-fructofuranose 1,6-bisphosphate (CHEBI:28013) as phosphate donor. Nuclear translocation is induced by PIAS3-mediated sumoylation and ERK2-mediated phosphorylation on Ser-37. Redirects glucose-derived carbons towards biosynthesis, indirectly supporting the Warburg effect, by regulating gene expression in the nucleus. This switch is tightly controlled by oncogenes, tumor suppressors and growth signals and affected by post-translational modifications of PKM2. \r\n\r\nImportant allosteric affectors for the dimeric state are human papilloma virus E7, promyelocytic leukemia (PML, P29590), EGFR-mediated-pY46-MUC1-C (P15941), phosphor-tyrosine proteins and SAICAR (succinyl-5-aminoimidazole-4-carboxamide-1-ribose-50-phosphate). The protein kinase activity is inhibited by the presence of ADP (CHEBI:16761) and the PKM2 activator beta-d-fructofuranose 1,6-bisphosphate (CHEBI:28013) in which case PKM2 reverts to pyruvate kinase activity. When bound to SAICAR it most likely forms a heterodimer but may retain its function as pyruvate kinase.","predictedComplex":false,"interactors":[{"ac":"EBI-4304679","identifier":"P14618-1","identifierLink":"https://www.uniprot.org/uniprotkb/P14618-1/entry","name":"PKM","description":"Pyruvate kinase PKM","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-3058","complexName":"PKM2 pyruvate kinase complex (tetramer)","organismName":"Homo sapiens; 9606","description":"A pyruvate kinase that catalyzes the phosphotransfer reaction between phosphoenolpyruvate (PEP, CHEBI:18021) and ADP (CHEBI:16761), producing pyruvate (CHEBI:15361) and ATP (CHEBI:15422), the final step in glycolysis. Beta-d-fructofuranose 1,6-bisphosphate (FBP) is the allosteric activator required for tetramerization of PKM2 (Lys-433 is critical).\r\n\r\nPKM2 is the predominant pyruvate kinase in fetal tissues, which is replaced by PKR (P30613-1) in red blood cells, PKL (P30613-2) in the liver, and PKM1 (P14618-2) in skeletal muscle, heart, and brain in adults. PKM2 remains the dominant M isoform in most adult tissues, and is the major pyruvate kinase in proliferating and cancer cells. \r\n\r\nCertain allosteric affectors stabilise the tetrameric state and promote tumorigenesis: e.g. non-phosphorylated MUC1-C (P15941) and death-associated protein kinase (DAPK, P53355).","predictedComplex":false,"interactors":[{"ac":"EBI-4304679","identifier":"P14618-1","identifierLink":"https://www.uniprot.org/uniprotkb/P14618-1/entry","name":"PKM","description":"Pyruvate kinase PKM","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-9352711","identifier":"CHEBI:28013","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:28013","name":"beta-d-fructofuranose 1,6-bisphosphate","description":"beta-D-fructofuranose 1,6-bisphosphate","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3059","complexName":"PKM2 pyruvate kinase complex (tetramer)","organismName":"Mus musculus; 10090","description":"A pyruvate kinase that catalyzes the phosphotransfer reaction between phosphoenolpyruvate (PEP, CHEBI:18021) and ADP (CHEBI:16761), producing pyruvate (CHEBI:15361) and ATP (CHEBI:15422), the final step in glycolysis. Beta-d-fructofuranose 1,6-bisphosphate (FBP) is the allosteric activator required for tetramerization of PKM2 (Lys-433 is critical). Certain allosteric affectors stabilise the tetrameric state and promote tumorigenesis: e.g. non-phosphorylated MUC1-C (Q02496) and death-associated protein kinase (DAPK, Q80YE7).\r\n\r\nPKM2 is the predominant pyruvate kinase in fetal tissues, which is replaced by PKR (P53657-1) in red blood cells, PKL in the liver (P53657-2), and PKM1 (P52480-2) in skeletal muscle, heart, and brain in adults. PKM2 remains the dominant M isoform in most adult tissues, and is the major pyruvate kinase in proliferating and cancer cells.","predictedComplex":false,"interactors":[{"ac":"EBI-647795","identifier":"P52480-1","identifierLink":"https://www.uniprot.org/uniprotkb/P52480-1/entry","name":"Pkm","description":"Pyruvate kinase PKM","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-9352711","identifier":"CHEBI:28013","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:28013","name":"beta-d-fructofuranose 1,6-bisphosphate","description":"beta-D-fructofuranose 1,6-bisphosphate","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3060","complexName":"PKM2 pyruvate kinase complex (dimer)","organismName":"Mus musculus; 10090","description":"A protein kinase promoting aerobic glycolysis under glucose starvation conditions when it switches from the highly active tetrameric pyruvate kinase (CPX-3058) to the less active dimeric protein kinase. Regulates gene expression and cell proliferation by binding transcription factors such as Histone pThr12-H3, Oct-4 (P20263), Stat3 (P42227), pTyr333-β-catenin (Q02248). Often, but not always, phosphorylates the transcription factor using beta-d-fructofuranose 1,6-bisphosphate (CHEBI:28013) as phosphate donor. Nuclear translocation is induced by PIAS3-mediated sumoylation and ERK2-mediated phosphorylation on Ser-37. Redirects glucose-derived carbons towards biosynthesis indirectly supporting the Warburg effect by regulating gene expression in the nucleus. This switch is tightly controlled by oncogenes, tumor suppressors and growth signals and affected by post-translational modifications of PKM2.\r\n\r\nImportant allosteric affectors for the dimeric state are human papilloma virus E7, promyelocytic leukemia (PML, Q60953), EGFR-mediated-pY46-MUC1-C (Q02496), phosphor-tyrosine proteins and SAICAR (succinyl-5-aminoimidazole-4-carboxamide-1-ribose-50-phosphate). The protein kinase activity is inhibited by the presence of ADP (CHEBI:16761) and the PKM2 activator beta-d-fructofuranose 1,6-bisphosphate (CHEBI:28013) in which case PKM2 reverts to pyruvate kinase activity. When bound to SAICAR it most likely forms a heterodimer but may retain its function as pyruvate kinase.","predictedComplex":false,"interactors":[{"ac":"EBI-647795","identifier":"P52480-1","identifierLink":"https://www.uniprot.org/uniprotkb/P52480-1/entry","name":"Pkm","description":"Pyruvate kinase PKM","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-3093","complexName":"PKM1 pyruvate kinase complex","organismName":"Homo sapiens; 9606","description":"A pyruvate kinase that catalyzes the phosphotransfer reaction between phosphoenolpyruvate (PEP, CHEBI:18021) and ADP (CHEBI:16761), producing pyruvate (CHEBI:15361) and ATP (CHEBI:15422), the final step in glycolysis. \r\n\r\nFound in most normal differentiated tissues and predominately in organs that require a high rate of energy generation, muscle, heart and brain.","predictedComplex":false,"interactors":[{"ac":"EBI-6694361","identifier":"P14618-2","identifierLink":"https://www.uniprot.org/uniprotkb/P14618-2/entry","name":"PKM","description":"Pyruvate kinase PKM","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-3094","complexName":"PKL pyruvate kinase complex","organismName":"Homo sapiens; 9606","description":"A pyruvate kinase that catalyzes the phosphotransfer reaction between phosphoenolpyruvate (PEP, CHEBI:18021) and ADP (CHEBI:16761), producing pyruvate (CHEBI:15361) and ATP (CHEBI:15422), the final step in glycolysis. \r\n\r\nProvides key regulation for maintaining the balance between gluconeogenesis and glycolysis. \r\n\r\nExpressed predominantly in liver.","predictedComplex":false,"interactors":[{"ac":"EBI-9352711","identifier":"CHEBI:28013","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:28013","name":"beta-d-fructofuranose 1,6-bisphosphate","description":"beta-D-fructofuranose 1,6-bisphosphate","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9545848","identifier":"P30613-2","identifierLink":"https://www.uniprot.org/uniprotkb/P30613-2/entry","name":"PKLR","description":"Pyruvate kinase PKLR","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-3095","complexName":"PKR pyruvate kinase complex","organismName":"Homo sapiens; 9606","description":"A pyruvate kinase that catalyzes the phosphotransfer reaction between phosphoenolpyruvate (PEP, CHEBI:18021) and ADP (CHEBI:16761), producing pyruvate (CHEBI:15361) and ATP (CHEBI:15422), the final step in glycolysis. \r\n\r\nProvides key regulation for maintaining the balance between gluconeogenesis and glycolysis. \r\n\r\nExpressed exclusively in red cells.","predictedComplex":false,"interactors":[{"ac":"EBI-9352711","identifier":"CHEBI:28013","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:28013","name":"beta-d-fructofuranose 1,6-bisphosphate","description":"beta-D-fructofuranose 1,6-bisphosphate","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9545678","identifier":"P30613-1","identifierLink":"https://www.uniprot.org/uniprotkb/P30613-1/entry","name":"PKLR","description":"Pyruvate kinase PKLR","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-3096","complexName":"PKM1 pyruvate kinase complex","organismName":"Mus musculus; 10090","description":"A pyruvate kinase that catalyzes the phosphotransfer reaction between phosphoenolpyruvate (PEP, CHEBI:18021) and ADP (CHEBI:16761), producing pyruvate (CHEBI:15361) and ATP (CHEBI:15422), the final step in glycolysis. \r\n\r\n\r\nFound in most normal differentiated tissues and predominately in organs that require a high rate of energy generation, muscle, heart and brain.","predictedComplex":false,"interactors":[{"ac":"EBI-9546875","identifier":"P52480-2","identifierLink":"https://www.uniprot.org/uniprotkb/P52480-2/entry","name":"Pkm","description":"Pyruvate kinase PKM","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-3097","complexName":"PKL pyruvate kinase complex","organismName":"Mus musculus; 10090","description":"A pyruvate kinase that catalyzes the phosphotransfer reaction between phosphoenolpyruvate (PEP, CHEBI:18021) and ADP (CHEBI:16761), producing pyruvate (CHEBI:15361) and ATP (CHEBI:15422), the final step in glycolysis. \r\n\r\nProvides key regulation for maintaining the balance between gluconeogenesis and glycolysis. \r\n\r\nExpressed predominantly in liver.","predictedComplex":false,"interactors":[{"ac":"EBI-9352711","identifier":"CHEBI:28013","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:28013","name":"beta-d-fructofuranose 1,6-bisphosphate","description":"beta-D-fructofuranose 1,6-bisphosphate","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9546929","identifier":"P53657-2","identifierLink":"https://www.uniprot.org/uniprotkb/P53657-2/entry","name":"Pklr","description":"Pyruvate kinase PKLR","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-3098","complexName":"PKR pyruvate kinase complex","organismName":"Mus musculus; 10090","description":"A pyruvate kinase that catalyzes the phosphotransfer reaction between phosphoenolpyruvate (PEP, CHEBI:18021) and ADP (CHEBI:16761), producing pyruvate (CHEBI:15361) and ATP (CHEBI:15422), the final step in glycolysis. \r\n\r\nProvides key regulation for maintaining the balance between gluconeogenesis and glycolysis. \r\n\r\nExpressed exclusively in red cells.","predictedComplex":false,"interactors":[{"ac":"EBI-9352711","identifier":"CHEBI:28013","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:28013","name":"beta-d-fructofuranose 1,6-bisphosphate","description":"beta-D-fructofuranose 1,6-bisphosphate","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9546978","identifier":"P53657-1","identifierLink":"https://www.uniprot.org/uniprotkb/P53657-1/entry","name":"Pklr","description":"Pyruvate kinase PKLR","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-3063","complexName":"Glutamate decarboxylase 1/2 complex","organismName":"Rattus norvegicus; 10116","description":"An essential enzyme that catalyzes the production of the inhibitory neurotransmitter GABA (gamma-aminobutyric acid, CHEBI:16865) from glutamate (CHEBI:16015) and controls fundamental processes such as neurogenesis, synaptogenesis, movement and tissue development, and protection against neural injury. Involved in intermediary metabolism, participating in the GABA shunt, which bypasses two steps of the TCA cycle. It is estimated that GAD1-GAD2 heterodimers constitute around 28% of the total GAD activity in cerebellar membranes.","predictedComplex":false,"interactors":[{"ac":"EBI-8851905","identifier":"CHEBI:18405","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18405","name":"pyridoxal 5'-phosphate","description":"pyridoxal 5'-phosphate","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9397328","identifier":"P18088","identifierLink":"https://www.uniprot.org/uniprotkb/P18088/entry","name":"Gad1","description":"Glutamate decarboxylase 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR45677","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9397355","identifier":"Q05683","identifierLink":"https://www.uniprot.org/uniprotkb/Q05683/entry","name":"Gad2","description":"Glutamate decarboxylase 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR45677","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3064","complexName":"Glutamate decarboxylase 1/2 complex","organismName":"Mus musculus; 10090","description":"An essential enzyme that catalyzes the production of the inhibitory neurotransmitter GABA (γ-aminobutyric acid, CHEBI:16865) from glutamate (CHEBI:16015) and controls fundamental processes such as neurogenesis, synaptogenesis, movement and tissue development, and protection against neural injury. Involved in intermediary metabolism, participating in the GABA shunt, which bypasses two steps of the TCA cycle. It is estimated that GAD1-GAD2 heterodimers constitute around 28% of the total GAD activity in cerebellar membranes.","predictedComplex":false,"interactors":[{"ac":"EBI-773498","identifier":"P48318","identifierLink":"https://www.uniprot.org/uniprotkb/P48318/entry","name":"Gad1","description":"Glutamate decarboxylase 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45677","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8313192","identifier":"P48320","identifierLink":"https://www.uniprot.org/uniprotkb/P48320/entry","name":"Gad2","description":"Glutamate decarboxylase 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45677","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8851905","identifier":"CHEBI:18405","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18405","name":"pyridoxal 5'-phosphate","description":"pyridoxal 5'-phosphate","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3065","complexName":"Glutamate decarboxylase 1/2 complex","organismName":"Homo sapiens; 9606","description":"An essential enzyme that catalyzes the production of the inhibitory neurotransmitter GABA (Gamma-aminobutyric acid, CHEBI:16865) from glutamate (CHEBI:16015) and controls fundamental processes such as neurogenesis, synaptogenesis, movement and tissue development, and protection against neural injury. Involved in intermediary metabolism, participating in the GABA shunt, which bypasses two steps of the TCA cycle. It is estimated that GAD1-GAD2 heterodimers constitute around 28% of the total GAD activity in cerebellar membranes.","predictedComplex":false,"interactors":[{"ac":"EBI-743184","identifier":"Q99259","identifierLink":"https://www.uniprot.org/uniprotkb/Q99259/entry","name":"GAD1","description":"Glutamate decarboxylase 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45677","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8851905","identifier":"CHEBI:18405","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18405","name":"pyridoxal 5'-phosphate","description":"pyridoxal 5'-phosphate","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9304251","identifier":"Q05329","identifierLink":"https://www.uniprot.org/uniprotkb/Q05329/entry","name":"GAD2","description":"Glutamate decarboxylase 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45677","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3068","complexName":"Inward rectifier potassium channel 2 complex","organismName":"Mus musculus; 10090","description":"Inward rectifier potassium channel Kir2.1 (coded for by the KCNJ2 gene) plays a key role in maintaining the correct resting potential in eukaryotic cells. The Kir2.1 channel is characterized by a strong inward rectification, in which K+ ions flow preferentially into rather than out of the cell. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. Inward rectification is produced by cytosolic polyamines and Mg2+ occluding the ion conductance pathway as K+ ions are flowing outward. These positively charged particles are then removed from the pore when K+ ions flow into the cell. Rectification is the primary means of gating for Kir2 channels.\r\n\r\nIn addition to rectification, another common feature of Kir channels is regulation by the membrane phospholipid PIP2. Opening of Kir channels requires PIP2 binding to basic and polar amino acids in the cytoplasmic domains, whereas depletion of PIP2 seems to close the channel.\r\n\r\nExpressed in brain, heart and skeletal muscle.","predictedComplex":false,"interactors":[{"ac":"EBI-703793","identifier":"P35561","identifierLink":"https://www.uniprot.org/uniprotkb/P35561/entry","name":"Kcnj2","description":"Inward rectifier potassium channel 2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3071","complexName":"Inward rectifier potassium channel 2 complex","organismName":"Homo sapiens; 9606","description":"Inward rectifier potassium channel Kir2.1 (coded for by the KCNJ2 gene) plays a key role in maintaining the correct resting potential and action potential duration in eukaryotic cells. The Kir2.1 channel is characterized by a strong inward rectification, in which K+ ions flow preferentially into rather than out of the cell. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. Inward rectification is produced by cytosolic polyamines and Mg2+ occluding the ion conductance pathway as K+ ions are flowing outward. These positively charged particles are then removed from the pore when K+ ions flow into the cell. Rectification is the primary means of gating for Kir2 channels.\r\n\r\nIn addition to rectification, another common feature of Kir channels is regulation by the membrane phospholipid PIP2. Opening of Kir channels requires PIP2 binding to basic and polar amino acids in the cytoplasmic domains, whereas depletion of PIP2 seems to close the channel.\r\n\r\nExpressed in brain, heart and skeletal muscle.","predictedComplex":false,"interactors":[{"ac":"EBI-703457","identifier":"P63252","identifierLink":"https://www.uniprot.org/uniprotkb/P63252/entry","name":"KCNJ2","description":"Inward rectifier potassium channel 2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3072","complexName":"Voltage-gated potassium channel complex variant 1","organismName":"Homo sapiens; 9606","description":"Mediates the repolarizing IKr current in the cardiac action potential, conducting potassium (K+) ions out of the muscle cells of the cardiac myocyte. This current is critical in correctly timing the return to the resting state (repolarization) of the cell membrane during the cardiac action potential. In the nervous system, the complex is mainly involved in regulating spike-frequency adaptation and controlling resting potential, and abnormal expression is associated with the onset of schizophrenia. The complex also participates in cell proliferation and differentiation, regulating apoptosis, and is involved in regulating the secretory activity of pancreatic beta cells and chromaffin cells, as well as in regulating the contractility of smooth-muscle cells in the portal vein, the jejunum, and the epididymal duct, possibly by regulating the excitability of these cells.","predictedComplex":false,"interactors":[{"ac":"EBI-7043557","identifier":"P15382","identifierLink":"https://www.uniprot.org/uniprotkb/P15382/entry","name":"KCNE1","description":"Potassium voltage-gated channel subfamily E member 1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15282","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-720643","identifier":"Q12809","identifierLink":"https://www.uniprot.org/uniprotkb/Q12809/entry","name":"KCNH2","description":"Voltage-gated inwardly rectifying potassium channel KCNH2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10217","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3073","complexName":"Voltage-gated potassium channel complex variant 2","organismName":"Homo sapiens; 9606","description":"Mediates the repolarizing IKr current in the cardiac action potential, conducting potassium (K+) ions out of the muscle cells of the cardiac myocyte. This current is critical in correctly timing the return to the resting state (repolarization) of the cell membrane during the cardiac action potential. In the nervous system, the complex is mainly involved in regulating spike-frequency adaptation and controlling resting potential, and abnormal expression is associated with the onset of schizophrenia. The complex also participates in cell proliferation and differentiation, regulating apoptosis, and is involved in regulating the secretory activity of pancreatic beta cells and chromaffin cells, as well as in regulating the contractility of smooth-muscle cells in the portal vein, the jejunum, and the epididymal duct, possibly by regulating the excitability of these cells.","predictedComplex":false,"interactors":[{"ac":"EBI-720643","identifier":"Q12809","identifierLink":"https://www.uniprot.org/uniprotkb/Q12809/entry","name":"KCNH2","description":"Voltage-gated inwardly rectifying potassium channel KCNH2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10217","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9511203","identifier":"Q9Y6J6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6J6/entry","name":"KCNE2","description":"Potassium voltage-gated channel subfamily E member 2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15282","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-579","complexName":"Carbamoyl-phosphate synthase arginine-specific","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Carbamoyl-phosphate synthase is a heterodimer consisting in the CPA1 and CPA2 subunits. CPS catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, as the first step in biosynthetic pathway leading to formation of arginine and/or urea. The small subunit (glutamine amidotransferase) binds and cleaves glutamine and the large subunit (synthetase) accepts the ammonia moiety cleaved from glutamine, binds all of the remaining substrates, and carries out all of the other catalytic events.","predictedComplex":false,"interactors":[{"ac":"EBI-4029","identifier":"P07258","identifierLink":"https://www.uniprot.org/uniprotkb/P07258/entry","name":"CPA1","description":"Carbamoyl phosphate synthase arginine-specific small chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11405","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4034","identifier":"P03965","identifierLink":"https://www.uniprot.org/uniprotkb/P03965/entry","name":"CPA2","description":"Carbamoyl phosphate synthase arginine-specific large chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11405","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-580","complexName":"mRNA capping enzyme complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the first step in mRNA cap formation. Consists of two subunits: an RNA 5'-triphosphatase (RTPase) and GTP:mRNA guanylyltransferase (GTase). The GTase subunit (CEG1) binds to the phosphorylated carboxyl-terminal domain of the largest subunit (CTD-P) of RNA polymerase II, coupling capping with transcription. CEG1 bound to the CTD-P is inactive unless allosterically activated by interaction with the RTPase subunit (CET1). CET1 removes the gamma-phosphate from the 5' end of the RNA substrate to leave a diphosphate end. CEG1 subsequently transfers the GMP moiety of GTP to the 5' end of RNA via an enzyme-GMP covalent reaction intermediate to form the structure GpppN1-.mRNA.","predictedComplex":false,"interactors":[{"ac":"EBI-10503","identifier":"Q01159","identifierLink":"https://www.uniprot.org/uniprotkb/Q01159/entry","name":"CEG1","description":"mRNA-capping enzyme subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10367","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4473","identifier":"O13297","identifierLink":"https://www.uniprot.org/uniprotkb/O13297/entry","name":"CET1","description":"mRNA-capping enzyme subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28118","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-581","complexName":"Casein kinase II complex, CKA1-CKA2 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Serine/threonine-protein kinase complex involved in regulation of cell cycle progression, presumably through phosphorylation of target proteins. CK2 may also have role(s) in inhibiting apoptosis. Phosphorylates serine or threonine residues proximal to acidic amino acids (consensus Ser-Xaa-Xaa-Acidic where acidic residue may be Glu, Asp, pSer or pTYr). Thought to be a dual-specificity kinase in yeast, also able to phosphorylate tyrosine residues, although with less favourable kinetic parameters. ATP or GTP can serve as a phosphate donor. Disruption of CKA1 or CKA2 is not lethal, but disruption of both is synthetic lethal. CKA1 and CKA2 functional overlap is not complete, as yeast with temperature sensitive alleles of CKA1 or CKA2 display distinct phenotypes and different combinations of CKA subunits affect substrate specificity and sub-cellular localization. Disruption of CKB1 or CKB2 causes sensitivity to NaCl and LiCl. Disruption of both CKB1 and CKB2 is not synthetic lethal, although the regulatory subunits are responsible for the structural integrity of the holoenzyme. Much of CK2B is phosphorylated on autophosphorylation site and also in a cell cycle-dependent manner.","predictedComplex":false,"interactors":[{"ac":"EBI-9533","identifier":"P15790","identifierLink":"https://www.uniprot.org/uniprotkb/P15790/entry","name":"CKA1","description":"Casein kinase II subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24054","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9548","identifier":"P19454","identifierLink":"https://www.uniprot.org/uniprotkb/P19454/entry","name":"CKA2","description":"Casein kinase II subunit alpha'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24054","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9563","identifier":"P43639","identifierLink":"https://www.uniprot.org/uniprotkb/P43639/entry","name":"CKB1","description":"Casein kinase II subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9578","identifier":"P38930","identifierLink":"https://www.uniprot.org/uniprotkb/P38930/entry","name":"CKB2","description":"Casein kinase II subunit beta'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-582","complexName":"Trehalose-6-phosphate synthase/phosphatase complex, tps3 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the production of trehalose from glucose-6-phosphate and UDP-glucose in a two step process. The Tps1 subunit is a trehalose-6-phosphate synthase (TPS) and catalyses the production of alpha,alpha-trehalose 6-phosphate from UDP-glucose and D-glucose 6-phosphate. Tps2 acts as a trehalose-6-phosphate phosphatase (TPP) to release trehalose as a final product. Tsp3 is a regulatory subunit appearing to be phosphorylated by PKA during stress recovery.","predictedComplex":false,"interactors":[{"ac":"EBI-19430","identifier":"Q00764","identifierLink":"https://www.uniprot.org/uniprotkb/Q00764/entry","name":"TPS1","description":"Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 56 kDa subunit","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10788","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19440","identifier":"P31688","identifierLink":"https://www.uniprot.org/uniprotkb/P31688/entry","name":"TPS2","description":"Trehalose-phosphatase","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10788","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19448","identifier":"P38426","identifierLink":"https://www.uniprot.org/uniprotkb/P38426/entry","name":"TPS3","description":"Trehalose synthase complex regulatory subunit TPS3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10788","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-583","complexName":"Trehalose-6-phosphate synthase/phosphatase complex, tsl1 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the production of trehalose from glucose-6-phosphate and UDP-glucose in a two step process. The Tps1 subunit is a trehalose-6-phosphate synthase (TPS) and catalyses the production of alpha,alpha-trehalose 6-phosphate from UDP-glucose and D-glucose 6-phosphate. Tps2 acts as a trehalose-6-phosphate phosphatase (TPP) to release trehalose as a final product. Tsl1 is a regulatory subunit and may act to stabilize the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-19430","identifier":"Q00764","identifierLink":"https://www.uniprot.org/uniprotkb/Q00764/entry","name":"TPS1","description":"Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 56 kDa subunit","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10788","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19440","identifier":"P31688","identifierLink":"https://www.uniprot.org/uniprotkb/P31688/entry","name":"TPS2","description":"Trehalose-phosphatase","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10788","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19638","identifier":"P38427","identifierLink":"https://www.uniprot.org/uniprotkb/P38427/entry","name":"TSL1","description":"Trehalose synthase complex regulatory subunit TSL1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10788","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-588","complexName":"Calcineurin complex variant 1","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A Ca2+/calmodulin-regulated Ser/Thr protein phosphatase, highly conserved through evolution and a critical component of Ca2+-regulated signaling in a wide range of unicellular and multicellular eukaryotes. Calcineurin is a heterodimer containing a catalytic (A) subunit complexed with an essential regulatory (B) subunit. Calcineurin function requires interaction of both subunits. The catalytic subunit contains an active site dinuclear metal center. The regulatory subunit is tightly associated, myristoylated and binds Ca2+ via four Ca2+-binding EF-hand motifs. Two redundant genes, CNA1 and CNA2, encode the catalytic subunit and their expression is regulated in a cell cycle-dependent manner. In the yeast, Ca2+ signaling mediated by calcineurin, is required for survival during environmental stress. One role of the phosphatase under these conditions is to activate gene expression through its regulation of the CRZ1 (P53968)  transcription factor. Calcineurin controls many other physiological processes in yeast, including cell cycle progression, cation homeostasis, morphogenesis, establishment of cell polarity and regulation of cell wall biosynthesis. Cells deficient for calcineurin are unable to survive pheromone-induced G1 arrest. When mobilization of internal calcium stores occurs, the catalytic subunit is bound by Ca2+-calmodulin and the active site is freed by displacement of the autoinhibitory domain.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-12771","identifier":"P23287","identifierLink":"https://www.uniprot.org/uniprotkb/P23287/entry","name":"CNA1","description":"Serine/threonine-protein phosphatase 2B catalytic subunit A1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3968","identifier":"P25296","identifierLink":"https://www.uniprot.org/uniprotkb/P25296/entry","name":"CNB1","description":"Calcineurin subunit B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-590","complexName":"Calcineurin complex variant 2","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A Ca2+/calmodulin-regulated Ser/Thr protein phosphatase, highly conserved through evolution and a critical component of Ca2+-regulated signaling in a wide range of unicellular and multicellular eukaryotes. Calcineurin is a heterodimer containing a catalytic (A) subunit complexed with an essential regulatory (B) subunit. Calcineurin function requires interaction of both subunits. The catalytic subunit contains an active site dinuclear metal center. The regulatory subunit is tightly associated, myristoylated and binds Ca2+ via four Ca2+-binding EF-hand motifs. Two redundant genes, CNA1 and CNA2, encode the catalytic subunit and their expression is regulated in a cell cycle-dependent manner. In the yeast, Ca2+ signaling mediated by calcineurin, is required for survival during environmental stress. One role of the phosphatase under these conditions is to activate gene expression through its regulation of the CRZ1 (P53968) transcription factor. Calcineurin controls many other physiological processes in yeast, including cell cycle progression, cation homeostasis, morphogenesis, establishment of cell polarity and regulation of cell wall biosynthesis. Cells deficient for calcineurin are unable to survive pheromone-induced G1 arrest. When mobilization of internal calcium stores occurs, the catalytic subunit is bound by Ca2+-calmodulin and the active site is freed by displacement of the autoinhibitory domain.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-12778","identifier":"P14747","identifierLink":"https://www.uniprot.org/uniprotkb/P14747/entry","name":"CMP2","description":"Serine/threonine-protein phosphatase 2B catalytic subunit A2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3968","identifier":"P25296","identifierLink":"https://www.uniprot.org/uniprotkb/P25296/entry","name":"CNB1","description":"Calcineurin subunit B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-597","complexName":"Calcineurin complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"A Ca2+/calmodulin-regulated Ser/Thr protein phosphatase, highly conserved through evolution and a critical component of Ca2+-regulated signaling in a wide range of unicellular and multicellular eukaryotes. Calcineurin is a heterodimer containing a catalytic (A) subunit complexed with an essential regulatory (B) subunit. Calcineurin function requires interaction of both subunits. The catalytic subunit contains an active site dinuclear metal center. The regulatory subunit is tightly associated, myristoylated and binds Ca2+ via four Ca2+-binding EF-hand motifs.  The gene  encoding calcineurin A in S. pombe, ppb1, is essential for mating and sporulation. ppb1 is transcriptionally regulated in a cell-cycle-dependent manner and is induced under conditions that promote mating. Deletion of the calcineurin A gene ppb1  in haploid S. pombe cells results in branched and multiply  septate cells with defects in septal positioning, polarity,  and cytokinesis. Overexpression of ppb1 in wild-type  S. pombe generates elongated cells with occasional aberrant  nuclear and spindle pole body positioning. Ca2+ signaling mediated by calcineurin, is required for survival during environmental stress. Calcineurin controls many other physiological processes, including cell cycle progression, cation homeostasis, morphogenesis, establishment of cell polarity and regulation of cell wall biosynthesis. When mobilization of internal calcium stores occurs, the catalytic subunit is bound by Ca2+-calmodulin and the active site is freed by displacement of the autoinhibitory domain.","predictedComplex":false,"interactors":[{"ac":"EBI-1250056","identifier":"Q9UU93","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UU93/entry","name":"cnb1","description":"Calcineurin subunit B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1250076","identifier":"Q12705","identifierLink":"https://www.uniprot.org/uniprotkb/Q12705/entry","name":"ppb1","description":"Serine/threonine-protein phosphatase 2B catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-607","complexName":"Actin-related protein 2/3 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Assembles branched actin networks capable of generating protrusive force and resisting mechanical deformation by stimulating new filament growth from the side of existing actin filaments associated with regions of the plasma membrane. Purified Arp2/3 complex is inactive but stimulates rapid actin polymerization in the presence of activator proteins, the most potent type being the VCA (Verprolin, cofilin, acidic) domain-containing Wiskott-Aldrich syndrome protein (WASP) family members. The Arp2/3 complex appears to bind VCA and an existing actin filament in a cooperative manner. Upon activation, ARP2 and ARP3 move into the side-by-side arrangement of consecutive actin subunits along the short pitch helical axis of an actin filament, mimicking a filamentous actin dimer and creating a template for new filament assembly.  The process appears to be ATP-dependent.","predictedComplex":false,"interactors":[{"ac":"EBI-2750","identifier":"P40518","identifierLink":"https://www.uniprot.org/uniprotkb/P40518/entry","name":"ARC15","description":"Actin-related protein 2/3 complex subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2757","identifier":"P33204","identifierLink":"https://www.uniprot.org/uniprotkb/P33204/entry","name":"ARC19","description":"Actin-related protein 2/3 complex subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22629","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2764","identifier":"Q05933","identifierLink":"https://www.uniprot.org/uniprotkb/Q05933/entry","name":"ARC18","description":"Actin-related protein 2/3 complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12391","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2770","identifier":"P53731","identifierLink":"https://www.uniprot.org/uniprotkb/P53731/entry","name":"ARC35","description":"Actin-related protein 2/3 complex subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12058","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2777","identifier":"P38328","identifierLink":"https://www.uniprot.org/uniprotkb/P38328/entry","name":"ARC40","description":"Actin-related protein 2/3 complex subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10709","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2927","identifier":"P32381","identifierLink":"https://www.uniprot.org/uniprotkb/P32381/entry","name":"ARP2","description":"Actin-related protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2933","identifier":"P47117","identifierLink":"https://www.uniprot.org/uniprotkb/P47117/entry","name":"ARP3","description":"Actin-related protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-609","complexName":"Signal recognition particle","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A conserved ribonucleoprotein particle, which includes in its structure a small cytoplasmic RNA (scRNA). In co-translational targeting of membrane and secretory proteins, SRP recognizes signal sequences as soon as they emerge from the ribosomal polypeptide exit tunnel and binds to the ribosome-nascent chain complex (RNC), leading to retardation of peptide elongation. The SRP-RNC complex is targeted to the endoplasmic reticulum (ER) membrane by interaction with the SRP receptor (SR).  After docking to the membrane, the RNC is transferred to the protein-conducting channel, the translocon, and protein synthesis continues. The SRP-SR complex dissociates from the ribosome and, as a result of GTP hydrolysis, SRP and SR dissociate from each other. The genes encoding scR1 and SRP54 are not essential for growth, although SRP-deficient cells grow poorly, suggesting that an alternative, SRP-independent targeting pathway(s) to the ER membrane exists.","predictedComplex":false,"interactors":[{"ac":"EBI-11175111","identifier":"URS00001CAAE9_559292","identifierLink":"http://rnacentral.org/rna/URS00001CAAE9_559292","name":"scr1 yeast_rna","description":"Signal Recognition Particle RNA yeast","stochiometry":"minValue: 1, maxValue: 1","interactorType":"signal recognition particle rna","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-16641","identifier":"P29478","identifierLink":"https://www.uniprot.org/uniprotkb/P29478/entry","name":"SEC65","description":"Signal recognition particle subunit SEC65","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR17453","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17977","identifier":"P38985","identifierLink":"https://www.uniprot.org/uniprotkb/P38985/entry","name":"SRP14","description":"Signal recognition particle subunit SRP14","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12013","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17984","identifier":"P32342","identifierLink":"https://www.uniprot.org/uniprotkb/P32342/entry","name":"SRP21","description":"Signal recognition particle subunit SRP21","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12834","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17997","identifier":"P20424","identifierLink":"https://www.uniprot.org/uniprotkb/P20424/entry","name":"SRP54","description":"Signal recognition particle subunit SRP54","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11564","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18004","identifier":"P38687","identifierLink":"https://www.uniprot.org/uniprotkb/P38687/entry","name":"SRP68","description":"Signal recognition particle subunit SRP68","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12860","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18011","identifier":"P38688","identifierLink":"https://www.uniprot.org/uniprotkb/P38688/entry","name":"SRP72","description":"Signal recognition particle subunit SRP72","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14094","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-636","complexName":"ISW1b chromatin remodeling complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"ATP-dependent chromatin remodeling complex, however ISW1b has a low affinity for nucleosomes resulting in a loss of nucleosome spacing and sliding activities. Appears to play a role in response to increases in temperature and is required for the transcriptional repression of a number of genes, this set differs from those repressed by ISW1a (CPX-637) with which it shares a catalytic subunit.","predictedComplex":false,"interactors":[{"ac":"EBI-21087","identifier":"P38144","identifierLink":"https://www.uniprot.org/uniprotkb/P38144/entry","name":"ISW1","description":"ISWI chromatin-remodeling complex ATPase ISW1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28077","identifier":"Q04213","identifierLink":"https://www.uniprot.org/uniprotkb/Q04213/entry","name":"IOC4","description":"ISWI one complex protein 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12550","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30191","identifier":"Q12072","identifierLink":"https://www.uniprot.org/uniprotkb/Q12072/entry","name":"IOC2","description":"ISWI one complex protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-637","complexName":"ISW1a chromatin remodeling complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"ATP-dependent chromatin remodeling complex which modulates the structure of chromatin to regulate a variety of cellular processes, including DNA replication, repair, chromosome segregation and transcription. Slides mononucleosomes from the end to the center of DNA and requires the flexible, acidic patch of the histone H4 tail to efficiently dock its translocase on the nucleosome, for stimulating the ATPase activity and inducing nucleosome mobility. Positions histone octamers in dinucleosomes more specifically than in mononucleosomes. Regularly spaces nucleosomes in vitro every 175 bp.  ISW1a bound to 33 bp of extranucleosomal DNA at both entry/exit sites is in an inactive conformation, it becomes  activated on binding to extranucleosomal DNA at only one entry/exit site. ISW1a bound to only one extranucleosomal DNA makes a stable contact with nucleosomal DNA two helical turns from the dyad axis, and this interaction is lost when ISW1a is bound to extranucleosomal DNA at both entry/exit sites. Required for the transcriptional repression of a number of genes, this set differs from those repressed by ISW1b (CPX-636) with which it shares a catalytic subunit.","predictedComplex":false,"interactors":[{"ac":"EBI-21087","identifier":"P38144","identifierLink":"https://www.uniprot.org/uniprotkb/P38144/entry","name":"ISW1","description":"ISWI chromatin-remodeling complex ATPase ISW1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22944","identifier":"P43596","identifierLink":"https://www.uniprot.org/uniprotkb/P43596/entry","name":"IOC3","description":"ISWI one complex protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-656","complexName":"SAGA complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A transcriptional co-activator complex with histone acetyltransferase activity. Recruited to gene loci by the interaction of TRA1 with specific transcriptional activators, and the bromodomain of GCN5 binds acetylated H3 and H4 N-terminal tails which potentiates cooperative nucleosome acetylation of histone H3 catalysed by the acetylation module. This opens up the chromatin landscape for binding of additional transcription factors and the pre-initiation complex. The DUB module facilitates elongation through deubiquitination of H2B which allows for the recruitment of the CTK1 kinase (Q03957) and subsequent Ser-2 phosophorylation of the Pol II C-terminal domain.","predictedComplex":false,"interactors":[{"ac":"EBI-1251050","identifier":"Q6WNK7","identifierLink":"https://www.uniprot.org/uniprotkb/Q6WNK7/entry","name":"SUS1","description":"SAGA complex subunit SUS1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12514","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17751","identifier":"P50875","identifierLink":"https://www.uniprot.org/uniprotkb/P50875/entry","name":"SPT20","description":"SAGA complex subunit SPT20","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13526","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17921","identifier":"P06844","identifierLink":"https://www.uniprot.org/uniprotkb/P06844/entry","name":"SPT3","description":"SAGA complex subunit SPT3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11380","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17958","identifier":"P35177","identifierLink":"https://www.uniprot.org/uniprotkb/P35177/entry","name":"SPT7","description":"SAGA complex subunit SPT7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17964","identifier":"P38915","identifierLink":"https://www.uniprot.org/uniprotkb/P38915/entry","name":"SPT8","description":"SAGA complex subunit SPT8","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19855","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18868","identifier":"P38129","identifierLink":"https://www.uniprot.org/uniprotkb/P38129/entry","name":"TAF5","description":"SAGA complex/transcription factor TFIID complex subunit TAF5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19879","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18876","identifier":"P53040","identifierLink":"https://www.uniprot.org/uniprotkb/P53040/entry","name":"TAF6","description":"SAGA complex/transcription factor TFIID complex subunit TAF6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10221","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18889","identifier":"Q12030","identifierLink":"https://www.uniprot.org/uniprotkb/Q12030/entry","name":"TAF10","description":"SAGA complex/transcription factor TFIID complex subunit TAF10","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21242","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19863","identifier":"P50102","identifierLink":"https://www.uniprot.org/uniprotkb/P50102/entry","name":"UBP8","description":"Ubiquitin carboxyl-terminal hydrolase 8","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21646","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21678","identifier":"P25554","identifierLink":"https://www.uniprot.org/uniprotkb/P25554/entry","name":"SGF29","description":"SAGA complex subunit SGF29","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21539","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2186","identifier":"Q02336","identifierLink":"https://www.uniprot.org/uniprotkb/Q02336/entry","name":"ADA2","description":"SAGA complex subunit ADA2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12374","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2192","identifier":"P32494","identifierLink":"https://www.uniprot.org/uniprotkb/P32494/entry","name":"NGG1","description":"SAGA complex subunit NGG1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13556","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23812","identifier":"P53165","identifierLink":"https://www.uniprot.org/uniprotkb/P53165/entry","name":"SGF73","description":"SAGA complex subunit SGF73","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47805","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-24638","identifier":"P38811","identifierLink":"https://www.uniprot.org/uniprotkb/P38811/entry","name":"TRA1","description":"SAGA complex/NuA4 acetyltransferase complex subunit TRA1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27500","identifier":"Q05027","identifierLink":"https://www.uniprot.org/uniprotkb/Q05027/entry","name":"TAF9","description":"SAGA complex/transcription factor TFIID complex subunit TAF9","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR48068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34550","identifier":"Q03067","identifierLink":"https://www.uniprot.org/uniprotkb/Q03067/entry","name":"SGF11","description":"SAGA complex subunit SGF11","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-35097","identifier":"Q03761","identifierLink":"https://www.uniprot.org/uniprotkb/Q03761/entry","name":"TAF12","description":"SAGA complex/transcription factor TFIID complex subunit TAF12","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4574","identifier":"P32657","identifierLink":"https://www.uniprot.org/uniprotkb/P32657/entry","name":"CHD1","description":"Chromo domain-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45623","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7458","identifier":"Q03330","identifierLink":"https://www.uniprot.org/uniprotkb/Q03330/entry","name":"GCN5","description":"Histone acetyltransferase GCN5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45750","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8287","identifier":"Q12060","identifierLink":"https://www.uniprot.org/uniprotkb/Q12060/entry","name":"HFI1","description":"SAGA complex subunit HFI1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21277","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-728","complexName":"ISW2 chromatin remodeling complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"ATP-dependent chromatin remodeling complex which is required for repression of early meiotic genes during mitotic cell growth. Slides mononucleosomes from the end to the center of DNA and requires the flexible, acidic patch of the histone H4 tail to efficiently dock its translocase on the nucleosome, for stimulating the ATPase activity and  inducing nucleosome mobility. Preferentially bind nucleosome substrates containing ~70 bp extranucleosomal DNA at one entry/exit site of the nucleosome. ISW2 interacts with three nucleosomal and extranucleosomal regions. Itc1 and Isw2 bind to the region 2 helical turns from the dyad axis and a region closest to the entry/exit site. Itc1 subunit makes extensive contacts with extranucleosomal DNA. The DPB4 subunit contacts extranucleosomal DNA 37-53 bp away from the entry/exit site of the nucleosome and probably serves as an anchor point for ISW2 on DNA. The DPB4/DLS1 dimer acts to affect the nucleosome spacing activity of the complex, the ability to sense an adjacent nucleosome and to regulate remodeling and may affect the target gene profile it regulates.","predictedComplex":false,"interactors":[{"ac":"EBI-23967","identifier":"P53125","identifierLink":"https://www.uniprot.org/uniprotkb/P53125/entry","name":"ITC1","description":"Imitation switch two complex protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR32075","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25910","identifier":"P40366","identifierLink":"https://www.uniprot.org/uniprotkb/P40366/entry","name":"DLS1","description":"Protein DLS1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10252","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29938","identifier":"Q04603","identifierLink":"https://www.uniprot.org/uniprotkb/Q04603/entry","name":"DPB4","description":"DNA polymerase epsilon subunit D","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46172","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31118","identifier":"Q08773","identifierLink":"https://www.uniprot.org/uniprotkb/Q08773/entry","name":"ISW2","description":"ISWI chromatin-remodeling complex ATPase ISW2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-734","complexName":"ISW2 chromatin remodeling complex variant 2","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"ATP-dependent chromatin remodeling complex which is required for repression of early meiotic genes during mitotic cell growth. Slides mononucleosomes from the end to the center of DNA and requires the flexible, acidic patch of the histone H4 tail to efficiently dock its translocase on the nucleosome, for stimulating the ATPase activity and  inducing nucleosome mobility. Preferentially bind nucleosome substrates containing ~70 bp extranucleosomal DNA at one entry/exit site of the nucleosome. ISW2 interacts with three nucleosomal and extranucleosomal regions. ITC1 and ISW2 bind to the region 2 helical turns from the dyad axis and a region closest to the entry/exit site. ITC1 subunit makes extensive contacts with extranucleosomal DNA. The absence of the histone fold dimer DPB4/DLS1 present in variant 1 (CPX-728) appears to alter the target gene profile regulated by this complex, the dimer acts to affect its nucleosome spacing  activity, the ability to sense an adjacent nucleosome and to regulate remodeling.","predictedComplex":false,"interactors":[{"ac":"EBI-23967","identifier":"P53125","identifierLink":"https://www.uniprot.org/uniprotkb/P53125/entry","name":"ITC1","description":"Imitation switch two complex protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR32075","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31118","identifier":"Q08773","identifierLink":"https://www.uniprot.org/uniprotkb/Q08773/entry","name":"ISW2","description":"ISWI chromatin-remodeling complex ATPase ISW2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2143","complexName":"Hpa2 acetyltransferase","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Acetyltransferase which catalyzes the transfer of an acetyl group from acetyl-CoA to an acceptor residue on histones H-3 and H-4 and also on polyamines. May also acetylate certain small basic proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-1254731","identifier":"CHEBI:15351","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15351","name":"acetyl-coa","description":null,"stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-34205","identifier":"Q06592","identifierLink":"https://www.uniprot.org/uniprotkb/Q06592/entry","name":"HPA2","description":"Histone acetyltransferase HPA2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10545","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-756","complexName":"Anaphase-Promoting core complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"APC, a key regulator of cell cycle progression, is a conserved  cullin-RING E3 ubiqutin ligase which facilitates multiubiqutination of cell cycle proteins, including cyclins, so marking them for proteasomal destruction. Generally believed that APC acts as a scaffold that brings E2 enzymes and substrates into close proximity. APC activity is required for metaphase-anaphase transition, mitotic exit, G1 phase and DNA replication. Targets securin for destruction, which is necessary for chromosome segregation. APC seems to have similar function in meiosis. Co-activators, CDC20 and CDH1, associate with APC core complex at specific stages of cell cycle, and are thought to be involved in substrate specificity. APC-Cdc20 (CPX-760) is active in presence of high cyclin-cdk activity in M phase but after metaphase when cyclin-cdk activity decreases, Cdh1 is dephosphorylated, CDC20 is degraded and APC-CDH1 (CPX-761) activated. Ama1 (CPX-762) is meiotic co-activator required for sporulation and contributes to securin degradation and cyclin Clb5 in anaphase of meiosis. All APC co-activators, characterized by the presence of sequence elements, C-box and the IR-tail, that mediate their binding to APC, contain a C-terminal WD40 domain, predicted to fold into a propeller-like structure, believed to recognize APC substrates by interacting with specific recognition elements in substrates, D-boxes and KEN-boxes. Genetic inactivation of APC is lethal.","predictedComplex":false,"interactors":[{"ac":"EBI-25433","identifier":"P40577","identifierLink":"https://www.uniprot.org/uniprotkb/P40577/entry","name":"MND2","description":"Anaphase-promoting complex subunit MND2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-2603","identifier":"P53068","identifierLink":"https://www.uniprot.org/uniprotkb/P53068/entry","name":"DOC1","description":"Anaphase-promoting complex subunit DOC1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12936","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29017","identifier":"P53886","identifierLink":"https://www.uniprot.org/uniprotkb/P53886/entry","name":"APC1","description":"Anaphase-promoting complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12827","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29698","identifier":"Q12157","identifierLink":"https://www.uniprot.org/uniprotkb/Q12157/entry","name":"APC11","description":"Anaphase-promoting complex subunit 11","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32842","identifier":"Q04601","identifierLink":"https://www.uniprot.org/uniprotkb/Q04601/entry","name":"APC4","description":"Anaphase-promoting complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13260","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-33330","identifier":"Q12379","identifierLink":"https://www.uniprot.org/uniprotkb/Q12379/entry","name":"SWM1","description":"Anaphase-promoting complex subunit SWM1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-33503","identifier":"Q12440","identifierLink":"https://www.uniprot.org/uniprotkb/Q12440/entry","name":"APC2","description":"Anaphase-promoting complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-35371","identifier":"Q08683","identifierLink":"https://www.uniprot.org/uniprotkb/Q08683/entry","name":"APC5","description":"Anaphase-promoting complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12830","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-36475","identifier":"Q12107","identifierLink":"https://www.uniprot.org/uniprotkb/Q12107/entry","name":"APC9","description":"Anaphase-promoting complex subunit 9","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-4208","identifier":"P09798","identifierLink":"https://www.uniprot.org/uniprotkb/P09798/entry","name":"CDC16","description":"Anaphase-promoting complex subunit CDC16","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4216","identifier":"P16522","identifierLink":"https://www.uniprot.org/uniprotkb/P16522/entry","name":"CDC23","description":"Anaphase-promoting complex subunit CDC23","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4245","identifier":"P14724","identifierLink":"https://www.uniprot.org/uniprotkb/P14724/entry","name":"CDC26","description":"Anaphase-promoting complex subunit CDC26","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-4249","identifier":"P38042","identifierLink":"https://www.uniprot.org/uniprotkb/P38042/entry","name":"CDC27","description":"Anaphase-promoting complex subunit CDC27","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-760","complexName":"Anaphase-Promoting Complex, CDC20 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"APC, a key regulator of cell cycle progression, is a conserved cullin-RING E3 ubiqutin ligase which facilitates multiubiqutination of cell cycle proteins, including cyclins, so marking them for proteasomal destruction. Generally believed that APC acts as a scaffold that brings E2 enzymes and substrates into close proximity. APC activity is required for metaphase-anaphase transition, mitotic exit, G1 phase and DNA replication. Targets securin for destruction, which is necessary for chromosome segregation. APC seems to have similar function in meiosis. Co-activators, CDC20 and CDH1, associate with APC core complex (CPX-756) at specific stages of cell cycle, and are thought to be involved in substrate specificity. APC-Cdc20 is active in presence of high cyclin-cdk activity in M phase but after metaphase when cyclin-cdk activity decreases, CDH1 is dephosphorylated, CDC20 is degraded and APC-Cdh1 (CPX-761) activated. Ama1 (CPX-762) is meiotic co-activator required for sporulation and contributes to securin degradation and cyclin Clb5 in anaphase of meiosis. All APC co-activators, characterized by the presence of sequence elements, C-box and the IR-tail, that mediate their binding to APC, contain a C-terminal WD40 domain, predicted to fold into a propeller-like structure, believed to recognize APC substrates by interacting with specific recognition elements in substrates, D-boxes and KEN-boxes. Genetic inactivation of APC is lethal.","predictedComplex":false,"interactors":[{"ac":"EBI-25433","identifier":"P40577","identifierLink":"https://www.uniprot.org/uniprotkb/P40577/entry","name":"MND2","description":"Anaphase-promoting complex subunit MND2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-2603","identifier":"P53068","identifierLink":"https://www.uniprot.org/uniprotkb/P53068/entry","name":"DOC1","description":"Anaphase-promoting complex subunit DOC1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12936","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29017","identifier":"P53886","identifierLink":"https://www.uniprot.org/uniprotkb/P53886/entry","name":"APC1","description":"Anaphase-promoting complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12827","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29698","identifier":"Q12157","identifierLink":"https://www.uniprot.org/uniprotkb/Q12157/entry","name":"APC11","description":"Anaphase-promoting complex subunit 11","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32842","identifier":"Q04601","identifierLink":"https://www.uniprot.org/uniprotkb/Q04601/entry","name":"APC4","description":"Anaphase-promoting complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13260","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-33330","identifier":"Q12379","identifierLink":"https://www.uniprot.org/uniprotkb/Q12379/entry","name":"SWM1","description":"Anaphase-promoting complex subunit SWM1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-33503","identifier":"Q12440","identifierLink":"https://www.uniprot.org/uniprotkb/Q12440/entry","name":"APC2","description":"Anaphase-promoting complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-35371","identifier":"Q08683","identifierLink":"https://www.uniprot.org/uniprotkb/Q08683/entry","name":"APC5","description":"Anaphase-promoting complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12830","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-36475","identifier":"Q12107","identifierLink":"https://www.uniprot.org/uniprotkb/Q12107/entry","name":"APC9","description":"Anaphase-promoting complex subunit 9","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-4208","identifier":"P09798","identifierLink":"https://www.uniprot.org/uniprotkb/P09798/entry","name":"CDC16","description":"Anaphase-promoting complex subunit CDC16","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4212","identifier":"P26309","identifierLink":"https://www.uniprot.org/uniprotkb/P26309/entry","name":"CDC20","description":"APC/C activator protein CDC20","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19918","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4216","identifier":"P16522","identifierLink":"https://www.uniprot.org/uniprotkb/P16522/entry","name":"CDC23","description":"Anaphase-promoting complex subunit CDC23","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 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All APC co-activators, characterized by the presence of sequence elements, C-box and the IR-tail, that mediate their binding to APC, contain a C-terminal WD40 domain, predicted to fold into a propeller-like structure, believed to recognize APC substrates by interacting with specific recognition elements in substrates, D-boxes and KEN-boxes. 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Generally believed that APC acts as a scaffold that brings E2 enzymes and substrates into close proximity. APC activity is required for metaphase-anaphase transition, mitotic exit, G1 phase and DNA replication. Targets securin for destruction, which is necessary for chromosome segregation. APC seems to have similar function in meiosis.. AMA1 is a meiotic co-activator required for sporulation and contributes to securin degradation and cyclin Clb5 in anaphase of meiosis. AMA1 activates APC/C-mediated degradation during multiple periods in meiosis, including late in the first meiotic division.  All APC co-activators, characterized by the presence of sequence elements, C-box and the IR-tail, that mediate their binding to APC, contain a C-terminal WD40 domain, predicted to fold into a propeller-like structure, believed to recognize APC substrates by interacting with specific recognition elements in substrates, D-boxes and KEN-boxes. Genetic inactivation of APC is lethal.","predictedComplex":false,"interactors":[{"ac":"EBI-23513","identifier":"P50082","identifierLink":"https://www.uniprot.org/uniprotkb/P50082/entry","name":"AMA1","description":"Meiosis-specific APC/C activator protein AMA1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19918","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25433","identifier":"P40577","identifierLink":"https://www.uniprot.org/uniprotkb/P40577/entry","name":"MND2","description":"Anaphase-promoting complex subunit MND2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-2603","identifier":"P53068","identifierLink":"https://www.uniprot.org/uniprotkb/P53068/entry","name":"DOC1","description":"Anaphase-promoting complex subunit DOC1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 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All APC co-activators, characterized by the presence of sequence elements, C-box and the IR-tail, that mediate their binding to APC, contain a C-terminal WD40 domain, predicted to fold into a propeller-like structure, believed to recognize APC substrates by interacting with specific recognition elements in substrates, D-boxes and KEN-boxes. Genetic inactivation of APC is lethal.","predictedComplex":false,"interactors":[{"ac":"EBI-1116472","identifier":"O94556","identifierLink":"https://www.uniprot.org/uniprotkb/O94556/entry","name":"cut23","description":"Anaphase-promoting complex subunit 8","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1160845","identifier":"Q9URV2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9URV2/entry","name":"cut4","description":"Anaphase-promoting complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12827","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1160859","identifier":"P41889","identifierLink":"https://www.uniprot.org/uniprotkb/P41889/entry","name":"cut9","description":"Anaphase-promoting complex subunit cut9","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 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All APC co-activators, characterized by the presence of sequence elements, C-box and the IR-tail, that mediate their binding to APC, contain a C-terminal WD40 domain, predicted to fold into a propeller-like structure, believed to recognize APC substrates by interacting with specific recognition elements in substrates, D-boxes and KEN-boxes. Genetic inactivation of APC is lethal.","predictedComplex":false,"interactors":[{"ac":"EBI-1116472","identifier":"O94556","identifierLink":"https://www.uniprot.org/uniprotkb/O94556/entry","name":"cut23","description":"Anaphase-promoting complex subunit 8","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1160845","identifier":"Q9URV2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9URV2/entry","name":"cut4","description":"Anaphase-promoting complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12827","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1160859","identifier":"P41889","identifierLink":"https://www.uniprot.org/uniprotkb/P41889/entry","name":"cut9","description":"Anaphase-promoting complex subunit cut9","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 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284812","xrefs":[{"identifier":"PTHR13260","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1251497","identifier":"Q9P4W7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P4W7/entry","name":"apc5","description":"Anaphase-promoting complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12830","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1251563","identifier":"O13916","identifierLink":"https://www.uniprot.org/uniprotkb/O13916/entry","name":"hcn1","description":"Anaphase-promoting complex subunit hcn1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-1251572","identifier":"O42971","identifierLink":"https://www.uniprot.org/uniprotkb/O42971/entry","name":"apc10","description":"Anaphase-promoting complex subunit 10","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 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Generally believed that APC acts as a scaffold that brings E2 enzymes and substrates into close proximity. APC activity is required for metaphase-anaphase transition, mitotic exit, G1 phase and DNA replication. Targets securin for destruction, which is necessary for chromosome segregation. APC seems to have similar function in meiosis. Co-activators, Slp1 and Srw1/Ste9, associate with APC core complex (CPX-763) at specific stages of cell cycle, and are thought to be involved in substrate specificity. APC-Slp1 (CPX-764) is active in presence of high cyclin-cdk activity in M phase but after metaphase when cyclin-cdk activity decreases, Srw1/Ste9 is dephosphorylated, Slp1 is degraded and APC-Srw1/Ste9 activated. Mfr1/Fzr1 (CPX-766) is meiotic co-activator required for sporulation. All APC co-activators, characterized by the presence of sequence elements, C-box and the IR-tail, that mediate their binding to APC, contain a C-terminal WD40 domain, predicted to fold into a propeller-like structure, believed to recognize APC substrates by interacting with specific recognition elements in substrates, D-boxes and KEN-boxes. Genetic inactivation of APC is lethal.","predictedComplex":false,"interactors":[{"ac":"EBI-1116472","identifier":"O94556","identifierLink":"https://www.uniprot.org/uniprotkb/O94556/entry","name":"cut23","description":"Anaphase-promoting complex subunit 8","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1160845","identifier":"Q9URV2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9URV2/entry","name":"cut4","description":"Anaphase-promoting complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12827","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1160859","identifier":"P41889","identifierLink":"https://www.uniprot.org/uniprotkb/P41889/entry","name":"cut9","description":"Anaphase-promoting complex subunit cut9","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 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Generally believed that APC acts as a scaffold that brings E2 enzymes and substrates into close proximity. APC activity is required for metaphase-anaphase transition, mitotic exit, G1 phase and DNA replication. Targets securin for destruction, which is necessary for chromosome segregation. APC seems to have similar function in meiosis. Co-activators, Slp1 and Srw1/Ste9, associate with APC core complex (CPX-763) at specific stages of cell cycle, and are thought to be involved in substrate specificity. APC-Slp1 (CPX-764) is active in presence of high cyclin-cdk activity in M phase but after metaphase when cyclin-cdk activity decreases, Srw1/Ste9 is dephosphorylated, Slp1 is degraded and APC-Srw1/Ste9 (CPX-765)activated. Mfr1/Fzr1 is meiotic co-activator required for sporulation. All APC co-activators, characterized by the presence of sequence elements, C-box and the IR-tail, that mediate their binding to APC, contain a C-terminal WD40 domain, predicted to fold into a propeller-like structure, believed to recognize APC substrates by interacting with specific recognition elements in substrates, D-boxes and KEN-boxes. Genetic inactivation of APC is lethal.","predictedComplex":false,"interactors":[{"ac":"EBI-1116472","identifier":"O94556","identifierLink":"https://www.uniprot.org/uniprotkb/O94556/entry","name":"cut23","description":"Anaphase-promoting complex subunit 8","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1160845","identifier":"Q9URV2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9URV2/entry","name":"cut4","description":"Anaphase-promoting complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12827","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1160859","identifier":"P41889","identifierLink":"https://www.uniprot.org/uniprotkb/P41889/entry","name":"cut9","description":"Anaphase-promoting complex subunit cut9","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 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284812","xrefs":[{"identifier":"PTHR13260","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1251497","identifier":"Q9P4W7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P4W7/entry","name":"apc5","description":"Anaphase-promoting complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12830","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1251563","identifier":"O13916","identifierLink":"https://www.uniprot.org/uniprotkb/O13916/entry","name":"hcn1","description":"Anaphase-promoting complex subunit hcn1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-1251572","identifier":"O42971","identifierLink":"https://www.uniprot.org/uniprotkb/O42971/entry","name":"apc10","description":"Anaphase-promoting complex subunit 10","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12936","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1251583","identifier":"O74358","identifierLink":"https://www.uniprot.org/uniprotkb/O74358/entry","name":"apc13","description":"Anaphase-promoting complex subunit 13","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28526","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1251592","identifier":"O42659","identifierLink":"https://www.uniprot.org/uniprotkb/O42659/entry","name":"apc14","description":"Anaphase-promoting complex subunit 14","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-1251604","identifier":"O94688","identifierLink":"https://www.uniprot.org/uniprotkb/O94688/entry","name":"apc15","description":"Anaphase-promoting complex subunit 15","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 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High amino acid levels drive GTP binding and the resulting active complex binds to RPTOR (Q8N122) thus recruiting the mTORC1 complex (CPX-503) to the lysosomal surface. Amino acid deprivation induces the conversion of the complex to its inactive GDP-bound state. GATOR1 (CPX-6226) functions as a GTPase activating protein (GAP) complex and stimulates RRAGB GTPase activity to turn it into its inactive GDP-bound form.","predictedComplex":false,"interactors":[{"ac":"EBI-25820308","identifier":"CHEBI:37565","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:37565","name":"gtp(4-)","description":"GTP(4-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-37001918","identifier":"CHEBI:58189","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58189","name":"gdp(3-)","description":"GDP(3-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-992949","identifier":"Q9NQL2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NQL2/entry","name":"RRAGD","description":"Ras-related GTP-binding protein D","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11259","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-993049","identifier":"Q5VZM2","identifierLink":"https://www.uniprot.org/uniprotkb/Q5VZM2/entry","name":"RRAGB","description":"Ras-related GTP-binding protein B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11259","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-769","complexName":"Casein kinase II complex, CKA1 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Serine/threonine-protein kinase complex involved in regulation of cell cycle progression, presumably through phosphorylation of target proteins. CK2 may also have role(s) in inhibiting apoptosis.Phosphorylates serine or threonine residues proximal to acidic amino acids (consensus Ser-Xaa-Xaa-Acidic where acidic residue may be Glu, Asp, pSer or pTYr). Thought to be a dual-specificity kinase in yeast, also able to phosphorylate tyrosine residues, although with less favourable kinetic parameters. ATP or GTP can serve as a phosphate donor. Disruption of CKA1 or CKA2 is not lethal, but disruption of both is synthetic lethal. CKA1 and CKA2 functional overlap is not complete, as yeast with temperature sensitive alleles of CKA1 or CKA2 display distinct phenotypes and different combinations of CKA subunits affect substrate specificity and sub-cellular localization. Disruption of CKB1 or CKB2 causes sensitivity to NaCl and LiCl. Disruption of both CKB1 and CKB2 is not synthetic lethal, although the regulatory subunits are responsible for the structural integrity of the holoenzyme. Much of CK2B is phosphorylated on autophosphorylation site and also in a cell cycle-dependent manner.","predictedComplex":false,"interactors":[{"ac":"EBI-9533","identifier":"P15790","identifierLink":"https://www.uniprot.org/uniprotkb/P15790/entry","name":"CKA1","description":"Casein kinase II subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24054","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9563","identifier":"P43639","identifierLink":"https://www.uniprot.org/uniprotkb/P43639/entry","name":"CKB1","description":"Casein kinase II subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9578","identifier":"P38930","identifierLink":"https://www.uniprot.org/uniprotkb/P38930/entry","name":"CKB2","description":"Casein kinase II subunit beta'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-770","complexName":"Casein kinase II complex, CKA2 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"CK2 is involved in regulation of cell cycle progression, presumably through phosphorylation of target proteins. CK2 may also have role(s) in inhibiting apoptosis.Phosphorylates serine or threonine residues proximal to acidic amino acids (consensus Ser-Xaa-Xaa-Acidic where acidic residue may be Glu, Asp, pSer or pTYr). Thought to be a dual-specificity kinase in yeast, also able to phosphorylate tyrosine residues, although with less favourable kinetic parameters. ATP or GTP can serve as a phosphate donor. Disruption of CKA1 or CKA2 is not lethal, but disruption of both is synthetic lethal. CKA1 and CKA2 functional overlap is not complete, as yeast with temperature sensitive alleles of CKA1 or CKA2 display distinct phenotypes and different combinations of CKA subunits affect substrate specificity and sub-cellular localization. Disruption of CKB1 or CKB2 causes sensitivity to NaCl and LiCl. Disruption of both CKB1 and CKB2 is not synthetic lethal, although the regulatory subunits are responsible for the structural integrity of the holoenzyme. Much of CK2B is phosphorylated on autophosphorylation site and also in a cell cycle-dependent manner.","predictedComplex":false,"interactors":[{"ac":"EBI-9548","identifier":"P19454","identifierLink":"https://www.uniprot.org/uniprotkb/P19454/entry","name":"CKA2","description":"Casein kinase II subunit alpha'","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24054","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9563","identifier":"P43639","identifierLink":"https://www.uniprot.org/uniprotkb/P43639/entry","name":"CKB1","description":"Casein kinase II subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9578","identifier":"P38930","identifierLink":"https://www.uniprot.org/uniprotkb/P38930/entry","name":"CKB2","description":"Casein kinase II subunit beta'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-771","complexName":"UTP-C complex variant 2","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A subcomplex of the 90S preribosome required for early processing of 18S rRNA and 40S ribosome formation.","predictedComplex":false,"interactors":[{"ac":"EBI-16019","identifier":"P25368","identifierLink":"https://www.uniprot.org/uniprotkb/P25368/entry","name":"RRP7","description":"Ribosomal RNA-processing protein 7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13191","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1878","identifier":"P53254","identifierLink":"https://www.uniprot.org/uniprotkb/P53254/entry","name":"UTP22","description":"U3 small nucleolar RNA-associated protein 22","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR17972","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9533","identifier":"P15790","identifierLink":"https://www.uniprot.org/uniprotkb/P15790/entry","name":"CKA1","description":"Casein kinase II subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24054","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9563","identifier":"P43639","identifierLink":"https://www.uniprot.org/uniprotkb/P43639/entry","name":"CKB1","description":"Casein kinase II subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9578","identifier":"P38930","identifierLink":"https://www.uniprot.org/uniprotkb/P38930/entry","name":"CKB2","description":"Casein kinase II subunit beta'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-772","complexName":"UTP-C complex variant 1","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A subcomplex of the 90S preribosome required for early processing of 18S rRNA and 40S ribosome formation.","predictedComplex":false,"interactors":[{"ac":"EBI-16019","identifier":"P25368","identifierLink":"https://www.uniprot.org/uniprotkb/P25368/entry","name":"RRP7","description":"Ribosomal RNA-processing protein 7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13191","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1878","identifier":"P53254","identifierLink":"https://www.uniprot.org/uniprotkb/P53254/entry","name":"UTP22","description":"U3 small nucleolar RNA-associated protein 22","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR17972","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9533","identifier":"P15790","identifierLink":"https://www.uniprot.org/uniprotkb/P15790/entry","name":"CKA1","description":"Casein kinase II subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24054","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9548","identifier":"P19454","identifierLink":"https://www.uniprot.org/uniprotkb/P19454/entry","name":"CKA2","description":"Casein kinase II subunit alpha'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24054","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9563","identifier":"P43639","identifierLink":"https://www.uniprot.org/uniprotkb/P43639/entry","name":"CKB1","description":"Casein kinase II subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9578","identifier":"P38930","identifierLink":"https://www.uniprot.org/uniprotkb/P38930/entry","name":"CKB2","description":"Casein kinase II subunit beta'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-773","complexName":"UTP-C complex variant 3","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A subcomplex of the 90S preribosome required for early processing of 18S rRNA and 40S ribosome formation.","predictedComplex":false,"interactors":[{"ac":"EBI-16019","identifier":"P25368","identifierLink":"https://www.uniprot.org/uniprotkb/P25368/entry","name":"RRP7","description":"Ribosomal RNA-processing protein 7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13191","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1878","identifier":"P53254","identifierLink":"https://www.uniprot.org/uniprotkb/P53254/entry","name":"UTP22","description":"U3 small nucleolar RNA-associated protein 22","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR17972","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9548","identifier":"P19454","identifierLink":"https://www.uniprot.org/uniprotkb/P19454/entry","name":"CKA2","description":"Casein kinase II subunit alpha'","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24054","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9563","identifier":"P43639","identifierLink":"https://www.uniprot.org/uniprotkb/P43639/entry","name":"CKB1","description":"Casein kinase II subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9578","identifier":"P38930","identifierLink":"https://www.uniprot.org/uniprotkb/P38930/entry","name":"CKB2","description":"Casein kinase II subunit beta'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-774","complexName":"CURI complex variant 1","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Plays a role in coupling ribosomal protein gene transcription and ribosomal RNA synthesis and processing. Acts to sequester the ribosomal protein (RP)-specific transcription factor, IFH1, to reduce transcription of RP genes during periods of growth inhibition.  Upon growth inhibition, the key regulator of cell growth, TORC1 is inactivated, which leads to rapid release of IFH1 from the RP gene promoter. RNA polymerase I activity inhibits the ability of UTP22, a component of both this complex and the SSU processome, to titrate IFH1 from RPG promoters. The CURI complex also activate transcription of RP genes since the CK2 component of the CURI complex can phosphorylate IFH1 at the sites essential for strong binding to FHL1 at the RP promoters.","predictedComplex":false,"interactors":[{"ac":"EBI-16019","identifier":"P25368","identifierLink":"https://www.uniprot.org/uniprotkb/P25368/entry","name":"RRP7","description":"Ribosomal RNA-processing protein 7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13191","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1878","identifier":"P53254","identifierLink":"https://www.uniprot.org/uniprotkb/P53254/entry","name":"UTP22","description":"U3 small nucleolar RNA-associated protein 22","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR17972","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9054","identifier":"P39520","identifierLink":"https://www.uniprot.org/uniprotkb/P39520/entry","name":"IFH1","description":"Protein IFH1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9533","identifier":"P15790","identifierLink":"https://www.uniprot.org/uniprotkb/P15790/entry","name":"CKA1","description":"Casein kinase II subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24054","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9548","identifier":"P19454","identifierLink":"https://www.uniprot.org/uniprotkb/P19454/entry","name":"CKA2","description":"Casein kinase II subunit alpha'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24054","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9563","identifier":"P43639","identifierLink":"https://www.uniprot.org/uniprotkb/P43639/entry","name":"CKB1","description":"Casein kinase II subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9578","identifier":"P38930","identifierLink":"https://www.uniprot.org/uniprotkb/P38930/entry","name":"CKB2","description":"Casein kinase II subunit beta'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-775","complexName":"CURI complex variant 2","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Plays a role in coupling ribosomal protein gene transcription and ribosomal RNA synthesis and processing. Acts to sequester the ribosomal protein (RP)-specific transcription factor, IFH1, to reduce transcription of RP genes during periods of growth inhibition.  Upon growth inhibition, the key regulator of cell growth, TORC1 is inactivated, which leads to rapid release of IFH1 from the RP gene promoter. RNA polymerase I activity inhibits the ability of UTP22, a component of both this complex and the SSU processome, to titrate IFH1 from RPG promoters. The CURI complex also activate transcription of RP genes since the CK2 component of the CURI complex can phosphorylate IFH1 at the sites essential for strong binding to FHL1 at the RP promoters.","predictedComplex":false,"interactors":[{"ac":"EBI-16019","identifier":"P25368","identifierLink":"https://www.uniprot.org/uniprotkb/P25368/entry","name":"RRP7","description":"Ribosomal RNA-processing protein 7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13191","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1878","identifier":"P53254","identifierLink":"https://www.uniprot.org/uniprotkb/P53254/entry","name":"UTP22","description":"U3 small nucleolar RNA-associated protein 22","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR17972","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9054","identifier":"P39520","identifierLink":"https://www.uniprot.org/uniprotkb/P39520/entry","name":"IFH1","description":"Protein IFH1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9533","identifier":"P15790","identifierLink":"https://www.uniprot.org/uniprotkb/P15790/entry","name":"CKA1","description":"Casein kinase II subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24054","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9563","identifier":"P43639","identifierLink":"https://www.uniprot.org/uniprotkb/P43639/entry","name":"CKB1","description":"Casein kinase II subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9578","identifier":"P38930","identifierLink":"https://www.uniprot.org/uniprotkb/P38930/entry","name":"CKB2","description":"Casein kinase II subunit beta'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-776","complexName":"CURI complex variant 3","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Plays a role in coupling ribosomal protein gene transcription and ribosomal RNA synthesis and processing. Acts to sequester the ribosomal protein (RP)-specific transcription factor, IFH1, to reduce transcription of RP genes during periods of growth inhibition.  Upon growth inhibition, the key regulator of cell growth, TORC1 is inactivated, which leads to rapid release of IFH1 from the RP gene promoter. RNA polymerase I activity inhibits the ability of UTP22, a component of both this complex and the SSU processome, to titrate IFH1 from RPG promoters. The CURI complex also activate transcription of RP genes since the CK2 component of the CURI complex can phosphorylate IFH1 at the sites essential for strong binding to FHL1 at the RP promoters.","predictedComplex":false,"interactors":[{"ac":"EBI-16019","identifier":"P25368","identifierLink":"https://www.uniprot.org/uniprotkb/P25368/entry","name":"RRP7","description":"Ribosomal RNA-processing protein 7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13191","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1878","identifier":"P53254","identifierLink":"https://www.uniprot.org/uniprotkb/P53254/entry","name":"UTP22","description":"U3 small nucleolar RNA-associated protein 22","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR17972","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9054","identifier":"P39520","identifierLink":"https://www.uniprot.org/uniprotkb/P39520/entry","name":"IFH1","description":"Protein IFH1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9548","identifier":"P19454","identifierLink":"https://www.uniprot.org/uniprotkb/P19454/entry","name":"CKA2","description":"Casein kinase II subunit alpha'","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24054","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9563","identifier":"P43639","identifierLink":"https://www.uniprot.org/uniprotkb/P43639/entry","name":"CKB1","description":"Casein kinase II subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9578","identifier":"P38930","identifierLink":"https://www.uniprot.org/uniprotkb/P38930/entry","name":"CKB2","description":"Casein kinase II subunit beta'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-777","complexName":"SAS acetyltransferase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Histone acetyltransferase (HAT) complex capable of acetylating both free histones and nucleosomes, although the nucleosomal HAT activity of SAS complex is relatively weak. Exclusively acetylates Lys-16 of histone H4 and may provide a barrier to Sir (silent information regulator) proteins that would prevent adjacent euchromatic regions from being transcriptionally inactivated. The complex appears to assemble in the nucleus, following the separate import of the components.","predictedComplex":false,"interactors":[{"ac":"EBI-16476","identifier":"P40963","identifierLink":"https://www.uniprot.org/uniprotkb/P40963/entry","name":"SAS2","description":"Histone acetyltransferase SAS2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31212","identifier":"Q99314","identifierLink":"https://www.uniprot.org/uniprotkb/Q99314/entry","name":"SAS5","description":"Something about silencing protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23195","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-38500","identifier":"Q04003","identifierLink":"https://www.uniprot.org/uniprotkb/Q04003/entry","name":"SAS4","description":"Something about silencing protein 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR38422","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-778","complexName":"TRM11-TRM112 tRNA (m2G10) methyltransferase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"S-adenosylmethionine-dependent methyltransferase responsible for the formation of N2-monomethylguanosine at position 10 (m2G10) in yeast cytoplasmic tRNA. The m2G10 is part of the body of the tRNA and is likely involved in tRNA folding and stability. m2G10 is stacked onto the m22G26 nucleotide which is methylated by Trm1 (P15565).","predictedComplex":false,"interactors":[{"ac":"EBI-28520","identifier":"P53738","identifierLink":"https://www.uniprot.org/uniprotkb/P53738/entry","name":"TRM112","description":"Multifunctional methyltransferase subunit TRM112","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12773","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30471","identifier":"Q12463","identifierLink":"https://www.uniprot.org/uniprotkb/Q12463/entry","name":"TRM11","description":"tRNA (guanine(10)-N(2))-methyltransferase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13370","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-779","complexName":"Elongator holoenzyme complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"N-acetyltransferase which acts to form modified wobble uridines in tRNA, such as 5-methoxycarbonylmethyl-uridine (mcm5U), 5-methoxycarbonylmethyl-2-thio-uridine (mcm5s2U), and 5-carbamoylmethyl-uridine (ncm5U). These sites  influence the recognition rate and affinity between incoming tRNAs and codons in the A site of the translating ribosome, stablizing transient pausing events thus supporting proper domain folding of the nascent polypeptide chains during  the elongation phase of the ribosome‐mediated translation process.","predictedComplex":false,"interactors":[{"ac":"EBI-23459","identifier":"P42935","identifierLink":"https://www.uniprot.org/uniprotkb/P42935/entry","name":"ELP2","description":"Elongator complex protein 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR44111","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27653","identifier":"Q04868","identifierLink":"https://www.uniprot.org/uniprotkb/Q04868/entry","name":"ELP6","description":"Elongator complex protein 6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR16184","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-33957","identifier":"Q02908","identifierLink":"https://www.uniprot.org/uniprotkb/Q02908/entry","name":"ELP3","description":"Elongator complex protein 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11135","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-35277","identifier":"Q02884","identifierLink":"https://www.uniprot.org/uniprotkb/Q02884/entry","name":"ELP4","description":"Elongator complex protein 4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12896","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9061","identifier":"P38874","identifierLink":"https://www.uniprot.org/uniprotkb/P38874/entry","name":"IKI1","description":"Elongator complex protein 5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15641","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9068","identifier":"Q06706","identifierLink":"https://www.uniprot.org/uniprotkb/Q06706/entry","name":"IKI3","description":"Elongator complex protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12747","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-780","complexName":"Signal recognition particle receptor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Mediates the co-translational targeting of membrane and secretory proteins. The signal recognition particle (SRP) binds to 9-12 large hydrophobic residues that constitute the signal sequences of nascent proteins as they emerge from the exit tunnel of the ribosome. The resulting targeting complex, composed of the SRP and the ribosome-nascent chain complex, then docks with the Signal recognition particle receptor.  This interaction catalyzes the GTP-dependent transfer of the nascent chain from SRP to the protein translocation apparatus in the ER membrane. Following GTP hydrolysis, the complex dissociates.","predictedComplex":false,"interactors":[{"ac":"EBI-18091","identifier":"P36057","identifierLink":"https://www.uniprot.org/uniprotkb/P36057/entry","name":"SRP102","description":"Signal recognition particle receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11485","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18098","identifier":"P32916","identifierLink":"https://www.uniprot.org/uniprotkb/P32916/entry","name":"SRP101","description":"Signal recognition particle receptor subunit alpha homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-989053","identifier":"CHEBI:15996","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15996","name":"gtp","description":"guanosine triphosphate - GTP","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-781","complexName":"NatC N-alpha-acetyltransferase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"N(alpha)-acetyltransferases, NatA (CPX-781), NatB (CPX-782) and NatC, carry out N-terminal acetylation, one of the most common co-translational modifications. Mak3 is the catalytic subunit of NatC. All three subunits are required for NatC activity. NatC substrates are rare but subclasses of proteins with Met-Ile, Met-Leu, Met-Trp, or Met-Phe termini are not acetylated in Mak3 deletion mutants.  All three deletion strains showed similar phenotypes, including slower growth on non-fermentable carbon sources at elevated temperature.","predictedComplex":false,"interactors":[{"ac":"EBI-10388","identifier":"Q03503","identifierLink":"https://www.uniprot.org/uniprotkb/Q03503/entry","name":"MAK3","description":"N-alpha-acetyltransferase 30","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45896","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10924","identifier":"Q02197","identifierLink":"https://www.uniprot.org/uniprotkb/Q02197/entry","name":"MAK10","description":"N-alpha-acetyltransferase 35, NatC auxiliary subunit","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21373","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10950","identifier":"P23059","identifierLink":"https://www.uniprot.org/uniprotkb/P23059/entry","name":"MAK31","description":"N-alpha-acetyltransferase 38, NatC auxiliary subunit","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-782","complexName":"NatB N-alpha-acetyltransferase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"N(alpha)-acetyltransferases, NatA (CPX-783), NatB and NatC (CPX-781), carry out N-terminal acetylation,  the covalent attachment of an acetyl group (CH3CO) to the free alpha-amino group (NH3+) at the N-terminal end of a polypeptide, one of the most common co-translational modifications. This changes the electrostatic properties of proteins and therefore protein function, stability and localization. NatB is responsible for the acetylation of methionine-acidic/hydrophilic N-termini (Met-Asp-, Met-Asn-, Met-Glu-, and Met-Gln-).","predictedComplex":false,"interactors":[{"ac":"EBI-31002","identifier":"Q06504","identifierLink":"https://www.uniprot.org/uniprotkb/Q06504/entry","name":"NAT3","description":"N-terminal acetyltransferase B complex catalytic subunit NAT3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45910","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5736","identifier":"Q12387","identifierLink":"https://www.uniprot.org/uniprotkb/Q12387/entry","name":"MDM20","description":"N-terminal acetyltransferase B complex subunit MDM20","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-783","complexName":"NatA N-alpha-acetyltransferase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"N(alpha)-acetyltransferases, NatA, NatB (CPX-782) and NatC (CPX-781), carry out N-terminal acetylation, one of the most common co-translational modifications. NatA is the major Nalpha-terminal acetyltransferase in the yeast cytosol, responsible for the acetylation of serine, alanine, threonine, and glycine. NAT1 anchors to the ribosome and interacts with nascent polypeptides.","predictedComplex":false,"interactors":[{"ac":"EBI-11868","identifier":"P12945","identifierLink":"https://www.uniprot.org/uniprotkb/P12945/entry","name":"NAT1","description":"N-terminal acetyltransferase A complex subunit NAT1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2796","identifier":"P07347","identifierLink":"https://www.uniprot.org/uniprotkb/P07347/entry","name":"ARD1","description":"N-terminal acetyltransferase A complex catalytic subunit ARD1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23091","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34404","identifier":"Q08689","identifierLink":"https://www.uniprot.org/uniprotkb/Q08689/entry","name":"NAT5","description":"N-alpha-acetyltransferase NAT5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR42919","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-828","complexName":"RTG transcription factor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Heterodimeric transcription factor involved in the regulation of nuclear genes, such as CIT2, in response to mitochondrial stress. Also essential for peroxisome proliferation. Binds to each of two identical non-E-box core sequences, 5-GGTCAC-3, in the 76-bp regulatory upstream activation sequence element of the CIT2 promoter.","predictedComplex":false,"interactors":[{"ac":"EBI-16312","identifier":"P32607","identifierLink":"https://www.uniprot.org/uniprotkb/P32607/entry","name":"RTG1","description":"Retrograde regulation protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-16328","identifier":"P38165","identifierLink":"https://www.uniprot.org/uniprotkb/P38165/entry","name":"RTG3","description":"Retrograde regulation protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45776","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-863","complexName":"INO80 chromatin remodeling complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Chromatin remodeling complex with both DNA-dependent ATPase activity, as well as 3'-5' helicase activity. Mobilizes mononucleosomes in an ATP-dependent manner thus regulating a distinct subset of genes. Also involved in multiple DNA repair pathways by its nucleosome remodeling ability, by regulating the accessibility of DNA repair proteins around the DNA double strand break site and by facilitating efficient homologous recombination.","predictedComplex":false,"interactors":[{"ac":"EBI-12010","identifier":"Q03435","identifierLink":"https://www.uniprot.org/uniprotkb/Q03435/entry","name":"NHP10","description":"Non-histone protein 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR48112","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18920","identifier":"P35189","identifierLink":"https://www.uniprot.org/uniprotkb/P35189/entry","name":"TAF14","description":"Transcription initiation factor TFIID subunit 14","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23195","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2169","identifier":"P60010","identifierLink":"https://www.uniprot.org/uniprotkb/P60010/entry","name":"ACT1","description":"Actin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22358","identifier":"P32617","identifierLink":"https://www.uniprot.org/uniprotkb/P32617/entry","name":"IES6","description":"Chromatin-remodeling complex subunit IES6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31200","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22617","identifier":"P40060","identifierLink":"https://www.uniprot.org/uniprotkb/P40060/entry","name":"IES5","description":"Ino eighty subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-22775","identifier":"P43579","identifierLink":"https://www.uniprot.org/uniprotkb/P43579/entry","name":"IES1","description":"Ino eighty subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR37287","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-24019","identifier":"P53115","identifierLink":"https://www.uniprot.org/uniprotkb/P53115/entry","name":"INO80","description":"Chromatin-remodeling ATPase INO80","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45685","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29144","identifier":"P40154","identifierLink":"https://www.uniprot.org/uniprotkb/P40154/entry","name":"IES2","description":"Ino eighty subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21561","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2939","identifier":"P80428","identifierLink":"https://www.uniprot.org/uniprotkb/P80428/entry","name":"ARP4","description":"Actin-related protein 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2951","identifier":"P53946","identifierLink":"https://www.uniprot.org/uniprotkb/P53946/entry","name":"ARP5","description":"Actin-related protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2967","identifier":"Q12386","identifierLink":"https://www.uniprot.org/uniprotkb/Q12386/entry","name":"ARP8","description":"Actin-like protein ARP8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30712","identifier":"Q03940","identifierLink":"https://www.uniprot.org/uniprotkb/Q03940/entry","name":"RVB1","description":"RuvB-like protein 1","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31814","identifier":"Q12464","identifierLink":"https://www.uniprot.org/uniprotkb/Q12464/entry","name":"RVB2","description":"RuvB-like protein 2","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-35758","identifier":"Q12345","identifierLink":"https://www.uniprot.org/uniprotkb/Q12345/entry","name":"IES3","description":"Ino eighty subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-35881","identifier":"Q08561","identifierLink":"https://www.uniprot.org/uniprotkb/Q08561/entry","name":"IES4","description":"Ino eighty subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-940","complexName":"ESCRT-I complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"The ESCRT machinery consists of ESCRT-0 (CPX-1622), -I (this complex), -II (CPX-1623), -III (CPX-1624) and -IV (VPS4 complex, CPX-334) and is required for the downregulation of cell-surface receptors and for the final membrane scission step during endocytosis. The ESCRT-I complex directs the lysosomal degradation of ubiquinated transmembrane proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-18076","identifier":"Q99176","identifierLink":"https://www.uniprot.org/uniprotkb/Q99176/entry","name":"SRN2","description":"Protein SRN2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20387","identifier":"Q02767","identifierLink":"https://www.uniprot.org/uniprotkb/Q02767/entry","name":"VPS28","description":"Vacuolar protein sorting-associated protein 28","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23478","identifier":"P42939","identifierLink":"https://www.uniprot.org/uniprotkb/P42939/entry","name":"MVB12","description":"Multivesicular body sorting factor 12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-411625","identifier":"P25604","identifierLink":"https://www.uniprot.org/uniprotkb/P25604/entry","name":"STP22","description":"Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23306","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-946","complexName":"SBF transcription complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Heteromeric transcription factor, composed of a regulatory subunit SWI6) and a DNA-binding protein (SWI4), that activates gene expression during the G1/S transition of the cell cycle. Binds to a sequence motif called the SCB element (Swi4/6 cell cycle box, CACGAAA) which acts as a late Gl-specific UAS element in genes predominantly involved in budding, and in membrane and cell-wall biosynthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-18626","identifier":"P25302","identifierLink":"https://www.uniprot.org/uniprotkb/P25302/entry","name":"SWI4","description":"Regulatory protein SWI4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43828","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18641","identifier":"P09959","identifierLink":"https://www.uniprot.org/uniprotkb/P09959/entry","name":"SWI6","description":"Regulatory protein SWI6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43828","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-950","complexName":"MBP transcription complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Heteromeric transcription factor, composed of a regulatory subunit (Swi6) and a DNA-binding protein (Mbp1), that activates gene expression during the G1/S transition of the cell cycle. Binds to a sequence motif called the MCB element (MluI cell cycle box, ACGCGTNA) which acts as a late Gl-specific UAS element in genes predominantly involved in DNA replication and repair .","predictedComplex":false,"interactors":[{"ac":"EBI-10485","identifier":"P39678","identifierLink":"https://www.uniprot.org/uniprotkb/P39678/entry","name":"MBP1","description":"Transcription factor MBP1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43828","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18641","identifier":"P09959","identifierLink":"https://www.uniprot.org/uniprotkb/P09959/entry","name":"SWI6","description":"Regulatory protein SWI6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43828","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-956","complexName":"GET complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for the post-translational delivery of tail-anchored (TA) proteins to the endoplasmic reticulum. GET1 and GET2 act as a membrane receptor for soluble GET3, which recognizes and selectively binds the transmembrane domain of TA proteins in the cytosol, delivered to it by the GET4-GET5 transmembrane domain recognition complex (CPX-1861). Cooperates with the HDEL receptor ERD2 (P18414) to mediate the ATP-dependent retrieval of resident endoplasmic reticulum proteins that contain a C-terminal HDEL retention signal from the Golgi to the endoplasmic reticulum.","predictedComplex":false,"interactors":[{"ac":"EBI-22604","identifier":"P40056","identifierLink":"https://www.uniprot.org/uniprotkb/P40056/entry","name":"GET2","description":"Golgi to ER traffic protein 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28263","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23722","identifier":"P53192","identifierLink":"https://www.uniprot.org/uniprotkb/P53192/entry","name":"GET1","description":"Golgi to ER traffic protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR42650","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2989","identifier":"Q12154","identifierLink":"https://www.uniprot.org/uniprotkb/Q12154/entry","name":"GET3","description":"ATPase GET3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10803","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-961","complexName":"Mitotic spindle assembly checkpoint, MAD1-MAD2 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Acts at the spindle checkpoint, in a surveillance mechanism that mediates a delay in the onset of anaphase, until all chromosomes are properly attached to the mitotic or meiotic spindle. Required for the checkpoint response to absence of spindle tension, localising only to unattached kinetochores but not to attached kinetochores that lack tension, and participate in a bipolar orientation defect signaling pathway. MAD2 adopts two distinct conformations; when unbound, it adopts an open conformation (O-Mad2) but upon binding to MAD1 (or CDC20, P26309), two beta-sheets move across the face of the protein to create the closed conformation (C-Mad2), with MAD1 now trapped within this fold. Upon mitotic entry, the Mad1-C-Mad2 core complex is recruited to kinetochores. Because Mad2 can dimerise, O-Mad2 from the cytosol can then be recruited to kinetochore-bound Mad1-C-Mad2. C-Mad2 within the Mad1-C-Mad2 core complex acts as a prion-like template, catalysing the conversion of additional O-Mad2 proteins to the closed conformation and in doing so binding Cdc20 (CPX-962).","predictedComplex":false,"interactors":[{"ac":"EBI-10354","identifier":"P40957","identifierLink":"https://www.uniprot.org/uniprotkb/P40957/entry","name":"MAD1","description":"Spindle assembly checkpoint component MAD1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23168","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10362","identifier":"P40958","identifierLink":"https://www.uniprot.org/uniprotkb/P40958/entry","name":"MAD2","description":"Mitotic spindle checkpoint component MAD2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-962","complexName":"Mitotic checkpoint complex, CDC20-MAD2 subcomplex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Acts at the spindle checkpoint, in a surveillance mechanism that mediates a metaphase delay, until all chromosomes are properly attached to the mitotic or meiotic spindle, by sequestering Cdc20, thus preventing the activation of the the ubiquitin ligase activity of the anaphase-promoting complex (CPX-760). This ensures all chromosomes are correctly attached in a bipolar fashion to the mitotic spindle.","predictedComplex":false,"interactors":[{"ac":"EBI-10362","identifier":"P40958","identifierLink":"https://www.uniprot.org/uniprotkb/P40958/entry","name":"MAD2","description":"Mitotic spindle checkpoint component MAD2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4212","identifier":"P26309","identifierLink":"https://www.uniprot.org/uniprotkb/P26309/entry","name":"CDC20","description":"APC/C activator protein CDC20","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19918","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-963","complexName":"Mitotic checkpoint complex, MAD2-MAD3-BUB3-CDC20","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Acts at the spindle checkpoint in a surveillance mechanism that mediates a delay in the onset of anaphase until all chromosomes are properly attached to the mitotic or meiotic spindle by inhibiting the anaphase-promoting complex (CPX-760), an E3 ubquitin ligase complex required for onset of anaphase. The Mitotic checkpoint complex is a more potent inhibitor of the APC/C than Mad2-Cdc20 alone (CPX-962).","predictedComplex":false,"interactors":[{"ac":"EBI-10362","identifier":"P40958","identifierLink":"https://www.uniprot.org/uniprotkb/P40958/entry","name":"MAD2","description":"Mitotic spindle checkpoint component MAD2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10369","identifier":"P47074","identifierLink":"https://www.uniprot.org/uniprotkb/P47074/entry","name":"MAD3","description":"Spindle assembly checkpoint component MAD3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14030","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3830","identifier":"P26449","identifierLink":"https://www.uniprot.org/uniprotkb/P26449/entry","name":"BUB3","description":"Spindle assembly checkpoint protein BUB3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4212","identifier":"P26309","identifierLink":"https://www.uniprot.org/uniprotkb/P26309/entry","name":"CDC20","description":"APC/C activator protein CDC20","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19918","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-964","complexName":"GTPase-activating BFA1-BUB2 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Acts as a two-component GTPase-activating complex for TEM1 (P38987) GTPase, thus regulating a signal transduction cascade, called the mitotic exit network (MEN), which is required for mitotic exit and cytokinesis. The BUB2/BFA1 GAP binds TEM1 GTPase at spindle poles, achieving an asymmetry during mitosis when the spindle is properly positioned, with the complex accumulating on the bud-directed old spindle pole. BUB2/BFA1 keeps TEM1 inactive until the spindle is properly oriented, thus inhibiting MEN activation. Upon spindle misalignment TEM1 localizes symmetrically on both SPBs and the Spindle Position Checkpoint (SPOC) inhibits TEM1 through the BUB2/BFA1 complex, thereby restraining the MEN until the spindle repositions correctly.","predictedComplex":false,"interactors":[{"ac":"EBI-3586","identifier":"P47113","identifierLink":"https://www.uniprot.org/uniprotkb/P47113/entry","name":"BFA1","description":"Mitotic check point protein BFA1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR35140","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3824","identifier":"P26448","identifierLink":"https://www.uniprot.org/uniprotkb/P26448/entry","name":"BUB2","description":"Mitotic check point protein BUB2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1036","complexName":"DNA mismatch repair MutSbeta complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Mismatch repair complex, involved in the recognition and repair of insertion/deletion mismatches. Active in both targeted gene replacement in which a targeted sequence in the genome is replaced with a selectable gene from a linear targeting DNA, and the single-strand annealing pathway of recombination between direct repeats. Direct repeats flanking a double-stranded break is annealed by RAD52 (P06778) and further stabilized by MSH2-MSH3 which has similar activities on both the leading and lagging strands of replication. MSH2-MSH3 appear to facilitate targeted integration by the two-end invasion pathway while simultaneously inhibiting the single-strand assimilation pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-11352","identifier":"P25847","identifierLink":"https://www.uniprot.org/uniprotkb/P25847/entry","name":"MSH2","description":"DNA mismatch repair protein MSH2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11361","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11362","identifier":"P25336","identifierLink":"https://www.uniprot.org/uniprotkb/P25336/entry","name":"MSH3","description":"DNA mismatch repair protein MSH3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11361","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1037","complexName":"DNA mismatch repair MutSalpha complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Mismatch repair complex, involved in the recognition and repair of base-base and small insertion/deletion mismatches that appear as a consequence of DNA polymerase errors during DNA synthesis.  The complex is most effective at repairing mismatches on the lagging strand of replication. Binding to a mismatched DNA which can bend, leads to stable association of MSH2 with DNA, inhibition of its ATP activity and formation of ATP-bound MSH2-MSH6 sliding clamps.  When MSH6 is bound to mismatched DNA and MSH2 to ATP, the complex can recruit MutLalpha and initiate the repair process. Binding of MSH2-MSH6 to a mismatch and provides a recognition signal for interactions with repair proteins that are involved in subsequent steps.","predictedComplex":false,"interactors":[{"ac":"EBI-11352","identifier":"P25847","identifierLink":"https://www.uniprot.org/uniprotkb/P25847/entry","name":"MSH2","description":"DNA mismatch repair protein MSH2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11361","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11383","identifier":"Q03834","identifierLink":"https://www.uniprot.org/uniprotkb/Q03834/entry","name":"MSH6","description":"DNA mismatch repair protein MSH6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11361","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1038","complexName":"PIP2-OAF1 transcription factor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Acts as a transcriptional activator to induce the transcription of genes encoding proteins involved in fatty acid beta-oxidation, a response called oleic acid induction, when cells grow on fatty acids as the sole carbon source. Recognizes and binds to the oleate response element (ORE or peroxisome box), two inverted CGG triplets spaced by 14 to 18 intervening nucleotides recently refined to CGGN3TNA/(R)N8-12CCG, in the promoter region of a number of peroxisomal genes. Activity is inhibited by OAF1 under non-inducing conditions and repressed by glucose.","predictedComplex":false,"interactors":[{"ac":"EBI-13436","identifier":"P52960","identifierLink":"https://www.uniprot.org/uniprotkb/P52960/entry","name":"PIP2","description":"Peroxisome proliferation transcriptional regulator","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31069","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20693","identifier":"P39720","identifierLink":"https://www.uniprot.org/uniprotkb/P39720/entry","name":"OAF1","description":"Oleate-activated transcription factor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31069","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1039","complexName":"COMPASS complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Histone methyltransferase that catalyzes methylation of Lys-4 of histone H3 and thus controls the silencing of telomeric regions. SWD1, SWD3, and SET1 constitute a core of the complex, and the absence of any of these subunits abolishes methylation of lysine 4 on histone H3. Subunits BRE2 and SDC1 are essential for trimethylation and important for mono- and dimethylation by the COMPASS complex. SPP1 is important for trimethylation, while SHG1 plays a minor role in trimethylation.","predictedComplex":false,"interactors":[{"ac":"EBI-16977","identifier":"P38827","identifierLink":"https://www.uniprot.org/uniprotkb/P38827/entry","name":"SET1","description":"Histone-lysine N-methyltransferase, H3 lysine-4 specific","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45814","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20737","identifier":"P39706","identifierLink":"https://www.uniprot.org/uniprotkb/P39706/entry","name":"SWD1","description":"COMPASS component SWD1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR44040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20881","identifier":"P38123","identifierLink":"https://www.uniprot.org/uniprotkb/P38123/entry","name":"SWD3","description":"COMPASS component SWD3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21106","identifier":"P38337","identifierLink":"https://www.uniprot.org/uniprotkb/P38337/entry","name":"SHG1","description":"COMPASS component SHG1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-26608","identifier":"P36104","identifierLink":"https://www.uniprot.org/uniprotkb/P36104/entry","name":"SWD2","description":"COMPASS component SWD2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19861","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27115","identifier":"P43132","identifierLink":"https://www.uniprot.org/uniprotkb/P43132/entry","name":"BRE2","description":"COMPASS component BRE2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10598","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32540","identifier":"Q03012","identifierLink":"https://www.uniprot.org/uniprotkb/Q03012/entry","name":"SPP1","description":"COMPASS component SPP1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46174","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-38307","identifier":"Q03323","identifierLink":"https://www.uniprot.org/uniprotkb/Q03323/entry","name":"SDC1","description":"COMPASS component SDC1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1040","complexName":"SKI complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Central component of the 3'-5' cytoplasmic mRNA degradation pathway which interacts with Ski7 (Q08491) to mediate degradation by the exosome. The Ski complex appears to thread RNAs directly to the exosome, coupling the helicase and the exoribonuclease through a continuous RNA channel.","predictedComplex":false,"interactors":[{"ac":"EBI-17260","identifier":"Q02793","identifierLink":"https://www.uniprot.org/uniprotkb/Q02793/entry","name":"SKI8","description":"Antiviral protein SKI8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR44090","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1851","identifier":"P35207","identifierLink":"https://www.uniprot.org/uniprotkb/P35207/entry","name":"SKI2","description":"Antiviral helicase SKI2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1861","identifier":"P17883","identifierLink":"https://www.uniprot.org/uniprotkb/P17883/entry","name":"SKI3","description":"Superkiller protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15704","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1041","complexName":"DASH complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Heterodecameric component of the kinetochore necessary for accurate chromosome segregation, supporting the dynamic attachment of mitotic chromosomes to the ends of shortening spindle microtubules. DASH forms closed rings around microtubules with a large gap between the DASH ring and the microtubule cylinder. A DASH-microtubule interface is believed to form, in which extensions from DASH rings reach across a gap between the ring and the microtubule and dock on the microtubule wall. DASH rings spontaneously oligomerize in the presence of microtubules of the mitotic spindle. DASH rings are processivity factors that allow kinetochores to translate along a single microtubule without dissociating. Each DASH ring may contain from 16-30 heterodecamers. The NDC80 complex (CPX-548) can simultaneously bind and bridge across two DASH complex rings through a tripartite interaction, each component of which is regulated by IPL1 kinase (P38991). This ensures a consistent spacing between rings. The complex may also may serve as a link between the kinetochore and the mitotic spindle.","predictedComplex":false,"interactors":[{"ac":"EBI-1379800","identifier":"P69852","identifierLink":"https://www.uniprot.org/uniprotkb/P69852/entry","name":"HSK3","description":"DASH complex subunit HSK3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28289","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23268","identifier":"P53267","identifierLink":"https://www.uniprot.org/uniprotkb/P53267/entry","name":"DAM1","description":"DASH complex subunit DAM1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28113","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23800","identifier":"P53168","identifierLink":"https://www.uniprot.org/uniprotkb/P53168/entry","name":"DUO1","description":"DASH complex subunit DUO1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28216","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26401","identifier":"P36131","identifierLink":"https://www.uniprot.org/uniprotkb/P36131/entry","name":"SPC34","description":"DASH complex subunit SPC34","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-26515","identifier":"P36162","identifierLink":"https://www.uniprot.org/uniprotkb/P36162/entry","name":"DAD2","description":"DASH complex subunit DAD2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26682","identifier":"P35734","identifierLink":"https://www.uniprot.org/uniprotkb/P35734/entry","name":"ASK1","description":"DASH complex subunit ASK1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28200","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-35662","identifier":"Q12248","identifierLink":"https://www.uniprot.org/uniprotkb/Q12248/entry","name":"DAD1","description":"DASH complex subunit DAD1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28025","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-38809","identifier":"Q03954","identifierLink":"https://www.uniprot.org/uniprotkb/Q03954/entry","name":"SPC19","description":"DASH complex subunit SPC19","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28262","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-975376","identifier":"P69850","identifierLink":"https://www.uniprot.org/uniprotkb/P69850/entry","name":"DAD3","description":"DASH complex subunit DAD3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28017","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-975389","identifier":"P69851","identifierLink":"https://www.uniprot.org/uniprotkb/P69851/entry","name":"DAD4","description":"DASH complex subunit DAD4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1101","complexName":"RNA polymerase I upstream activating factor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Binds tightly to the upstream element of the yeast Pol I promoter and is essential for a high level of transcription of the 35S rRNA gene. UAF has dual functions: both as a positive transcription factor for Pol I, and as a silencer for Pol II transcription of rRNA genes. Deletion of any one of the subunit protein genes encoding essential nonhistone proteins causes derepression of Pol II transcription of the 35S rRNA genes. The association of H3 and H4 with the other UAF components is important for the stability of UAF in vivo and, hence, for rRNA transcription by Pol I. Initiation of transcription requires the assembly of UAF, the core factor (CPX-1836), the TATA binding protein SPT15 (P13393), and RNAP-I (CPX-1664) with RRN3 (P36070) on the upstream element and core promoter. Upon transcription initiation, UAF, RRN3 and CF dissociate from the promoter.","predictedComplex":false,"interactors":[{"ac":"EBI-15981","identifier":"Q02983","identifierLink":"https://www.uniprot.org/uniprotkb/Q02983/entry","name":"RRN5","description":"RNA polymerase I-specific transcription initiation factor RRN5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28079","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15994","identifier":"P53437","identifierLink":"https://www.uniprot.org/uniprotkb/P53437/entry","name":"RRN9","description":"RNA polymerase I-specific transcription initiation factor RRN9","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-15998","identifier":"P38204","identifierLink":"https://www.uniprot.org/uniprotkb/P38204/entry","name":"RRN10","description":"RNA polymerase I-specific transcription initiation factor RRN10","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28054","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-37084","identifier":"Q08747","identifierLink":"https://www.uniprot.org/uniprotkb/Q08747/entry","name":"UAF30","description":"Upstream activation factor subunit UAF30","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8098","identifier":"P61830","identifierLink":"https://www.uniprot.org/uniprotkb/P61830/entry","name":"HHT1","description":"Histone H3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11426","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8113","identifier":"P02309","identifierLink":"https://www.uniprot.org/uniprotkb/P02309/entry","name":"HHF1","description":"Histone H4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10484","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1102","complexName":"Ribonucleoside-diphosphate reductase variant 1","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the reduction of ribonucleotides to the corresponding deoxyribonucleotides, an essential step in the de novo synthesis of monomeric precursors for DNA replication and repair. The catalytically active form is an alpha2beta2 tetramer. The homodimeric alpha subunit, called R1, houses the active site, composed of redox-active disulfides, and binding sites for allosteric effectors, ribonucleoside diphosphates. The beta subunit, called R2, contains a di-iron cluster that in its reduced state reacts with dioxygen to form a stable tyrosyl radical (Y*) and a di-iron(III) cluster. This essential Y* is proposed to generate a thiyl radical, located on a cysteine residue in the R1 active site, that initiates ribonucleotide reduction. The enzyme is allosterically controlled by relative levels of dNTPs. This variant is found in all cell states, a related variant (CPX-1103) is only found in damaged or growth-arrested cells.  the small subunit, RNR2-RNR4, is nuclear while the large subunit, RNR1, is cytoplasmic. In response to S-phase or DNA-damage, RNR2-RNR4 enters the cytoplasm to bind RNR1.","predictedComplex":false,"interactors":[{"ac":"EBI-11472102","identifier":"CHEBI:24875","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:24875","name":"iron cation","description":"iron cation","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-15234","identifier":"P21524","identifierLink":"https://www.uniprot.org/uniprotkb/P21524/entry","name":"RNR1","description":"Ribonucleoside-diphosphate reductase large chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11573","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15240","identifier":"P09938","identifierLink":"https://www.uniprot.org/uniprotkb/P09938/entry","name":"RNR2","description":"Ribonucleoside-diphosphate reductase small chain 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23409","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15251","identifier":"P49723","identifierLink":"https://www.uniprot.org/uniprotkb/P49723/entry","name":"RNR4","description":"Ribonucleoside-diphosphate reductase small chain 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23409","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1103","complexName":"Ribonucleoside-diphosphate reductase variant 2","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the reduction of ribonucleotides to the corresponding deoxyribonucleotides, an essential step in the de novo synthesis of monomeric precursors for DNA replication and repair. The catalytically active form of the enzyme (CPX-1102)  is an alpha2beta2 tetramer. The heterodimeric alpha subunits, called R1, house the active site, composed of redox-active disulfides, and binding sites for allosteric effectors, ribonucleoside diphosphates. The beta subunit, called R2, contains a di-iron cluster that in its reduced state reacts with dioxygen to form a stable tyrosyl radical (Y*) and a di-iron(III) cluster. This essential Y* is proposed to generate a thiyl radical, located on a cysteine residue in the R1 active site, that initiates ribonucleotide reduction. The enzyme is allosterically controlled by relative levels of dNTPs. In damaged cells or cells arrested for DNA synthesis, the small subunits (RNR2-RNR4) associate with a heterodimer of RNR1 and the damage-inducible RNR3.","predictedComplex":false,"interactors":[{"ac":"EBI-11472102","identifier":"CHEBI:24875","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:24875","name":"iron cation","description":"iron cation","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-15234","identifier":"P21524","identifierLink":"https://www.uniprot.org/uniprotkb/P21524/entry","name":"RNR1","description":"Ribonucleoside-diphosphate reductase large chain 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11573","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15240","identifier":"P09938","identifierLink":"https://www.uniprot.org/uniprotkb/P09938/entry","name":"RNR2","description":"Ribonucleoside-diphosphate reductase small chain 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23409","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15246","identifier":"P21672","identifierLink":"https://www.uniprot.org/uniprotkb/P21672/entry","name":"RNR3","description":"Ribonucleoside-diphosphate reductase large chain 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11573","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15251","identifier":"P49723","identifierLink":"https://www.uniprot.org/uniprotkb/P49723/entry","name":"RNR4","description":"Ribonucleoside-diphosphate reductase small chain 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23409","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1162","complexName":"Fatty-acyl-CoA synthase","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. Consists of a multifunctional enzyme composed of two non-identical alpha and beta subunits which are organized in an alpha6beta6 complex with 6 sites of fatty acid synthesis. The alpha subunit, FAS2, contains domains for acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. The beta subunit, FAS 1, contains domains for [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase.","predictedComplex":false,"interactors":[{"ac":"EBI-6795","identifier":"P07149","identifierLink":"https://www.uniprot.org/uniprotkb/P07149/entry","name":"FAS1","description":"Fatty acid synthase subunit beta","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10982","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6806","identifier":"P19097","identifierLink":"https://www.uniprot.org/uniprotkb/P19097/entry","name":"FAS2","description":"Fatty acid synthase subunit alpha","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10982","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1899","complexName":"Spc105 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Located to the kinetochore, interacts with centromere proteins. This complex has a role in kinetochore-microtubule binding and spindle assembly checkpoint.","predictedComplex":false,"interactors":[{"ac":"EBI-23870","identifier":"P53148","identifierLink":"https://www.uniprot.org/uniprotkb/P53148/entry","name":"SPC105","description":"Outer kinetochore KNL1 complex subunit SPC105","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28260","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32446","identifier":"Q04431","identifierLink":"https://www.uniprot.org/uniprotkb/Q04431/entry","name":"KRE28","description":"Outer kinetochore KNL1 complex subunit KRE28","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1186","complexName":"Kinetochore MIS12 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for normal chromosome alignment and segregation, kinetochore formation during mitosis, proper kinetochore microtubule attachments and for the spindle assembly checkpoint. The complex plays a role in establishing a bipolar spindle-kinetochore interaction by joining kinetochore subunits contacting DNA to those contacting microtubules. Mis12/MIND is part of a tridentate linker layer, which also contains the Ndc80 (CPX-548) and COMA (CPX-1187) complexes. Evidence suggests interactions between COMA, MIND, and Ndc80 complexes. The Mis12/MIND complex is a platform onto which outer kinetochore proteins assemble, including microtubule-binding proteins. It is proposed to have a distinct function with respect to force generation and microtubule attachment. In the absence of MIND, there is bipolar binding without the generation of sufficient pulling force to cause centromere stretching and transient sister-chromatid separation. MIND requires CBF3 complex for assembly onto centromeric DNA. Different combinations of MIND subunits have been found, which may reflect the regulated steps in kinetochore assembly.","predictedComplex":false,"interactors":[{"ac":"EBI-11606","identifier":"P39731","identifierLink":"https://www.uniprot.org/uniprotkb/P39731/entry","name":"MTW1","description":"Kinetochore-associated protein MTW1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12098","identifier":"P47149","identifierLink":"https://www.uniprot.org/uniprotkb/P47149/entry","name":"NNF1","description":"Kinetochore-associated protein NNF1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15459","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25398","identifier":"P40568","identifierLink":"https://www.uniprot.org/uniprotkb/P40568/entry","name":"DSN1","description":"Kinetochore-associated protein DSN1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14778","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-33666","identifier":"Q12143","identifierLink":"https://www.uniprot.org/uniprotkb/Q12143/entry","name":"NSL1","description":"Kinetochore-associated protein NSL1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31749","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1187","complexName":"COMA complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Heterotetrameric subcomplex of a larger central kinetochore CTF19 complex (CPX-1156).  COMA is part of a tridentate linker layer, which also contains the Ndc80 (CPX-548) and MIND (CPX-1186) complexes. Although the COMA, MIND, and Ndc80 complexes assemble independently, evidence suggests subsequent interactions. COMA is a platform onto which outer kinetochore proteins assemble, including microtubule-binding proteins. It is proposed to have a distinct function with respect to force generation and microtubule attachment. In the absence of COMA, there is bipolar binding without the generation of sufficient pulling force to cause centromere stretching and transient sister-chromatid separation. COMA requires CBF3 complex (CPX-1898) for assembly onto centromeric DNA. Different combinations of COMA subunits have been found, which may reflect the regulated steps in kinetochore assembly.","predictedComplex":false,"interactors":[{"ac":"EBI-20972","identifier":"P38313","identifierLink":"https://www.uniprot.org/uniprotkb/P38313/entry","name":"AME1","description":"Inner kinetochore subunit AME1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-23429","identifier":"P53298","identifierLink":"https://www.uniprot.org/uniprotkb/P53298/entry","name":"OKP1","description":"Inner kinetochore subunit OKP1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-32349","identifier":"Q06675","identifierLink":"https://www.uniprot.org/uniprotkb/Q06675/entry","name":"MCM21","description":"Inner kinetochore subunit MCM21","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-5199","identifier":"Q02732","identifierLink":"https://www.uniprot.org/uniprotkb/Q02732/entry","name":"CTF19","description":"Inner kinetochore subunit CTF19","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-2147","complexName":"Ire1 serine/threonine-protein kinase/endoribonuclease complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Endoplasmic reticulum localized, type-I transmembrane homodimer which forms in response to the accumulation of unfolded protein in the ER and evokes the unfolded protein response (UPR) by splicing the mRNA encoding master transcriptional regulator of the UPR,  HAC1 (P41546). IRE1 cleaves a single phosphodiester bond in each of two RNA hairpins (with non-specific base paired stems and loops of consensus sequence CNCNNGN, where N is any base) to remove an intervening intron from the target transcript. IRE1 auto-activates via transphosphorylation following binding of unfolded proteins to its N-termini.","predictedComplex":false,"interactors":[{"ac":"EBI-9364","identifier":"P32361","identifierLink":"https://www.uniprot.org/uniprotkb/P32361/entry","name":"IRE1","description":"Serine/threonine-protein kinase/endoribonuclease IRE1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13954","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3232","complexName":"CKM complex variant 1","organismName":"Homo sapiens; 9606","description":"Reversibly associates with the Mediator complex (CPX-3227). Mediator lacking the CKM complex has a stimulatory effect on basal transcription. In contrast, Mediator containing the sub-complex represses basal transcription. This effect is independent of kinase activity but binding of the complex to Mediator may interfere with RNAPII recruitment and repress transcription re-initiation. Variant 1 and 2 have been shown to regulate different, but overlapping sets of target genes.","predictedComplex":false,"interactors":[{"ac":"EBI-394357","identifier":"Q93074","identifierLink":"https://www.uniprot.org/uniprotkb/Q93074/entry","name":"MED12","description":"Mediator of RNA polymerase II transcription subunit 12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46007","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394377","identifier":"P49336","identifierLink":"https://www.uniprot.org/uniprotkb/P49336/entry","name":"CDK8","description":"Cyclin-dependent kinase 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394440","identifier":"Q9UHV7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UHV7/entry","name":"MED13","description":"Mediator of RNA polymerase II transcription subunit 13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48249","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395261","identifier":"P24863","identifierLink":"https://www.uniprot.org/uniprotkb/P24863/entry","name":"CCNC","description":"Cyclin-C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3263","complexName":"CKM complex variant 2","organismName":"Homo sapiens; 9606","description":"Reversibly associates with the Mediator complex (CPX-3227). Mediator lacking the CKM complex has a stimulatory effect on basal transcription. In contrast, Mediator containing the sub-complex represses basal transcription. This effect is independent of kinase activity but binding of the complex to Mediator may interfere with RNAPII recruitment and repress transcription re-initiation. Variant 1 and 2 have been shown to regulate different, but overlapping sets of target genes. Other variants of this complex may exist, containing MED12L (Q86YW9) and/or MED13L (Q71F56) but their existence has not been proven.","predictedComplex":false,"interactors":[{"ac":"EBI-394357","identifier":"Q93074","identifierLink":"https://www.uniprot.org/uniprotkb/Q93074/entry","name":"MED12","description":"Mediator of RNA polymerase II transcription subunit 12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46007","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394440","identifier":"Q9UHV7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UHV7/entry","name":"MED13","description":"Mediator of RNA polymerase II transcription subunit 13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48249","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-394593","identifier":"Q9BWU1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BWU1/entry","name":"CDK19","description":"Cyclin-dependent kinase 19","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395261","identifier":"P24863","identifierLink":"https://www.uniprot.org/uniprotkb/P24863/entry","name":"CCNC","description":"Cyclin-C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3266","complexName":"CKM complex variant 1","organismName":"Mus musculus; 10090","description":"Reversibly associates with the Mediator complex (CPX-3264). Mediator lacking the CKM complex has a stimulatory effect on basal transcription. In contrast, Mediator containing the sub-complex represses basal transcription. This effect is independent of kinase activity but binding of the complex to Mediator may interfere with RNAPII recruitment and repress transcription re-initiation. Variant 1 and 2 have been shown to regulate different, but overlapping sets of target genes.","predictedComplex":false,"interactors":[{"ac":"EBI-5744969","identifier":"A2AGH6","identifierLink":"https://www.uniprot.org/uniprotkb/A2AGH6/entry","name":"Med12","description":"Mediator of RNA polymerase II transcription subunit 12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46007","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5745218","identifier":"Q5SWW4","identifierLink":"https://www.uniprot.org/uniprotkb/Q5SWW4/entry","name":"Med13","description":"Mediator of RNA polymerase II transcription subunit 13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR48249","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5745402","identifier":"Q8R3L8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R3L8/entry","name":"Cdk8","description":"Cyclin-dependent kinase 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9847822","identifier":"Q62447","identifierLink":"https://www.uniprot.org/uniprotkb/Q62447/entry","name":"Ccnc","description":"Cyclin-C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3267","complexName":"CKM complex variant 2","organismName":"Mus musculus; 10090","description":"Reversibly associates with the Mediator complex (CPX-3264). Mediator lacking the CKM complex has a stimulatory effect on basal transcription. In contrast, Mediator containing the sub-complex represses basal transcription. This effect is independent of kinase activity but binding of the complex to Mediator may interfere with RNAPII recruitment and repress transcription re-initiation. Variant 1 and 2 have been shown to regulate different, but overlapping sets of target genes.","predictedComplex":false,"interactors":[{"ac":"EBI-5744969","identifier":"A2AGH6","identifierLink":"https://www.uniprot.org/uniprotkb/A2AGH6/entry","name":"Med12","description":"Mediator of RNA polymerase II transcription subunit 12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46007","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5745218","identifier":"Q5SWW4","identifierLink":"https://www.uniprot.org/uniprotkb/Q5SWW4/entry","name":"Med13","description":"Mediator of RNA polymerase II transcription subunit 13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR48249","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9847822","identifier":"Q62447","identifierLink":"https://www.uniprot.org/uniprotkb/Q62447/entry","name":"Ccnc","description":"Cyclin-C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9847870","identifier":"Q8BWD8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BWD8/entry","name":"Cdk19","description":"Cyclin-dependent kinase 19","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3078","complexName":"Ric1-Rgp1 guanyl-nucleotide exchange factor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Guanine nucleotide exchange factor (GEF) that activates YPT6 (Q99260), by exchanging bound GDP for free GTP. YPT6 is a Rab GTPase which mediates the fusion of vesicles from endosomes at the Golgi apparatus and, once activated, recruits the GARP tethering complex (CPX-1718).","predictedComplex":false,"interactors":[{"ac":"EBI-15080","identifier":"P16664","identifierLink":"https://www.uniprot.org/uniprotkb/P16664/entry","name":"RGP1","description":"Guanine nucleotide exchange factor subunit RGP1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12507","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15183","identifier":"P40395","identifierLink":"https://www.uniprot.org/uniprotkb/P40395/entry","name":"RIC1","description":"Guanine nucleotide exchange factor subunit RIC1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22746","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1622","complexName":"ESCRT-0 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"The ESCRT machinery consists of ESCRT-0 (this complex), -I (CPX-940), -II (CPX-1623), -III (CPX-1624) and -IV (VPS4 complex, CPX-334) and is required for the downregulation of cell-surface receptors and for the final membrane scission step during endocytosis. ESCRT-0 binds PI3P on endosomes and ubiquitinated cargo via VPS27, recruiting clathrin and sequestering ubiquitylated cargo in clathrin-coated microdomains. HSE1 recruits ESCRT-1 and initiates the multivesicular body (MVB) pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-1382","identifier":"P38753","identifierLink":"https://www.uniprot.org/uniprotkb/P38753/entry","name":"HSE1","description":"Class E vacuolar protein-sorting machinery protein HSE1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45929","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20380","identifier":"P40343","identifierLink":"https://www.uniprot.org/uniprotkb/P40343/entry","name":"VPS27","description":"Vacuolar protein sorting-associated protein 27","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47794","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1623","complexName":"ESCRT-II complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"The ESCRT machinery consists of ESCRT-0 (CPX-1622), -I (CPX-940), -II (this complex), -III (CPX-1624) and -IV (VPS4 complex, CPX-334) and is required for the downregulation of cell-surface receptors and for the final membrane scission step during endocytosis. ESCRT-II transiently associates with endosomes and facilitates recruitment of ESCRT-III components to membranes.","predictedComplex":false,"interactors":[{"ac":"EBI-25595","identifier":"P47142","identifierLink":"https://www.uniprot.org/uniprotkb/P47142/entry","name":"VPS25","description":"Vacuolar protein-sorting-associated protein 25","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13149","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30277","identifier":"Q12483","identifierLink":"https://www.uniprot.org/uniprotkb/Q12483/entry","name":"SNF8","description":"Vacuolar-sorting protein SNF8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12806","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-36540","identifier":"Q06696","identifierLink":"https://www.uniprot.org/uniprotkb/Q06696/entry","name":"VPS36","description":"Vacuolar protein-sorting-associated protein 36","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13128","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1624","complexName":"ESCRT-III complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A membrane fission complex that is part of the ESCRT machinery of ESCRT-0 (CPX-1622), -I (CPX-940), -II (CPX-1623), -III (this complex) and -IV (VPS4 complex, CPX-334). It is involved in multiple membrane fission processes: a) the final step of cell organelle fusion processes such as the biogenesis of intraluminal vesicles (ILV) in multivesicular bodies (MVB, a type of late endosomes), fusion of autophagosomes with MVB or lysosomes and amphisomes or MVB with lysosomes, thereby playing a crucial role in processes like autophagy and downregulation of cell-surface receptors, b) polarity, c) migration, d) miRNA activity, e) mRNA transport, f) repair of plasma membrane wounds, g) the final scission of cytokineses, h) nuclear envelope sealing by annular fusion, i) nuclear pore complex (NPC) surveillance and j) extraction of defective NPCs. \r\n\r\nESCRT-III assembles into a highly ordered filament-like hetero-oligomer, which may spatially restrict membrane-curvature-inducing factors to initiate budding away from the cytoplasm. VPS20 nucleates the homo-oligomerization of SNF7 that is capped by VPS24. VPS24 recruits VPS2, initiates VPS4-dependent ESCRT-III dissasembly and binds phosphatidylinositol 3,5-diphosphate.","predictedComplex":false,"interactors":[{"ac":"EBI-17554","identifier":"P39929","identifierLink":"https://www.uniprot.org/uniprotkb/P39929/entry","name":"SNF7","description":"Vacuolar-sorting protein SNF7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26574","identifier":"P36108","identifierLink":"https://www.uniprot.org/uniprotkb/P36108/entry","name":"DID4","description":"DOA4-independent degradation protein 4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26653","identifier":"P36095","identifierLink":"https://www.uniprot.org/uniprotkb/P36095/entry","name":"VPS24","description":"Vacuolar protein-sorting-associated protein 24","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28157","identifier":"Q04272","identifierLink":"https://www.uniprot.org/uniprotkb/Q04272/entry","name":"VPS20","description":"Vacuolar protein sorting-associated protein 20","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1625","complexName":"HOPS tethering complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Multisubunit tethering complex involved in endo-lysosomal vesicle  trafficking and lysosome biogenesis by cross-linking two membranes, and facilitating the formation of a SNARE complex during fusion. Required for the delivery of vacuolar proteins and homotypic fusion of vacuoles and controls the clearance of late endosomes and autophagosomes during heterophagy and autophagy through promoting fusion of these vesicles with the vacuole Controls homotypic vacuole-vacuole fusion by regulating vesicle docking to the vacuole through its interaction with soluble  SNAREs (CPX-1887), the GTP-bound form of the Rab protein YPT7 (P32939) and phosphoinositides. HOPS indirectly facilitates trans-SNARE complex formation by tethering membranes then protects newly formed trans-SNARE complexes from disassembly by SEC17/SEC18 (P32602/P18759). Reduces the levels of noncanonical trans-SNARE complexes formed during fusion, and further reduces the capacity of these mismatched complexes to undergo fusion. HOPS function is regulated through phosphorylation of its VPS41 subunit by YCK3 which lowers its affinity for vacuolar lipids.","predictedComplex":false,"interactors":[{"ac":"EBI-13130","identifier":"P27801","identifierLink":"https://www.uniprot.org/uniprotkb/P27801/entry","name":"PEP3","description":"Vacuolar membrane protein PEP3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23323","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20355","identifier":"Q03308","identifierLink":"https://www.uniprot.org/uniprotkb/Q03308/entry","name":"VPS16","description":"Vacuolar protein sorting-associated protein 16","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12811","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20395","identifier":"P20795","identifierLink":"https://www.uniprot.org/uniprotkb/P20795/entry","name":"VPS33","description":"Vacuolar protein sorting-associated protein 33","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11679","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20422","identifier":"Q07468","identifierLink":"https://www.uniprot.org/uniprotkb/Q07468/entry","name":"VAM6","description":"Vacuolar morphogenesis protein 6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20432","identifier":"P38959","identifierLink":"https://www.uniprot.org/uniprotkb/P38959/entry","name":"VPS41","description":"Vacuolar protein sorting-associated protein 41","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12616","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6450","identifier":"P12868","identifierLink":"https://www.uniprot.org/uniprotkb/P12868/entry","name":"PEP5","description":"E3 ubiquitin-protein ligase PEP5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23323","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1626","complexName":"CORVET tethering complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Multisubunit tethering complex involved in early endosomal fusions by cross-linking two membranes, and facilitating the formation of a SNARE complex during fusion. Cooperates with Rab GTPases to capture vesicles and trap them prior to the action of SNAREs. Catalyses either vacuole fission into sub-compartments or vacuole-endosome fusion, or both, by interacting with the Rab GTPase VPS21 (P36017) to promote tethering and fusion of RAB5/VPS21-positive membranes.","predictedComplex":false,"interactors":[{"ac":"EBI-13130","identifier":"P27801","identifierLink":"https://www.uniprot.org/uniprotkb/P27801/entry","name":"PEP3","description":"Vacuolar membrane protein PEP3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23323","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20355","identifier":"Q03308","identifierLink":"https://www.uniprot.org/uniprotkb/Q03308/entry","name":"VPS16","description":"Vacuolar protein sorting-associated protein 16","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12811","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20395","identifier":"P20795","identifierLink":"https://www.uniprot.org/uniprotkb/P20795/entry","name":"VPS33","description":"Vacuolar protein sorting-associated protein 33","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11679","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20469","identifier":"P23643","identifierLink":"https://www.uniprot.org/uniprotkb/P23643/entry","name":"VPS3","description":"Vacuolar protein sorting-associated protein 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20488","identifier":"P39702","identifierLink":"https://www.uniprot.org/uniprotkb/P39702/entry","name":"VPS8","description":"Vacuolar protein sorting-associated protein 8","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12616","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6450","identifier":"P12868","identifierLink":"https://www.uniprot.org/uniprotkb/P12868/entry","name":"PEP5","description":"E3 ubiquitin-protein ligase PEP5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23323","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1627","complexName":"RAVE complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Mediates both the biosynthetic assembly and the glucose-induced reassembly of the V-ATPase (CPX-1193). Binds to V1 released from the vacuolar membrane by glucose deprivation and releases V1 upon glucose readdition. Appears to be aiding cytosolic V1 complexes to assemble with V0 at the membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-25471","identifier":"P47104","identifierLink":"https://www.uniprot.org/uniprotkb/P47104/entry","name":"RAV1","description":"Regulator of V-ATPase in vacuolar membrane protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13950","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30629","identifier":"Q03956","identifierLink":"https://www.uniprot.org/uniprotkb/Q03956/entry","name":"RAV2","description":"Regulator of V-ATPase in vacuolar membrane protein 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13618","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4090","identifier":"P52286","identifierLink":"https://www.uniprot.org/uniprotkb/P52286/entry","name":"SKP1","description":"Suppressor of kinetochore protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1628","complexName":"RNA decapping complex, DCP1-DCP2","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP.  Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. The activity of this complex is tightly regulated to prevent premature degradation of the transcript.","predictedComplex":false,"interactors":[{"ac":"EBI-270","identifier":"P53550","identifierLink":"https://www.uniprot.org/uniprotkb/P53550/entry","name":"DCP2","description":"m7GpppN-mRNA hydrolase","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23114","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-38519","identifier":"Q12517","identifierLink":"https://www.uniprot.org/uniprotkb/Q12517/entry","name":"DCP1","description":"mRNA-decapping enzyme subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR16290","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1629","complexName":"TIM22 mitochondrial inner membrane twin-pore carrier translocase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Mediates the insertion and lateral release of multi-spanning membrane precursor proteins into the mitochondrial inner membrane  in  a  membrane  potential-dependent  manner following translocation into the mitochondrion. Most mitochondrial proteins are synthesized in the cytosol,  imported into mitochondria, sorted to one of the four submitochondrial compartments, where they function, and attain their functional native conformation, which is often facilitated by assembly into the membrane or a multiprotein complex.","predictedComplex":false,"interactors":[{"ac":"EBI-11303","identifier":"P32830","identifierLink":"https://www.uniprot.org/uniprotkb/P32830/entry","name":"TIM12","description":"Mitochondrial import inner membrane translocase subunit TIM12","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11038","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25878","identifier":"P47045","identifierLink":"https://www.uniprot.org/uniprotkb/P47045/entry","name":"TIM54","description":"Mitochondrial import inner membrane translocase subunit TIM54","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12358","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30499","identifier":"Q08749","identifierLink":"https://www.uniprot.org/uniprotkb/Q08749/entry","name":"TIM18","description":"Mitochondrial import inner membrane translocase subunit TIM18","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13337","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9108","identifier":"O74700","identifierLink":"https://www.uniprot.org/uniprotkb/O74700/entry","name":"TIM9","description":"Mitochondrial import inner membrane translocase subunit TIM9","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13172","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9115","identifier":"P87108","identifierLink":"https://www.uniprot.org/uniprotkb/P87108/entry","name":"TIM10","description":"Mitochondrial import inner membrane translocase subunit TIM10","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11038","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9132","identifier":"Q12328","identifierLink":"https://www.uniprot.org/uniprotkb/Q12328/entry","name":"TIM22","description":"Mitochondrial import inner membrane translocase subunit TIM22","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14110","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1630","complexName":"Mitochondrial processing peptidase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Metalloprotease which cleaves off the N-terminal presequence from nuclear encoded mitochondrial precursor proteins, such as the sequence that targets the proteins to the mitochondrial matrix.  Common features for cleavage of the extension peptides by MPP are a proximal basic amino acid residue, usually arginine at the P2 position, distal N-terminal basic residues generally 3-10 residues from the proximal arginine and an aromatic or less often another type of bulky hydrophobic residue at position P1'; MPP also prefers polar residues such as histidine, serine, and threonine at positions P2' and P3'.","predictedComplex":false,"interactors":[{"ac":"EBI-11205","identifier":"P11914","identifierLink":"https://www.uniprot.org/uniprotkb/P11914/entry","name":"MAS2","description":"Mitochondrial-processing peptidase subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11851","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11212","identifier":"P10507","identifierLink":"https://www.uniprot.org/uniprotkb/P10507/entry","name":"MAS1","description":"Mitochondrial-processing peptidase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11851","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1631","complexName":"tRNA (adenine(58)-N(1))-methyltransferase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the transfer of a methyl group from the cofactor S-adenosyl-l-methionine (CHEBI:67040) to N1 of adenine-58 to give 1-methyladenosine (m1A58) in initiator methionyl-tRNA.  This is required for maintaining  the stability of the initiator methionine tRNAiMet.","predictedComplex":false,"interactors":[{"ac":"EBI-7416","identifier":"P46959","identifierLink":"https://www.uniprot.org/uniprotkb/P46959/entry","name":"GCD14","description":"tRNA (adenine(58)-N(1))-methyltransferase catalytic subunit TRM61","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12133","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8995","identifier":"P41814","identifierLink":"https://www.uniprot.org/uniprotkb/P41814/entry","name":"GCD10","description":"tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1632","complexName":"trm8-trm82 tRNA (guanine-N(7)-)-methyltransferase","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for 7-methylguanosine modification (m7G46) of tRNA. The m7G46 modification is required to prevent tRNA levels decay in a rapid tRNA degradation pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-19486","identifier":"Q03774","identifierLink":"https://www.uniprot.org/uniprotkb/Q03774/entry","name":"TRM82","description":"tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit TRM82","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR16288","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19552","identifier":"Q12009","identifierLink":"https://www.uniprot.org/uniprotkb/Q12009/entry","name":"TRM8","description":"tRNA (guanine-N(7)-)-methyltransferase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23417","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1633","complexName":"Transcription factor TFIIA complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Transcription factor complex that regulates transcription initiation from RNA polymerase II promoters. Binding to the transcription factor complex TFIID-TBP enhances assembly of the transcriptional preinitiation complex PIC and its binding to the DNA at the TATA-box by displacing transcription inhibitors.","predictedComplex":false,"interactors":[{"ac":"EBI-19316","identifier":"P32773","identifierLink":"https://www.uniprot.org/uniprotkb/P32773/entry","name":"TOA1","description":"Transcription initiation factor IIA large subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12694","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19323","identifier":"P32774","identifierLink":"https://www.uniprot.org/uniprotkb/P32774/entry","name":"TOA2","description":"Transcription initiation factor IIA subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1634","complexName":"Protein farnesyltransferase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the transfer of a 15-carbon lipid, the farnesyl moiety, from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X (CaaX box).\r\n\r\nThe hydrophobic farnesyl moiety aids membrane attachment of the target proteins which include many essential signal transduction proteins, including members of the Ras superfamily. Farnesylation is essential both for normal functioning of these proteins, and for the transforming activity of oncogenic mutants.","predictedComplex":false,"interactors":[{"ac":"EBI-14806","identifier":"P22007","identifierLink":"https://www.uniprot.org/uniprotkb/P22007/entry","name":"RAM1","description":"Protein farnesyltransferase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11774","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14814","identifier":"P29703","identifierLink":"https://www.uniprot.org/uniprotkb/P29703/entry","name":"RAM2","description":"Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1635","complexName":"Protein geranylgeranyltransferase type I complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the transfer of a 20-carbon lipid, the geranyl-geranyl moiety, from geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X (CaaX box). The Zn2+ is required for peptide, but not for isoprenoid, substrate binding.\r\n\r\nThe hydrophobic geranyl-geranyl moiety aids membrane attachment of the target proteins which include many essential signal transduction proteins, including members of the Ras superfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-14814","identifier":"P29703","identifierLink":"https://www.uniprot.org/uniprotkb/P29703/entry","name":"RAM2","description":"Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3961","identifier":"P18898","identifierLink":"https://www.uniprot.org/uniprotkb/P18898/entry","name":"CDC43","description":"Geranylgeranyl transferase type-1 subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11774","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1636","complexName":"Protein geranylgeranyltransferase type II complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the transfer of a 20-hydrocarbon geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to a Rab protein having the C-terminal sequence -XXCC, -XCXC and -CCXX , where both cysteines may become modified. Requires both Zn2+ and Mg2+ for maximal activity. The Rab escort protein, MRS6, is the substrate-binding subunit (component A) of the complex which binds unprenylated Rab proteins and presents the substrate peptide to the catalytic component B. Component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-14799","identifier":"P32864","identifierLink":"https://www.uniprot.org/uniprotkb/P32864/entry","name":"MRS6","description":"Rab proteins geranylgeranyltransferase component A","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11787","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3559","identifier":"P20133","identifierLink":"https://www.uniprot.org/uniprotkb/P20133/entry","name":"BET2","description":"Geranylgeranyl transferase type-2 subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11774","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3573","identifier":"Q00618","identifierLink":"https://www.uniprot.org/uniprotkb/Q00618/entry","name":"BET4","description":"Geranylgeranyl transferase type-2 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1637","complexName":"F-actin capping protein complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Caps the barbed end of the actin filament thereby blocking the exchange of subunits at these ends. The complex is an essential component for the reconstitution of movement powered by actin polymerization and is important for actin assembly and cell motility.","predictedComplex":false,"interactors":[{"ac":"EBI-4003","identifier":"P28495","identifierLink":"https://www.uniprot.org/uniprotkb/P28495/entry","name":"CAP1","description":"F-actin-capping protein subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10653","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4013","identifier":"P13517","identifierLink":"https://www.uniprot.org/uniprotkb/P13517/entry","name":"CAP2","description":"F-actin-capping protein subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1638","complexName":"Oligosaccharyltransferase complex, OST6 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Transfers the dolicholphosphate-linked core oligosaccharide to selected Asn-X-Ser/Thr sequences of the nascent polypeptide chain, a key step in N-glycosylation of secretory and membrane-bound proteins in the lumen of the endoplasmic reticulum. The two variant complexes may be involved in the recognition of different protein substrates, perhaps in combination with their recruitment to the two different protein translocation machineries. Variant 1 may be involved in N-glycosylation of a group of proteins, necessary for cell wall formation or for growth at high temperature and binds to the Ssh1 translocon complex (CPX-1834).","predictedComplex":false,"interactors":[{"ac":"EBI-12651","identifier":"P41543","identifierLink":"https://www.uniprot.org/uniprotkb/P41543/entry","name":"OST1","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21049","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12658","identifier":"P33767","identifierLink":"https://www.uniprot.org/uniprotkb/P33767/entry","name":"WBP1","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit WBP1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10830","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12666","identifier":"Q02795","identifierLink":"https://www.uniprot.org/uniprotkb/Q02795/entry","name":"SWP1","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit SWP1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12640","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12673","identifier":"P46964","identifierLink":"https://www.uniprot.org/uniprotkb/P46964/entry","name":"OST2","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10705","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12689","identifier":"Q99380","identifierLink":"https://www.uniprot.org/uniprotkb/Q99380/entry","name":"OST4","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-12696","identifier":"Q03723","identifierLink":"https://www.uniprot.org/uniprotkb/Q03723/entry","name":"OST6","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12692","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12704","identifier":"Q92316","identifierLink":"https://www.uniprot.org/uniprotkb/Q92316/entry","name":"OST5","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-18447","identifier":"P39007","identifierLink":"https://www.uniprot.org/uniprotkb/P39007/entry","name":"STT3","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13872","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1639","complexName":"Oligosaccharyltransferase complex, OST3 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Transfers the dolicholphosphate-linked core oligosaccharide to selected Asn-X-Ser/Thr sequences of the nascent polypeptide chain, a key step in N-glycosylation of secretory and membrane-bound proteins in the lumen of the endoplasmic reticulum. The two variant complexes may be involved in the recognition of different protein substrates, perhaps in combination with their recruitment to the two different protein translocation machineries. Variant 2 binds to SEC61 translocon complex (CPX-1833).","predictedComplex":false,"interactors":[{"ac":"EBI-12651","identifier":"P41543","identifierLink":"https://www.uniprot.org/uniprotkb/P41543/entry","name":"OST1","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21049","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12658","identifier":"P33767","identifierLink":"https://www.uniprot.org/uniprotkb/P33767/entry","name":"WBP1","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit WBP1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10830","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12666","identifier":"Q02795","identifierLink":"https://www.uniprot.org/uniprotkb/Q02795/entry","name":"SWP1","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit SWP1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12640","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12673","identifier":"P46964","identifierLink":"https://www.uniprot.org/uniprotkb/P46964/entry","name":"OST2","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10705","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12680","identifier":"P48439","identifierLink":"https://www.uniprot.org/uniprotkb/P48439/entry","name":"OST3","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12692","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12689","identifier":"Q99380","identifierLink":"https://www.uniprot.org/uniprotkb/Q99380/entry","name":"OST4","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-12704","identifier":"Q92316","identifierLink":"https://www.uniprot.org/uniprotkb/Q92316/entry","name":"OST5","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-18447","identifier":"P39007","identifierLink":"https://www.uniprot.org/uniprotkb/P39007/entry","name":"STT3","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13872","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1640","complexName":"Nucleotide excision repair factor 2 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Nucleotide excision repair damage-recognition heterodimer. Binds damaged DNA and recruits the NEF1 and NEF3 complexes. Rad4 inserts a beta-hairpin through the DNA duplex, causing the two damaged base pairs to flip out of the double helix. Lesion recognition does not appear to be based in structural discrimination between normal and damaged DNA by Rad4/XPC, but may be due to a ‘kinetic gating’ mechanism, whereby the DNA lesion selectivity arises mainly from the kinetic competition between Rad4-induced DNA opening and the residence time of Rad4 at a given site.","predictedComplex":false,"interactors":[{"ac":"EBI-14668","identifier":"P32628","identifierLink":"https://www.uniprot.org/uniprotkb/P32628/entry","name":"RAD23","description":"UV excision repair protein RAD23","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10621","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14766","identifier":"P14736","identifierLink":"https://www.uniprot.org/uniprotkb/P14736/entry","name":"RAD4","description":"DNA repair protein RAD4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12135","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1641","complexName":"GINS complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for the initiation of replication and for replication fork progression, mediating interactions with replication factors. Binds to and enhances the enzymatic function of the MCM helicase (CPX-2944) during the initiation and elongation stages of replication. Core component of the replicative helicase CMG (CPX-297) complex that serves as the replicative helicase unwinding duplex DNA ahead of moving replication fork during chromosome duplication. Also appears to interact with and stimulate the polymerase activities of DNA polymerase epsilon  complex (CPX-2110) and the DNA polymerase alpha:primase complex (CPX-2091).","predictedComplex":false,"interactors":[{"ac":"EBI-22066","identifier":"Q12488","identifierLink":"https://www.uniprot.org/uniprotkb/Q12488/entry","name":"PSF1","description":"DNA replication complex GINS protein PSF1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12914","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25936","identifier":"P40359","identifierLink":"https://www.uniprot.org/uniprotkb/P40359/entry","name":"PSF2","description":"DNA replication complex GINS protein PSF2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12772","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30392","identifier":"Q12146","identifierLink":"https://www.uniprot.org/uniprotkb/Q12146/entry","name":"PSF3","description":"DNA replication complex GINS protein PSF3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22768","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-37437","identifier":"Q03406","identifierLink":"https://www.uniprot.org/uniprotkb/Q03406/entry","name":"SLD5","description":"DNA replication complex GINS protein SLD5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21206","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1642","complexName":"General transcription factor complex TFIID","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"General transcription factor complex that acts as the primary core promoter recognition factor in the initiation of RNA polymerase II (Pol II)-dependent transcription. The TBP subunit of TFIID recognizes and binds to the TATA box (if present), while TAF1 and TAF2 interact with the Initiator element (Inr), and TAF1 and the TAF6-TAF9 module recognizes the downstream core promoter element (DPE). Other core promoter elements, such as the motif ten element (MTE), may also be involved. Binding of the general transcription factor complex TFIIA (CPX-1633) enhances binding of TFIID to the core promoter and nucleates  pre-initiation complex (PIC) assembly. Following recruitment of TFIIA to TFIID, TFIIB, TFIIF, Pol II, TFIIE (CPX-1658) and TFIIH are successively assembled at the core promoter, allowing the PIC to initiate Pol II transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-11231","identifier":"P50105","identifierLink":"https://www.uniprot.org/uniprotkb/P50105/entry","name":"TAF4","description":"Transcription initiation factor TFIID subunit 4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15138","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18855","identifier":"P46677","identifierLink":"https://www.uniprot.org/uniprotkb/P46677/entry","name":"TAF1","description":"Transcription initiation factor TFIID subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13900","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18862","identifier":"P23255","identifierLink":"https://www.uniprot.org/uniprotkb/P23255/entry","name":"TAF2","description":"Transcription initiation factor TFIID subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15137","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18868","identifier":"P38129","identifierLink":"https://www.uniprot.org/uniprotkb/P38129/entry","name":"TAF5","description":"SAGA complex/transcription factor TFIID complex subunit TAF5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19879","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18876","identifier":"P53040","identifierLink":"https://www.uniprot.org/uniprotkb/P53040/entry","name":"TAF6","description":"SAGA complex/transcription factor TFIID complex subunit TAF6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10221","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18884","identifier":"Q04226","identifierLink":"https://www.uniprot.org/uniprotkb/Q04226/entry","name":"TAF11","description":"Transcription initiation factor TFIID subunit 11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13218","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18889","identifier":"Q12030","identifierLink":"https://www.uniprot.org/uniprotkb/Q12030/entry","name":"TAF10","description":"SAGA complex/transcription factor TFIID complex subunit TAF10","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21242","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18897","identifier":"P11747","identifierLink":"https://www.uniprot.org/uniprotkb/P11747/entry","name":"TAF13","description":"Transcription initiation factor TFIID subunit 13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11380","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18920","identifier":"P35189","identifierLink":"https://www.uniprot.org/uniprotkb/P35189/entry","name":"TAF14","description":"Transcription initiation factor TFIID subunit 14","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23195","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19129","identifier":"P13393","identifierLink":"https://www.uniprot.org/uniprotkb/P13393/entry","name":"SPT15","description":"TATA-box-binding protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10126","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27490","identifier":"Q05021","identifierLink":"https://www.uniprot.org/uniprotkb/Q05021/entry","name":"TAF7","description":"Transcription initiation factor TFIID subunit 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12228","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27500","identifier":"Q05027","identifierLink":"https://www.uniprot.org/uniprotkb/Q05027/entry","name":"TAF9","description":"SAGA complex/transcription factor TFIID complex subunit TAF9","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR48068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27947","identifier":"Q03750","identifierLink":"https://www.uniprot.org/uniprotkb/Q03750/entry","name":"TAF8","description":"Transcription initiation factor TFIID subunit 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-35097","identifier":"Q03761","identifierLink":"https://www.uniprot.org/uniprotkb/Q03761/entry","name":"TAF12","description":"SAGA complex/transcription factor TFIID complex subunit TAF12","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-36697","identifier":"Q12297","identifierLink":"https://www.uniprot.org/uniprotkb/Q12297/entry","name":"TAF3","description":"Transcription initiation factor TFIID subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1643","complexName":"UDP-N-acetylglucosamine transferase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyses the second step of eukaryotic N-linked glycosylation in endoplasmic reticulum, transferring an N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to GlcNAc-PP-Dolichol. Alg14 is a membrane protein that recruits the cytosolic Alg13 protein to the ER, Alg13 contains the catalytic domain of the UDP-GlcNAc transferase, but cytosolic Alg13 is not active unless bound to Alg14 at the ER membrane suggesting the formation of the Alg13/14 complex is crucial for UDP-GlcNAc transferase activity.","predictedComplex":false,"interactors":[{"ac":"EBI-21477","identifier":"P38242","identifierLink":"https://www.uniprot.org/uniprotkb/P38242/entry","name":"ALG14","description":"UDP-N-acetylglucosamine transferase subunit ALG14","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12154","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23770","identifier":"P53178","identifierLink":"https://www.uniprot.org/uniprotkb/P53178/entry","name":"ALG13","description":"UDP-N-acetylglucosamine transferase subunit ALG13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47043","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1644","complexName":"HOP2-MND1 recombination assembly factor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Recombinase cofactor that activates both RAD51 (P25454)- and DMC1 (P25453)-mediated homologous pairing during homologous recombination. Acts to stabilize the presynaptic filament, a right-handed helical nucleoprotein strand generated  by RAD51 and DMC1 from single-stranded DNA derived from the nucleolytic processing of a primary lesion. The HOP2-MND1 complex synergizes with the filament to assemble the synaptic complex, and promotes DMC1-/RAD51-mediated strand exchange between the presynaptic filament and recombining double-stranded DNA to form a D-loop, acting with RAD54 (P32863), a nucleosome remodeler, to promote homologous pairing with the nucleosomal double-stranded DNA.","predictedComplex":false,"interactors":[{"ac":"EBI-24091","identifier":"P53102","identifierLink":"https://www.uniprot.org/uniprotkb/P53102/entry","name":"MND1","description":"Meiotic nuclear division protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15938","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8460","identifier":"P53187","identifierLink":"https://www.uniprot.org/uniprotkb/P53187/entry","name":"HOP2","description":"Homologous-pairing protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15938","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1645","complexName":"Ste4-Ste18 heterodimer","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Signal-transmitting component of the G protein heterotrimer in the pheremone response pathway. Activation of the Ste2 receptor by mating pheromone leads to GTP binding and dissociation of the G protein alpha subunit (Gpa1, P08539) from the G protein beta and gamma subunit complex (STE4 and STW18).  STE4-STE18 activate the downstream pheromone signaling MAP kinase cascade leading to expression of mating-specific genes, inducing cell cycle arrest in G1, promoting polarized cell growth to form mating projections (shmoos), and establishing the changes in plasma membrane, cell wall and nuclear envelope to permit cell-cell fusion (plasmogamy) and fusion of the two haploid nuclei (karyogamy).","predictedComplex":false,"interactors":[{"ac":"EBI-7390","identifier":"P18851","identifierLink":"https://www.uniprot.org/uniprotkb/P18851/entry","name":"STE4","description":"Guanine nucleotide-binding protein subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7397","identifier":"P18852","identifierLink":"https://www.uniprot.org/uniprotkb/P18852/entry","name":"STE18","description":"Guanine nucleotide-binding protein subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28189","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1646","complexName":"G protein heterotrimer","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Inactive form of the G protein signal-transmitting component in the pheremone response pathway. Activation of the Ste2 receptor by mating pheromone leads to GTP binding and dissociation of the G protein alpha subunit (GPA1) from the G protein beta and gamma subunits (CPX-1645).","predictedComplex":false,"interactors":[{"ac":"EBI-7376","identifier":"P08539","identifierLink":"https://www.uniprot.org/uniprotkb/P08539/entry","name":"GPA1","description":"Guanine nucleotide-binding protein alpha-1 subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10218","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7390","identifier":"P18851","identifierLink":"https://www.uniprot.org/uniprotkb/P18851/entry","name":"STE4","description":"Guanine nucleotide-binding protein subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7397","identifier":"P18852","identifierLink":"https://www.uniprot.org/uniprotkb/P18852/entry","name":"STE18","description":"Guanine nucleotide-binding protein subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28189","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1647","complexName":"SF3B complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Spliceosomal complex, an essential factor for splicing of pre-mRNA. Part of the U2 snRNP as well as the U11/U12 di-snRNP. Present in the pre-spliceosomal A complex and the fully assembled catalytic active spliceosomes.","predictedComplex":false,"interactors":[{"ac":"EBI-29456","identifier":"Q06835","identifierLink":"https://www.uniprot.org/uniprotkb/Q06835/entry","name":"RDS3","description":"Pre-mRNA-splicing factor RDS3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13120","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-519","identifier":"Q04693","identifierLink":"https://www.uniprot.org/uniprotkb/Q04693/entry","name":"RSE1","description":"Pre-mRNA-splicing factor RSE1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-654","identifier":"Q02554","identifierLink":"https://www.uniprot.org/uniprotkb/Q02554/entry","name":"CUS1","description":"Cold sensitive U2 snRNA suppressor 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12785","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-664","identifier":"P49955","identifierLink":"https://www.uniprot.org/uniprotkb/P49955/entry","name":"HSH155","description":"U2 snRNP component HSH155","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8579","identifier":"Q99181","identifierLink":"https://www.uniprot.org/uniprotkb/Q99181/entry","name":"HSH49","description":"Protein HSH49","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-970846","identifier":"P0C074","identifierLink":"https://www.uniprot.org/uniprotkb/P0C074/entry","name":"YSF3","description":"RDS3 complex subunit 10","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR20978","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1648","complexName":"SF3A complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Essential role in pre-mRNA splicing. A core component of the mature U2 snRNP (small nuclear ribonucleoprotein particle), a dynamic 17S particle which assembles as part of the spliceosome. Displacement of SF3A from the spliceosome initiates the first step of the splicing reaction.","predictedComplex":false,"interactors":[{"ac":"EBI-511","identifier":"P19736","identifierLink":"https://www.uniprot.org/uniprotkb/P19736/entry","name":"PRP9","description":"Pre-mRNA-splicing factor PRP9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12786","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603","identifier":"P32524","identifierLink":"https://www.uniprot.org/uniprotkb/P32524/entry","name":"PRP21","description":"Pre-mRNA-splicing factor PRP21","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15316","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-688","identifier":"Q07350","identifierLink":"https://www.uniprot.org/uniprotkb/Q07350/entry","name":"PRP11","description":"Pre-mRNA-splicing factor PRP11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23205","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1649","complexName":"RES complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for efficient splicing as well as nuclear retention of pre-mRNA.Promotes the efficient formation of the activated Bact spliceosomal complex from the U4/U6.U5 tri-snRNP (CPX-25).","predictedComplex":false,"interactors":[{"ac":"EBI-24073","identifier":"P46947","identifierLink":"https://www.uniprot.org/uniprotkb/P46947/entry","name":"BUD13","description":"Pre-mRNA-splicing factor CWC26","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-25387","identifier":"P40565","identifierLink":"https://www.uniprot.org/uniprotkb/P40565/entry","name":"IST3","description":"U2 snRNP component IST3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45880","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27110","identifier":"Q07930","identifierLink":"https://www.uniprot.org/uniprotkb/Q07930/entry","name":"PML1","description":"Pre-mRNA leakage protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23308","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1650","complexName":"Collagen type I trimer","organismName":"Homo sapiens; 9606","description":"Forms the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite.","predictedComplex":false,"interactors":[{"ac":"EBI-982999","identifier":"P02452","identifierLink":"https://www.uniprot.org/uniprotkb/P02452/entry","name":"COL1A1","description":"Collagen alpha-1(I) chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-983038","identifier":"P08123","identifierLink":"https://www.uniprot.org/uniprotkb/P08123/entry","name":"COL1A2","description":"Collagen alpha-2(I) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2956","complexName":"Collagen type I trimer","organismName":"Mus musculus; 10090","description":"Form the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite.","predictedComplex":false,"interactors":[{"ac":"EBI-1634830","identifier":"P11087","identifierLink":"https://www.uniprot.org/uniprotkb/P11087/entry","name":"Col1a1","description":"Collagen alpha-1(I) chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8357501","identifier":"Q01149","identifierLink":"https://www.uniprot.org/uniprotkb/Q01149/entry","name":"Col1a2","description":"Collagen alpha-2(I) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3101","complexName":"Collagen type I trimer","organismName":"Bos taurus; 9913","description":"Form the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite.","predictedComplex":false,"interactors":[{"ac":"EBI-2432384","identifier":"P02453","identifierLink":"https://www.uniprot.org/uniprotkb/P02453/entry","name":"COL1A1","description":"Collagen alpha-1(I) chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2432455","identifier":"P02465","identifierLink":"https://www.uniprot.org/uniprotkb/P02465/entry","name":"COL1A2","description":"Collagen alpha-2(I) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2075","complexName":"Cyclin D1-CDK4 complex","organismName":"Rattus norvegicus; 10116","description":"Required for G1 to S phase transition of the mitotic cell cycle. Phosphorylation of Rb proteins by cyclin D:CDK4 complexes leads to their partial inactivation which allows transcription of E2F-controlled genes such as cyclin E1, which activates the downstream Cdk2 kinase. Complex formation enables substrate binding to the kinase, leads to a rearrangement of the catalytic site and exposes Thr-172 of CDK4 for phosphorylation and subsequent activation.","predictedComplex":false,"interactors":[{"ac":"EBI-847291","identifier":"P35426","identifierLink":"https://www.uniprot.org/uniprotkb/P35426/entry","name":"Cdk4","description":"Cyclin-dependent kinase 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-847299","identifier":"P39948","identifierLink":"https://www.uniprot.org/uniprotkb/P39948/entry","name":"Ccnd1","description":"G1/S-specific cyclin-D1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2076","complexName":"Cyclin D2-CDK4 complex","organismName":"Rattus norvegicus; 10116","description":"Required for G1 to S phase transition of the mitotic cell cycle. Phosphorylation of Rb proteins by cyclin D:CDK4 complexes leads to their partial inactivation which allows transcription of E2F-controlled genes such as cyclin E1, which activates the downstream Cdk2 kinase. Complex formation enables substrate binding to the kinase, leads to a rearrangement of the catalytic site and exposes Thr-172 of CDK4 for phosphorylation and subsequent activation.","predictedComplex":false,"interactors":[{"ac":"EBI-847291","identifier":"P35426","identifierLink":"https://www.uniprot.org/uniprotkb/P35426/entry","name":"Cdk4","description":"Cyclin-dependent kinase 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-847319","identifier":"Q04827","identifierLink":"https://www.uniprot.org/uniprotkb/Q04827/entry","name":"Ccnd2","description":"G1/S-specific cyclin-D2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2077","complexName":"Cyclin D3-CDK4 complex","organismName":"Mus musculus; 10090","description":"Required for G1 to S phase transition of the mitotic cell cycle. Phosphorylation of Rb proteins by cyclin D:CDK4 complexes leads to their partial inactivation which allows transcription of E2F-controlled genes such as cyclin E1, which activates the downstream Cdk2 kinase. Complex formation enables substrate binding to the kinase, leads to a rearrangement of the catalytic site and exposes Thr-172 of CDK4 for phosphorylation and subsequent activation.","predictedComplex":false,"interactors":[{"ac":"EBI-847225","identifier":"P30285","identifierLink":"https://www.uniprot.org/uniprotkb/P30285/entry","name":"Cdk4","description":"Cyclin-dependent kinase 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-847337","identifier":"P30282","identifierLink":"https://www.uniprot.org/uniprotkb/P30282/entry","name":"Ccnd3","description":"G1/S-specific cyclin-D3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2078","complexName":"Cyclin D3-CDK4 complex","organismName":"Rattus norvegicus; 10116","description":"Required for G1 to S phase transition of the mitotic cell cycle. Phosphorylation of Rb proteins by cyclin D:CDK4 complexes leads to their partial inactivation which allows transcription of E2F-controlled genes such as cyclin E1, which activates the downstream Cdk2 kinase. 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MCM2-7 complexes unwind the double stranded DNA at the origins, recruit DNA polymerases and initiate DNA synthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-457049","identifier":"P97310","identifierLink":"https://www.uniprot.org/uniprotkb/P97310/entry","name":"Mcm2","description":"DNA replication licensing factor MCM2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-457132","identifier":"P97311","identifierLink":"https://www.uniprot.org/uniprotkb/P97311/entry","name":"Mcm6","description":"DNA replication licensing factor MCM6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-457170","identifier":"P49717","identifierLink":"https://www.uniprot.org/uniprotkb/P49717/entry","name":"Mcm4","description":"DNA replication licensing factor MCM4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-457180","identifier":"Q61881","identifierLink":"https://www.uniprot.org/uniprotkb/Q61881/entry","name":"Mcm7","description":"DNA replication licensing factor MCM7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-913666","identifier":"P25206","identifierLink":"https://www.uniprot.org/uniprotkb/P25206/entry","name":"Mcm3","description":"DNA replication licensing factor MCM3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-913678","identifier":"P49718","identifierLink":"https://www.uniprot.org/uniprotkb/P49718/entry","name":"Mcm5","description":"DNA replication licensing factor MCM5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2942","complexName":"MCM complex","organismName":"Drosophila melanogaster; 7227","description":"Essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells, associates with the origins of DNA replication to form part of the pre-replicative complex. 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MCM2-7 complexes unwind the double stranded DNA at the origins, recruit DNA polymerases and initiate DNA synthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-103930","identifier":"Q9XYU1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XYU1/entry","name":"Mcm3","description":"DNA replication licensing factor Mcm3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-138228","identifier":"P49735","identifierLink":"https://www.uniprot.org/uniprotkb/P49735/entry","name":"Mcm2","description":"DNA replication licensing factor Mcm2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-175772","identifier":"Q26454","identifierLink":"https://www.uniprot.org/uniprotkb/Q26454/entry","name":"dpa","description":"DNA replication licensing factor MCM4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-496657","identifier":"Q9XYU0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XYU0/entry","name":"Mcm7","description":"DNA replication licensing factor Mcm7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-83298","identifier":"Q9VGW6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VGW6/entry","name":"Mcm5","description":"DNA replication licensing factor Mcm5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-869161","identifier":"Q9V461","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V461/entry","name":"Mcm6","description":"DNA replication licensing factor Mcm6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2943","complexName":"MCM complex","organismName":"Xenopus laevis; 8355","description":"Essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells, associates with the origins of DNA replication to form part of the pre-replicative complex. Activation of the MCM complex at origins by cyclin-dependent kinases and the Cdc7 protein kinase leads to initiation of DNA synthesis. MCM2-7 complexes unwind the double stranded DNA at the origins, recruit DNA polymerases and initiate DNA synthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-491720","identifier":"P49739","identifierLink":"https://www.uniprot.org/uniprotkb/P49739/entry","name":"mmcm3","description":"Maternal DNA replication licensing factor mcm3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Xenopus laevis; 8355","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-876842","identifier":"Q7ZY18","identifierLink":"https://www.uniprot.org/uniprotkb/Q7ZY18/entry","name":"zmcm6-b","description":"Zygotic DNA replication licensing factor mcm6-B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Xenopus laevis; 8355","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-876852","identifier":"Q91876","identifierLink":"https://www.uniprot.org/uniprotkb/Q91876/entry","name":"mcm7-a","description":"DNA replication licensing factor mcm7-A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Xenopus laevis; 8355","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-876864","identifier":"P55861","identifierLink":"https://www.uniprot.org/uniprotkb/P55861/entry","name":"mcm2","description":"DNA replication licensing factor mcm2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Xenopus laevis; 8355","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-876871","identifier":"P30664","identifierLink":"https://www.uniprot.org/uniprotkb/P30664/entry","name":"mcm4-b","description":"DNA replication licensing factor mcm4-B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Xenopus laevis; 8355","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-876879","identifier":"P55862","identifierLink":"https://www.uniprot.org/uniprotkb/P55862/entry","name":"mcm5-a","description":"DNA replication licensing factor mcm5-A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Xenopus laevis; 8355","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2944","complexName":"MCM complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells, associates with the origins of DNA replication to form part of the pre-replicative complex. 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MCM2-7 complexes unwind the double stranded DNA at the origins, recruit DNA polymerases and initiate DNA synthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-10533","identifier":"P29469","identifierLink":"https://www.uniprot.org/uniprotkb/P29469/entry","name":"MCM2","description":"DNA replication licensing factor MCM2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10541","identifier":"P24279","identifierLink":"https://www.uniprot.org/uniprotkb/P24279/entry","name":"MCM3","description":"DNA replication licensing factor MCM3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10549","identifier":"P29496","identifierLink":"https://www.uniprot.org/uniprotkb/P29496/entry","name":"MCM5","description":"Minichromosome maintenance protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10556","identifier":"P53091","identifierLink":"https://www.uniprot.org/uniprotkb/P53091/entry","name":"MCM6","description":"DNA replication licensing factor MCM6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4300","identifier":"P38132","identifierLink":"https://www.uniprot.org/uniprotkb/P38132/entry","name":"MCM7","description":"DNA replication licensing factor MCM7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4326","identifier":"P30665","identifierLink":"https://www.uniprot.org/uniprotkb/P30665/entry","name":"MCM4","description":"DNA replication licensing factor MCM4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2945","complexName":"MCM complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells, associates with the origins of DNA replication to form part of the pre-replicative complex. 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MCM2-7 complexes unwind the double stranded DNA at the origins, recruit DNA polymerases and initiate DNA synthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-783248","identifier":"P40377","identifierLink":"https://www.uniprot.org/uniprotkb/P40377/entry","name":"mcm2","description":"DNA replication licensing factor mcm2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-913795","identifier":"P30666","identifierLink":"https://www.uniprot.org/uniprotkb/P30666/entry","name":"mcm3","description":"DNA replication licensing factor mcm3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-913806","identifier":"P29458","identifierLink":"https://www.uniprot.org/uniprotkb/P29458/entry","name":"mcm4","description":"DNA replication licensing factor mcm4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-913821","identifier":"P41389","identifierLink":"https://www.uniprot.org/uniprotkb/P41389/entry","name":"mcm5","description":"DNA replication licensing factor mcm5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-913838","identifier":"P49731","identifierLink":"https://www.uniprot.org/uniprotkb/P49731/entry","name":"mcm6","description":"DNA replication licensing factor mcm6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-913851","identifier":"O75001","identifierLink":"https://www.uniprot.org/uniprotkb/O75001/entry","name":"mcm7","description":"DNA replication licensing factor mcm7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3111","complexName":"Glucose transporter complex 1","organismName":"Homo sapiens; 9606","description":"Ubiquitously expressed, class I facilitative glucose transporter found in high levels in erythrocyes and endothelial cells of the brain. Critical regulator of glucose use, storage and the hormonal control of metabolism. May also transport dehydroascorbic acid.","predictedComplex":false,"interactors":[{"ac":"EBI-717153","identifier":"P11166","identifierLink":"https://www.uniprot.org/uniprotkb/P11166/entry","name":"SLC2A1","description":"Solute carrier family 2, facilitated glucose transporter member 1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23503","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3112","complexName":"Glucose transporter complex 1","organismName":"Mus musculus; 10090","description":"Ubiquitously expressed, class I facilitative glucose transporter found in high levels in erythrocyes and endothelial cells of the brain. Critical regulator of glucose use, storage and the hormonal control of metabolism. May also transport dehydroascorbic acid (By similarity).","predictedComplex":false,"interactors":[{"ac":"EBI-646060","identifier":"P17809","identifierLink":"https://www.uniprot.org/uniprotkb/P17809/entry","name":"Slc2a1","description":"Solute carrier family 2, facilitated glucose transporter member 1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23503","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3113","complexName":"Glucose transporter complex 1","organismName":"Rattus norvegicus; 10116","description":"Ubiquitously expressed, class I facilitative glucose transporter found in high levels in erythrocyes and endothelial cells of the brain. Critical regulator of glucose use, storage and the hormonal control of metabolism. May also transport dehydroascorbic acid (By similarity).","predictedComplex":false,"interactors":[{"ac":"EBI-960654","identifier":"P11167","identifierLink":"https://www.uniprot.org/uniprotkb/P11167/entry","name":"Slc2a1","description":"Solute carrier family 2, facilitated glucose transporter member 1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR23503","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3168","complexName":"Methionine adenosyltransferase complex variant 1","organismName":"Homo sapiens; 9606","description":"Liver specific enzyme complex which catalyses the formation of S-adenosylmethionine from L-methionine and ATP. The reaction comprises of two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate. Requires divalent cations for catalysis, and monovalent cations for activation. Plays an essential role in the preservation of the quiescent and differentiated status of the hepatocyte. MAT I is present in lower amounts than MAT III and is probably predominantly responsible for S-adenosylmethionine biosynthesis under normal conditions. Under high methionine cencentrations,  MAT III, the predominant liver form, switches to a higher specific activity conformation (hysteretic behaviour) and rapidly eliminates methionine excess.","predictedComplex":false,"interactors":[{"ac":"EBI-967087","identifier":"Q00266","identifierLink":"https://www.uniprot.org/uniprotkb/Q00266/entry","name":"MAT1A","description":"S-adenosylmethionine synthase isoform type-1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3169","complexName":"Methionine adenosyltransferase complex variant 3","organismName":"Homo sapiens; 9606","description":"Liver specific enzyme complex which catalyses the formation of S-adenosylmethionine from L-methionine and ATP. 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At high methionine concentrations, MAT III, the predominant liver form, switches to a higher specific activity conformation (hysteretic behaviour) and rapidly eliminates methionine excess.","predictedComplex":false,"interactors":[{"ac":"EBI-967087","identifier":"Q00266","identifierLink":"https://www.uniprot.org/uniprotkb/Q00266/entry","name":"MAT1A","description":"S-adenosylmethionine synthase isoform type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3182","complexName":"Methionine adenosyltransferase complex variant 1","organismName":"Mus musculus; 10090","description":"Liver specific enzyme complex which catalyses the formation of S-adenosylmethionine from L-methionine and ATP. Requires divalent cations for catalysis, and monovalent cations for activation. Plays an essential role in the preservation of the quiescent and differentiated status of the hepatocyte. MAT I is present in lower amounts than MAT III and is probably predominantly responsible for S-adenosylmethionine biosynthesis under normal conditions. At high methionine concentrations,  MAT III, the predominant liver form, switches to a higher specific activity conformation (hysteretic behaviour) and rapidly eliminates methionine excess (By similarity).","predictedComplex":false,"interactors":[{"ac":"EBI-968123","identifier":"Q91X83","identifierLink":"https://www.uniprot.org/uniprotkb/Q91X83/entry","name":"Mat1a","description":"S-adenosylmethionine synthase isoform type-1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3183","complexName":"Methionine adenosyltransferase complex variant 3","organismName":"Mus musculus; 10090","description":"Liver specific enzyme complex which catalyses the formation of S-adenosylmethionine from L-methionine and ATP. Requires divalent cations for catalysis, and monovalent cations for activation. Plays an essential role in the preservation of the quiescent and differentiated status of the hepatocyte. MAT I is present in lower amounts than MAT III and is probably predominantly responsible for S-adenosylmethionine biosynthesis under normal conditions. At high methionine concentrations, MAT III, the predominant liver form, switches to a higher specific activity conformation (hysteretic behaviour) and rapidly eliminates methionine excess (By similarity).","predictedComplex":false,"interactors":[{"ac":"EBI-968123","identifier":"Q91X83","identifierLink":"https://www.uniprot.org/uniprotkb/Q91X83/entry","name":"Mat1a","description":"S-adenosylmethionine synthase isoform type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1900","complexName":"Chromosomal passenger complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Serine/threonine kinase complex which ensures chromosome bi-orientation on the mitotic spindle during metaphase by phosphorylating multiple kinetochore components. It destabilizes monopolar attachments by phosphorylating key proteins at the kinetophore. The opposing Chromosomal Passenger complex and Glc7 (P32598) activities ensure that chromosomes achieve a bipolar attachment to the spindle. Monopolar attachments do not produce tension across sister kinetochores (and the complex may act by sensing this absence of tension). The Chromosome passenger complex is conserved from yeast to man and is an essential regulator of diverse aspects of mitosis that ensure faithful chromosome segregation.  The complex undergoes changes in its localization throughout mitosis: in early mitosis it presumably localizes to chromosome arms while later in metaphase it is found at the centromere.  At anaphase onset it re-localizes to mitotic spindle microtubules accumulating in the midbody in late anaphase where it promotes spindle disassembly and cytokinesis.  In budding yeast it seems to follow the positive ends of depolimerizing microtubules in late anaphase.  It also plays a role in contractile ring formation and regulation of abscission in cytokinesis.","predictedComplex":false,"interactors":[{"ac":"EBI-20842","identifier":"P38283","identifierLink":"https://www.uniprot.org/uniprotkb/P38283/entry","name":"SLI15","description":"Inner centromere protein SLI15","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-3648","identifier":"P47134","identifierLink":"https://www.uniprot.org/uniprotkb/P47134/entry","name":"BIR1","description":"Chromosomal passenger complex protein BIR1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46771","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9319","identifier":"P38991","identifierLink":"https://www.uniprot.org/uniprotkb/P38991/entry","name":"IPL1","description":"Aurora kinase","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24350","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9513736","identifier":"Q3E7Y6","identifierLink":"https://www.uniprot.org/uniprotkb/Q3E7Y6/entry","name":"NBL1","description":"N-terminal-borealin-like protein","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3070","complexName":"HRD1 E3 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Transmembrane E3 ubiquitin ligase complex involved in the endoplasmic reticulum-associated degradation (ERAD) pathway, directing misfolded proteins to proteasomal degradation. Required for ERAD-L, -M subpathways which degrade proteins with misfolded luminal or transmembrane domains, respectively. The HRD1 core complex acts together with the E2 ubiquitin conjugating enzymes Cue1-Ubc7 (CPX-2948) and UBC1 (P21734) and also the Cdc48p-Npl4p-Ufd1p AAA ATPase complex (CPX-2946).","predictedComplex":false,"interactors":[{"ac":"EBI-27730","identifier":"Q04228","identifierLink":"https://www.uniprot.org/uniprotkb/Q04228/entry","name":"UBX2","description":"UBX domain-containing protein 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23322","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27760","identifier":"Q03714","identifierLink":"https://www.uniprot.org/uniprotkb/Q03714/entry","name":"USA1","description":"U1 SNP1-associating protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-31647","identifier":"Q05787","identifierLink":"https://www.uniprot.org/uniprotkb/Q05787/entry","name":"HRD3","description":"ERAD-associated E3 ubiquitin-protein ligase component HRD3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34938","identifier":"Q99220","identifierLink":"https://www.uniprot.org/uniprotkb/Q99220/entry","name":"YOS9","description":"Protein OS-9 homolog","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15414","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-37613","identifier":"Q08109","identifierLink":"https://www.uniprot.org/uniprotkb/Q08109/entry","name":"HRD1","description":"ERAD-associated E3 ubiquitin-protein ligase HRD1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22765","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5761","identifier":"P38307","identifierLink":"https://www.uniprot.org/uniprotkb/P38307/entry","name":"DER1","description":"Degradation in the endoplasmic reticulum protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11009","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1941","complexName":"Exon junction core complex, MAGOH variant","organismName":"Homo sapiens; 9606","description":"Plays a role in translation, surveillance and localization of the maturing mRNA molecules. Deposited by spliceosomes at a conserved position of a pre-messenger RNA strand located upstream of exon junctions formed during RNA splicing. The EJC remains stably bound at this position as the mature messenger ribonucleoprotein particle is exported to the cytoplasm, potentially promoting export through its close association with the TREX complex. Binds RNA primarily through EIF4A3, a sequence-independent DEAD box protein that grasps RNA stably only when associated with its partners, RBM8A/Y14 and MAGOH which inhibit the DEAD-box protein EIF4A3 ATPase activity, trapping the ATP-bound EJC core onto spliced mRNA in a stable conformation. The EJC core serves as a binding platform for additional factors which together then interface with numerous machineries controlling mRNA export, translation, and decay. Discriminates between premature and normal translation termination events by providing architectural information regarding the position of (former) introns. When translation terminates on an mRNA upstream of at least one EJC, UPF3 (Q9H1J1/Q9BZI7) and its cofactors UPF1 (Q9H1J1) and UPF2 (Q9HAU5) orchestrate a series of events that destabilize the message by a process known as nonsense-mediated mRNA decay (NMD). Also enhances translation of newly synthesized mRNAs through interactions between POLDIP3 (Q9BY77) and activated S6-kinase.","predictedComplex":false,"interactors":[{"ac":"EBI-299104","identifier":"P38919","identifierLink":"https://www.uniprot.org/uniprotkb/P38919/entry","name":"EIF4A3","description":"Eukaryotic initiation factor 4A-III","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47958","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-299118","identifier":"O15234","identifierLink":"https://www.uniprot.org/uniprotkb/O15234/entry","name":"CASC3","description":"Protein CASC3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13434","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-299134","identifier":"P61326","identifierLink":"https://www.uniprot.org/uniprotkb/P61326/entry","name":"MAGOH","description":"Protein mago nashi homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12638","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-447231","identifier":"Q9Y5S9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5S9/entry","name":"RBM8A","description":"RNA-binding protein 8A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1942","complexName":"Exon junction subcomplex MAGOH-Y14","organismName":"Homo sapiens; 9606","description":"Component of the exon-junction complex (EJC, CPX-1941) that is formed in the nucleus and exported to the cytoplasm as part of the mature messenger ribonucleoprotein particle. Binding of the EJC key regulator PYM1 (Q9BRP8) to MAGOH-Y14 in the cytoplasm triggers disassembly of the EJC. MAGOH-Y14 complex remains bound in the same position on the spliced mRNA and requires translation of the mRNA for removal. When interacting with PYM1, associates with mRNA-degradation factors, including the mRNA-decapping complex and exoribonucleases and may play a role in preventing mRNA degradation during mRNA biogenesis. This complex itself does not bind RNA. Binding to IPO13 (O94829) leads to import back into the nucleus prior to reassembly of the EJC.","predictedComplex":false,"interactors":[{"ac":"EBI-299134","identifier":"P61326","identifierLink":"https://www.uniprot.org/uniprotkb/P61326/entry","name":"MAGOH","description":"Protein mago nashi homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12638","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-447231","identifier":"Q9Y5S9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5S9/entry","name":"RBM8A","description":"RNA-binding protein 8A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-58","complexName":"Methionine adenosyltransferase complex variant 1","organismName":"Rattus norvegicus; 10116","description":"Liver specific enzyme complex which catalyses the formation of S-adenosylmethionine from L-methionine and ATP. Requires divalent cations for catalysis, and monovalent cations for activation. Plays an essential role in the preservation of the quiescent and differentiated status of the hepatocyte. MAT I is present in lower amounts than MAT III and is probably predominantly responsible for S-adenosylmethionine biosynthesis under normal conditions. At high methionine concentrations,  MAT III, the predominant liver form, switches to a higher specific activity conformation (hysteretic behaviour) and rapidly eliminates methionine excess.","predictedComplex":false,"interactors":[{"ac":"EBI-961260","identifier":"P13444","identifierLink":"https://www.uniprot.org/uniprotkb/P13444/entry","name":"Mat1a","description":"S-adenosylmethionine synthase isoform type-1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-59","complexName":"Methionine adenosyltransferase complex variant 3","organismName":"Rattus norvegicus; 10116","description":"Liver specific enzyme complex which catalyses the formation of S-adenosylmethionine from L-methionine and ATP. Requires divalent cations for catalysis, and monovalent cations for activation. Plays an essential role in the preservation of the quiescent and differentiated status of the hepatocyte. MAT I is present in lower amounts than MAT III and is probably predominantly responsible for S-adenosylmethionine biosynthesis under normal conditions. At high methionine concentrations, MAT III, the predominant liver form, switches to a higher specific activity conformation (hysteretic behaviour) and rapidly eliminates methionine excess (By similarity).","predictedComplex":false,"interactors":[{"ac":"EBI-961260","identifier":"P13444","identifierLink":"https://www.uniprot.org/uniprotkb/P13444/entry","name":"Mat1a","description":"S-adenosylmethionine synthase isoform type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1921","complexName":"U2 small nuclear ribonucleoprotein auxiliary factor complex","organismName":"Homo sapiens; 9606","description":"Ribonucleoprotein complex that recognizes an consensus AG-dinucleotide at the splice site junction and a preceding polypyrimidine tract and recruits the U2 small nuclear ribonucleoprotein particle (snRNP) of the spliceosome during the removal of intervening sequences (introns) separating protein-coding regions within pre-mRNAs. The 65-kDa subunit (U2AF2), contacts the polypyrimidine-tract, and the 35-kDa subunit (U2AF1), interacts with the AG dinucleotide at the 3' splice site.","predictedComplex":false,"interactors":[{"ac":"EBI-632461","identifier":"Q01081","identifierLink":"https://www.uniprot.org/uniprotkb/Q01081/entry","name":"U2AF1","description":"Splicing factor U2AF 35 kDa subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12620","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742339","identifier":"P26368","identifierLink":"https://www.uniprot.org/uniprotkb/P26368/entry","name":"U2AF2","description":"Splicing factor U2AF 65 kDa subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1968","complexName":"Molybdopterin-synthase adenylyltransferase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Involved in molybdopterin cofactor (Moco) biosynthesis under anaerobic conditions. MoeB catalyses the adenylation of MoaD by ATP, activating the C terminus of the MoaD subunit of molybdopterin synthase (CPX-1970) to form MoaD-adenylate, which is subsequently converted to a thiocarboxylate for the generation of the dithiolene group of molybdopterin. .\r\n\r\nReceives a sulfur moiety from iscS (P0a6b7).","predictedComplex":false,"interactors":[{"ac":"EBI-554366","identifier":"P30748","identifierLink":"https://www.uniprot.org/uniprotkb/P30748/entry","name":"moaD","description":"Molybdopterin synthase sulfur carrier subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33359","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-554435","identifier":"P12282","identifierLink":"https://www.uniprot.org/uniprotkb/P12282/entry","name":"moeB","description":"Molybdopterin-synthase adenylyltransferase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1970","complexName":"Molybdopterin synthase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Involved in molybdopterin cofactor (Moco) biosynthesis under anaerobic conditions converting molybdopterin precursor Z (CHEBI:52994) to molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by moaD.","predictedComplex":false,"interactors":[{"ac":"EBI-554366","identifier":"P30748","identifierLink":"https://www.uniprot.org/uniprotkb/P30748/entry","name":"moaD","description":"Molybdopterin synthase sulfur carrier subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33359","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-554376","identifier":"P30749","identifierLink":"https://www.uniprot.org/uniprotkb/P30749/entry","name":"moaE","description":"Molybdopterin synthase catalytic subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR23404","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1974","complexName":"Nitrate reductase A complex","organismName":"Escherichia coli (strain K12); 83333","description":"Inducible nitrate reductase complex involved in electron transport during anaerobic respiration: electrons are passed from the formate dehydrogenase-N (Fdh-N) complex (CPX-1975) to the nitrate reductase complex via a quinone-quinol redox reaction. Within Nitrate redctase A, the distal heme molecule of NarI receives electrons from quinol (hydroquinone), passes them on to the proximal heme which passes it down a Fe-S cluster chain to the molybdopterin cofactor Mo-bisMGD where nitrate is reduced to nitrite.\r\n\r\nThe collaboration of these two complexes contributes to the proton motive force: electrons are ultimately donated to Fdh-N by formate in the periplasm, transported to the cytoplasm and accepted by nitrate. Hydrogen ions are transported in the opposite direction: Quinone is reduced to quinol by cytoplasmic protons which are in turn released into the periplasm when quinol is oxidized to quinone.\r\n\r\nExpression of the thenarGHJI operon isinduced by nitrate.","predictedComplex":false,"interactors":[{"ac":"EBI-11297461","identifier":"CHEBI:21137","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:21137","name":"tri-mu-sulfido-mu3-sulfido-triiron","description":"tri-mu-sulfido-mu3-sulfido-triiron","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-11426020","identifier":"CHEBI:60539","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60539","name":"mo(=o)-bis(molybdopterin guanine dinucleotide)(4-)","description":"Mo(=O)-bis(molybdopterin guanine dinucleotide)(4-)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-547248","identifier":"P09152","identifierLink":"https://www.uniprot.org/uniprotkb/P09152/entry","name":"narG","description":"Respiratory nitrate reductase 1 alpha chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-555067","identifier":"P11349","identifierLink":"https://www.uniprot.org/uniprotkb/P11349/entry","name":"narH","description":"Respiratory nitrate reductase 1 beta chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43518","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-560344","identifier":"P11350","identifierLink":"https://www.uniprot.org/uniprotkb/P11350/entry","name":"narI","description":"Respiratory nitrate reductase 1 gamma chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30598","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3175","complexName":"Endopeptidase ClpAP complex","organismName":"Escherichia coli (strain K12); 83333","description":"ATP-dependent serine protease which degrades intracellular unfolded or misfolded proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-370625","identifier":"P0A6G7","identifierLink":"https://www.uniprot.org/uniprotkb/P0A6G7/entry","name":"clpP","description":"ATP-dependent Clp protease proteolytic subunit","stochiometry":"minValue: 14, maxValue: 14","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10381","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-546140","identifier":"P0ABH9","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABH9/entry","name":"clpA","description":"ATP-dependent Clp protease ATP-binding subunit ClpA","stochiometry":"minValue: 12, maxValue: 12","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11638","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3176","complexName":"Endopeptidase ClpXP complex","organismName":"Escherichia coli (strain K12); 83333","description":"ATP-dependent serine protease which degrades intracellular unfolded or misfolded proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-370625","identifier":"P0A6G7","identifierLink":"https://www.uniprot.org/uniprotkb/P0A6G7/entry","name":"clpP","description":"ATP-dependent Clp protease proteolytic subunit","stochiometry":"minValue: 14, maxValue: 14","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10381","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-547386","identifier":"P0A6H1","identifierLink":"https://www.uniprot.org/uniprotkb/P0A6H1/entry","name":"clpX","description":"ATP-dependent Clp protease ATP-binding subunit ClpX","stochiometry":"minValue: 12, maxValue: 12","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR48102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3178","complexName":"Endopeptidase ClpP complex","organismName":"Escherichia coli (strain K12); 83333","description":"ATP-dependent serine protease which degrades intracellular unfolded or misfolded proteins. ClpP on its own can degrade only small peptides (<5 amino acids) or full-length unfolded proteins with low efficiency and requires association to the ClpA or ClpX ATPases to efficiently process larger peptides and folded proteins. In the absence of the ATPase complex, ClpP is assumed to be in a closed conformation.","predictedComplex":false,"interactors":[{"ac":"EBI-370625","identifier":"P0A6G7","identifierLink":"https://www.uniprot.org/uniprotkb/P0A6G7/entry","name":"clpP","description":"ATP-dependent Clp protease proteolytic subunit","stochiometry":"minValue: 14, maxValue: 14","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10381","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3091","complexName":"Aspartate carbamoyltransferase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the committed step in pyrimidine nucleotide biosynthesis and allosterically regulates the pathway. The enzyme is activated by ATP,  inhibited by CTP and can be further inhibited by UTP, although UTP alone has little effect on activity. The catalytic mechanism is ordered, Carbamoyl phosphate binds before aspartate and carbamoyl aspartate leaves before phosphate.","predictedComplex":false,"interactors":[{"ac":"EBI-906620","identifier":"P0A786","identifierLink":"https://www.uniprot.org/uniprotkb/P0A786/entry","name":"pyrB","description":"Aspartate carbamoyltransferase catalytic subunit","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11405","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-906630","identifier":"P0A7F3","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7F3/entry","name":"pyrI","description":"Aspartate carbamoyltransferase regulatory chain","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR35805","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 6, maxValue: 6","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3139","complexName":"RAD55-RAD57 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Role in the early stages of the homologous recombination DNA damage repair process. Recruited by the Shu complex (CPX-3087) to the sites of single-stranded DNA gaps left by replication-blocking lesions to complete error-free DNA-damage tolerance. Counteracts the anti-recombination activity of the SRS2 helicase (P12954) by associating with the RAD51 (P25454)-ssDNA filament, rendering it more stable than a nucleoprotein filament containing RAD51 alone. stimulates RAD51 filament assembly onto RPA-coated single-stranded DNA. The RAD51/RAD55-AD57 co-filament resists disruption by the SRS2 anti-recombinase by blocking SRS2 translocation. The complex is also involved in double-strand break repair.","predictedComplex":false,"interactors":[{"ac":"EBI-14737","identifier":"P38953","identifierLink":"https://www.uniprot.org/uniprotkb/P38953/entry","name":"RAD55","description":"DNA repair protein RAD55","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14744","identifier":"P25301","identifierLink":"https://www.uniprot.org/uniprotkb/P25301/entry","name":"RAD57","description":"DNA repair protein RAD57","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-376","complexName":"Pyruvate dehydrogenase E1 heterotetramer","organismName":"Homo sapiens; 9606","description":"The pyruvate dehydrogenase complex (PDC) catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). Eukaryotic PDC is a highly organized multienzyme complex with the core structure formed by 60 subunits of dihydrolipoamide acetyltransferase (E2) and 12 monomers of dihydrolipoamide dehydrogenase-binding protein (E3BP) to which other components of the complex are bound: 20-30  heterotetramers (alpha2beta2) of pyruvate dehydrogenase (E1), 6-12 homodimers of dihydrolipoamide dehydrogenase  (E3), 1-2 homo (or hetero) dimers of pyruvate dehydrogenase kinase and 2-3 heterodimers of phosphopyruvate dehydrogenase phosphatase. E1 catalyzes the first irreversible and rate-limiting step in the PDC catalyzed reactions, i.e. the thiamine pyrophosphate (TPP)-dependent decarboxylation of pyruvic acid with formation of 2-a-hydroxyethylidene-TPP and carbon dioxide and reductive acetylation of lipoyl moieties of E2. Heterotetrameric E1 has two active sites that interact with each other during catalysis, each using TPP and magnesium ion as cofactors and each formed on the interface between the alpha and beta subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-1035872","identifier":"P11177","identifierLink":"https://www.uniprot.org/uniprotkb/P11177/entry","name":"PDHB","description":"Pyruvate dehydrogenase E1 component subunit beta, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11624","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-715747","identifier":"P08559","identifierLink":"https://www.uniprot.org/uniprotkb/P08559/entry","name":"PDHA1","description":"Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11516","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9691551","identifier":"CHEBI:58937","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58937","name":"thiamine(1+) diphosphate(3-)","description":"thiamine(1+) diphosphate(3-)","stochiometry":"minValue: 3, maxValue: 3","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-377","complexName":"Pyruvate dehydrogenase E1 heterotetramer","organismName":"Mus musculus; 10090","description":"The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). Eukaryotic PDC is a  highly organized multienzyme complex with the core  structure formed by 60 subunits of dihydrolipoamide  acetyltransferase (E2) and 12 monomers of dihydrolipoamide  dehydrogenase-binding protein (E3BP) to which  other components of the complex are bound: 20-30  heterotetramers (alpha2beta2) of pyruvate dehydrogenase (E1),  6-12 homodimers of dihydrolipoamide dehydrogenase  (E3), 1-2 homo (or hetero) dimers of pyruvate dehydrogenase  kinase and 2-3 heterodimers of phosphopyruvate  dehydrogenase phosphatase. E1 catalyzes the first irreversible and rate-limiting step  in the PDC catalyzed reactions, i.e. the thiamine pyrophosphate  (TPP)-dependent decarboxylation of pyruvic  acid with formation of 2-a-hydroxyethylidene-TPP and carbon dioxide and reductive acetylation of  lipoyl moieties of E2. Heterotetrameric E1 has two  active sites that interact with each other during catalysis, each using TPP and magnesium ion  as cofactors and each formed on the interface between the alpha and beta subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-773613","identifier":"P35486","identifierLink":"https://www.uniprot.org/uniprotkb/P35486/entry","name":"Pdha1","description":"Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11516","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-773622","identifier":"Q9D051","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D051/entry","name":"Pdhb","description":"Pyruvate dehydrogenase E1 component subunit beta, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11624","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9691551","identifier":"CHEBI:58937","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58937","name":"thiamine(1+) diphosphate(3-)","description":"thiamine(1+) diphosphate(3-)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-378","complexName":"Pyruvate dehydrogenase E1 heterotetramer","organismName":"Rattus norvegicus; 10116","description":"The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). Eukaryotic PDC is a  highly organized multienzyme complex with the core  structure formed by 60 subunits of dihydrolipoamide  acetyltransferase (E2) and 12 monomers of dihydrolipoamide  dehydrogenase-binding protein (E3BP) to which  other components of the complex are bound: 20-30  heterotetramers (alpha2beta2) of pyruvate dehydrogenase (E1),  6-12 homodimers of dihydrolipoamide dehydrogenase  (E3), 1-2 homo (or hetero) dimers of pyruvate dehydrogenase  kinase and 2-3 heterodimers of phosphopyruvate  dehydrogenase phosphatase. E1 catalyzes the first irreversible and rate-limiting step  in the PDC catalyzed reactions, i.e. the thiamine pyrophosphate  (TPP)-dependent decarboxylation of pyruvic  acid with formation of 2-a-hydroxyethylidene-TPP and carbon dioxide and reductive acetylation of  lipoyl moieties of E2. Heterotetrameric E1 has two  active sites that interact with each other during catalysis, each using TPP and magnesium ion  as cofactors and each formed on the interface between the alpha and beta subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-1163773","identifier":"P26284","identifierLink":"https://www.uniprot.org/uniprotkb/P26284/entry","name":"Pdha1","description":"Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11516","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-917663","identifier":"P49432","identifierLink":"https://www.uniprot.org/uniprotkb/P49432/entry","name":"Pdhb","description":"Pyruvate dehydrogenase E1 component subunit beta, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11624","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9691551","identifier":"CHEBI:58937","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58937","name":"thiamine(1+) diphosphate(3-)","description":"thiamine(1+) diphosphate(3-)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-403","complexName":"RNA degradosome","organismName":"Escherichia coli (strain K12); 83333","description":"Key role in mRNA degradation and RNA processing. RNA binds to RnaE, RhlB helicase is necessary to unwind the RNA secondary structures and, once unwound, the 3'-5' decay of the transcripts is ensued by phosphate-dependent PNPase. RNase E bound-enolase may connect cellular metabolic status with post-transcriptional gene regulation and link RNA degradation to glycolytic processes. A dynamic set of minor components of this complex may regulate its function and compartmentalization.","predictedComplex":false,"interactors":[{"ac":"EBI-368855","identifier":"P0A6P9","identifierLink":"https://www.uniprot.org/uniprotkb/P0A6P9/entry","name":"eno","description":"Enolase","stochiometry":"minValue: 16, maxValue: 16","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11902","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-548080","identifier":"P05055","identifierLink":"https://www.uniprot.org/uniprotkb/P05055/entry","name":"pnp","description":"Polyribonucleotide nucleotidyltransferase","stochiometry":"minValue: 12, maxValue: 12","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11252","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549958","identifier":"P21513","identifierLink":"https://www.uniprot.org/uniprotkb/P21513/entry","name":"rne","description":"Ribonuclease E","stochiometry":"minValue: 12, maxValue: 12","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30001","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-555806","identifier":"P0A8J8","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8J8/entry","name":"rhlB","description":"ATP-dependent RNA helicase RhlB","stochiometry":"minValue: 8, maxValue: 8","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR47959","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-415","complexName":"DNA replication factor C complex, RFC1 variant","organismName":"Homo sapiens; 9606","description":"DNA-dependent ATPase that functions with PCNA (CPX-538) to confer processivity on DNA polymerase delta. RFC uses the energy of ATP binding and hydrolysis to recruit PCNA to DNA, break one clamp interface, and topologically link the clamp to primed template DNA during the duplication of chromosomal DNA prior to cell division. After loading PCNA, RFC then dissociates, allowing PCNA to function with Pol-delta","predictedComplex":false,"interactors":[{"ac":"EBI-1055010","identifier":"P40938","identifierLink":"https://www.uniprot.org/uniprotkb/P40938/entry","name":"RFC3","description":"Replication factor C subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-476409","identifier":"P35250","identifierLink":"https://www.uniprot.org/uniprotkb/P35250/entry","name":"RFC2","description":"Replication factor C subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-476616","identifier":"P35251","identifierLink":"https://www.uniprot.org/uniprotkb/P35251/entry","name":"RFC1","description":"Replication factor C subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23389","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-476655","identifier":"P35249","identifierLink":"https://www.uniprot.org/uniprotkb/P35249/entry","name":"RFC4","description":"Replication factor C subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712376","identifier":"P40937","identifierLink":"https://www.uniprot.org/uniprotkb/P40937/entry","name":"RFC5","description":"Replication factor C subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-472","complexName":"DNA replication factor C complex","organismName":"Mus musculus; 10090","description":"DNA-dependent ATPase that functions with PCNA (CPX-541) to confer processivity on DNA polymerase delta. RFC uses the energy of ATP binding and hydrolysis to recruit PCNA to DNA, break one clamp interface, and topologically link the clamp to primed template DNA during the duplication of chromosomal DNA prior to cell division. After loading PCNA, RFC then dissociates, allowing PCNA to function with Pol-delta RFC consists of five subunits in a spiral arrangement, each subunit being AAA+ family proteins, and the complex contains four ATP sites located at subunit interfaces. A cavity exists in the center of this protein spiral that accommodates double-stranded DNA. Conserved polar and positively charged residues line the cavity and interact with DNA. There is a gap between two subunits, RFC1 and RFC5, which may provide an exit path for single-stranded DNA from the central cavity.","predictedComplex":false,"interactors":[{"ac":"EBI-1180260","identifier":"Q99J62","identifierLink":"https://www.uniprot.org/uniprotkb/Q99J62/entry","name":"Rfc4","description":"Replication factor C subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1180268","identifier":"Q9D0F6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D0F6/entry","name":"Rfc5","description":"Replication factor C subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1180276","identifier":"Q9WUK4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WUK4/entry","name":"Rfc2","description":"Replication factor C subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1180287","identifier":"P35601","identifierLink":"https://www.uniprot.org/uniprotkb/P35601/entry","name":"Rfc1","description":"Replication factor C subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23389","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-529792","identifier":"Q8R323","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R323/entry","name":"Rfc3","description":"Replication factor C subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-473","complexName":"TOM40 mitochondrial outer membrane translocase core complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Core cation-selective high-conductance channel of the mitochondrial outer membrane preprotein translocase, through which nuclear-encoded precursor proteins cross the membrane in an unfolded state.  Most mitochondrial proteins are synthesized in the cytosol,  imported into mitochondria, sorted to one of the four submitochondrial compartments, where they function, and attain their functional native conformation, which is often facilitated by assembly into the membrane or a multiprotein complex. The existance of this core complex may be an artefact of the purification process but yeast cells lacking the receptor subunits (TOM20 and TOM70) are viable and import proteins at a reduced rate into the mitochondria.","predictedComplex":false,"interactors":[{"ac":"EBI-12501","identifier":"P80967","identifierLink":"https://www.uniprot.org/uniprotkb/P80967/entry","name":"TOM5","description":"Mitochondrial import receptor subunit TOM5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28188","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12508","identifier":"P33448","identifierLink":"https://www.uniprot.org/uniprotkb/P33448/entry","name":"TOM6","description":"Mitochondrial import receptor subunit TOM6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-12515","identifier":"P53507","identifierLink":"https://www.uniprot.org/uniprotkb/P53507/entry","name":"TOM7","description":"Mitochondrial import receptor subunit TOM7","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR34944","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12527","identifier":"P49334","identifierLink":"https://www.uniprot.org/uniprotkb/P49334/entry","name":"TOM22","description":"Mitochondrial import receptor subunit TOM22","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12504","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12539","identifier":"P23644","identifierLink":"https://www.uniprot.org/uniprotkb/P23644/entry","name":"TOM40","description":"Mitochondrial import receptor subunit TOM40","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-474","complexName":"TOM40 mitochondrial outer membrane translocase holocomplex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Translocase in the outer mitochondrial membrane that mediates the import of precursor protein and mediates inset of some resident outer membrane proteins.   Most mitochondrial proteins are synthesized in the cytosol,  imported into mitochondria, sorted to one of the four submitochondrial compartments, where they function, and attain their functional native conformation, which is often facilitated by assembly into the membrane or a multiprotein complex. The holo TOM complex contains two or three pores, each of which has a diameter of approximately 20A. When translocation by the TOM complex is coupled with that by the TIM23 or TIM22 complex, the TOM channel can operate as a passive pore to allow passage of the polypeptide segment, which is `pulled' by the TIM complex with the aid of differenial membrane potential and/or ATP. When translocation is uncoupled from the inner-membrane translocators, the TOM complex uses both the stop-transfer pathway, which consists of two steps, the first requiring a membrane potential and an ATP-dependent chaperone mHsp70, and a second mechanism involving the folding of an N-terminal domain that has already crossed the outer membrane and can function as a trap in the intermembrane space to drive translocation of the C-terminal part of the protein by a Brownian ratchet mechanism.","predictedComplex":false,"interactors":[{"ac":"EBI-12501","identifier":"P80967","identifierLink":"https://www.uniprot.org/uniprotkb/P80967/entry","name":"TOM5","description":"Mitochondrial import receptor subunit TOM5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28188","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12508","identifier":"P33448","identifierLink":"https://www.uniprot.org/uniprotkb/P33448/entry","name":"TOM6","description":"Mitochondrial import receptor subunit TOM6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-12515","identifier":"P53507","identifierLink":"https://www.uniprot.org/uniprotkb/P53507/entry","name":"TOM7","description":"Mitochondrial import receptor subunit TOM7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR34944","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12522","identifier":"P35180","identifierLink":"https://www.uniprot.org/uniprotkb/P35180/entry","name":"TOM20","description":"Mitochondrial import receptor subunit TOM20","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12430","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12527","identifier":"P49334","identifierLink":"https://www.uniprot.org/uniprotkb/P49334/entry","name":"TOM22","description":"Mitochondrial import receptor subunit TOM22","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12504","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12539","identifier":"P23644","identifierLink":"https://www.uniprot.org/uniprotkb/P23644/entry","name":"TOM40","description":"Mitochondrial import receptor subunit TOM40","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12551","identifier":"P07213","identifierLink":"https://www.uniprot.org/uniprotkb/P07213/entry","name":"TOM70","description":"Mitochondrial import receptor subunit TOM70","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46208","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-538","complexName":"PCNA homotrimer","organismName":"Homo sapiens; 9606","description":"Role in DNA replication, repair, cell-cycle control, and chromatin remodeling. Exists as a double back-to-back homotrimeric ring which encircles double-stranded DNA and slides spontaneously across it. Loaded onto at template-primer junctions synthesized on unwound DNA during S phase in an ATP-dependent process by replication factor C (CPX-415), where it recruits replicative DNA polymerases and stimulates their activity. The process of chromatin assembly is tightly coupled to DNA replication or repair and the double homotrimer allows DNA polymerase delta to binds to one homotrimer whilst the chromatin assembly factor-1 CNOT7 binds to the other.","predictedComplex":false,"interactors":[{"ac":"EBI-358311","identifier":"P12004","identifierLink":"https://www.uniprot.org/uniprotkb/P12004/entry","name":"PCNA","description":"Proliferating cell nuclear antigen","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11352","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-540","complexName":"Mitochondrial inner membrane pre-sequence translocase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Mediates the translocation of presequence-containing proteins across the inner membrane. Tim50 promotes the interaction of a presequence-carrying preprotein emerging from the Tom40 channel with the intermembrane space domain of the receptor Tom22. Tethering of Tim21 to Tom22 may allow the preprotein to be released from the TOM complex and engage with the Tim23 channel. Tim21 also promotes dissociation of the motor PAM from the TIM23 complex, a PAM-free TIM23 complex promotes inner membrane sorting of of cleavable preproteins with a hydrophobic sorting signal.  Tim17 causes PAM association to the TIM23core upon Tim21 dissociation.","predictedComplex":false,"interactors":[{"ac":"EBI-1208610","identifier":"Q9USM7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9USM7/entry","name":"tim23","description":"Mitochondrial import inner membrane translocase subunit tim23","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15371","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1208618","identifier":"O13636","identifierLink":"https://www.uniprot.org/uniprotkb/O13636/entry","name":"tim50","description":"Mitochondrial import inner membrane translocase subunit tim50","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1208627","identifier":"P87130","identifierLink":"https://www.uniprot.org/uniprotkb/P87130/entry","name":"tim17","description":"Mitochondrial import inner membrane translocase subunit tim17","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10485","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1208635","identifier":"O94618","identifierLink":"https://www.uniprot.org/uniprotkb/O94618/entry","name":"tim21","description":"Mitochondrial import inner membrane translocase subunit tim21","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13032","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-541","complexName":"PCNA homotrimer","organismName":"Mus musculus; 10090","description":"Role in DNA replication, repair, cell-cycle control, and chromatin remodeling. Exists as a double back-to-back homotrimeric ring which encircles double-stranded DNA and slides spontaneously across it. Loaded onto at template-primer junctions synthesized on unwound DNA during S phase in an ATP-dependent process by replication factor C (CPX-472), where it recruits replicative DNA polymerases and stimulates their activity. The process of chromatin assembly is tightly coupled to DNA replication or repair and the double homotrimer allows DNA polymerase delta to binds to one homotrimer whilst the chromatin assembly factor-1 CNOT7  binds to the other.","predictedComplex":false,"interactors":[{"ac":"EBI-1173716","identifier":"P17918","identifierLink":"https://www.uniprot.org/uniprotkb/P17918/entry","name":"Pcna","description":"Proliferating cell nuclear antigen","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11352","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-542","complexName":"PCNA homotrimer","organismName":"Rattus norvegicus; 10116","description":"Role in DNA replication, repair, cell-cycle control, and chromatin remodeling. Exists as a double back-to-back homotrimeric ring which encircles double-stranded DNA and slides spontaneously across it. Loaded onto at template-primer junctions synthesized on unwound DNA during S phase in an ATP-dependent process by replication factor C (CPX-472), where it recruits replicative DNA polymerases and stimulates their activity. The process of chromatin assembly is tightly coupled to DNA replication or repair and the double homotrimer allows DNA polymerase delta to binds to one homotrimer whilst the chromatin assembly factor-1 CNOT7  binds to the other (By similarity).","predictedComplex":false,"interactors":[{"ac":"EBI-1208689","identifier":"P04961","identifierLink":"https://www.uniprot.org/uniprotkb/P04961/entry","name":"Pcna","description":"Proliferating cell nuclear antigen","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11352","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-543","complexName":"PCNA homotrimer","organismName":"Drosophila melanogaster; 7227","description":"Role in DNA replication, repair, cell-cycle control, and chromatin remodeling. Exists as a double back-to-back homotrimeric ring which encircles double-stranded DNA and slides spontaneously across it. Loaded onto at template-primer junctions synthesized on unwound DNA during S phase in an ATP-dependent process by replication factor C (CPX-472), where it recruits replicative DNA polymerases and stimulates their activity. The process of chromatin assembly is tightly coupled to DNA replication or repair and the double homotrimer allows DNA polymerase delta to binds to one homotrimer whilst the chromatin assembly factor-1 CNOT7  binds to the other (By similarity).","predictedComplex":false,"interactors":[{"ac":"EBI-148806","identifier":"P17917","identifierLink":"https://www.uniprot.org/uniprotkb/P17917/entry","name":"PCNA","description":"Proliferating cell nuclear antigen","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11352","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-544","complexName":"PCNA homotrimer","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Role in DNA replication, repair, cell-cycle control, and chromatin remodeling. Exists as a double back-to-back homotrimeric ring which encircles double-stranded DNA and slides spontaneously across it. Loaded onto at template-primer junctions synthesized on unwound DNA during S phase in an ATP-dependent process by replication factor C (CPX-545), where it recruits replicative DNA polymerases and stimulates their activity. The process of chromatin assembly is tightly coupled to DNA replication or repair and the double homotrimer allows DNA polymerase delta to binds to one homotrimer whilst the chromatin assembly factor-1 CNOT7  binds to the other.","predictedComplex":false,"interactors":[{"ac":"EBI-12993","identifier":"P15873","identifierLink":"https://www.uniprot.org/uniprotkb/P15873/entry","name":"POL30","description":"Proliferating cell nuclear antigen","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11352","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-545","complexName":"DNA replication factor C complex, RFC1 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"DNA-dependent ATPase that functions with PCNA (CPX-544) to confer processivity on DNA polymerase delta. RFC uses the energy of ATP binding and hydrolysis to recruit PCNA to DNA, break one clamp interface, and topologically link the clamp to primed template DNA during the duplication of chromosomal DNA prior to cell division. After loading PCNA, RFC then dissociates, allowing PCNA to function with Pol-delta","predictedComplex":false,"interactors":[{"ac":"EBI-14985","identifier":"P38630","identifierLink":"https://www.uniprot.org/uniprotkb/P38630/entry","name":"RFC1","description":"Replication factor C subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23389","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14992","identifier":"P40348","identifierLink":"https://www.uniprot.org/uniprotkb/P40348/entry","name":"RFC2","description":"Replication factor C subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15000","identifier":"P38629","identifierLink":"https://www.uniprot.org/uniprotkb/P38629/entry","name":"RFC3","description":"Replication factor C subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15009","identifier":"P40339","identifierLink":"https://www.uniprot.org/uniprotkb/P40339/entry","name":"RFC4","description":"Replication factor C subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15016","identifier":"P38251","identifierLink":"https://www.uniprot.org/uniprotkb/P38251/entry","name":"RFC5","description":"Replication factor C subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-546","complexName":"DNA replication factor C complex, RFC1 variant","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"DNA-dependent ATPase that functions with PCNA (CPX-547) to confer processivity on DNA polymerase delta. RFC uses the energy of ATP binding and hydrolysis to recruit PCNA to DNA, break one clamp interface, and topologically link the clamp to primed template DNA during the duplication of chromosomal DNA prior to cell division. After loading PCNA, RFC then dissociates, allowing PCNA to function with Pol-delta","predictedComplex":false,"interactors":[{"ac":"EBI-1208914","identifier":"O60182","identifierLink":"https://www.uniprot.org/uniprotkb/O60182/entry","name":"rfc1","description":"Replication factor C subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23389","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1208934","identifier":"Q09843","identifierLink":"https://www.uniprot.org/uniprotkb/Q09843/entry","name":"rfc2","description":"Replication factor C subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1208954","identifier":"O14003","identifierLink":"https://www.uniprot.org/uniprotkb/O14003/entry","name":"rfc3","description":"Replication factor C subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1208980","identifier":"O94449","identifierLink":"https://www.uniprot.org/uniprotkb/O94449/entry","name":"rfc4","description":"Replication factor C subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1208995","identifier":"O94697","identifierLink":"https://www.uniprot.org/uniprotkb/O94697/entry","name":"rfc5","description":"Replication factor C subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-547","complexName":"PCNA homotrimer","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Role in DNA replication, repair, cell-cycle control, and chromatin remodeling. Exists as a double back-to-back homotrimeric ring which encircles double-stranded DNA and slides spontaneously across it. Loaded onto at template-primer junctions synthesized on unwound DNA during S phase in an ATP-dependent process by replication factor C (CPX-546), where it recruits replicative DNA polymerases and stimulates their activity. The process of chromatin assembly is tightly coupled to DNA replication or repair and the double homotrimer allows DNA polymerase delta to binds to one homotrimer whilst the chromatin assembly factor-1 CNOT7  binds to the other.","predictedComplex":false,"interactors":[{"ac":"EBI-768724","identifier":"Q03392","identifierLink":"https://www.uniprot.org/uniprotkb/Q03392/entry","name":"pcn1","description":"Proliferating cell nuclear antigen","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11352","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-548","complexName":"NDC80 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Crucial for the stable kinetochore-microtubule attachments that are needed to sustain the centromere tensions involved in achieving proper chromosome alignment in eukaryotic cells, with a role in chromosome alignment and microtubule-dependent control of MAD1/MAD2 and dynein complexes at kinetochores. Loss-of-function mutation of any of 4 subunits in yeast causes disrupted kinetochore-microtubule binding and inactivation of the spindle checkpoint, leading to high rate of chromosome loss.","predictedComplex":false,"interactors":[{"ac":"EBI-12377","identifier":"P33895","identifierLink":"https://www.uniprot.org/uniprotkb/P33895/entry","name":"NUF2","description":"Kinetochore protein NUF2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21650","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22458","identifier":"P40014","identifierLink":"https://www.uniprot.org/uniprotkb/P40014/entry","name":"SPC25","description":"Kinetochore protein SPC25","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-25247","identifier":"P40460","identifierLink":"https://www.uniprot.org/uniprotkb/P40460/entry","name":"NDC80","description":"Kinetochore protein NDC80","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10643","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27228","identifier":"Q04477","identifierLink":"https://www.uniprot.org/uniprotkb/Q04477/entry","name":"SPC24","description":"Kinetochore protein SPC24","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22142","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-549","complexName":"Ndc80 complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Crucial for the stable kinetochore-microtubule attachments that are needed to sustain the centromere tensions involved in achieving proper chromosome alignment in eukaryotic cells, with a role in chromosome alignment and microtubule-dependent control of MAD1-MAD2 (CPX-961) and dynein complexes at kinetochores. Loss-of-function mutation of any of 4 subunits in yeast causes disrupted kinetochore-microtubule binding and inactivation of the spindle checkpoint, leading to high rate of chromosome loss. Ndc80 complex is rod-like with a globular head at each end. Ndc80 and Nuf2 form one head and part of rod and Spc24 and Spc25 form rest of rod and other head.","predictedComplex":false,"interactors":[{"ac":"EBI-1002524","identifier":"Q10198","identifierLink":"https://www.uniprot.org/uniprotkb/Q10198/entry","name":"ndc80","description":"Kinetochore protein ndc80","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10643","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1002565","identifier":"Q10173","identifierLink":"https://www.uniprot.org/uniprotkb/Q10173/entry","name":"nuf2","description":"Kinetochore protein nuf2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR21650","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1002585","identifier":"Q9UST6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UST6/entry","name":"spc24","description":"Kinetochore protein spc24","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR22142","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1003107","identifier":"Q10430","identifierLink":"https://www.uniprot.org/uniprotkb/Q10430/entry","name":"spc25","description":"Kinetochore protein spc25","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR14281","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-550","complexName":"Ndc80 complex","organismName":"Homo sapiens; 9606","description":"Crucial for the stable kinetochore-microtubule attachments that are needed to sustain the centromere tensions involved in achieving proper chromosome alignment in eukaryotic cells, with a role in chromosome alignment and microtubule-dependent control of MAD1/MAD2 and dynein complexes at kinetochores. The Ndc80 complex localizes to kinetochores and acts as direct or indirect kinetochore receptor for Mps1, Mad1, Mad2, Zw10 and Rod. The effects of Ndc80 depletion on the spindle checkpoint range from complete inactivation to sustained activation followed by cell death. This range of effects may be explained by penetrance of depletion phenotype. Ndc80 complex is rod-like with a globular head at each end. Ndc80 and Nuf2 form one head and part of rod and Spc24 and Spc25 form rest of rod and other head.\r\n\r\nKNL1 (CPX-5644), MIS12 (CPX-5643) and NCD80 form the KMN protein network.","predictedComplex":false,"interactors":[{"ac":"EBI-715849","identifier":"O14777","identifierLink":"https://www.uniprot.org/uniprotkb/O14777/entry","name":"NDC80","description":"Kinetochore protein NDC80 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10643","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724102","identifier":"Q9BZD4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BZD4/entry","name":"NUF2","description":"Kinetochore protein Nuf2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21650","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-999900","identifier":"Q8NBT2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NBT2/entry","name":"SPC24","description":"Kinetochore protein Spc24","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22142","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-999909","identifier":"Q9HBM1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HBM1/entry","name":"SPC25","description":"Kinetochore protein Spc25","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14281","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-551","complexName":"Ndc80 complex","organismName":"Mus musculus; 10090","description":"Crucial for the stable kinetochore-microtubule attachments that are needed to sustain the centromere tensions involved in achieving proper chromosome alignment in eukaryotic cells, with a role in chromosome alignment and microtubule-dependent control of MAD1/MAD2 and dynein complexes at kinetochores. The Ndc80 complex localizes to kinetochores and acts as direct or indirect kinetochore receptor for Mps1, Mad1, Mad2, Zw10 and Rod. The effects of Ndc80 depletion on the spindle checkpoint range from complete inactivation to sustained activation followed by cell death. This range of effects may be explained by penetrance of depletion phenotype. Ndc80 complex is rod-like with a globular head at each end. Ndc80 and Nuf2 form one head and part of rod and Spc24 and Spc25 form rest of rod and other head. (By similarity).","predictedComplex":false,"interactors":[{"ac":"EBI-1209376","identifier":"Q99P69","identifierLink":"https://www.uniprot.org/uniprotkb/Q99P69/entry","name":"Nuf2","description":"Kinetochore protein Nuf2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21650","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1209394","identifier":"Q9D083","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D083/entry","name":"Spc24","description":"Kinetochore protein Spc24","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22142","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1209414","identifier":"Q3UA16","identifierLink":"https://www.uniprot.org/uniprotkb/Q3UA16/entry","name":"Spc25","description":"Kinetochore protein Spc25","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14281","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-309872","identifier":"Q9D0F1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D0F1/entry","name":"Ndc80","description":"Kinetochore protein NDC80 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10643","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-552","complexName":"PCNA homotrimer","organismName":"Xenopus laevis; 8355","description":"Role in DNA replication, repair, cell-cycle control, and chromatin remodeling. Exists as a double back-to-back homotrimeric ring which encircles double-stranded DNA and slides spontaneously across it. Loaded onto at template-primer junctions synthesized on unwound DNA during S phase in an ATP-dependent process by replication factor C (CPX-472), where it recruits replicative DNA polymerases and stimulates their activity. The process of chromatin assembly is tightly coupled to DNA replication or repair and the double homotrimer allows DNA polymerase delta to binds to one homotrimer whilst the chromatin assembly factor-1 CNOT7  binds to the other.","predictedComplex":false,"interactors":[{"ac":"EBI-1210838","identifier":"P18248","identifierLink":"https://www.uniprot.org/uniprotkb/P18248/entry","name":"pcna","description":"Proliferating cell nuclear antigen","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Xenopus laevis; 8355","xrefs":[{"identifier":"PTHR11352","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-553","complexName":"Mitochondrial isocitrate dehydrogenase complex (NAD+)","organismName":"Homo sapiens; 9606","description":"Tricarboxylic acid cycle enzyme which catalyzes the conversion of threo-Ds-isocitrate to alpha-ketoglutarate and carbon dioxide, important for regulatory control of mitochondrial energy metabolism. Allosterically regulated, activated by citrate and ADP, inhibited by ATP. There are two binding sites per tetramer for each of its ligands: isocitrate, Mn2+, NAD, ADP, NADH, and NADPH. During the oxidative decarboxylation, NAD reacts with Mn2+-isocitrate. The active sites are shared between the Mn2+-binding alpha and gamma subunits and between the NAD-binding alpha and beta subunits. The allosteric activator ADP has been found to be associated with only the beta and gamma subunits. Subunit IDH3B exists in two isoforms - when beta1 (O43837-1) is in the complex the pH optimum for IDH activity lowers from 8.0 to 7.6 in comparison to beta2 (O43837-2).","predictedComplex":false,"interactors":[{"ac":"EBI-1210876","identifier":"P51553","identifierLink":"https://www.uniprot.org/uniprotkb/P51553/entry","name":"IDH3G","description":"Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11835","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355999","identifier":"P50213","identifierLink":"https://www.uniprot.org/uniprotkb/P50213/entry","name":"IDH3A","description":"Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11835","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-725377","identifier":"O43837","identifierLink":"https://www.uniprot.org/uniprotkb/O43837/entry","name":"IDH3B","description":"Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11835","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9097897","identifier":"CHEBI:60240","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60240","name":"divalent metal cation","description":"divalent metal cation","stochiometry":"minValue: 6, maxValue: 6","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-554","complexName":"6-phosphofructokinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the phosphorylation of fructose 6-phosphate to fructose 1,6-bisphosphate in the presence of MgATP, the first irreversible step for glycolysis. The enzyme is stablilized in the presence of Fructose 6-P and exhibits cooperative binding of Fructose 6-P. Its activity is controlled by many allosteric activators and inhibitors (including ATP), showing its crucial role in regulation of glycolytic flux. The enzyme can exist in either the active R-state or inhibited T-state. The effectors either modulate the affinity of Pfk for Fructose 6-P or overcome inhibitory effects. Pfk is an octamer composed of 4 alpha and 4 beta subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-9428","identifier":"P16861","identifierLink":"https://www.uniprot.org/uniprotkb/P16861/entry","name":"PFK1","description":"ATP-dependent 6-phosphofructokinase subunit alpha","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13697","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9435","identifier":"P16862","identifierLink":"https://www.uniprot.org/uniprotkb/P16862/entry","name":"PFK2","description":"ATP-dependent 6-phosphofructokinase subunit beta","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13697","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-555","complexName":"6-phosphofructokinase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"6-phosphofructokinase catalyzes the phosphorylation of fructose 6-phosphate to fructose 1,6-bisphosphate in the presence of MgATP, the first irreversible step for glycolysis. The enzyme exhibits weak cooperative binding of Fructose 6-P. Its activity is controlled by many allosteric activators and inhibitors (including ATP),showing its crucial role in regulation of glycolytic flux. The effectors either modulate the affinity of Pfk for Fructose 6-P or overcome inhibitory effects.","predictedComplex":false,"interactors":[{"ac":"EBI-1215407","identifier":"O42938","identifierLink":"https://www.uniprot.org/uniprotkb/O42938/entry","name":"pfk1","description":"ATP-dependent 6-phosphofructokinase","stochiometry":"minValue: 8, maxValue: 8","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13697","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-556","complexName":"Mitochondrial isocitrate dehydrogenase complex (NAD+)","organismName":"Mus musculus; 10090","description":"Tricarboxylic acid cycle enzyme which catalyzes the conversion of threo-Ds-isocitrate to alpha-ketoglutarate and carbon dioxide, important for regulatory control of mitochondrial energy metabolism. Allosterically regulated, activated by citrate and ADP, inhibited by ATP. There are two binding sites per tetramer for each of its ligands: isocitrate, Mn2+, NAD, ADP, NADH, and NADPH. During the oxidative decarboxylation, NAD reacts with Mn2+-isocitrate. The active sites are shared between the Mn2+-binding alpha and gamma subunits and between the NAD-binding alpha and beta subunits. The allosteric activator ADP has been found to be associated with only the beta and gamma subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-299873","identifier":"Q9D6R2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D6R2/entry","name":"Idh3a","description":"Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11835","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-773408","identifier":"Q91VA7","identifierLink":"https://www.uniprot.org/uniprotkb/Q91VA7/entry","name":"Idh3b","description":"Isocitrate dehydrogenase [NAD] subunit, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11835","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-773416","identifier":"P70404","identifierLink":"https://www.uniprot.org/uniprotkb/P70404/entry","name":"Idh3g","description":"Isocitrate dehydrogenase [NAD] subunit gamma 1, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11835","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9097897","identifier":"CHEBI:60240","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60240","name":"divalent metal cation","description":"divalent metal cation","stochiometry":"minValue: 6, maxValue: 6","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-557","complexName":"Mitochondrial isocitrate dehydrogenase complex (NAD+)","organismName":"Rattus norvegicus; 10116","description":"Tricarboxylic acid cycle enzyme which catalyzes the conversion of threo-Ds-isocitrate to alpha-ketoglutarate and carbon dioxide, important for regulatory control of mitochondrial energy metabolism. Allosterically regulated, activated by citrate and ADP, inhibited by ATP. There are two binding sites per tetramer for each of its ligands: isocitrate, Mn2+, NAD, ADP, NADH, and NADPH. During the oxidative decarboxylation, NAD reacts with Mn2+-isocitrate. The active sites are shared between the Mn2+-binding alpha and gamma subunits and between the NAD-binding alpha and beta subunits. The allosteric activator ADP has been found to be associated with only the beta and gamma subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-1216909","identifier":"Q68FX0","identifierLink":"https://www.uniprot.org/uniprotkb/Q68FX0/entry","name":"Idh3B","description":"Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11835","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1216916","identifier":"P41565","identifierLink":"https://www.uniprot.org/uniprotkb/P41565/entry","name":"Idh3g","description":"Isocitrate dehydrogenase [NAD] subunit gamma 1, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11835","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9097897","identifier":"CHEBI:60240","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60240","name":"divalent metal cation","description":"divalent metal cation","stochiometry":"minValue: 6, maxValue: 6","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-919767","identifier":"Q99NA5","identifierLink":"https://www.uniprot.org/uniprotkb/Q99NA5/entry","name":"Idh3a","description":"Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11835","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-558","complexName":"Mitochondrial isocitrate dehydrogenase complex (NAD+)","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A tricarboxylic acid cycle enzyme which catalyzes the conversion of threo-Ds-isocitrate to alpha-ketoglutarate and carbon dioxide, important for regulatory control of mitochondrial energy metabolism. Allosterically regulated, activated by citrate and ADP, inhibited by ATP and NADH. Binds specifically and with high affinity to 5'-untranslated regions of yeast mitochondrial mRNAs.","predictedComplex":false,"interactors":[{"ac":"EBI-8878","identifier":"P28834","identifierLink":"https://www.uniprot.org/uniprotkb/P28834/entry","name":"IDH1","description":"Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11835","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8883","identifier":"P28241","identifierLink":"https://www.uniprot.org/uniprotkb/P28241/entry","name":"IDH2","description":"Isocitrate dehydrogenase [NAD] subunit 2, mitochondrial","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11835","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9097897","identifier":"CHEBI:60240","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60240","name":"divalent metal cation","description":"divalent metal cation","stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-559","complexName":"Mitochondrial isocitrate dehydrogenase complex (NAD+)","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Tricarboxylic acid cycle enzyme which catalyzes the conversion of threo-Ds-isocitrate to alpha-ketoglutarate and carbon dioxide, important for regulatory control of mitochondrial energy metabolism. Allosterically regulated, activated by citrate and ADP, inhibited by ATP and NADH. Binds specifically and with high affinity to 5'-untranslated regions of yeast mitochondrial mRNAs.","predictedComplex":false,"interactors":[{"ac":"EBI-1216983","identifier":"O13696","identifierLink":"https://www.uniprot.org/uniprotkb/O13696/entry","name":"idh1","description":"Isocitrate dehydrogenase [NAD] subunit 1, mitochondrial","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11835","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1216996","identifier":"Q9USP8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9USP8/entry","name":"idh2","description":"Isocitrate dehydrogenase [NAD] subunit 2, mitochondrial","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11835","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9097897","identifier":"CHEBI:60240","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60240","name":"divalent metal cation","description":"divalent metal cation","stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-560","complexName":"Mitochondrial respiratory chain complex III","organismName":"Homo sapiens; 9606","description":"Key role in aerobic respiration, in which mitochondrial enzymes accept electrons from electron carriers reduced in glycolysis and the tricarboxylic acid cycle.  Ubiquinol-cytochrome c reductase pumps protons into the intermembrane space, creating an electrochemical gradient. This is achieved by oxidizing ubiquinol (ubihydroquinone) which reacts from the membrane phase, reducing cytochrome c in the intermembrane space, and using the free energy change to transport  H+ ions across the membrane from the matrix to the inter membrane space. Quinol oxidation occurs in a bifurcated reaction, in which one electron is transferred to a high potential chain and the other to a low potential chain. The high potential chain, consisting of the iron sulfur protein, cyt c1 and cyt c2, transfers the first electron from quinol to an acceptor (cytochrome oxidase). The low potential chain consists of two cyt b hemes, which serve as a pathway through which electrons are transferred across the coupling membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-1051424","identifier":"P22695","identifierLink":"https://www.uniprot.org/uniprotkb/P22695/entry","name":"UQCRC2","description":"Cytochrome b-c1 complex subunit 2, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11851","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1052596","identifier":"P31930","identifierLink":"https://www.uniprot.org/uniprotkb/P31930/entry","name":"UQCRC1","description":"Cytochrome b-c1 complex subunit 1, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11851","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11172266","identifier":"CHEBI:49601","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49601","name":"fe2s2 iron-sulfur cluster","description":"Fe2S2 iron-sulfur cluster","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1224427","identifier":"P07919","identifierLink":"https://www.uniprot.org/uniprotkb/P07919/entry","name":"UQCRH","description":"Cytochrome b-c1 complex subunit 6, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15336","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1224441","identifier":"P00156","identifierLink":"https://www.uniprot.org/uniprotkb/P00156/entry","name":"MT-CYB","description":"Cytochrome b","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19271","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1224485","identifier":"O14957","identifierLink":"https://www.uniprot.org/uniprotkb/O14957/entry","name":"UQCR11","description":"Cytochrome b-c1 complex subunit 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15420","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1224495","identifier":"Q9UDW1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UDW1/entry","name":"UQCR10","description":"Cytochrome b-c1 complex subunit 9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12980","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1224514","identifier":"P08574","identifierLink":"https://www.uniprot.org/uniprotkb/P08574/entry","name":"CYC1","description":"Cytochrome c1, heme protein, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-720294","identifier":"O14949","identifierLink":"https://www.uniprot.org/uniprotkb/O14949/entry","name":"UQCRQ","description":"Cytochrome b-c1 complex subunit 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743128","identifier":"P14927","identifierLink":"https://www.uniprot.org/uniprotkb/P14927/entry","name":"UQCRB","description":"Cytochrome b-c1 complex subunit 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12022","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9098778","identifier":"P47985-PRO_0000307241","identifierLink":"https://www.uniprot.org/uniprotkb/P47985-PRO_0000307241/entry","name":"UQCRFS1","description":"Cytochrome b-c1 complex subunit 9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-9098790","identifier":"P47985-PRO_0000030664","identifierLink":"https://www.uniprot.org/uniprotkb/P47985-PRO_0000030664/entry","name":"UQCRFS1","description":"Cytochrome b-c1 complex subunit Rieske, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-561","complexName":"Mitochondrial respiratory chain complex II","organismName":"Homo sapiens; 9606","description":"Key role in aerobic respiration, in which mitochondrial enzymes accept electrons from electron carriers reduced in glycolysis and the tricarboxylic acid cycle. Catalyzes the oxidation of succinate to fumarate as part of tricarboxylic acid cycle and and transfers the electrons to coenzyme Q of the respiratory chain to form ubiquinol. Under most conditions the electrons are used to reduce oxygen, allowing ATP synthesis. SDHA and SDHB form the catalytic dimer that is anchored to the matrix surface of the mitochondrial inner membrane by SDHC and SDHD, integral membrane proteins of the membrane dimer. Electrons flow from succinate to the FAD, and sequentially through the [2Fe:2S], the [4Fe:4S], and the [3Fe:4S] clusters. From there, electrons enter the membrane dimer which contains a b-type heme and the active site for ubiquinone reduction.","predictedComplex":false,"interactors":[{"ac":"EBI-1056481","identifier":"P21912","identifierLink":"https://www.uniprot.org/uniprotkb/P21912/entry","name":"SDHB","description":"Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11921","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1057265","identifier":"P31040","identifierLink":"https://www.uniprot.org/uniprotkb/P31040/entry","name":"SDHA","description":"Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11632","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11297461","identifier":"CHEBI:21137","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:21137","name":"tri-mu-sulfido-mu3-sulfido-triiron","description":"tri-mu-sulfido-mu3-sulfido-triiron","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1224539","identifier":"Q99643","identifierLink":"https://www.uniprot.org/uniprotkb/Q99643/entry","name":"SDHC","description":"Succinate dehydrogenase cytochrome b560 subunit, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10978","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1224553","identifier":"O14521","identifierLink":"https://www.uniprot.org/uniprotkb/O14521/entry","name":"SDHD","description":"Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13337","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1225103","identifier":"CHEBI:26355","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:26355","name":"heme b","description":"Heme b","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-46449825","identifier":"CHEBI:190135","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:190135","name":"di-mu-sulfido-diiron","description":"di-mu-sulfido-diiron","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-562","complexName":"Mitochondrial respiratory chain complex II","organismName":"Mus musculus; 10090","description":"Key role in aerobic respiration, in which mitochondrial enzymes accept electrons from electron carriers reduced in glycolysis and the tricarboxylic acid cycle. 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From there, electrons enter the membrane dimer which contains a b-type heme and the active site for ubiquinone reduction.","predictedComplex":false,"interactors":[{"ac":"EBI-11172266","identifier":"CHEBI:49601","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49601","name":"fe2s2 iron-sulfur cluster","description":"Fe2S2 iron-sulfur cluster","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-11297461","identifier":"CHEBI:21137","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:21137","name":"tri-mu-sulfido-mu3-sulfido-triiron","description":"tri-mu-sulfido-mu3-sulfido-triiron","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1225105","identifier":"CHEBI:16238","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16238","name":"fad","description":"FAD - Flavin adenine dinucleotide","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-16791","identifier":"P33421","identifierLink":"https://www.uniprot.org/uniprotkb/P33421/entry","name":"SDH3","description":"Succinate dehydrogenase [ubiquinone] cytochrome b subunit, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10978","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16796","identifier":"P37298","identifierLink":"https://www.uniprot.org/uniprotkb/P37298/entry","name":"SDH4","description":"Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13337","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-5851","identifier":"Q00711","identifierLink":"https://www.uniprot.org/uniprotkb/Q00711/entry","name":"SDH1","description":"Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11632","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5856","identifier":"P21801","identifierLink":"https://www.uniprot.org/uniprotkb/P21801/entry","name":"SDH2","description":"Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11921","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-566","complexName":"Mitochondrial respiratory chain complex II","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Key role in aerobic respiration, in which mitochondrial enzymes accept electrons from electron carriers reduced in glycolysis and the tricarboxylic acid cycle. Catalyzes the oxidation of succinate to fumarate as part of tricarboxylic acid cycle and and transfers the electrons to coenzyme Q of the respiratory chain to form ubiquinol. Under most conditions the electrons are used to reduce oxygen, allowing ATP synthesis. Sdh1 and Sdh2 form the catalytic dimer that is anchored to the matrix surface of the mitochondrial inner membrane by Sdh3 and Sdh4, integral membrane proteins of the membrane dimer. Electrons flow from succinate to the FAD, and sequentially through the [2Fe:2S], the [4Fe:4S], and the [3Fe:4S] clusters. From there, electrons enter the membrane dimer which contains a b-type heme and the active site for ubiquinone reduction.","predictedComplex":false,"interactors":[{"ac":"EBI-11172266","identifier":"CHEBI:49601","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49601","name":"fe2s2 iron-sulfur cluster","description":"Fe2S2 iron-sulfur cluster","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-11297461","identifier":"CHEBI:21137","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:21137","name":"tri-mu-sulfido-mu3-sulfido-triiron","description":"tri-mu-sulfido-mu3-sulfido-triiron","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1225103","identifier":"CHEBI:26355","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:26355","name":"heme b","description":"Heme b","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1225105","identifier":"CHEBI:16238","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16238","name":"fad","description":"FAD - Flavin adenine dinucleotide","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1225137","identifier":"Q9UTJ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UTJ7/entry","name":"sdh1","description":"Probable succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11632","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1225151","identifier":"P21911","identifierLink":"https://www.uniprot.org/uniprotkb/P21911/entry","name":"sdh2","description":"Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11921","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1225165","identifier":"O74882","identifierLink":"https://www.uniprot.org/uniprotkb/O74882/entry","name":"sdh3","description":"Succinate dehydrogenase cytochrome B subunit, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10978","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1225172","identifier":"Q9P7X0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P7X0/entry","name":"sdh4","description":"Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13337","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-567","complexName":"Mitochondrial respiratory chain complex III","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Key role in aerobic respiration, in which mitochondrial enzymes accept electrons from electron carriers reduced in glycolysis and the tricarboxylic acid cycle.  Ubiquinol-cytochrome c reductase pumps protons into the intermembrane space, creating an electrochemical gradient. This is achieved by oxidizing ubiquinol (ubihydroquinone) which reacts from the membrane phase, reducing cytochrome c in the intermembrane space, and using the free energy change to transport  H+ ions across the membrane from the matrix to the inter membrane space. Quinol oxidation occurs in a bifurcated reaction, in which one electron is transferred to a high potential chain and the other to a low potential chain. The high potential chain, consisting of the iron sulfur protein, cyt c1 and cyt c2, transfers the first electron from quinol to an acceptor (cytochrome oxidase). The low potential chain consists of two cyt b hemes, which serve as a pathway through which electrons are transferred across the coupling membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-11172266","identifier":"CHEBI:49601","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49601","name":"fe2s2 iron-sulfur cluster","description":"Fe2S2 iron-sulfur cluster","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-19922","identifier":"P07256","identifierLink":"https://www.uniprot.org/uniprotkb/P07256/entry","name":"COR1","description":"Cytochrome b-c1 complex subunit 1, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11851","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19929","identifier":"P07257","identifierLink":"https://www.uniprot.org/uniprotkb/P07257/entry","name":"QCR2","description":"Cytochrome b-c1 complex subunit 2, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11851","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19938","identifier":"P00128","identifierLink":"https://www.uniprot.org/uniprotkb/P00128/entry","name":"QCR7","description":"Cytochrome b-c1 complex subunit 7, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12022","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19947","identifier":"P22289","identifierLink":"https://www.uniprot.org/uniprotkb/P22289/entry","name":"QCR9","description":"Cytochrome b-c1 complex subunit 9, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12980","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19956","identifier":"P00127","identifierLink":"https://www.uniprot.org/uniprotkb/P00127/entry","name":"QCR6","description":"Cytochrome b-c1 complex subunit 6, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15336","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19965","identifier":"P08067","identifierLink":"https://www.uniprot.org/uniprotkb/P08067/entry","name":"RIP1","description":"Cytochrome b-c1 complex subunit Rieske, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19972","identifier":"P08525","identifierLink":"https://www.uniprot.org/uniprotkb/P08525/entry","name":"QCR8","description":"Cytochrome b-c1 complex subunit 8, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19979","identifier":"P37299","identifierLink":"https://www.uniprot.org/uniprotkb/P37299/entry","name":"QCR10","description":"Cytochrome b-c1 complex subunit 10, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28254","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5357","identifier":"P07143","identifierLink":"https://www.uniprot.org/uniprotkb/P07143/entry","name":"CYT1","description":"Cytochrome c1, heme protein, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5385","identifier":"P00163","identifierLink":"https://www.uniprot.org/uniprotkb/P00163/entry","name":"COB","description":"Cytochrome b","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19271","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-568","complexName":"Chromatin assembly factor 1 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes de novo assembly of nucleosomes onto newly synthesized DNA, involved in chromatin assembly following both DNA replication and some forms of DNA repair. Binds modified histones H3 and H4 and deposits them as a tetramer, preferentially onto replicating DNA, in a step coupled to the replication process. This is followed by deposition of a pair of dimers of histones H2A and H2B mediated by other factor(s) in a process not necessarily coupled to DNA replication. The histone core of nucleosomes consists of two copies of each of histones H2A, H2B, H3 and H4. CAF-1 nucleosome deposition is thought to be involved in heterochromatic silencing. CAF-1 is not required for yeast cell proliferation, suggesting other pathway(s) can compensate.","predictedComplex":false,"interactors":[{"ac":"EBI-11391","identifier":"P13712","identifierLink":"https://www.uniprot.org/uniprotkb/P13712/entry","name":"MSI1","description":"Histone-binding protein MSI1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3913","identifier":"Q12495","identifierLink":"https://www.uniprot.org/uniprotkb/Q12495/entry","name":"RLF2","description":"Chromatin assembly factor 1 subunit A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15272","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3920","identifier":"Q04199","identifierLink":"https://www.uniprot.org/uniprotkb/Q04199/entry","name":"CAC2","description":"Chromatin assembly factor 1 subunit B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15271","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-569","complexName":"Chromatin assembly factor 1 complex","organismName":"Homo sapiens; 9606","description":"Catalyzes de novo assembly of nucleosomes onto newly synthesized DNA, involved in chromatin assembly following both DNA replication and some forms of DNA repair. Binds modified histones H3 and H4 and deposits them as a tetramer, preferentially onto replicating DNA, in a step coupled to the replication process. This is followed by deposition of a pair of dimers of histones H2A and H2B mediated by other factor(s) in a process not necessarily coupled to DNA replication. CAF-1 facilitates right-handed DNA wrapping of H3-H4 tetramers. The histone core of nucleosomes consists of two copies of each of histones H2A, H2B, H3 and H4. CAF-1 nucleosome deposition is thought to be involved in heterochromatic silencing. CAF-1 is essential for S-phase progression in mammalian cells.","predictedComplex":false,"interactors":[{"ac":"EBI-1020839","identifier":"Q13111","identifierLink":"https://www.uniprot.org/uniprotkb/Q13111/entry","name":"CHAF1A","description":"Chromatin assembly factor 1 subunit A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15272","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1052944","identifier":"Q13112","identifierLink":"https://www.uniprot.org/uniprotkb/Q13112/entry","name":"CHAF1B","description":"Chromatin assembly factor 1 subunit B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15271","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-620823","identifier":"Q09028","identifierLink":"https://www.uniprot.org/uniprotkb/Q09028/entry","name":"RBBP4","description":"Histone-binding protein RBBP4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-570","complexName":"Chromatin assembly factor 1 complex","organismName":"Mus musculus; 10090","description":"Catalyzes de novo assembly of nucleosomes onto newly synthesized DNA, involved in chromatin assembly following both DNA replication and some forms of DNA repair. Binds modified histones H3 and H4 and deposits them as a tetramer, preferentially onto replicating DNA, in a step coupled to the replication process. This is followed by deposition of a pair of dimers of histones H2A and H2B mediated by other factor(s) in a process not necessarily coupled to DNA replication. The histone core of nucleosomes consists of two copies of each of histones H2A, H2B, H3 and H4. CAF-1 nucleosome deposition is thought to be involved in   heterochromatic silencing.  CAF-1 is essential for S-phase progression in mammalian cells.","predictedComplex":false,"interactors":[{"ac":"EBI-1236740","identifier":"Q9D0N7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D0N7/entry","name":"Chaf1b","description":"Chromatin assembly factor 1 subunit B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15271","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302291","identifier":"Q60972","identifierLink":"https://www.uniprot.org/uniprotkb/Q60972/entry","name":"Rbbp4","description":"Histone-binding protein RBBP4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-639217","identifier":"Q9QWF0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9QWF0/entry","name":"Chaf1a","description":"Chromatin assembly factor 1 subunit A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15272","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-577","complexName":"Mitochondrial respiratory chain complex I","organismName":"Homo sapiens; 9606","description":"Catalyses the first step of electron transport by the oxidation of NADH, thus providing two electrons for the reduction of ubiquinone. Electron transfer is coupled with the translocation of protons across the membrane, generating a proton motive force. An additional protein, NDUFA4L2 (Q9NRX3), may also be part of the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-1043922","identifier":"P28331","identifierLink":"https://www.uniprot.org/uniprotkb/P28331/entry","name":"NDUFS1","description":"NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1045087","identifier":"Q16795","identifierLink":"https://www.uniprot.org/uniprotkb/Q16795/entry","name":"NDUFA9","description":"NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12126","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1053340","identifier":"O95139","identifierLink":"https://www.uniprot.org/uniprotkb/O95139/entry","name":"NDUFB6","description":"NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11172266","identifier":"CHEBI:49601","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49601","name":"fe2s2 iron-sulfur cluster","description":"Fe2S2 iron-sulfur cluster","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1224806","identifier":"O75306","identifierLink":"https://www.uniprot.org/uniprotkb/O75306/entry","name":"NDUFS2","description":"NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11993","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1224896","identifier":"O75489","identifierLink":"https://www.uniprot.org/uniprotkb/O75489/entry","name":"NDUFS3","description":"NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1225105","identifier":"CHEBI:16238","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16238","name":"fad","description":"FAD - Flavin adenine dinucleotide","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1237250","identifier":"P51970","identifierLink":"https://www.uniprot.org/uniprotkb/P51970/entry","name":"NDUFA8","description":"NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13344","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1245485","identifier":"O95168","identifierLink":"https://www.uniprot.org/uniprotkb/O95168/entry","name":"NDUFB4","description":"NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 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Proteins residing in the IMS are transported across the outer membrane in a largely unfolded state and the complex appears to play a role as a folding assistant.","predictedComplex":false,"interactors":[{"ac":"EBI-21740","identifier":"P25573","identifierLink":"https://www.uniprot.org/uniprotkb/P25573/entry","name":"MGR1","description":"Mitochondrial inner membrane i-AAA protease supercomplex subunit MGR1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-27224","identifier":"Q04472","identifierLink":"https://www.uniprot.org/uniprotkb/Q04472/entry","name":"MGR3","description":"Mitochondrial inner membrane i-AAA protease supercomplex subunit MGR3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28142","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27785","identifier":"P32795","identifierLink":"https://www.uniprot.org/uniprotkb/P32795/entry","name":"YME1","description":"Mitochondrial inner membrane i-AAA protease supercomplex subunit YME1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1656","complexName":"General transcription factor TFIIIC complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Transcription factor required for Pol III transcription complex assembly. Mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Assembles the initiation complex TFIIIB-TFIIIC-tDNA upstream of the transcription start site, which is sufficient for RNA polymerase III (CPX-2660) recruitment and function.","predictedComplex":false,"interactors":[{"ac":"EBI-19150","identifier":"P32367","identifierLink":"https://www.uniprot.org/uniprotkb/P32367/entry","name":"TFC1","description":"Transcription factor tau 95 kDa subunit","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13230","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19154","identifier":"P34111","identifierLink":"https://www.uniprot.org/uniprotkb/P34111/entry","name":"TFC3","description":"Transcription factor tau 138 kDa subunit","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15180","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19159","identifier":"P33339","identifierLink":"https://www.uniprot.org/uniprotkb/P33339/entry","name":"TFC4","description":"Transcription factor tau 131 kDa subunit","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29851","identifier":"Q06339","identifierLink":"https://www.uniprot.org/uniprotkb/Q06339/entry","name":"TFC6","description":"Transcription factor tau 91 kDa subunit","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15052","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31399","identifier":"Q12308","identifierLink":"https://www.uniprot.org/uniprotkb/Q12308/entry","name":"TFC8","description":"Transcription factor tau 60 kDa subunit","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-33456","identifier":"Q12415","identifierLink":"https://www.uniprot.org/uniprotkb/Q12415/entry","name":"TFC7","description":"Transcription factor tau 55 kDa subunit","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR16469","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1657","complexName":"Nuclear cap-binding complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Binds co-transcriptionally to the 5-prime, m7GpppG-cap (m7G-cap) structures of all RNA polymerase II transcripts (mRNAs and pre-miRNAs). Required for processes such as pre-mRNA splicing through commitment complex and spliceosome formation, export of mRNA out of the nucleus in association with NPL3 (Q01560), degradation of nuclear mRNAs, primary miRNA processing and miRNA-mediated RNA interference. In the cytosol, importin-beta interacts with CBC-bound importin-alpha (CPX-1068) and promotes the dissociation of the RNA from CBC. Importin-complex-bound CBC gets reimported into the nucleus for reuse.","predictedComplex":false,"interactors":[{"ac":"EBI-33556","identifier":"Q08920","identifierLink":"https://www.uniprot.org/uniprotkb/Q08920/entry","name":"CBC2","description":"Nuclear cap-binding protein subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR18847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-745","identifier":"P34160","identifierLink":"https://www.uniprot.org/uniprotkb/P34160/entry","name":"STO1","description":"Nuclear cap-binding protein complex subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1658","complexName":"General transcription factor complex TFIIE","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for mRNA synthesis of many, but not all, genes in yeast. In the transcription process, TFIIE regulates TFIIH kinase activity that phosphorylates the carboxy-terminal domain of the largest subunit of RNA polymerase II. Required for the opening of DNA, to allow transcription initiation. DNA opening occurs around the tip of the Pol II clamp and the TFIIE  ‘extended winged helix’ domain. TFIIF (CPX-1149) and TFIIE bind open promoter DNA from opposite sides of the Pol II cleft.  TFIIF adopts an extended induced structure that allows it to retain the upstream DNA-SPT15-TFIIB assembly on the wall and to bind the DNA bubble. TFIIF and TFIIE encircle and retain the DNA and TFIIE may then act to stabilize the open DNA structure.","predictedComplex":false,"interactors":[{"ac":"EBI-18903","identifier":"P36100","identifierLink":"https://www.uniprot.org/uniprotkb/P36100/entry","name":"TFA1","description":"Transcription initiation factor IIE subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18907","identifier":"P36145","identifierLink":"https://www.uniprot.org/uniprotkb/P36145/entry","name":"TFA2","description":"Transcription initiation factor IIE subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12716","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1659","complexName":"General transcription factor TFIIH complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A general transcription factor which plays a central role in both RNA polymerase II transcription and DNA repair. Component of the Pol II preinitiation complex.  The TFIIH subunit XPB is an ATP-dependent translocase that promotes DNA strand separation and promoter escape. During the transition from initiation to promoter clearance, the kinase subunit Kin28 phosphorylates Ser-5 and Ser-7 within the Pol II carboxyl terminal domain (CTD). This phosphorylation initiates a cascade of phosphorylation/dephosphorylation events on the CTD that correlates with dissociation of Pol II from the initiation machinery and its association with elongation and mRNA processing factors. This is the only general transcription factor with enzyme activity. During nucleotide excision repair, TFIIH is required for opening DNA around lesions that disrupt base pairing to permit excision of the damaged DNA and its replacement by a new DNA fragment.","predictedComplex":false,"interactors":[{"ac":"EBI-14683","identifier":"Q00578","identifierLink":"https://www.uniprot.org/uniprotkb/Q00578/entry","name":"SSL2","description":"General transcription and DNA repair factor IIH helicase/translocase subunit XPB/SSL2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11274","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14762","identifier":"P06839","identifierLink":"https://www.uniprot.org/uniprotkb/P06839/entry","name":"RAD3","description":"General transcription and DNA repair factor IIH helicase subunit XPD/RAD3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11472","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18198","identifier":"Q04673","identifierLink":"https://www.uniprot.org/uniprotkb/Q04673/entry","name":"SSL1","description":"General transcription and DNA repair factor IIH subunit SSL1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12695","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19146","identifier":"P32776","identifierLink":"https://www.uniprot.org/uniprotkb/P32776/entry","name":"TFB1","description":"General transcription and DNA repair factor IIH subunit TFB1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12856","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2095127","identifier":"Q3E7C1","identifierLink":"https://www.uniprot.org/uniprotkb/Q3E7C1/entry","name":"TFB5","description":"General transcription and DNA repair factor IIH subunit TFB5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28580","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2345544","identifier":"Q02939","identifierLink":"https://www.uniprot.org/uniprotkb/Q02939/entry","name":"TFB2","description":"General transcription and DNA repair factor IIH subunit TFB2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13152","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29826","identifier":"Q12004","identifierLink":"https://www.uniprot.org/uniprotkb/Q12004/entry","name":"TFB4","description":"General transcription and DNA repair factor IIH subunit TFB4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12831","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31406","identifier":"Q03290","identifierLink":"https://www.uniprot.org/uniprotkb/Q03290/entry","name":"TFB3","description":"RNA polymerase II transcription factor B subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12683","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-35196","identifier":"Q08816","identifierLink":"https://www.uniprot.org/uniprotkb/Q08816/entry","name":"TFB6","description":"General transcription and DNA repair factor IIH subunit TFB6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR37781","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4385","identifier":"P37366","identifierLink":"https://www.uniprot.org/uniprotkb/P37366/entry","name":"CCL1","description":"Cyclin CCL1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9691","identifier":"P06242","identifierLink":"https://www.uniprot.org/uniprotkb/P06242/entry","name":"KIN28","description":"Serine/threonine-protein kinase KIN28","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1660","complexName":"General transcription factor complex TFIIK","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Protein kinase component of transcription factor IIH (TFIIH) which phosphorylates the C-terminal domain of RNA polymerase II during transition from transcription to elongation after preinitiation complex (PIC) formation, thereby positively regulating transcription. TFIIH is essential for both basal and activated transcription, and is involved in nucleotide excision repair of damaged DNA. It is unclear whether this module has a role independent of that as a sub-complex of TFIIH.","predictedComplex":false,"interactors":[{"ac":"EBI-31406","identifier":"Q03290","identifierLink":"https://www.uniprot.org/uniprotkb/Q03290/entry","name":"TFB3","description":"RNA polymerase II transcription factor B subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12683","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4385","identifier":"P37366","identifierLink":"https://www.uniprot.org/uniprotkb/P37366/entry","name":"CCL1","description":"Cyclin CCL1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9691","identifier":"P06242","identifierLink":"https://www.uniprot.org/uniprotkb/P06242/entry","name":"KIN28","description":"Serine/threonine-protein kinase KIN28","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1661","complexName":"SPT4-SPT5 transcription elongation factor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"An essential RNA polymerase II elongation factor which functions in the control of RNAP II processivity. Mediates both activation and inhibition of transcription elongation, and plays a role in pre-mRNA processing. This complex seems to be important for the stability of the RNA polymerase II elongation machinery on the chromatin template but not for the inherent ability of this machinery to translocate down the gene. Binds  RNA in a sequence-specific manner by recognizing multiple AA repeat sequences and a region within the conserved NusG N-terminal (NGN) domain of SPT5 contacts the non-template strand of DNA both upstream of RNAPII and in the transcription bubble.","predictedComplex":false,"interactors":[{"ac":"EBI-17928","identifier":"P32914","identifierLink":"https://www.uniprot.org/uniprotkb/P32914/entry","name":"SPT4","description":"Transcription elongation factor SPT4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12882","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17937","identifier":"P27692","identifierLink":"https://www.uniprot.org/uniprotkb/P27692/entry","name":"SPT5","description":"Transcription elongation factor SPT5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11125","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1662","complexName":"Negative cofactor 2 transcriptional regulator complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Represses RNA polymerase II transcription through binding to SPT15/TBP and thereby inhibiting the assembly of the preinitiation complex. The NC2 complex may also mediate transcriptional activation from TATA-driven promoters through association with SPT15/TBP and may form a larger, DNA-dependent, assembly with the Mot1-TBP complex (CPX-1141).","predictedComplex":false,"interactors":[{"ac":"EBI-11908","identifier":"P40096","identifierLink":"https://www.uniprot.org/uniprotkb/P40096/entry","name":"BUR6","description":"Negative cofactor 2 complex subunit alpha","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10252","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-37723","identifier":"Q92317","identifierLink":"https://www.uniprot.org/uniprotkb/Q92317/entry","name":"NCB2","description":"Negative cofactor 2 complex subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46138","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1663","complexName":"CYC8-TUP1 corepressor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Corepressor complex with a role in the repression of many genes in a wide variety of physiological processes including heme-regulated and catabolite repressed genes. May also be involved in the derepression of at least some target genes. The complex is recruited to target genes by interaction with DNA-bound transcriptional repressors, like MATALPHA2, MIG1, RFX1 and SKO1. The complex recruits histone deacetylases to produce a repressive chromatin structure, interacts with hypoacetylated N-terminal tails of histones H3 and H4 that have been programmed for repression by the action of histone deacetylases, and interferes directly with the transcriptional machinery by associating with the RNA polymerase II mediator complex. Undergoes transient hyperosmotic stress-induced SUMOylation and inclusion formation, which are important for the regulation of hyperosmotic-stress genes, for example the activation of glycerol biosynthesis genes.","predictedComplex":false,"interactors":[{"ac":"EBI-18215","identifier":"P14922","identifierLink":"https://www.uniprot.org/uniprotkb/P14922/entry","name":"CYC8","description":"General transcriptional corepressor CYC8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14017","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19654","identifier":"P16649","identifierLink":"https://www.uniprot.org/uniprotkb/P16649/entry","name":"TUP1","description":"General transcriptional corepressor TUP1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR44156","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1664","complexName":"DNA-directed RNA Polymerase I complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the transcription of ribosomal RNA from a DNA template by acting as a nucleotidyl transferase that polymerizes ribonucleotides at the 3' end of an RNA transcript synthesizing precursors of rRNAs. \r\n\r\nForms inactive dimers whereas initiation-competent Pol I is monomeric. Initiation of transcription requires the assembly of the upstream activating factor (UAF, CPX-1101), the core factor (CPX-1836), the TATA binding protein SPT15, and RNAP-I with RRN3 on the upstream element and core promoter. Upon transcription initiation, UAF, RRN3 and CF dissociate from the promoter.","predictedComplex":false,"interactors":[{"ac":"EBI-15730","identifier":"P10964","identifierLink":"https://www.uniprot.org/uniprotkb/P10964/entry","name":"RPA190","description":"DNA-directed RNA polymerase I subunit RPA190","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19376","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15736","identifier":"P22138","identifierLink":"https://www.uniprot.org/uniprotkb/P22138/entry","name":"RPA135","description":"DNA-directed RNA polymerase I subunit RPA135","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR20856","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15741","identifier":"Q01080","identifierLink":"https://www.uniprot.org/uniprotkb/Q01080/entry","name":"RPA49","description":"DNA-directed RNA polymerase I subunit RPA49","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14440","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15745","identifier":"P46669","identifierLink":"https://www.uniprot.org/uniprotkb/P46669/entry","name":"RPA43","description":"DNA-directed RNA polymerase I subunit RPA43","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12709","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15750","identifier":"P50106","identifierLink":"https://www.uniprot.org/uniprotkb/P50106/entry","name":"RPA14","description":"DNA-directed RNA polymerase I subunit RPA14","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-15756","identifier":"P32529","identifierLink":"https://www.uniprot.org/uniprotkb/P32529/entry","name":"RPA12","description":"DNA-directed RNA polymerase I subunit RPA12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15781","identifier":"P20434","identifierLink":"https://www.uniprot.org/uniprotkb/P20434/entry","name":"RPB5","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10535","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15786","identifier":"P20435","identifierLink":"https://www.uniprot.org/uniprotkb/P20435/entry","name":"RPO26","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47227","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15794","identifier":"P20436","identifierLink":"https://www.uniprot.org/uniprotkb/P20436/entry","name":"RPB8","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10917","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15802","identifier":"P22139","identifierLink":"https://www.uniprot.org/uniprotkb/P22139/entry","name":"RPB10","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23431","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15831","identifier":"P07703","identifierLink":"https://www.uniprot.org/uniprotkb/P07703/entry","name":"RPC40","description":"DNA-directed RNA polymerases I and III subunit RPAC1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15846","identifier":"P28000","identifierLink":"https://www.uniprot.org/uniprotkb/P28000/entry","name":"RPC19","description":"DNA-directed RNA polymerases I and III subunit RPAC2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13946","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15850","identifier":"P40422","identifierLink":"https://www.uniprot.org/uniprotkb/P40422/entry","name":"RPC10","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26109","identifier":"P47006","identifierLink":"https://www.uniprot.org/uniprotkb/P47006/entry","name":"RPA34","description":"DNA-directed RNA polymerase I subunit RPA34","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1665","complexName":"DNA ligase IV complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"DNA ligase which catalyses the final ligation step in the non-homologous end-joining DNA repair pathway. Ligates DNA strands to restore the continuity of the chromosome in non-homologous end joining DNA double-strand break repair. Interacts with the Ku70:Ku80 (CPX-1732) and MRX CPX-1872) complexes.","predictedComplex":false,"interactors":[{"ac":"EBI-23865","identifier":"P53150","identifierLink":"https://www.uniprot.org/uniprotkb/P53150/entry","name":"LIF1","description":"Non-homologous end-joining factor LIF1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-5983","identifier":"Q08387","identifierLink":"https://www.uniprot.org/uniprotkb/Q08387/entry","name":"DNL4","description":"DNA ligase 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45997","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1666","complexName":"MutLalpha endonuclease complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Mn2+-dependent endonuclease which nicks a DNA strand containing a pre-existing nick, presumably to provide an entry site for a mispair excision reaction. Required for DNA mismatch repair (MMR), correcting base-base mismatches and insertion-deletion loops resulting from DNA replication, DNA damage or from recombination events between non-identical sequences during meiosis. ATP binding  induces a conformational change in the MSH2-MSH6 (CPX-1037) and MSH2-MSH3 (CPX-1036) complexes which converts these to a clamp form that slides along the DNA and leads to recruitment of MutLalpha, MutLbeta (CPX-1667) and MLH1-MLH3 (CPX-1668). Plays a major role in maintaining the genetic stability of simple sequence repeats, by suppressing recombination between slightly divergent or homeologous DNA sequences, and in the repair of heteroduplex sites present in meiotic recombination intermediates. The MLH1-PMS1 heterodimer acts as the major Mlh heterodimer in MMR and is thought to coordinate Msh-DNA binding with downstream repair factors.","predictedComplex":false,"interactors":[{"ac":"EBI-11003","identifier":"P38920","identifierLink":"https://www.uniprot.org/uniprotkb/P38920/entry","name":"MLH1","description":"DNA mismatch repair protein MLH1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13561","identifier":"P14242","identifierLink":"https://www.uniprot.org/uniprotkb/P14242/entry","name":"PMS1","description":"DNA mismatch repair protein PMS1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1667","complexName":"MutLbeta endonuclease complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Mn2+-dependent endonuclease which nicks a DNA strand containing a pre-existing nick, presumably to provide an entry site for a mispair excision reaction. Required for DNA mismatch repair (MMR), correcting base-base mismatches and insertion-deletion loops resulting from DNA replication, DNA damage or from recombination events between non-identical sequences during meiosis. ATP binding  induces a conformational change in the MSH2-MSH6 (CPX-1037) and MSH2-MSH3 (CPX-1036) complexes which converts these to a clamp form that slides along the DNA and leads to recruitment of MutLalpha (CPX-1666) , MutLbeta and MLH1-MLH3 (CPX-1668).. This complex has been proposed to be an accessory factor that acts in conjunction with MLH1-PMS1 (CPX-1666) in maintaining the genetic stability of simple sequence repeats, by suppressing recombination between slightly divergent or homeologous DNA sequences, and in the repair of heteroduplex sites present in meiotic recombination intermediates. It may play a role in regulating between different crossover pathways.","predictedComplex":false,"interactors":[{"ac":"EBI-11003","identifier":"P38920","identifierLink":"https://www.uniprot.org/uniprotkb/P38920/entry","name":"MLH1","description":"DNA mismatch repair protein MLH1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-33369","identifier":"Q07980","identifierLink":"https://www.uniprot.org/uniprotkb/Q07980/entry","name":"MLH2","description":"DNA mismatch repair protein MLH2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1668","complexName":"MLH1-MLH3 endonuclease complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Mn2+-dependent endonuclease which nicks a DNA strand containing a pre-existing nick, presumably to provide an entry site for a mispair excision reaction. Required for DNA mismatch repair (MMR), correcting base-base mismatches and insertion-deletion loops resulting from DNA replication, DNA damage or from recombination events between non-identical sequences during meiosis. ATP binding  induces a conformational change in the MSH2-MSH6 (CPX-1037) and MSH2-MSH3 (CPX-1036) complexes which converts these to a clamp form that slides along the DNA and leads to recruitment of MutLalpha  (CPX-1666), MutLbeta (CPX-1667) and MLH1-MLH3. Appears to substitute  in a minor way MutLalpha, for  maintaining the genetic stability of simple sequence repeats, by suppressing recombination between slightly divergent or homeologous DNA sequences, and in the repair of heteroduplex sites present in meiotic recombination intermediates.","predictedComplex":false,"interactors":[{"ac":"EBI-11003","identifier":"P38920","identifierLink":"https://www.uniprot.org/uniprotkb/P38920/entry","name":"MLH1","description":"DNA mismatch repair protein MLH1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31634","identifier":"Q12083","identifierLink":"https://www.uniprot.org/uniprotkb/Q12083/entry","name":"MLH3","description":"DNA mismatch repair protein MLH3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1669","complexName":"RENT complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Regulates transcriptional silencing at the rDNA locus. Silencing within the yeast rDNA repeats inhibits hyperrecombination, represses transcription from foreign promoters, regulates cell cycle progression and extends replicative life span.Interaction with FOB1 is required for the association of the RENT complex with the rDNA non-transcribed spacer region and for silencing at this location.","predictedComplex":false,"interactors":[{"ac":"EBI-17219","identifier":"P06700","identifierLink":"https://www.uniprot.org/uniprotkb/P06700/entry","name":"SIR2","description":"NAD-dependent histone deacetylase SIR2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11085","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25953","identifier":"P47035","identifierLink":"https://www.uniprot.org/uniprotkb/P47035/entry","name":"NET1","description":"Nucleolar protein NET1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28196","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4192","identifier":"Q00684","identifierLink":"https://www.uniprot.org/uniprotkb/Q00684/entry","name":"CDC14","description":"Tyrosine-protein phosphatase CDC14","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23339","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1670","complexName":"MUS81-MMS4 structure-specific endonuclease complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Structure-specific endonuclease that plays an important role in rescuing stalled replication forks and resolving the mitotic recombination intermediates. Has a substrate preference for branched DNA structures with a 5-prime end at the branch nick with cleavage probably occurring approximately half a helical turn upstream of the free 5-prime end. Resolves the four-way Holliday junction (HJ) in which the two recombining DNAs are covalently-linked junctions in crossover formation during meiotic recombination, however, its ability to cut intact HJs was found to be very limited in comparison with other structures, suggesting that a HJ precursor (such as a nicked HJ) might be its preferred DNA substrate. In mitotic cells, the activity of MUS81-MMS4 is low during S-phase, but phosphorylation of the MMS4 leads to complex activation at the onset of mitosis by the collaborative actions of two cell cycle kinases: CDC28 (P00546) and CDC5 (P32562).","predictedComplex":false,"interactors":[{"ac":"EBI-21547","identifier":"P38257","identifierLink":"https://www.uniprot.org/uniprotkb/P38257/entry","name":"MMS4","description":"Crossover junction endonuclease MMS4","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-33508","identifier":"Q04149","identifierLink":"https://www.uniprot.org/uniprotkb/Q04149/entry","name":"MUS81","description":"Crossover junction endonuclease MUS81","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13451","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 3, maxValue: 3","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1671","complexName":"Prefoldin co-chaperone complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Hexameric molecular chaperone complex which interacts with nascent polypeptide chains, binds specifically to cytosolic chaperonin and transfers target proteins to it. Specifically promotes the formation of properly folded and functional alpha- and gamma-tubulin","predictedComplex":false,"interactors":[{"ac":"EBI-13224","identifier":"P46988","identifierLink":"https://www.uniprot.org/uniprotkb/P46988/entry","name":"PFD1","description":"Prefoldin subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR20903","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13239","identifier":"P48363","identifierLink":"https://www.uniprot.org/uniprotkb/P48363/entry","name":"PAC10","description":"Prefoldin subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12409","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13246","identifier":"P53900","identifierLink":"https://www.uniprot.org/uniprotkb/P53900/entry","name":"GIM3","description":"Prefoldin subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21100","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13253","identifier":"Q04493","identifierLink":"https://www.uniprot.org/uniprotkb/Q04493/entry","name":"GIM5","description":"Prefoldin subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12674","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13260","identifier":"P52553","identifierLink":"https://www.uniprot.org/uniprotkb/P52553/entry","name":"YKE2","description":"Prefoldin subunit 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21431","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2342435","identifier":"P40005","identifierLink":"https://www.uniprot.org/uniprotkb/P40005/entry","name":"GIM4","description":"Prefoldin subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13303","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1672","complexName":"alpha-1,6-mannosyltransferase complex, M-Pol I variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Role in the initiation and extension of an alpha -1,6-linked polymannose backbone as a first step in mannan synthesis, a branched polymer attached to the glycans of many of the proteins destined for the cell wall.","predictedComplex":false,"interactors":[{"ac":"EBI-11082","identifier":"P39107","identifierLink":"https://www.uniprot.org/uniprotkb/P39107/entry","name":"MNN9","description":"Mannan polymerase complexes subunit MNN9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20237","identifier":"P23642","identifierLink":"https://www.uniprot.org/uniprotkb/P23642/entry","name":"VAN1","description":"Mannan polymerase I complex VAN1 subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1673","complexName":"Replication fork protection complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for chromosome segregation during meiosis and DNA damage repair. Acts at the intra-S-phase checkpoint pathway to stabilize stalled replication forks by maintaining the replisome at the arrested sites. Coordinates leading and lagging strand synthesis and moves with the replication fork, transfering cohesin from the front of the fork to the newly synthesized DNA. Stabilizes replication forks in a configuration that is recognized by replication checkpoint sensors and protects stalled replication forks against the fork-releasing activity of RRM3 helicase. The complex recruits the checkpoint mediator MRC1 (P25588) to the replisome to perform its checkpoint function.","predictedComplex":false,"interactors":[{"ac":"EBI-28093","identifier":"Q04659","identifierLink":"https://www.uniprot.org/uniprotkb/Q04659/entry","name":"CSM3","description":"Chromosome segregation in meiosis protein 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28257","identifier":"P53840","identifierLink":"https://www.uniprot.org/uniprotkb/P53840/entry","name":"TOF1","description":"Topoisomerase 1-associated factor 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22940","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1674","complexName":"MON1-CCZ1 guanyl-nucleotide exchange factor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Guanyl-nucleotide exchange factor complex required to activate the endosomal GTPase Rab7 required for fusion of multivesicular bodies/late endosomes and of autophagosomes to lysosomes. Maintains proper vacuole morphology in vacuole delivery pathways by regulating fusion of vesicles with the vacuole at the tethering/docking stage. Regulates the SNARE complex during the coordinated priming and docking stages of fusion. May play a role in early-to-late endosome conversion. Mon1 interacts with Rab5 family GTPases and phosphatidylinositol phosphate lipids to recruit the complex to endosomes. For binding to autophagosomes, Ccz1 instead interacts with ATG8 and lipid packing defects.","predictedComplex":false,"interactors":[{"ac":"EBI-21608","identifier":"P38273","identifierLink":"https://www.uniprot.org/uniprotkb/P38273/entry","name":"CCZ1","description":"Vacuolar fusion protein CCZ1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23945","identifier":"P53129","identifierLink":"https://www.uniprot.org/uniprotkb/P53129/entry","name":"MON1","description":"Vacuolar fusion protein MON1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13027","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1675","complexName":"Septin complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A  heterooligomeric complex, formed from GTP-binding proteins, that polymerizes end-to-end into filaments  at the bud neck. Play a role in cytokinesis, assembling early in the cell cycle as a patch at the incipient bud site and forming a ring approximate 15 minutes before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck. The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Septins are also involved in cell morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization and spore wall formation.","predictedComplex":false,"interactors":[{"ac":"EBI-22083","identifier":"Q07657","identifierLink":"https://www.uniprot.org/uniprotkb/Q07657/entry","name":"SHS1","description":"Seventh homolog of septin 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4174","identifier":"P25342","identifierLink":"https://www.uniprot.org/uniprotkb/P25342/entry","name":"CDC10","description":"Cell division control protein 10","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4178","identifier":"P32458","identifierLink":"https://www.uniprot.org/uniprotkb/P32458/entry","name":"CDC11","description":"Cell division control protein 11","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4182","identifier":"P32468","identifierLink":"https://www.uniprot.org/uniprotkb/P32468/entry","name":"CDC12","description":"Cell division control protein 12","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4429","identifier":"P32457","identifierLink":"https://www.uniprot.org/uniprotkb/P32457/entry","name":"CDC3","description":"Cell division control protein 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1676","complexName":"ATG1/ULK1 protein kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Central regulator of autophagy initiation. Essential for recruitment of Atg proteins to the pre-autophagosomal structure, the putative site for autophagosome formation, under starvation condition, resulting in the sequestration of cytoplasmic proteins and organelles for bulk degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-2657","identifier":"P53104","identifierLink":"https://www.uniprot.org/uniprotkb/P53104/entry","name":"ATG1","description":"Serine/threonine-protein kinase ATG1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24348","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30856","identifier":"Q06410","identifierLink":"https://www.uniprot.org/uniprotkb/Q06410/entry","name":"ATG17","description":"Autophagy-related protein 17","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28005","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34768","identifier":"Q12421","identifierLink":"https://www.uniprot.org/uniprotkb/Q12421/entry","name":"ATG31","description":"Autophagy-related protein 31","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-36188","identifier":"Q06628","identifierLink":"https://www.uniprot.org/uniprotkb/Q06628/entry","name":"ATG13","description":"Autophagy-related protein 13","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13430","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-38752","identifier":"Q12092","identifierLink":"https://www.uniprot.org/uniprotkb/Q12092/entry","name":"ATG29","description":"Autophagy-related protein 29","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR40012","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1677","complexName":"Phosphatidylinositol 3-kinase complex II","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes phosphorylation of phosphatidyl inositol, one of the major phospholipids in the cell, specifically at the d-3 position of the inositol ring, to generate PtdIns(3)P. Directs the synthesis of a specific endosomal pool of PtdIns3P, which is required for recruitment/activation of the retromer complex, thereby ensuring efficient endosome-to-Golgi retrograde transport.","predictedComplex":false,"interactors":[{"ac":"EBI-20347","identifier":"P22219","identifierLink":"https://www.uniprot.org/uniprotkb/P22219/entry","name":"VPS15","description":"Serine/threonine-protein kinase VPS15","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR17583","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20405","identifier":"P22543","identifierLink":"https://www.uniprot.org/uniprotkb/P22543/entry","name":"VPS34","description":"Phosphatidylinositol 3-kinase VPS34","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2670","identifier":"Q02948","identifierLink":"https://www.uniprot.org/uniprotkb/Q02948/entry","name":"VPS30","description":"Vacuolar protein sorting-associated protein 30","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12768","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29972","identifier":"Q05919","identifierLink":"https://www.uniprot.org/uniprotkb/Q05919/entry","name":"VPS38","description":"Vacuolar protein sorting-associated protein 38","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15157","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1678","complexName":"TRAMP complex variant 4-1","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Recognises and bind to  pre-ribosomal RNA and snoRNAs leading to their rapid degradation by the nuclear exosome (CPX-599). Adds a short oligo(A) tail to the RNA which is assumed to make it a better substrate for 3'-end degradation. There is evidence that the various TRAMP complexes (CPX-1678, CPX-1679, CPX-1680) exhibit some substrate specificity.","predictedComplex":false,"interactors":[{"ac":"EBI-11592","identifier":"P47047","identifierLink":"https://www.uniprot.org/uniprotkb/P47047/entry","name":"MTR4","description":"ATP-dependent RNA helicase DOB1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19517","identifier":"P53632","identifierLink":"https://www.uniprot.org/uniprotkb/P53632/entry","name":"PAP2","description":"Poly(A) RNA polymerase protein 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2045008","identifier":"P40985","identifierLink":"https://www.uniprot.org/uniprotkb/P40985/entry","name":"HUL4","description":"Probable E3 ubiquitin-protein ligase HUL4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45622","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25083","identifier":"P40507","identifierLink":"https://www.uniprot.org/uniprotkb/P40507/entry","name":"AIR1","description":"Protein AIR1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46543","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1679","complexName":"TRAMP complex variant 4-2","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Recognises and bind to  pre-ribosomal RNA and snoRNAs leading to their rapid degradation by the nuclear exosome (CPX-599). Adds a short oligo(A) tail to the RNA which is assumed to make it a better substrate for 3'-end degradation. There is evidence that the various TRAMP complexes (CPX-1678, CPX-1679, CPX-1680) exhibit some substrate specificity with TRAMP4-2 targetting RNAPII transcripts, particularly mRNA 5' ends, close to the transition start site and also the CUT, SUT, and XUT ncRNAs.","predictedComplex":false,"interactors":[{"ac":"EBI-11592","identifier":"P47047","identifierLink":"https://www.uniprot.org/uniprotkb/P47047/entry","name":"MTR4","description":"ATP-dependent RNA helicase DOB1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19517","identifier":"P53632","identifierLink":"https://www.uniprot.org/uniprotkb/P53632/entry","name":"PAP2","description":"Poly(A) RNA polymerase protein 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2045008","identifier":"P40985","identifierLink":"https://www.uniprot.org/uniprotkb/P40985/entry","name":"HUL4","description":"Probable E3 ubiquitin-protein ligase HUL4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45622","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31475","identifier":"Q12476","identifierLink":"https://www.uniprot.org/uniprotkb/Q12476/entry","name":"AIR2","description":"Protein AIR2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46543","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1680","complexName":"TRAMP complex variant 5-1","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Recognises and bind to pre-ribosomal RNA and snoRNAs leading to their rapid degradation by the nuclear exosome (CPX-599). Adds a short oligo(A) tail to the RNA which is assumed to make it a better substrate for 3'-end degradation.  There is evidence that the various TRAMP complexes (CPX-1678, CPX-1679, CPX-1680) exhibit some substrate specificity with TRAMP5-1 preferentially targeting the ITS1 spacer region of 35S pre-rRNA","predictedComplex":false,"interactors":[{"ac":"EBI-11592","identifier":"P47047","identifierLink":"https://www.uniprot.org/uniprotkb/P47047/entry","name":"MTR4","description":"ATP-dependent RNA helicase DOB1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19525","identifier":"P48561","identifierLink":"https://www.uniprot.org/uniprotkb/P48561/entry","name":"TRF5","description":"Poly(A) RNA polymerase protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25083","identifier":"P40507","identifierLink":"https://www.uniprot.org/uniprotkb/P40507/entry","name":"AIR1","description":"Protein AIR1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46543","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1681","complexName":"Monopolin complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Essential for clamping microtubule binding sites, ensuring orientation of sister kinetochores to the same pole (monopolar kinetochore attachment) during meiosis I.","predictedComplex":false,"interactors":[{"ac":"EBI-22001","identifier":"P25651","identifierLink":"https://www.uniprot.org/uniprotkb/P25651/entry","name":"CSM1","description":"Monopolin complex subunit CSM1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28006","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22643","identifier":"P40065","identifierLink":"https://www.uniprot.org/uniprotkb/P40065/entry","name":"MAM1","description":"Monopolin complex subunit MAM1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-32189","identifier":"Q04087","identifierLink":"https://www.uniprot.org/uniprotkb/Q04087/entry","name":"LRS4","description":"Monopolin complex subunit LRS4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-8536","identifier":"P29295","identifierLink":"https://www.uniprot.org/uniprotkb/P29295/entry","name":"HRR25","description":"Casein kinase I homolog HRR25","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11909","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1682","complexName":"Histone acetyltransferase B","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Acetylates Lys-12 and Lys-5 of non-chromatin-bound histone H4, an essential step in the regulation of chromatin activity and of telomeric silencing.","predictedComplex":false,"interactors":[{"ac":"EBI-31911","identifier":"Q12373","identifierLink":"https://www.uniprot.org/uniprotkb/Q12373/entry","name":"HIF1","description":"HAT1-interacting factor 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-8176","identifier":"Q12341","identifierLink":"https://www.uniprot.org/uniprotkb/Q12341/entry","name":"HAT1","description":"Histone acetyltransferase type B catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12046","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8185","identifier":"P39984","identifierLink":"https://www.uniprot.org/uniprotkb/P39984/entry","name":"HAT2","description":"Histone acetyltransferase type B subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1683","complexName":"DBF2-MOB1 protein kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Serine/threonine proein kinase complex with a role in exit from mitosis during the cell cycle. Once activated, the complex translocates to the nucleus where it phosphorylates an unknown protein to dislodge CDC14 (Q00684) from NET1 (P47035), resulting in diffusion of CDC14 throughout the nucleus. Phosphorylates CDC14 on several sites that flank the C-terminal nuclear localization signal (NLS) sequences, thereby inhibiting the NLS. Because of this, phosphorylated CDC14 molecules that escape to the cytoplasm cannot efficiently return to the nucleus and dephosphorylate substrates such as CDH1 (P53197) and SWI5 (P08153). Phosphorylates chitin synthase CHS2 (P14180) to regulate cytokinesis.","predictedComplex":false,"interactors":[{"ac":"EBI-11119","identifier":"P40484","identifierLink":"https://www.uniprot.org/uniprotkb/P40484/entry","name":"MOB1","description":"DBF2 kinase activator protein MOB1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5569","identifier":"P22204","identifierLink":"https://www.uniprot.org/uniprotkb/P22204/entry","name":"DBF2","description":"Cell cycle protein kinase DBF2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24356","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1684","complexName":"CBK1-MOB2 kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for the final event of cell division, destruction of an extracellular septum that forms between mother and daughter cells during cytokinesis. Plays a role in the RAM pathway which regulates the ACE2 (P21192) transcription factor, which  turns on expression of septum-destroying hydrolases and plays a role in the polarized morphogenesis of bud site selection, bud development, and cell separation. The complex is ctivated by the hippo-like kinase KIC1 (P38692).","predictedComplex":false,"interactors":[{"ac":"EBI-11125","identifier":"P43563","identifierLink":"https://www.uniprot.org/uniprotkb/P43563/entry","name":"MOB2","description":"CBK1 kinase activator protein MOB2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4110","identifier":"P53894","identifierLink":"https://www.uniprot.org/uniprotkb/P53894/entry","name":"CBK1","description":"Serine/threonine-protein kinase CBK1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24356","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1685","complexName":"BUR1-BUR2 kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Implicated in transcription elongation. Phosphorylates the UBC2/RAD6 ubiquitin-conjugating enzyme (E2), leading to monoubiquitination of histone H2B, the localization of the PAF1 complex (CPX-1726) to chromatin, and the silencing of telomeric-associated genes. Also required for histone H3 Lys-4 trimethylation. Recruited to the C-terminal repeat domain of the largest subunit of RNA Pol II, RPB1 (P04050),  phosphorylated on Ser-5 to augment Ser-2 phosphorylation by the carboxy-terminal domain protein kinase complex (CPX-1710) early in the transcription cycle.","predictedComplex":false,"interactors":[{"ac":"EBI-17078","identifier":"P23293","identifierLink":"https://www.uniprot.org/uniprotkb/P23293/entry","name":"SGV1","description":"Serine/threonine-protein kinase BUR1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30948","identifier":"Q05949","identifierLink":"https://www.uniprot.org/uniprotkb/Q05949/entry","name":"BUR2","description":"Protein BUR2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1687","complexName":"Thp1-Sac3 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Functions in transcription-coupled mRNA export from the nucleus to the cytoplasm. Dock export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), by association with components of the nuclear mRNA export machinery (MEX67-MTR2 and SUB2) in the nucleoplasm and the nucleoporin NUP1 at the nuclear basket.","predictedComplex":false,"interactors":[{"ac":"EBI-16425","identifier":"P46674","identifierLink":"https://www.uniprot.org/uniprotkb/P46674/entry","name":"SAC3","description":"Nuclear mRNA export protein SAC3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12436","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32097","identifier":"Q08231","identifierLink":"https://www.uniprot.org/uniprotkb/Q08231/entry","name":"THP1","description":"Nuclear mRNA export protein THP1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12732","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1688","complexName":"PHO80-PHO85 kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Cyclin-dependent protein kinase that negatively regulates the phosphate starvation response by controlling both the localization and activity of the transcription factor PHO4 (P07270). PHO4, in turn, activates transcription of phosphate acquisition genes.","predictedComplex":false,"interactors":[{"ac":"EBI-13310","identifier":"P20052","identifierLink":"https://www.uniprot.org/uniprotkb/P20052/entry","name":"PHO80","description":"PHO85 cyclin PHO80","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13327","identifier":"P17157","identifierLink":"https://www.uniprot.org/uniprotkb/P17157/entry","name":"PHO85","description":"Cyclin-dependent protein kinase PHO85","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1689","complexName":"PCL6-PHO85 kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Cyclin-dependent protein kinase which phosphorylates and inactivates GLC8 (P41818), which then modulates GLC7 type-1 protein phosphatase (P38229), thus controlling glycogen phosphorylase and glycogen synthase activities in response to nutrient availability.","predictedComplex":false,"interactors":[{"ac":"EBI-13327","identifier":"P17157","identifierLink":"https://www.uniprot.org/uniprotkb/P17157/entry","name":"PHO85","description":"Cyclin-dependent protein kinase PHO85","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22555","identifier":"P40038","identifierLink":"https://www.uniprot.org/uniprotkb/P40038/entry","name":"PCL6","description":"PHO85 cyclin-6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1690","complexName":"PCL7-PHO85 kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Cyclin-dependent protein kinase that phosphorylates and inactivates GLC8 (P41818), which then modulates GLC7 type-1 protein phosphatases (P38229), thus controlling glycogen phosphorylase and glycogen synthase activities in response to nutrient availability.","predictedComplex":false,"interactors":[{"ac":"EBI-13327","identifier":"P17157","identifierLink":"https://www.uniprot.org/uniprotkb/P17157/entry","name":"PHO85","description":"Cyclin-dependent protein kinase PHO85","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25021","identifier":"P40186","identifierLink":"https://www.uniprot.org/uniprotkb/P40186/entry","name":"PCL7","description":"PHO85 cyclin-7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1691","complexName":"PCL8-PHO85 kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Cyclin-dependent protein kinase that phosphorylates and inactivates GSY2 (P27472), a regulatory enzyme in glycogen synthesis, thus controlling glycogen synthase activities in response to nutrient availability.","predictedComplex":false,"interactors":[{"ac":"EBI-13327","identifier":"P17157","identifierLink":"https://www.uniprot.org/uniprotkb/P17157/entry","name":"PHO85","description":"Cyclin-dependent protein kinase PHO85","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-37056","identifier":"Q08966","identifierLink":"https://www.uniprot.org/uniprotkb/Q08966/entry","name":"PCL8","description":"PHO85 cyclin-8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1692","complexName":"PCL10-PHO85 kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Cyclin-dependent protein kinase that phosphorylates and inactivates GSY2 (P27472), a regulatory enzyme in glycogen synthesis, thus controlling glycogen synthase activities in response to nutrient availability.","predictedComplex":false,"interactors":[{"ac":"EBI-13327","identifier":"P17157","identifierLink":"https://www.uniprot.org/uniprotkb/P17157/entry","name":"PHO85","description":"Cyclin-dependent protein kinase PHO85","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23973","identifier":"P53124","identifierLink":"https://www.uniprot.org/uniprotkb/P53124/entry","name":"PCL10","description":"PHO85 cyclin-10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1693","complexName":"CLG1-PHO85 kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Cyclin-dependent protein kinase with a role in cell integrity and polarized cell growth. Phosphorylates the chaperone protein SSA1 (P10591), a chaperone that is essential for protection of the cyclin CLN3 (P13365), essential for the control of the cell cycle at the G1/S (start) transition, from the degradation machinery. Acts to positively regulate autophagy through promoting the degradation of SIC1, a negative regulator of autophagy.","predictedComplex":false,"interactors":[{"ac":"EBI-13327","identifier":"P17157","identifierLink":"https://www.uniprot.org/uniprotkb/P17157/entry","name":"PHO85","description":"Cyclin-dependent protein kinase PHO85","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4762","identifier":"P35190","identifierLink":"https://www.uniprot.org/uniprotkb/P35190/entry","name":"CLG1","description":"PHO85 cyclin CLG1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1694","complexName":"PCL2-PHO85 kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Cyclin-dependent protein kinase essential for the control of the cell cycle at the G1/S (start) transition. Phosphorylates RVS167 which functions in actin cytoskeleton regulation and is required for the formation of endocytic vesicles at the plasma membrane. Positively controls degradation of sphingoid long chain base kinase LCB4 (Q12246) by phosphorylation, which is required for its ubiquitination and degradation. LCB4 catalyses the formation of sphingoid long-chain base 1-phosphates which have roles in roles in heat stress resistance, diauxic shift, and Ca2+ mobilization.","predictedComplex":false,"interactors":[{"ac":"EBI-13327","identifier":"P17157","identifierLink":"https://www.uniprot.org/uniprotkb/P17157/entry","name":"PHO85","description":"Cyclin-dependent protein kinase PHO85","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4499","identifier":"P25693","identifierLink":"https://www.uniprot.org/uniprotkb/P25693/entry","name":"PCL2","description":"PHO85 cyclin-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1695","complexName":"PCL1-PHO85 kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Cyclin-dependent protein kinase essential for the control of the cell cycle at the G1/S (start) transition. Positively controls degradation of sphingoid long chain base kinase LCB4 (Q12246) by phosphorylation, which is required for its ubiquitination and degradation. LCB4 catalyses the formation of sphingoid long-chain base 1-phosphates which have roles in roles in heat stress resistance, diauxic shift, and Ca2+ mobilization. Also involved in phosphorylation of the CDK inhibitor (CKI) SIC1 (P38634), which is required for its ubiquitination and degradation, releasing repression of B-type cyclins and promoting exit from mitosis.","predictedComplex":false,"interactors":[{"ac":"EBI-13327","identifier":"P17157","identifierLink":"https://www.uniprot.org/uniprotkb/P17157/entry","name":"PHO85","description":"Cyclin-dependent protein kinase PHO85","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4495","identifier":"P24867","identifierLink":"https://www.uniprot.org/uniprotkb/P24867/entry","name":"PCL1","description":"PHO85 cyclin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1696","complexName":"PCL5-PHO85 kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Cyclin-dependent protein kinase that positively controls degradation of transcription factor GCN4 (P03069) under favorable growth conditions. GCN4 is a master transcriptional regulator of amino acid and vitamin biosynthetic enzymes, whose expression is upregulated in response to amino acid starvation Phosphorylation of GCN4 is required for its degradation by the E3 ubiquitin ligase complex SCF-Cdc4 (CPX-3234). Amino acid starvation reduces PCL5-PHO85-associated GCN4 kinase activity and leads to stabilization of GCN4","predictedComplex":false,"interactors":[{"ac":"EBI-13327","identifier":"P17157","identifierLink":"https://www.uniprot.org/uniprotkb/P17157/entry","name":"PHO85","description":"Cyclin-dependent protein kinase PHO85","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4504","identifier":"P38794","identifierLink":"https://www.uniprot.org/uniprotkb/P38794/entry","name":"PCL5","description":"PHO85 cyclin-5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1697","complexName":"PCL9-PHO85 kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Active in the M/G1 phase of the cell cycle.","predictedComplex":false,"interactors":[{"ac":"EBI-13327","identifier":"P17157","identifierLink":"https://www.uniprot.org/uniprotkb/P17157/entry","name":"PHO85","description":"Cyclin-dependent protein kinase PHO85","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-38090","identifier":"Q12477","identifierLink":"https://www.uniprot.org/uniprotkb/Q12477/entry","name":"PCL9","description":"PHO85 cyclin-9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1698","complexName":"EMP24 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Plays a role in selective transport processes at the ER-Golgi interface by tethering both COPI (CPX-1652) and COPII (CPX-2523) complexes via dilysine motives on EMP24 and ERV25. May initially recruit the deactivated form of ARF1 (P11076), facilitating the formation of a COPI priming complex and subsequently enabling efficient budding. In addition, the ability of p24 proteins to oligomerize and to present multiple coatomer-binding motifs may promote COPI budding by docking coatomer more firmly to the membrane.  Required for the export of glycosylphosphatidylinositol-anchored proteins to the Golgi apparatus through interaction with the SEC23-LST1 COPII cargo recruitment complex (CPX-1341).","predictedComplex":false,"interactors":[{"ac":"EBI-6431","identifier":"P32803","identifierLink":"https://www.uniprot.org/uniprotkb/P32803/entry","name":"EMP24","description":"Endosomal protein P24B","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22811","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6581","identifier":"Q05359","identifierLink":"https://www.uniprot.org/uniprotkb/Q05359/entry","name":"ERP1","description":"Protein ERP1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22811","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6587","identifier":"P39704","identifierLink":"https://www.uniprot.org/uniprotkb/P39704/entry","name":"ERP2","description":"Protein ERP2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22811","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6642","identifier":"P54837","identifierLink":"https://www.uniprot.org/uniprotkb/P54837/entry","name":"ERV25","description":"Endoplasmic reticulum vesicle protein 25","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22811","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1699","complexName":"CLN1-CDC28 kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Cyclin-dependent protein kinase complex required for the control of the cell cycle at the G1/S (start) transition, controlling the trigger of post-Start processes such as spindle pole body duplication, and the initiation of DNA replication. CSK1 is required for activity of CLN-CDC28 complexes. The protein may also play a role in complex stability and substrate recognition.","predictedComplex":false,"interactors":[{"ac":"EBI-4253","identifier":"P00546","identifierLink":"https://www.uniprot.org/uniprotkb/P00546/entry","name":"CDC28","description":"Cyclin-dependent kinase 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4479","identifier":"P20437","identifierLink":"https://www.uniprot.org/uniprotkb/P20437/entry","name":"CLN1","description":"G1/S-specific cyclin CLN1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4746","identifier":"P20486","identifierLink":"https://www.uniprot.org/uniprotkb/P20486/entry","name":"CKS1","description":"Cyclin-dependent kinases regulatory subunit","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23415","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1700","complexName":"CLN3-CDC28 kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Cyclin-dependent protein kinase complex required for the control of the cell cycle at the G1/S (start) transition, controlling the trigger of post-Start processes such as spindle pole body duplication, and the initiation of DNA replication. CSK1 is required for activity of CLN-CDC28 complexes. The protein may also play a role in complex stability and substrate recognition.","predictedComplex":false,"interactors":[{"ac":"EBI-4253","identifier":"P00546","identifierLink":"https://www.uniprot.org/uniprotkb/P00546/entry","name":"CDC28","description":"Cyclin-dependent kinase 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4490","identifier":"P13365","identifierLink":"https://www.uniprot.org/uniprotkb/P13365/entry","name":"CLN3","description":"G1/S-specific cyclin CLN3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4746","identifier":"P20486","identifierLink":"https://www.uniprot.org/uniprotkb/P20486/entry","name":"CKS1","description":"Cyclin-dependent kinases regulatory subunit","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23415","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1701","complexName":"CLB2-CDC28 kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Cyclin-dependent protein kinase complex required for the control of the cell cycle at the G2/M (mitosis) transition. Mitotic cyclin-CDKs (M-CDKs) regulate accurate chromosome segregation through mitosis. Also plays a role in enhancing double-stranded DNA damage response and repair by targeting the chromatin remodeling factor Fun30.","predictedComplex":false,"interactors":[{"ac":"EBI-4253","identifier":"P00546","identifierLink":"https://www.uniprot.org/uniprotkb/P00546/entry","name":"CDC28","description":"Cyclin-dependent kinase 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4515","identifier":"P24869","identifierLink":"https://www.uniprot.org/uniprotkb/P24869/entry","name":"CLB2","description":"G2/mitotic-specific cyclin-2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1702","complexName":"CLB5-CDC28 kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Cyclin-dependent protein kinase complex required for the control of the cell cycle during S-phase where it is required to activate DNA replication. Essential for initiation of meiotic recombination because it phosphorylates Ser-30 of MER2, a meiosis-specific double-strand break (DSB) protein, which primes Mer2 for subsequent phosphorylation by DDK on Ser29, creating a negatively charged patch necessary for DSB formation. Also plays a role in enhancing DNA damage response and repair by targeting the chromatin remodeling factor Fun30.","predictedComplex":false,"interactors":[{"ac":"EBI-4253","identifier":"P00546","identifierLink":"https://www.uniprot.org/uniprotkb/P00546/entry","name":"CDC28","description":"Cyclin-dependent kinase 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4538","identifier":"P30283","identifierLink":"https://www.uniprot.org/uniprotkb/P30283/entry","name":"CLB5","description":"S-phase entry cyclin-5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1703","complexName":"Prohibitin complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Chaperone which functions to protect the cell from imbalances in the production of mitochondrial proteins by stabilizing newly synthesised mitochondrial-encoded proteins. Prohibitin-deficient cells have a reduced replicative lifespan, associated with mitochondrial decline and display morphological changes of aging.","predictedComplex":false,"interactors":[{"ac":"EBI-13360","identifier":"P40961","identifierLink":"https://www.uniprot.org/uniprotkb/P40961/entry","name":"PHB1","description":"Prohibitin-1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23530","identifier":"P50085","identifierLink":"https://www.uniprot.org/uniprotkb/P50085/entry","name":"PHB2","description":"Prohibitin-2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1704","complexName":"MutSgamma meiotic recombination complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Binds to double Holliday Junctions and other DNA repair intermediates. Binding physically entraps at least one, and possibly two, duplexes of double-stranded DNA, thereby stabilising the recombination intermediate.","predictedComplex":false,"interactors":[{"ac":"EBI-11371","identifier":"P40965","identifierLink":"https://www.uniprot.org/uniprotkb/P40965/entry","name":"MSH4","description":"MutS protein homolog 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11361","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11377","identifier":"Q12175","identifierLink":"https://www.uniprot.org/uniprotkb/Q12175/entry","name":"MSH5","description":"MutS protein homolog 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11361","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1705","complexName":"BUD14-GLC7 phosphatase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Protein phosphatase complex which is important for bud site selection. Regulates microtubule dynamics at the cortex by acting as a specific activator of the dynein complex at the bud cortex. May also play a role in the regulation of transcription by the CCR4-NOT complex (CPX-1800) by phosphorylating and modifying the activity of the MSN2 transcription factor (P33748).","predictedComplex":false,"interactors":[{"ac":"EBI-13715","identifier":"P32598","identifierLink":"https://www.uniprot.org/uniprotkb/P32598/entry","name":"GLC7","description":"Serine/threonine-protein phosphatase PP1-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11668","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-20747","identifier":"P27637","identifierLink":"https://www.uniprot.org/uniprotkb/P27637/entry","name":"BUD14","description":"Bud site selection protein 14","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47775","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1706","complexName":"Acyl-CoA ceramide synthase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Synthesizes ceramide from the reaction of a C26 fatty acyl-CoA with a sphingoid base, thus controlling cell growth, and mediating different cellular events, such as apoptosis, growth arrest, endocytosis and stress response.","predictedComplex":false,"interactors":[{"ac":"EBI-10035","identifier":"P38703","identifierLink":"https://www.uniprot.org/uniprotkb/P38703/entry","name":"LAG1","description":"Ceramide synthase LAG1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12560","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26585","identifier":"P28496","identifierLink":"https://www.uniprot.org/uniprotkb/P28496/entry","name":"LAC1","description":"Ceramide synthase LAC1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12560","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27640","identifier":"Q03579","identifierLink":"https://www.uniprot.org/uniprotkb/Q03579/entry","name":"LIP1","description":"Ceramide synthase subunit LIP1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1707","complexName":"Ornithine carbamoyltransferase arginase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Complex in which the activity of ornithine carbamoyltransferase (OTCase) is inhibited whereas arginase remains catalytically active thus preventing the recycling of ornithine produced by arginase by OTCase - an example of  epiarginase control. Complex forms in the presence of ornithine and arginine.","predictedComplex":false,"interactors":[{"ac":"EBI-12712","identifier":"P05150","identifierLink":"https://www.uniprot.org/uniprotkb/P05150/entry","name":"ARG3","description":"Ornithine carbamoyltransferase","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 6, maxValue: 6","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2856","identifier":"P00812","identifierLink":"https://www.uniprot.org/uniprotkb/P00812/entry","name":"CAR1","description":"Arginase","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43782","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1708","complexName":"Nucleotide-excision repair factor 1 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Role in nucleotide-excision repair; possesses DNA damage recognition and endodeoxynuclease activities.","predictedComplex":false,"interactors":[{"ac":"EBI-14637","identifier":"P06838","identifierLink":"https://www.uniprot.org/uniprotkb/P06838/entry","name":"RAD10","description":"DNA repair protein RAD10","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-14641","identifier":"P28519","identifierLink":"https://www.uniprot.org/uniprotkb/P28519/entry","name":"RAD14","description":"DNA repair protein RAD14","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10142","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14752","identifier":"P06777","identifierLink":"https://www.uniprot.org/uniprotkb/P06777/entry","name":"RAD1","description":"DNA repair protein RAD1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10150","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1709","complexName":"Nucleotide excision repair factor 4 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"An ATP-dependent damage recognition factor required for repair of damaged, nontranscribed DNA, in a process whereby DNA is incised on both sides of the lesion, resulting in the removal of a fragment approximately 25-30 nucleotides long. Locates damage on the non-transcribed strand and in transcriptionally inactive regions of the genome, with ABF1 binding to specific sites increasing the efficiency of the repair process. RAD16 appears to generate superhelical torsion in the DNA in one direction originating from the ABF1-binding site and may remodel chromatin to generate the space for DNA repair synthesis. Subsequent to binding the DNA lesion, the NEF4 complex may serve as a nucleation site for the assembly of the other repair components for dual incision to occur.","predictedComplex":false,"interactors":[{"ac":"EBI-14645","identifier":"P31244","identifierLink":"https://www.uniprot.org/uniprotkb/P31244/entry","name":"RAD16","description":"DNA repair protein RAD16","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45626","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14780","identifier":"P06779","identifierLink":"https://www.uniprot.org/uniprotkb/P06779/entry","name":"RAD7","description":"DNA repair protein RAD7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13382","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3410","identifier":"P14164","identifierLink":"https://www.uniprot.org/uniprotkb/P14164/entry","name":"ABF1","description":"ARS-binding factor 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1710","complexName":"Carboxy-terminal domain protein kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Cyclin-dependent protein that phosphorylates RNA polymerase II (RNAPII, CPX-2662) on the carboxyl-terminal repeat domain (CTD) of its largest subunit RPB1 (P04050), which is important for efficient transcription elongation, mRNA 3′-end processing, and transcription termination of small noncoding RNAs. Also plays a role in RNA polymerase I (RNAPI, CPX-1664) transcription. Increases the correct decoding of mRNA during translation elongation by phosphorylating residue Ser-238 of RPS2 (P25443), a protein of the small ribosomal subunit (CPX-1599). Directs the association of SET2 (P46995) to RNAP II, which results in the establishment of H3K36 methylation and deacetylated chromatin in the bodies of genes. Also regulates SET1-mediated H3K4 methylation which marks the 5′ end of transcribed genes, promoting association of chromatin-remodeling and histone-modifying enzymes.","predictedComplex":false,"interactors":[{"ac":"EBI-5230","identifier":"Q03957","identifierLink":"https://www.uniprot.org/uniprotkb/Q03957/entry","name":"CTK1","description":"CTD kinase subunit alpha","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5236","identifier":"P46962","identifierLink":"https://www.uniprot.org/uniprotkb/P46962/entry","name":"CTK2","description":"CTD kinase subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5241","identifier":"P46963","identifierLink":"https://www.uniprot.org/uniprotkb/P46963/entry","name":"CTK3","description":"CTD kinase subunit gamma","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28291","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1711","complexName":"RIX1 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for 3-prime maturation of the 5.8 S rRNA, a late pre-rRNA processing step. May also play an essential role in ATP-dependent maturation and nuclear export of nascent 60S subunits from the nucleoplasm to the cytoplasm.","predictedComplex":false,"interactors":[{"ac":"EBI-24606","identifier":"P38803","identifierLink":"https://www.uniprot.org/uniprotkb/P38803/entry","name":"IPI1","description":"Pre-rRNA-processing protein IPI1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR16056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-24899","identifier":"P38883","identifierLink":"https://www.uniprot.org/uniprotkb/P38883/entry","name":"RIX1","description":"Pre-rRNA-processing protein RIX1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR34105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29063","identifier":"P53877","identifierLink":"https://www.uniprot.org/uniprotkb/P53877/entry","name":"IPI3","description":"Pre-rRNA-processing protein IPI3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR18763","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1712","complexName":"Gin4 serine/threonine kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Serine/threonine kinase complex that assembles when cells enter mitosis. The associated GIN4 molecules present in this complex phosphorylate each other, leading to GIN4 hyperphosphorylation and activation. This mechanism appears to ensure GIN4 is only activated during mitosis. GIN4 is involved in septin ring formation during mitosis.","predictedComplex":false,"interactors":[{"ac":"EBI-11850","identifier":"P25293","identifierLink":"https://www.uniprot.org/uniprotkb/P25293/entry","name":"NAP1","description":"Nucleosome assembly protein","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11875","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22083","identifier":"Q07657","identifierLink":"https://www.uniprot.org/uniprotkb/Q07657/entry","name":"SHS1","description":"Seventh homolog of septin 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28997","identifier":"P53890","identifierLink":"https://www.uniprot.org/uniprotkb/P53890/entry","name":"BNI5","description":"Bud neck protein 5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-4174","identifier":"P25342","identifierLink":"https://www.uniprot.org/uniprotkb/P25342/entry","name":"CDC10","description":"Cell division control protein 10","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4178","identifier":"P32458","identifierLink":"https://www.uniprot.org/uniprotkb/P32458/entry","name":"CDC11","description":"Cell division control protein 11","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4182","identifier":"P32468","identifierLink":"https://www.uniprot.org/uniprotkb/P32468/entry","name":"CDC12","description":"Cell division control protein 12","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4429","identifier":"P32457","identifierLink":"https://www.uniprot.org/uniprotkb/P32457/entry","name":"CDC3","description":"Cell division control protein 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7595","identifier":"Q12263","identifierLink":"https://www.uniprot.org/uniprotkb/Q12263/entry","name":"GIN4","description":"Serine/threonine-protein kinase GIN4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1713","complexName":"Collagen type II trimer","organismName":"Homo sapiens; 9606","description":"The major component of cartilage.","predictedComplex":false,"interactors":[{"ac":"EBI-2431412","identifier":"P02458","identifierLink":"https://www.uniprot.org/uniprotkb/P02458/entry","name":"COL2A1","description":"Collagen alpha-1(II) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2957","complexName":"Collagen type II trimer","organismName":"Mus musculus; 10090","description":"The major component of cartilage.","predictedComplex":false,"interactors":[{"ac":"EBI-738477","identifier":"P28481","identifierLink":"https://www.uniprot.org/uniprotkb/P28481/entry","name":"Col2a1","description":"Collagen alpha-1(II) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3105","complexName":"Collagen type II trimer","organismName":"Bos taurus; 9913","description":"The major component of cartilage.","predictedComplex":false,"interactors":[{"ac":"EBI-5281315","identifier":"P02459","identifierLink":"https://www.uniprot.org/uniprotkb/P02459/entry","name":"COL2A1","description":"Collagen alpha-1(II) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1714","complexName":"Collagen type III trimer","organismName":"Homo sapiens; 9606","description":"Occurs in most soft connective tissues. Bonded to type I collagen (CPX-1650) by covalent lysine-derived cross-links.","predictedComplex":false,"interactors":[{"ac":"EBI-2431491","identifier":"P02461","identifierLink":"https://www.uniprot.org/uniprotkb/P02461/entry","name":"COL3A1","description":"Collagen alpha-1(III) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2958","complexName":"Collagen type III trimer","organismName":"Mus musculus; 10090","description":"Occurs in most soft connective tissues. Bonded to type I collagen (CPX-2956) by covalent lysine-derived cross-links.","predictedComplex":false,"interactors":[{"ac":"EBI-6856893","identifier":"P08121","identifierLink":"https://www.uniprot.org/uniprotkb/P08121/entry","name":"Col3a1","description":"Collagen alpha-1(III) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3106","complexName":"Collagen type III trimer","organismName":"Bos taurus; 9913","description":"Occurs in most soft connective tissues. Bonded to type I collagen (CPX-3101) by covalent lysine-derived cross-links.","predictedComplex":false,"interactors":[{"ac":"EBI-9630749","identifier":"P04258","identifierLink":"https://www.uniprot.org/uniprotkb/P04258/entry","name":"COL3A1","description":"Collagen alpha-1(III) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR24637","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1715","complexName":"TORC1 serine/threonine-protein kinase complex, TOR1 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Serine/threonine-protein kinase signalling complex which senses diverse inputs, such as nitrogen- and carbon-containing nutrients, hormonal stimulation, various stresses, availability of energy within the cell and oxygen and mediates temporal control of cell growth via regulation of translation, transcription, ribosome biogenesis, nutrient transport, and autophagy. Coordinates cell size by regulating timing of G1-S cell cycle progression by mediating G1 cyclin/CDK activation as well as through destabilization of the SIC1 (P38634) CDK inhibitor.","predictedComplex":false,"interactors":[{"ac":"EBI-19374","identifier":"P35169","identifierLink":"https://www.uniprot.org/uniprotkb/P35169/entry","name":"TOR1","description":"Serine/threonine-protein kinase TOR1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-24864","identifier":"P38873","identifierLink":"https://www.uniprot.org/uniprotkb/P38873/entry","name":"KOG1","description":"Target of rapamycin complex 1 subunit KOG1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12848","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28598","identifier":"P41318","identifierLink":"https://www.uniprot.org/uniprotkb/P41318/entry","name":"LST8","description":"Target of rapamycin complex subunit LST8","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-37395","identifier":"Q08921","identifierLink":"https://www.uniprot.org/uniprotkb/Q08921/entry","name":"TCO89","description":"Target of rapamycin complex 1 subunit TCO89","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22794","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1716","complexName":"TORC1 serine/threonine-protein kinase complex, TOR2 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Serine/threonine-protein kinase signalling complex which senses diverse inputs, such as nitrogen- and carbon-containing nutrients, hormonal stimulation, various stresses, availability of energy within the cell and oxygen and mediates temporal control of cell growth via regulation of translation, transcription, ribosome biogenesis, nutrient transport, and autophagy. Coordinates cell size by regulating timing of G1-S cell cycle progression by mediating G1 cyclin/CDK activation as well as through destabilization of the SIC1 (P38634) CDK inhibitor.","predictedComplex":false,"interactors":[{"ac":"EBI-19385","identifier":"P32600","identifierLink":"https://www.uniprot.org/uniprotkb/P32600/entry","name":"TOR2","description":"Serine/threonine-protein kinase TOR2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-24864","identifier":"P38873","identifierLink":"https://www.uniprot.org/uniprotkb/P38873/entry","name":"KOG1","description":"Target of rapamycin complex 1 subunit KOG1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12848","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28598","identifier":"P41318","identifierLink":"https://www.uniprot.org/uniprotkb/P41318/entry","name":"LST8","description":"Target of rapamycin complex subunit LST8","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-37395","identifier":"Q08921","identifierLink":"https://www.uniprot.org/uniprotkb/Q08921/entry","name":"TCO89","description":"Target of rapamycin complex 1 subunit TCO89","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22794","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1717","complexName":"TORC2 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Serine/threonine-protein kinase signalling complex required for responses to starvation and stress conditions. Required for cytokinetic actomyosin ring (CAR) morphology and constriction, controls polarity of the actin cytoskeleton, and.regulates the timing and fidelity of cytokinesis.","predictedComplex":false,"interactors":[{"ac":"EBI-19385","identifier":"P32600","identifierLink":"https://www.uniprot.org/uniprotkb/P32600/entry","name":"TOR2","description":"Serine/threonine-protein kinase TOR2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22621","identifier":"P40061","identifierLink":"https://www.uniprot.org/uniprotkb/P40061/entry","name":"TSC11","description":"Target of rapamycin complex 2 subunit TSC11","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13298","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25889","identifier":"P47041","identifierLink":"https://www.uniprot.org/uniprotkb/P47041/entry","name":"BIT61","description":"Target of rapamycin complex 2 subunit BIT61","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR32428","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28131","identifier":"Q04749","identifierLink":"https://www.uniprot.org/uniprotkb/Q04749/entry","name":"AVO2","description":"Target of rapamycin complex 2 subunit AVO2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24161","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28598","identifier":"P41318","identifierLink":"https://www.uniprot.org/uniprotkb/P41318/entry","name":"LST8","description":"Target of rapamycin complex subunit LST8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29284","identifier":"Q08236","identifierLink":"https://www.uniprot.org/uniprotkb/Q08236/entry","name":"AVO1","description":"Target of rapamycin complex 2 subunit AVO1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13335","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1718","complexName":"GARP tethering complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Tethering complex required for retrograde traffic from both the early and late endosomes to the Golgi during vesicle trafficking,sorting cargo for recycling to the plasma membrane or degradation in vacuoles. Links the vesicle through the SNARE proteins such as TGL1 (Q03322) to the Golgi, leading to membrane fusion between late Golgi and endosomal vesicles.  Required for the recycling of amino-phospholipid flippases and cell wall synthesis proteins, thus playing a role in lipid homeostasis. Essential role in meiotic progression and spore formation.","predictedComplex":false,"interactors":[{"ac":"EBI-16418","identifier":"P39904","identifierLink":"https://www.uniprot.org/uniprotkb/P39904/entry","name":"VPS52","description":"Vacuolar protein sorting-associated protein 52","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14190","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25828","identifier":"P47061","identifierLink":"https://www.uniprot.org/uniprotkb/P47061/entry","name":"VPS53","description":"Vacuolar protein sorting-associated protein 53","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12820","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26352","identifier":"P36116","identifierLink":"https://www.uniprot.org/uniprotkb/P36116/entry","name":"VPS51","description":"Vacuolar protein sorting-associated protein 51","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-36751","identifier":"Q12071","identifierLink":"https://www.uniprot.org/uniprotkb/Q12071/entry","name":"VPS54","description":"Vacuolar protein sorting-associated protein 54","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12965","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1719","complexName":"Exomer complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Cargo adaptor complex that mediates the trafficking of certain cargoes from the trans-Golgi network/early endosomes to the plasma membrane. Forms a coat structure on vesicles involved in exocytosis of specific cargo proteins, including chitin synthase CHS3 (P29465), from the trans-Golgi network to the cell surface. Recruited by GTP-bound ARF1 (P11076).","predictedComplex":false,"interactors":[{"ac":"EBI-26374","identifier":"P36122","identifierLink":"https://www.uniprot.org/uniprotkb/P36122/entry","name":"BCH2","description":"Protein BCH2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31975","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27508","identifier":"Q05029","identifierLink":"https://www.uniprot.org/uniprotkb/Q05029/entry","name":"BCH1","description":"Protein BCH1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31975","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32770","identifier":"Q08754","identifierLink":"https://www.uniprot.org/uniprotkb/Q08754/entry","name":"BUD7","description":"Bud site selection protein 7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31975","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4640","identifier":"Q12114","identifierLink":"https://www.uniprot.org/uniprotkb/Q12114/entry","name":"CHS5","description":"Chitin biosynthesis protein CHS5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4649","identifier":"P40955","identifierLink":"https://www.uniprot.org/uniprotkb/P40955/entry","name":"CHS6","description":"Chitin biosynthesis protein CHS6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31975","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1720","complexName":"RNase H2 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Specifically degrades the RNA species of RNA:DNA duplexes and removal of ribonucleotides misincorporated in genomic DNA, thus, preventing genomic instability and the accumulation of aberrant nucleic acid. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication.","predictedComplex":false,"interactors":[{"ac":"EBI-15663","identifier":"P53942","identifierLink":"https://www.uniprot.org/uniprotkb/P53942/entry","name":"RNH201","description":"Ribonuclease H2 subunit A","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10954","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-33805","identifier":"Q12338","identifierLink":"https://www.uniprot.org/uniprotkb/Q12338/entry","name":"RNH203","description":"Ribonuclease H2 subunit C","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-33940","identifier":"Q05635","identifierLink":"https://www.uniprot.org/uniprotkb/Q05635/entry","name":"RNH202","description":"Ribonuclease H2 subunit B","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1721","complexName":"Mitochondrial respiratory chain complex IV, COX5A variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Key role in aerobic respiration, in which mitochondrial enzymes accept electrons from electron carriers reduced in glycolysis and the tricarboxylic acid cycle. A complex metalloprotein that transfers electrons from reduced cytochrome c to molecular oxygen and conserves the free energy released in this exergonic reaction by maintaining a transmembrane proton gradient which is utilized to drive the synthesis of ATP or ion transport across the membrane. The four protons consumed in the reduction of one oxygen molecule to water are taken from the mitochondrial matrix and, coupled to this reaction, four additional protons are translocated from the matrix to the intermembrane space.","predictedComplex":false,"interactors":[{"ac":"EBI-12592690","identifier":"CHEBI:23378","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:23378","name":"copper cation","description":"copper cation","stochiometry":"minValue: 3, maxValue: 3","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2050505","identifier":"P10174","identifierLink":"https://www.uniprot.org/uniprotkb/P10174/entry","name":"COX7","description":"Cytochrome c oxidase subunit 7, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-2435921","identifier":"P00401","identifierLink":"https://www.uniprot.org/uniprotkb/P00401/entry","name":"COX1","description":"Cytochrome c oxidase subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 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559292","xrefs":[]},{"ac":"EBI-2435975","identifier":"P00424-PRO_0000006097","identifierLink":"https://www.uniprot.org/uniprotkb/P00424-PRO_0000006097/entry","name":"COX5A","description":"Cytochrome c oxidase subunit 5A, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-2435978","identifier":"P00427-PRO_0000006108","identifierLink":"https://www.uniprot.org/uniprotkb/P00427-PRO_0000006108/entry","name":"COX6","description":"Cytochrome c oxidase subunit 6, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-2435983","identifier":"P32799-PRO_0000006127","identifierLink":"https://www.uniprot.org/uniprotkb/P32799-PRO_0000006127/entry","name":"COX13","description":"Cytochrome c oxidase subunit 13, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 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A complex metalloprotein that transfers electrons from reduced cytochrome c to molecular oxygen and conserves the free energy released in this exergonic reaction by maintaining a transmembrane proton gradient which is utilized to drive the synthesis of ATP or ion transport across the membrane. The four protons consumed in the reduction of one oxygen molecule to water are taken from the mitochondrial matrix and, coupled to this reaction, four additional protons are translocated from the matrix to the intermembrane space. This variant contains subunit 5B, in place of 5a, expression of which is switched on when the O2 concentration drops below a threshold of 0.5 uM O2, and results in a cytochrome-c oxidase which has a higher turnover rate for nitric oxide production. This thought to be a positive feedback mechanism in which mitochondrially produced nitric oxide induces expression of COX5b, whose protein product then functions to enhance the ability of Cytochrome c to produce nitric oxide in hypoxic/anoxic cells.","predictedComplex":false,"interactors":[{"ac":"EBI-12592690","identifier":"CHEBI:23378","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:23378","name":"copper cation","description":"copper cation","stochiometry":"minValue: 3, maxValue: 3","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2050505","identifier":"P10174","identifierLink":"https://www.uniprot.org/uniprotkb/P10174/entry","name":"COX7","description":"Cytochrome c oxidase subunit 7, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-2435921","identifier":"P00401","identifierLink":"https://www.uniprot.org/uniprotkb/P00401/entry","name":"COX1","description":"Cytochrome c oxidase subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 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559292","xrefs":[]},{"ac":"EBI-2435994","identifier":"P04039-PRO_0000006173","identifierLink":"https://www.uniprot.org/uniprotkb/P04039-PRO_0000006173/entry","name":"COX8","description":"Cytochrome c oxidase subunit 8, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-2436493","identifier":"P00425-PRO_0000006098","identifierLink":"https://www.uniprot.org/uniprotkb/P00425-PRO_0000006098/entry","name":"COX5B","description":"Cytochrome c oxidase subunit 5B, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-5078","identifier":"Q01519","identifierLink":"https://www.uniprot.org/uniprotkb/Q01519/entry","name":"COX12","description":"Cytochrome c oxidase subunit 12, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 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9913","xrefs":[{"identifier":"PTHR14619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1724","complexName":"Collagen type IV trimer variant 2","organismName":"Homo sapiens; 9606","description":"Basement membranes are formed by a fine network of collagen IV fibres  that are laced together and entrap large associated molecules.","predictedComplex":false,"interactors":[{"ac":"EBI-2432407","identifier":"Q14031","identifierLink":"https://www.uniprot.org/uniprotkb/Q14031/entry","name":"COL4A6","description":"Collagen alpha-6(IV) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-726908","identifier":"P29400","identifierLink":"https://www.uniprot.org/uniprotkb/P29400/entry","name":"COL4A5","description":"Collagen alpha-5(IV) chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2960","complexName":"Collagen type IV trimer variant 2","organismName":"Mus musculus; 10090","description":"Basement membranes are formed by a fine network of collagen IV fibres  that are laced together and entrap large associated molecules.","predictedComplex":false,"interactors":[{"ac":"EBI-9213088","identifier":"Q63ZW6","identifierLink":"https://www.uniprot.org/uniprotkb/Q63ZW6/entry","name":"Col4a5","description":null,"stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9213105","identifier":"B1AVK5","identifierLink":"https://www.uniprot.org/uniprotkb/B1AVK5/entry","name":"Col4a6","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 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This assembly process requires lateral interactions between triple helices at two levels. In the short N-terminal triple-helical 7S domain, four  triple helical domains from four different molecules assemble head to tail to form the structure known as a spider whose legs are made of a long triple helical region made of several triple helical domains interrupted by short nontriple helical sequences. In the tissue the molecules interact laterally by this region in a staggered fashion. Finally, interactions of nontriple helical COOH-terminal NC1 domains (IPR001442) to form dimers are responsible for tail-to-tail binding of type IV  molecules.","predictedComplex":false,"interactors":[{"ac":"EBI-9213088","identifier":"Q63ZW6","identifierLink":"https://www.uniprot.org/uniprotkb/Q63ZW6/entry","name":"Col4a5","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9213137","identifier":"Q9QZS0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9QZS0/entry","name":"Col4a3","description":"Collagen alpha-3(IV) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9213160","identifier":"Q9QZR9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9QZR9/entry","name":"Col4a4","description":"Collagen alpha-4(IV) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1726","complexName":"PAF1 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A multifunctional complex involved in  many aspects of RNA polymerase II (Pol II) transcriptional regulation, including transcriptional elongation, 3'-terminal end processing, and histone modification. Role in 3'-end formation of mRNAs, required for the recruitment of cleavage and polyadenylation factors CFT1 and PCF11 to RNA polymerase II. Required for activation of the RAD6/UBC2-BRE1 ubiquitin ligase complex, which ubiquitinates histone H2B to form H2BK123ub1. Also required for the methylation of histone H3 by the COMPASS complex (CPX-1039) to form H3K4me, by SET2 to form H3K36me, and by DOT1 to form H3K79me.","predictedComplex":false,"interactors":[{"ac":"EBI-10108","identifier":"P38439","identifierLink":"https://www.uniprot.org/uniprotkb/P38439/entry","name":"LEO1","description":"RNA polymerase-associated protein LEO1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23146","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12855","identifier":"P38351","identifierLink":"https://www.uniprot.org/uniprotkb/P38351/entry","name":"PAF1","description":"RNA polymerase II-associated protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23188","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16303","identifier":"P53064","identifierLink":"https://www.uniprot.org/uniprotkb/P53064/entry","name":"RTF1","description":"RNA polymerase-associated protein RTF1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29913","identifier":"Q06697","identifierLink":"https://www.uniprot.org/uniprotkb/Q06697/entry","name":"CDC73","description":"Cell division control protein 73","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12466","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5283","identifier":"P89105","identifierLink":"https://www.uniprot.org/uniprotkb/P89105/entry","name":"CTR9","description":"RNA polymerase-associated protein CTR9","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14027","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1727","complexName":"Collagen type V trimer variant 1","organismName":"Homo sapiens; 9606","description":"Form the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite.","predictedComplex":false,"interactors":[{"ac":"EBI-2464511","identifier":"P20908","identifierLink":"https://www.uniprot.org/uniprotkb/P20908/entry","name":"COL5A1","description":"Collagen alpha-1(V) chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2464544","identifier":"P05997","identifierLink":"https://www.uniprot.org/uniprotkb/P05997/entry","name":"COL5A2","description":"Collagen alpha-2(V) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2962","complexName":"Collagen type V trimer variant 1","organismName":"Mus musculus; 10090","description":"Form the fibrils of tendon, ligaments and bones, also present in skin. 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In bones the fibrils are mineralized with calcium hydroxyapatite.","predictedComplex":false,"interactors":[{"ac":"EBI-738337","identifier":"Q9JLI2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JLI2/entry","name":"Col5a3","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-762024","identifier":"O88207","identifierLink":"https://www.uniprot.org/uniprotkb/O88207/entry","name":"Col5a1","description":"Collagen alpha-1(V) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9213185","identifier":"Q3U962","identifierLink":"https://www.uniprot.org/uniprotkb/Q3U962/entry","name":"Col5a2","description":"Collagen alpha-2(V) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1729","complexName":"Collagen type V trimer variant 3","organismName":"Homo sapiens; 9606","description":"Form the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite.","predictedComplex":false,"interactors":[{"ac":"EBI-2464511","identifier":"P20908","identifierLink":"https://www.uniprot.org/uniprotkb/P20908/entry","name":"COL5A1","description":"Collagen alpha-1(V) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2964","complexName":"Collagen type V trimer variant 3","organismName":"Mus musculus; 10090","description":"Form the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite.","predictedComplex":false,"interactors":[{"ac":"EBI-762024","identifier":"O88207","identifierLink":"https://www.uniprot.org/uniprotkb/O88207/entry","name":"Col5a1","description":"Collagen alpha-1(V) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1730","complexName":"Peroxisomal ABC transporter complex PXA1-PXA2","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Peroxisomal ABC transporter involved in transmembrane transport of long chain fatty acids, most likely in their CoA ester form, into the peroxisomal matrix prior to beta-oxidation. Very long chain acyl-CoA esters are hydrolyzed by the PXA1-PXA2 complex prior to the transport of their fatty acid portion into the peroxisomes with the CoA being released into the cytoplasm.","predictedComplex":false,"interactors":[{"ac":"EBI-14344","identifier":"P41909","identifierLink":"https://www.uniprot.org/uniprotkb/P41909/entry","name":"PXA1","description":"Peroxisomal long-chain fatty acid import protein 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11384","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2464632","identifier":"P34230","identifierLink":"https://www.uniprot.org/uniprotkb/P34230/entry","name":"PXA2","description":"Peroxisomal long-chain fatty acid import protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11384","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1731","complexName":"DNA replication factor C complex, CTF18 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"DNA-dependent ATPase clamp-loader/unloader complex required for efficient establishment of chromosome cohesion during S-phase and may load or unload POL30/PCNA. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA.","predictedComplex":false,"interactors":[{"ac":"EBI-14992","identifier":"P40348","identifierLink":"https://www.uniprot.org/uniprotkb/P40348/entry","name":"RFC2","description":"Replication factor C subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15000","identifier":"P38629","identifierLink":"https://www.uniprot.org/uniprotkb/P38629/entry","name":"RFC3","description":"Replication factor C subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15009","identifier":"P40339","identifierLink":"https://www.uniprot.org/uniprotkb/P40339/entry","name":"RFC4","description":"Replication factor C subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15016","identifier":"P38251","identifierLink":"https://www.uniprot.org/uniprotkb/P38251/entry","name":"RFC5","description":"Replication factor C subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4560","identifier":"P49956","identifierLink":"https://www.uniprot.org/uniprotkb/P49956/entry","name":"CTF18","description":"Chromosome transmission fidelity protein 18","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23389","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5216","identifier":"P38877","identifierLink":"https://www.uniprot.org/uniprotkb/P38877/entry","name":"CTF8","description":"Chromosome transmission fidelity protein 8","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-5661","identifier":"P25559","identifierLink":"https://www.uniprot.org/uniprotkb/P25559/entry","name":"DCC1","description":"Sister chromatid cohesion protein DCC1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13395","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1732","complexName":"Ku70:Ku80 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Single-stranded DNA-dependent 3-prime to 5-prime ATP-dependent helicase complex which binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. Required for non-homologous end joining DNA double stranded break repair. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Appears to have a role in recruitment of telomerase and CDC13 to the telomere and the subsequent telomere elongation. Required also for telomere recombination to repair telomeric ends in the absence of telomerase.","predictedComplex":false,"interactors":[{"ac":"EBI-8214","identifier":"P32807","identifierLink":"https://www.uniprot.org/uniprotkb/P32807/entry","name":"YKU70","description":"ATP-dependent DNA helicase II subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12604","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8224","identifier":"Q04437","identifierLink":"https://www.uniprot.org/uniprotkb/Q04437/entry","name":"YKU80","description":"ATP-dependent DNA helicase II subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12604","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1733","complexName":"NOC1-NOC2 pre-ribosome maturation complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Associates with 90S and 66S pre-ribosomes and is enriched in the nucleolus. Required for for intranuclear movement and maturation of ribosomal precursor particles.","predictedComplex":false,"interactors":[{"ac":"EBI-10944","identifier":"Q12176","identifierLink":"https://www.uniprot.org/uniprotkb/Q12176/entry","name":"MAK21","description":"Ribosome biogenesis protein MAK21","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29259","identifier":"P39744","identifierLink":"https://www.uniprot.org/uniprotkb/P39744/entry","name":"NOC2","description":"Nucleolar complex protein 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12687","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1734","complexName":"NOC2-NOC3 pre-ribosome maturation complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Associates with 66S pre-ribosomes and is mainly nucleoplasmic. Required for intranuclear movement and maturation of ribosomal precursor particles.","predictedComplex":false,"interactors":[{"ac":"EBI-29259","identifier":"P39744","identifierLink":"https://www.uniprot.org/uniprotkb/P39744/entry","name":"NOC2","description":"Nucleolar complex protein 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12687","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-36093","identifier":"Q07896","identifierLink":"https://www.uniprot.org/uniprotkb/Q07896/entry","name":"NOC3","description":"Nucleolar complex-associated protein 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14428","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1735","complexName":"NOP14-NOC4 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"required for biogenesis of the small ribosomal subunit formation and subsequent export to the cytoplasm.The nucleolar localization of Nop14 is dependent on Noc4.","predictedComplex":false,"interactors":[{"ac":"EBI-35157","identifier":"Q99207","identifierLink":"https://www.uniprot.org/uniprotkb/Q99207/entry","name":"NOP14","description":"Nucleolar complex protein 14","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23183","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-36459","identifier":"Q06512","identifierLink":"https://www.uniprot.org/uniprotkb/Q06512/entry","name":"NOC4","description":"Nucleolar complex protein 4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12455","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1736","complexName":"Collagen type VI trimer","organismName":"Homo sapiens; 9606","description":"May play a role as an interface between the main collagen fibril network and the cells.","predictedComplex":false,"interactors":[{"ac":"EBI-2465913","identifier":"P12109","identifierLink":"https://www.uniprot.org/uniprotkb/P12109/entry","name":"COL6A1","description":"Collagen alpha-1(VI) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2465936","identifier":"P12111","identifierLink":"https://www.uniprot.org/uniprotkb/P12111/entry","name":"COL6A3","description":"Collagen alpha-3(VI) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-928749","identifier":"P12110","identifierLink":"https://www.uniprot.org/uniprotkb/P12110/entry","name":"COL6A2","description":"Collagen alpha-2(VI) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2965","complexName":"Collagen type VI trimer","organismName":"Mus musculus; 10090","description":"May play a role as an interface between the main collagen fibril network and the cells.","predictedComplex":false,"interactors":[{"ac":"EBI-8344999","identifier":"Q02788","identifierLink":"https://www.uniprot.org/uniprotkb/Q02788/entry","name":"Col6a2","description":"Collagen alpha-2(VI) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8345547","identifier":"Q04857","identifierLink":"https://www.uniprot.org/uniprotkb/Q04857/entry","name":"Col6a1","description":"Collagen alpha-1(VI) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9213287","identifier":"E9PWQ3","identifierLink":"https://www.uniprot.org/uniprotkb/E9PWQ3/entry","name":"Col6a3","description":"Collagen alpha-3(VI) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5770","complexName":"MERS-CoV nucleocapsid complex","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","description":"Forms the helical ribonucleocapsid (RNP) of the SARS-CoV coronavirus. Packages the positive strand viral genome RNA and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M (K9N7A1). Recognises and binds to a packaging signal, a cis-regulatory element encoded within the viral RNA. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. \r\n\r\nMay form viral-like particles (VLPs) together with proteins M, E  (K9N5R3) and S (K9N5Q8) without the requirement of genomic RNA (by similarity from SARS-CoV, CPX-5720). \r\n\r\nBy analogy from SARS-CoV-2 (CPX-5686), may inhibit type I interferon (IFN-beta) activation and downstream innate immune responses.","predictedComplex":false,"interactors":[{"ac":"EBI-25592177","identifier":"K9N4V7","identifierLink":"https://www.uniprot.org/uniprotkb/K9N4V7/entry","name":"N","description":"Nucleoprotein","stochiometry":null,"interactorType":"protein","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","xrefs":[]}]},{"complexAC":"CPX-5772","complexName":"MERS-CoV NSP3-NSP4 complex","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","description":"Complex of the MERS coronavirus involved in inducing rearrangement of the host membranes to form double-membrane vesicles which may form a framework for viral genome replication by localizing and concentrating the necessary factors and possibly providing protection from host cell defenses. \r\n\r\nThe multi-spanning transmembrane domains in nsp3 and nsp4 may serve as a scaffold for the assembly of the membrane-associated replication/transcription complex (RTC), a large multisubunit assembly that is comprised of more than a dozen proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-25592237","identifier":"K9N7C7-PRO_0000422441","identifierLink":"https://www.uniprot.org/uniprotkb/K9N7C7-PRO_0000422441/entry","name":"rep","description":"Papain-like proteinase nsp3","stochiometry":null,"interactorType":"protein","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","xrefs":[]},{"ac":"EBI-25592244","identifier":"K9N7C7-PRO_0000422442","identifierLink":"https://www.uniprot.org/uniprotkb/K9N7C7-PRO_0000422442/entry","name":"rep","description":"Non-structural protein 4","stochiometry":null,"interactorType":"protein","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","xrefs":[]}]},{"complexAC":"CPX-5774","complexName":"Cubam cobalamin uptake receptor complex","organismName":"Homo sapiens; 9606","description":"Endocytic receptor essential for intestinal vitamin B12 (B12/cobalamin, CHEBI:30411) uptake and for protein reabsorption from the kidney filtrate. B12, bound to the carrier protein CBLIF (P27352), docks to the receptor and is then internalized via receptor-mediated endocytosis.","predictedComplex":false,"interactors":[{"ac":"EBI-11510881","identifier":"Q9BXJ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BXJ7/entry","name":"AMN","description":"Protein amnionless","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14995","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 12, maxValue: 12","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-3953632","identifier":"O60494","identifierLink":"https://www.uniprot.org/uniprotkb/O60494/entry","name":"CUBN","description":"Cubilin","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47537","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5777","complexName":"MERS-CoV main protease complex","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","description":"The 3C-like protease of the MERS coronavirus required for processing the polyproteins that are translated from the viral RNA. Cleaves at 11 cleavage sites on the large polyprotein 1ab (K9N7C7); the recognition sequence at most sites is [ILMVF]-Q-|-[SGACN].","predictedComplex":false,"interactors":[{"ac":"EBI-25592576","identifier":"K9N7C7-PRO_0000422443","identifierLink":"https://www.uniprot.org/uniprotkb/K9N7C7-PRO_0000422443/entry","name":"rep","description":"3C-like proteinase nsp5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","xrefs":[]}]},{"complexAC":"CPX-5778","complexName":"MERS-CoV NSP9 complex","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","description":"RNA binding complex of the MERS coronavirus. It has been speculated that nsp9 dimers bind to single-stranded nascent and template strands as they emerge from the channel of the nsp7-nsp8 primase complex (CPX-5746) at a time when stable secondary structures have not yet formed, protecting ssRNAs from ribonucleolytic cleavage.","predictedComplex":false,"interactors":[{"ac":"EBI-25592866","identifier":"K9N7C7-PRO_0000422447","identifierLink":"https://www.uniprot.org/uniprotkb/K9N7C7-PRO_0000422447/entry","name":"rep","description":"Viral protein genome-linked nsp9","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","xrefs":[]}]},{"complexAC":"CPX-5779","complexName":"MERS-CoV polymerase complex","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","description":"RNA-directed 5'-3' RNA polymerase of the MERS coronavirus which consists of the main polymerase protein NSP12 and a stoichiometric variant of the primase complex (CPX-5746). Extends partially double-stranded RNA templates and is probably also required for transcription initiation, though the mechanism for this has yet to be determined. Complex formation enhances dsRNA binding of the individual protomers.","predictedComplex":false,"interactors":[{"ac":"EBI-25592074","identifier":"K9N7C7-PRO_0000422445","identifierLink":"https://www.uniprot.org/uniprotkb/K9N7C7-PRO_0000422445/entry","name":"rep","description":"Non-structural protein 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","xrefs":[]},{"ac":"EBI-25592080","identifier":"K9N7C7-PRO_0000422446","identifierLink":"https://www.uniprot.org/uniprotkb/K9N7C7-PRO_0000422446/entry","name":"rep","description":"Non-structural protein 8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","xrefs":[]},{"ac":"EBI-25592936","identifier":"K9N7C7-PRO_0000422449","identifierLink":"https://www.uniprot.org/uniprotkb/K9N7C7-PRO_0000422449/entry","name":"rep","description":"RNA-directed RNA polymerase nsp12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","xrefs":[]}]},{"complexAC":"CPX-5780","complexName":"lambdaN-dependent processive transcription antitermination complex","organismName":"Escherichia coli (strain K12); 83333","description":"Enables lambdoid phages to switch from immediate-early to delayed-early gene expression during lytic growth, allowing the RNA polymerase (RNAP) enzyme to read through intrinsic and rho-dependent terminators. The lambdaN protein binds and reorganizes RNAP components, and repositions nusA on RNAP, thereby redirecting nascent RNA and sequestering the upstream branch of a terminator hairpin. Formation of this complex may also hinder RNA engagement of termination factor rho (P0AG30) and/or obstruct rho translocation on the transcript.","predictedComplex":false,"interactors":[{"ac":"EBI-369628","identifier":"P0AFG0","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFG0/entry","name":"nusG","description":"Transcription termination/antitermination protein NusG","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30265","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-370560","identifier":"P0A800","identifierLink":"https://www.uniprot.org/uniprotkb/P0A800/entry","name":"rpoZ","description":"DNA-directed RNA polymerase subunit omega","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4478701","identifier":"P03045","identifierLink":"https://www.uniprot.org/uniprotkb/P03045/entry","name":"N","description":"Antitermination protein N","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia phage lambda; 2681611","xrefs":[]},{"ac":"EBI-543604","identifier":"P0A8T7","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8T7/entry","name":"rpoC","description":"DNA-directed RNA polymerase subunit beta'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR19376","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544602","identifier":"P0A7R5","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7R5/entry","name":"rpsJ","description":"Small ribosomal subunit protein uS10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11700","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544985","identifier":"P0A7Z4","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7Z4/entry","name":"rpoA","description":"DNA-directed RNA polymerase subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32108","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544996","identifier":"P0A8V2","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8V2/entry","name":"rpoB","description":"DNA-directed RNA polymerase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR20856","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-551571","identifier":"P0AFF6","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFF6/entry","name":"nusA","description":"Transcription termination/antitermination protein NusA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR22648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-555387","identifier":"P0A780","identifierLink":"https://www.uniprot.org/uniprotkb/P0A780/entry","name":"nusB","description":"Transcription antitermination protein NusB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11078","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-5781","complexName":"gadE-rcsB DNA-binding transcription factor complex","organismName":"Escherichia coli (strain K12); 83333","description":"Transcription factor complex regulated independently of rcsB phosphorylation status. Required for survival in extreme acidic conditions, regulating expression of several genes involved in acid resistance.These include two glutamate decarboxylase isoforms, gadA and gadB, which consume intracellular protons in decarboxylating glutamate.","predictedComplex":false,"interactors":[{"ac":"EBI-369670","identifier":"P0DMC7","identifierLink":"https://www.uniprot.org/uniprotkb/P0DMC7/entry","name":"rcsB","description":"Transcriptional regulatory protein RcsB","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43214","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-562022","identifier":"P63204","identifierLink":"https://www.uniprot.org/uniprotkb/P63204/entry","name":"gadE","description":"Transcriptional regulator GadE","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]}]},{"complexAC":"CPX-5782","complexName":"Tol-Pal cell envelope complex","organismName":"Escherichia coli (strain K12); 83333","description":"Required for the co-ordinated invagination of the envelope layers during cell fission, using proton motive force to establish transient trans-envelope connections at/near the septal ring to draw the outer membrane onto the invaginating proteoglycan and inner membrane layers. Ion potential over the inner membrane is converted by tolQ and R to drive a conformational change in tolA, extending it through meshes of newly split murein to reach for free pal in the outer membrane. On bindng a pal molecule, tolA snaps back, drawing pal inwards, and then disassociates, allowing pal to engage the proteoglycan layer. Also acts to transport colicins classified in group A (colicins A, E1 to E9, K, N, and cloacin DF13) from the outer membrane across the periplasm.","predictedComplex":false,"interactors":[{"ac":"EBI-1120026","identifier":"P19934","identifierLink":"https://www.uniprot.org/uniprotkb/P19934/entry","name":"tolA","description":"Tol-Pal system protein TolA","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-1124760","identifier":"P0A912","identifierLink":"https://www.uniprot.org/uniprotkb/P0A912/entry","name":"pal","description":"Peptidoglycan-associated lipoprotein","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30128","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25593254","identifier":"P0ABU9","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABU9/entry","name":"tolQ","description":"Tol-Pal system protein TolQ","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-558394","identifier":"P0ABV6","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABV6/entry","name":"tolR","description":"Tol-Pal system protein TolR","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7180728","identifier":"P0A855","identifierLink":"https://www.uniprot.org/uniprotkb/P0A855/entry","name":"tolB","description":"Tol-Pal system protein TolB","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42972","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5783","complexName":"MERS-CoV 3'-5' exoribonuclease proof-reading complex","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","description":"The MERS coronavirus 3'-5' exoribonuclease complex which strictly targets double-stranded RNA and can also selectively remove a mismatched ribonucleotide at the 3'-end of a dsRNA substrate. Formation of the NSP10-NSP14 complex strongly enhances the exonuclease activity of the bifunctional NSP14 and enhances the fidelity of RNA synthesis by correcting nucleotide incorporation errors made by the RNA-dependent RNA polymerase. May bind to, and act with the nsp7/nsp8/nsp12 polymerase complex (CPX-5779). Proof-reading exonuclease activity may explain why coronaviruses have the largest RNA genomes known to date. Complex formation does not appear to effect the C-terminal N7-methyltransferase activity of NSP14 involved in RNA cap modification.","predictedComplex":false,"interactors":[{"ac":"EBI-25594384","identifier":"K9N7C7-PRO_0000422448","identifierLink":"https://www.uniprot.org/uniprotkb/K9N7C7-PRO_0000422448/entry","name":"rep","description":"Non-structural protein 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","xrefs":[]},{"ac":"EBI-25594390","identifier":"K9N7C7-PRO_0000422451","identifierLink":"https://www.uniprot.org/uniprotkb/K9N7C7-PRO_0000422451/entry","name":"rep","description":"Guanine-N7 methyltransferase nsp14","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","xrefs":[]}]},{"complexAC":"CPX-5784","complexName":"MERS-CoV NSP10-NSP16 2'-O-methyltransferase complex","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","description":"2'-O-methyltransferase complex of the MERS coronavirus which mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs using S-adenosyl-L-methionine (SAM, CHEBI:15414) as the methyl donor. The cap structure is essential for efficient splicing, nuclear export, translation and mRNA stability.","predictedComplex":false,"interactors":[{"ac":"EBI-25594384","identifier":"K9N7C7-PRO_0000422448","identifierLink":"https://www.uniprot.org/uniprotkb/K9N7C7-PRO_0000422448/entry","name":"rep","description":"Non-structural protein 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","xrefs":[]},{"ac":"EBI-25594444","identifier":"K9N7C7-PRO_0000422453","identifierLink":"https://www.uniprot.org/uniprotkb/K9N7C7-PRO_0000422453/entry","name":"rep","description":"2'-O-methyltransferase nsp16","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","xrefs":[]}]},{"complexAC":"CPX-5785","complexName":"MERS-CoV NSP15 complex","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","description":"The MERS coronavirus uridylate-specific endoribonuclease complex which cleaves RNA of uridylates through the formation of a 2′-3′ cyclic phosphodiester and 5'-hydroxyl termini, acting on both, single-and double stranded RNA.","predictedComplex":false,"interactors":[{"ac":"EBI-25592093","identifier":"K9N7C7-PRO_0000422452","identifierLink":"https://www.uniprot.org/uniprotkb/K9N7C7-PRO_0000422452/entry","name":"rep","description":"Uridylate-specific endoribonuclease nsp15","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","xrefs":[]}]},{"complexAC":"CPX-5786","complexName":"AMPK complex, alpha1-beta1-gamma2 variant","organismName":"Homo sapiens; 9606","description":"Energy sensor serine/threonine kinase that plays a key role in regulating cellular energy metabolism. Energy stress manifests as a drop in the ratio of adenosine triphosphate (ATP) to AMP/ADP, which activates AMPK's kinase activity, allowing it to upregulate ATP-generating catabolic pathways and to reduce energy-consuming catabolic pathways and cellular programs: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators.","predictedComplex":false,"interactors":[{"ac":"EBI-1181405","identifier":"Q13131","identifierLink":"https://www.uniprot.org/uniprotkb/Q13131/entry","name":"PRKAA1","description":"5'-AMP-activated protein kinase catalytic subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2959705","identifier":"Q9UGJ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UGJ0/entry","name":"PRKAG2","description":"5'-AMP-activated protein kinase subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-719769","identifier":"Q9Y478","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y478/entry","name":"PRKAB1","description":"5'-AMP-activated protein kinase subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5787","complexName":"AMPK complex, alpha2-beta1-gamma1 variant","organismName":"Homo sapiens; 9606","description":"Energy sensor serine/threonine kinase that plays a key role in regulating cellular energy metabolism. Energy stress manifests as a drop in the ratio of adenosine triphosphate (ATP) to AMP/ADP, which activates AMPK's kinase activity, allowing it to upregulate ATP-generating catabolic pathways and to reduce energy-consuming catabolic pathways and cellular programs: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators.\r\n\r\nIt has, preferentially, a nuclear localisation.","predictedComplex":false,"interactors":[{"ac":"EBI-1181439","identifier":"P54619","identifierLink":"https://www.uniprot.org/uniprotkb/P54619/entry","name":"PRKAG1","description":"5'-AMP-activated protein kinase subunit gamma-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1383852","identifier":"P54646","identifierLink":"https://www.uniprot.org/uniprotkb/P54646/entry","name":"PRKAA2","description":"5'-AMP-activated protein kinase catalytic subunit alpha-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-719769","identifier":"Q9Y478","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y478/entry","name":"PRKAB1","description":"5'-AMP-activated protein kinase subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5789","complexName":"MERS-CoV NSP10-NSP16 2'-O-methyltransferase complex","organismName":"Human betacoronavirus 2c EMC/2012; 1235996","description":"2'-O-methyltransferase complex of the MERS coronavirus which mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs using S-adenosyl-L-methionine (SAM,CHEBI:15414) as the methyl donor. The cap structure is essential for efficient splicing, nuclear export, translation and mRNA stability.","predictedComplex":false,"interactors":[{"ac":"EBI-25565992","identifier":"K0BWD0","identifierLink":"https://www.uniprot.org/uniprotkb/K0BWD0/entry","name":"orf1ab","description":"ORF1ab polyprotein","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Human betacoronavirus 2c EMC/2012; 1235996","xrefs":[]}]},{"complexAC":"CPX-5790","complexName":"AMPK complex, alpha2-beta2-gamma1 variant","organismName":"Homo sapiens; 9606","description":"Energy sensor serine/threonine kinase that plays a key role in regulating cellular energy metabolism. Energy stress manifests as a drop in the ratio of adenosine triphosphate (ATP) to AMP/ADP, which activates AMPK's kinase activity, allowing it to upregulate ATP-generating catabolic pathways and to reduce energy-consuming catabolic pathways and cellular programs: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators.\r\n\r\nOnly three AMPK complexes are present in skeletal muscle: alpha2-beta2-gamma3 (CPX-5840) which is activated during exercises; and alpha1-beta2-gamma1(CPX-5791) and alpha2-beta2-gamma1 (CPX-5790) predominant in resting conditions.","predictedComplex":false,"interactors":[{"ac":"EBI-1053424","identifier":"O43741","identifierLink":"https://www.uniprot.org/uniprotkb/O43741/entry","name":"PRKAB2","description":"5'-AMP-activated protein kinase subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1181439","identifier":"P54619","identifierLink":"https://www.uniprot.org/uniprotkb/P54619/entry","name":"PRKAG1","description":"5'-AMP-activated protein kinase subunit gamma-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1383852","identifier":"P54646","identifierLink":"https://www.uniprot.org/uniprotkb/P54646/entry","name":"PRKAA2","description":"5'-AMP-activated protein kinase catalytic subunit alpha-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5791","complexName":"AMPK complex, alpha1-beta2-gamma1 variant","organismName":"Homo sapiens; 9606","description":"Energy sensor serine/threonine kinase that plays a key role in regulating cellular energy metabolism. Energy stress manifests as a drop in the ratio of adenosine triphosphate (ATP) to AMP/ADP, which activates AMPK's kinase activity, allowing it to upregulate ATP-generating catabolic pathways and to reduce energy-consuming catabolic pathways and cellular programs: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators.\r\n\r\nOnly three AMPK complexes are present in skeletal muscle: alpha2-beta2-gamma3 (CPX-5840) which is activated during exercises; and alpha1-beta2-gamma1(CPX-5791) and alpha2-beta2-gamma1 (CPX-5790) predominant in resting conditions.","predictedComplex":false,"interactors":[{"ac":"EBI-1053424","identifier":"O43741","identifierLink":"https://www.uniprot.org/uniprotkb/O43741/entry","name":"PRKAB2","description":"5'-AMP-activated protein kinase subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1181405","identifier":"Q13131","identifierLink":"https://www.uniprot.org/uniprotkb/Q13131/entry","name":"PRKAA1","description":"5'-AMP-activated protein kinase catalytic subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1181439","identifier":"P54619","identifierLink":"https://www.uniprot.org/uniprotkb/P54619/entry","name":"PRKAG1","description":"5'-AMP-activated protein kinase subunit gamma-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5801","complexName":"ZHP-1-ZHP-2 complex","organismName":"Caenorhabditis elegans; 6239","description":"Required for crossover formation and subsequent chromosome segregation during meiotic recombination. During meiotic pachytene, recruited to the Synaptonemal complex (CPX-3388) in between homologous chromosome pairs, where it promotes the accumulation of pro-crossover proteins including the ZHP-3-ZHP-4 heterodimer (CPX-5802), at a designated crossover site along the recombination intermediate. Limits the number of crossover sites along a recombination intermediate by restricting the association of these pro-crossover proteins with other recombination sites during late prophase. Plays a role in chromosome remodeling following crossover formation to promote two successive rounds of chromosome segregation during meiosis.","predictedComplex":false,"interactors":[{"ac":"EBI-2415375","identifier":"Q95R14","identifierLink":"https://www.uniprot.org/uniprotkb/Q95R14/entry","name":"zhp-1","description":"Zip homologous protein 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR22663","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2415382","identifier":"Q9U3L0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9U3L0/entry","name":"zhp-2","description":"Zip homologous protein 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR22663","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5802","complexName":"ZHP-3-ZHP-4 meiotic pro-crossover complex","organismName":"Caenorhabditis elegans; 6239","description":"Required for crossover formation and subsequent chromosome segregation during meiotic recombination. During meiotic pachytene, recruited by the ZHP-1-ZHP-2 heterodimer (CPX-5801) to designated crossover sites along the recombination intermediate to stabilizes other pro-crossover factors such as rmh-1 (P91399), msh-5 (Q19272) and cosa-1 (Q9BL45). This in turn faciliates crossover and the formation of chiasma in each meiotic nucleus at the late pachytene stage of meiosis.","predictedComplex":false,"interactors":[{"ac":"EBI-25597963","identifier":"C6KRL6","identifierLink":"https://www.uniprot.org/uniprotkb/C6KRL6/entry","name":"zhp-3","description":"Zip homologous protein 3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR22663","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2920397","identifier":"Q8MYP1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8MYP1/entry","name":"zhp-4","description":"Zip homologous protein 4","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR22663","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5824","complexName":"NineTeen Core complex","organismName":"Homo sapiens; 9606","description":"Required for catalytic activation of the spliceosome and is an integral component of active spliceosomes. During or after U4 small nuclear RNP (snRNP) release, the NineTeen (NTC) complex is recruited into the spliceosome as it transitions from the B complex (CPX-26435) to the B-act (CPX-26441) formation stage where it stabilizes the U5/U6 snRNP in the B-act and remains associated with the spliceosome during the second step of splicing. The NTC is highly conserved and it is likely that it performs the same functions across all species. Also plays a central role in regulating DNA damage response (DDR) and maintaining cellular homeostasis.","predictedComplex":false,"interactors":[{"ac":"EBI-1050106","identifier":"O75934","identifierLink":"https://www.uniprot.org/uniprotkb/O75934/entry","name":"BCAS2","description":"Pre-mRNA-splicing factor SPF27","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13296","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1051504","identifier":"O43660","identifierLink":"https://www.uniprot.org/uniprotkb/O43660/entry","name":"PLRG1","description":"Pleiotropic regulator 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19923","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2371709","identifier":"Q9P013","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P013/entry","name":"CWC15","description":"Spliceosome-associated protein CWC15 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12718","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-351896","identifier":"P11142","identifierLink":"https://www.uniprot.org/uniprotkb/P11142/entry","name":"HSPA8","description":"Heat shock cognate 71 kDa protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-374880","identifier":"Q99459","identifierLink":"https://www.uniprot.org/uniprotkb/Q99459/entry","name":"CDC5L","description":"Cell division cycle 5-like protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45885","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395746","identifier":"Q9UMS4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UMS4/entry","name":"PRPF19","description":"Pre-mRNA-processing factor 19","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43995","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-748128","identifier":"Q8WYA6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WYA6/entry","name":"CTNNBL1","description":"Beta-catenin-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14978","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5825","complexName":"PRP19-CDC5L complex","organismName":"Mus musculus; 10090","description":"Forms an integral part of the spliceosome and is required for activating pre-mRNA splicing by  participating in the rearrangement of small nuclear ribonucleoprotein (snRNP) particles. May also play a role in the response to DNA damage (DDR).","predictedComplex":false,"interactors":[{"ac":"EBI-2552123","identifier":"Q6A068","identifierLink":"https://www.uniprot.org/uniprotkb/Q6A068/entry","name":"Cdc5l","description":"Cell division cycle 5-like protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45885","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-433443","identifier":"P63017","identifierLink":"https://www.uniprot.org/uniprotkb/P63017/entry","name":"Hspa8","description":"Heat shock cognate 71 kDa protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR19375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6260977","identifier":"Q99KP6","identifierLink":"https://www.uniprot.org/uniprotkb/Q99KP6/entry","name":"Prpf19","description":"Pre-mRNA-processing factor 19","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR43995","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8338047","identifier":"Q9JHS9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JHS9/entry","name":"Cwc15","description":"Spliceosome-associated protein CWC15 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12718","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8338374","identifier":"Q9CWL8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CWL8/entry","name":"Ctnnbl1","description":"Beta-catenin-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14978","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8338824","identifier":"Q9D287","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D287/entry","name":"Bcas2","description":"Pre-mRNA-splicing factor SPF27","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13296","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8339071","identifier":"Q922V4","identifierLink":"https://www.uniprot.org/uniprotkb/Q922V4/entry","name":"Plrg1","description":"Pleiotropic regulator 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR19923","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5826","complexName":"Kv7.1 channel complex","organismName":"Mus musculus; 10090","description":"Voltage-dependent potassium channels that plays major roles in tuning neuronal and cardiomyocyte excitability by acting as a brake for neuronal firing and by controlling cardiomyocyte repolarization. Calmodulin acts as obligate subunit of the Kv7.1 channel.","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-397460","identifier":"P62204","identifierLink":"https://www.uniprot.org/uniprotkb/P62204/entry","name":"Calm1","description":"Calmodulin","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-9869724","identifier":"P97414","identifierLink":"https://www.uniprot.org/uniprotkb/P97414/entry","name":"Kcnq1","description":"Potassium voltage-gated channel subfamily KQT member 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11537","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5828","complexName":"NF-kappaB DNA-binding transcription factor complex, p50/p65","organismName":"Homo sapiens; 9606","description":"Transcription factor that binds at kappa-B sites in the DNA of its target genes where it acts as a transcriptional activator. Present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis.","predictedComplex":false,"interactors":[{"ac":"EBI-697771","identifier":"P19838-PRO_0000030311","identifierLink":"https://www.uniprot.org/uniprotkb/P19838-PRO_0000030311/entry","name":"NFKB1","description":"Nuclear factor NF-kappa-B p50 subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-73886","identifier":"Q04206","identifierLink":"https://www.uniprot.org/uniprotkb/Q04206/entry","name":"RELA","description":"Transcription factor p65","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24169","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5829","complexName":"NF-kappaB DNA-binding transcription factor complex, p52/p65","organismName":"Homo sapiens; 9606","description":"Transcription factor that binds at kappa-B sites in the DNA of it target genes where it acts as a transcriptional activator. Present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis.","predictedComplex":false,"interactors":[{"ac":"EBI-73886","identifier":"Q04206","identifierLink":"https://www.uniprot.org/uniprotkb/Q04206/entry","name":"RELA","description":"Transcription factor p65","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24169","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9869360","identifier":"Q00653-PRO_0000030322","identifierLink":"https://www.uniprot.org/uniprotkb/Q00653-PRO_0000030322/entry","name":"NFKB2","description":"Nuclear factor NF-kappa-B p52 subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-5830","complexName":"NF-kappaB DNA-binding transcription factor complex, p52/c-Rel","organismName":"Homo sapiens; 9606","description":"Transcription factor that binds at kappa-B sites in the DNA of it target genes where it acts as a transcriptional activator. 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Present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis.","predictedComplex":false,"interactors":[{"ac":"EBI-307352","identifier":"Q04864","identifierLink":"https://www.uniprot.org/uniprotkb/Q04864/entry","name":"REL","description":"Proto-oncogene c-Rel","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24169","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-73886","identifier":"Q04206","identifierLink":"https://www.uniprot.org/uniprotkb/Q04206/entry","name":"RELA","description":"Transcription factor p65","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24169","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5835","complexName":"NF-kappaB DNA-binding transcription factor complex, p65/p65","organismName":"Homo sapiens; 9606","description":"Transcription factor that binds at kappa-B sites in the DNA of its target genes where it acts as a transcriptional activator. Present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis.","predictedComplex":false,"interactors":[{"ac":"EBI-73886","identifier":"Q04206","identifierLink":"https://www.uniprot.org/uniprotkb/Q04206/entry","name":"RELA","description":"Transcription factor p65","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24169","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5836","complexName":"NF-kappaB DNA-binding transcription factor complex, c-Rel/c-Rel","organismName":"Homo sapiens; 9606","description":"Transcription factor that binds at kappa-B sites in the DNA of its target genes where it acts as a transcriptional activator. Present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis.","predictedComplex":false,"interactors":[{"ac":"EBI-307352","identifier":"Q04864","identifierLink":"https://www.uniprot.org/uniprotkb/Q04864/entry","name":"REL","description":"Proto-oncogene c-Rel","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24169","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5837","complexName":"NF-kappaB transcription regulation complex, p50-p52","organismName":"Homo sapiens; 9606","description":"Transcription factor that binds at kappa-B sites in the DNA of its target genes where it acts as a transcriptional regulator. Present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. p50:p52 dimers lack a  trans-activating domain,, and therefore repress transcription in the absence of co-activating factors and p65","predictedComplex":false,"interactors":[{"ac":"EBI-697771","identifier":"P19838-PRO_0000030311","identifierLink":"https://www.uniprot.org/uniprotkb/P19838-PRO_0000030311/entry","name":"NFKB1","description":"Nuclear factor NF-kappa-B p50 subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-9869360","identifier":"Q00653-PRO_0000030322","identifierLink":"https://www.uniprot.org/uniprotkb/Q00653-PRO_0000030322/entry","name":"NFKB2","description":"Nuclear factor NF-kappa-B p52 subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-5838","complexName":"NF-kappaB transcription regulation complex, p50/p50","organismName":"Homo sapiens; 9606","description":"Transcription factor that binds at kappa-B sites in the DNA of its target genes where it acts as a transcriptional regulator. 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AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators.\r\n\r\nOnly three AMPK complexes are present in skeletal muscle: alpha2-beta2-gamma3 (CPX-5840) which is activated during exercises; and alpha1-beta2-gamma1(CPX-5791) and alpha2-beta2-gamma1 (CPX-5790) predominant in resting conditions.","predictedComplex":false,"interactors":[{"ac":"EBI-1053424","identifier":"O43741","identifierLink":"https://www.uniprot.org/uniprotkb/O43741/entry","name":"PRKAB2","description":"5'-AMP-activated protein kinase subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1383852","identifier":"P54646","identifierLink":"https://www.uniprot.org/uniprotkb/P54646/entry","name":"PRKAA2","description":"5'-AMP-activated protein kinase catalytic subunit alpha-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7428853","identifier":"Q9UGI9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UGI9/entry","name":"PRKAG3","description":"5'-AMP-activated protein kinase subunit gamma-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5841","complexName":"AMPK complex, alpha1-beta2-gamma3 variant","organismName":"Homo sapiens; 9606","description":"Energy sensor serine/threonine kinase that plays a key role in regulating cellular energy metabolism. 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AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators.\r\n\r\nIt has, preferentially, a nuclear localisation.","predictedComplex":false,"interactors":[{"ac":"EBI-11566288","identifier":"Q8BRK8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BRK8/entry","name":"Prkaa2","description":"5'-AMP-activated protein kinase catalytic subunit alpha-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2366248","identifier":"Q9R078","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R078/entry","name":"Prkab1","description":"5'-AMP-activated protein kinase subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7927886","identifier":"O54950","identifierLink":"https://www.uniprot.org/uniprotkb/O54950/entry","name":"Prkag1","description":"5'-AMP-activated protein kinase subunit gamma-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5853","complexName":"AMPK complex, alpha1-beta2-gamma1 variant","organismName":"Mus musculus; 10090","description":"Energy sensor serine/threonine kinase that plays a key role in regulating cellular energy metabolism. 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AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators.\r\n\r\nOnly three AMPK complexes are present in skeletal muscle: alpha2-beta2-gamma3 (CPX-5854) which is activated during exercises; and alpha1-beta2-gamma1(CPX-5853) and alpha2-beta2-gamma1 (CPX-5851) predominant in resting conditions.","predictedComplex":false,"interactors":[{"ac":"EBI-7282395","identifier":"Q5EG47","identifierLink":"https://www.uniprot.org/uniprotkb/Q5EG47/entry","name":"Prkaa1","description":"5'-AMP-activated protein kinase catalytic subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7927886","identifier":"O54950","identifierLink":"https://www.uniprot.org/uniprotkb/O54950/entry","name":"Prkag1","description":"5'-AMP-activated protein kinase subunit gamma-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8328017","identifier":"Q6PAM0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PAM0/entry","name":"Prkab2","description":"5'-AMP-activated protein kinase subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5854","complexName":"AMPK complex, alpha2-beta2-gamma3 variant","organismName":"Mus musculus; 10090","description":"Energy sensor serine/threonine kinase that plays a key role in regulating cellular energy metabolism. Energy stress manifests as a drop in the ratio of adenosine triphosphate (ATP) to AMP/ADP, which activates AMPK's kinase activity, allowing it to upregulate ATP-generating catabolic pathways and to reduce energy-consuming catabolic pathways and cellular programs: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators.\r\n\r\nOnly three AMPK complexes are present in skeletal muscle: alpha2-beta2-gamma3 (CPX-5854) which is activated during exercises; and alpha1-beta2-gamma1(CPX-5853) and alpha2-beta2-gamma1 (CPX-5851) predominant in resting conditions.","predictedComplex":false,"interactors":[{"ac":"EBI-11566288","identifier":"Q8BRK8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BRK8/entry","name":"Prkaa2","description":"5'-AMP-activated protein kinase catalytic subunit alpha-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25621512","identifier":"Q8BGM7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BGM7/entry","name":"Prkag3","description":"5'-AMP-activated protein kinase subunit gamma-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8328017","identifier":"Q6PAM0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PAM0/entry","name":"Prkab2","description":"5'-AMP-activated protein kinase subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5855","complexName":"AMPK complex, alpha1-beta2-gamma3 variant","organismName":"Mus musculus; 10090","description":"Energy sensor serine/threonine kinase that plays a key role in regulating cellular energy metabolism. Energy stress manifests as a drop in the ratio of adenosine triphosphate (ATP) to AMP/ADP, which activates AMPK's kinase activity, allowing it to upregulate ATP-generating catabolic pathways and to reduce energy-consuming catabolic pathways and cellular programs: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators.","predictedComplex":false,"interactors":[{"ac":"EBI-25621512","identifier":"Q8BGM7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BGM7/entry","name":"Prkag3","description":"5'-AMP-activated protein kinase subunit gamma-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7282395","identifier":"Q5EG47","identifierLink":"https://www.uniprot.org/uniprotkb/Q5EG47/entry","name":"Prkaa1","description":"5'-AMP-activated protein kinase catalytic subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8328017","identifier":"Q6PAM0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PAM0/entry","name":"Prkab2","description":"5'-AMP-activated protein kinase subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5856","complexName":"AMPK complex, alpha1-beta1-gamma3 variant","organismName":"Mus musculus; 10090","description":"Energy sensor serine/threonine kinase that plays a key role in regulating cellular energy metabolism. Energy stress manifests as a drop in the ratio of adenosine triphosphate (ATP) to AMP/ADP, which activates AMPK's kinase activity, allowing it to upregulate ATP-generating catabolic pathways and to reduce energy-consuming catabolic pathways and cellular programs: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators.","predictedComplex":false,"interactors":[{"ac":"EBI-2366248","identifier":"Q9R078","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R078/entry","name":"Prkab1","description":"5'-AMP-activated protein kinase subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25621512","identifier":"Q8BGM7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BGM7/entry","name":"Prkag3","description":"5'-AMP-activated protein kinase subunit gamma-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7282395","identifier":"Q5EG47","identifierLink":"https://www.uniprot.org/uniprotkb/Q5EG47/entry","name":"Prkaa1","description":"5'-AMP-activated protein kinase catalytic subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5857","complexName":"AMPK complex, alpha2-beta1-gamma3 variant","organismName":"Mus musculus; 10090","description":"Energy sensor serine/threonine kinase that plays a key role in regulating cellular energy metabolism. Energy stress manifests as a drop in the ratio of adenosine triphosphate (ATP) to AMP/ADP, which activates AMPK's kinase activity, allowing it to upregulate ATP-generating catabolic pathways and to reduce energy-consuming catabolic pathways and cellular programs: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators.","predictedComplex":false,"interactors":[{"ac":"EBI-11566288","identifier":"Q8BRK8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BRK8/entry","name":"Prkaa2","description":"5'-AMP-activated protein kinase catalytic subunit alpha-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2366248","identifier":"Q9R078","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R078/entry","name":"Prkab1","description":"5'-AMP-activated protein kinase subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25621512","identifier":"Q8BGM7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BGM7/entry","name":"Prkag3","description":"5'-AMP-activated protein kinase subunit gamma-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5858","complexName":"AMPK complex, alpha2-beta1-gamma2 variant","organismName":"Mus musculus; 10090","description":"Energy sensor serine/threonine kinase that plays a key role in regulating cellular energy metabolism. Energy stress manifests as a drop in the ratio of adenosine triphosphate (ATP) to AMP/ADP, which activates AMPK's kinase activity, allowing it to upregulate ATP-generating catabolic pathways and to reduce energy-consuming catabolic pathways and cellular programs: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators.","predictedComplex":false,"interactors":[{"ac":"EBI-11566288","identifier":"Q8BRK8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BRK8/entry","name":"Prkaa2","description":"5'-AMP-activated protein kinase catalytic subunit alpha-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2366148","identifier":"Q91WG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q91WG5/entry","name":"Prkag2","description":"5'-AMP-activated protein kinase subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2366248","identifier":"Q9R078","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R078/entry","name":"Prkab1","description":"5'-AMP-activated protein kinase subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5859","complexName":"AMPK complex, alpha2-beta2-gamma2 variant","organismName":"Mus musculus; 10090","description":"Energy sensor serine/threonine kinase that plays a key role in regulating cellular energy metabolism. Energy stress manifests as a drop in the ratio of adenosine triphosphate (ATP) to AMP/ADP, which activates AMPK's kinase activity, allowing it to upregulate ATP-generating catabolic pathways and to reduce energy-consuming catabolic pathways and cellular programs: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators.","predictedComplex":false,"interactors":[{"ac":"EBI-11566288","identifier":"Q8BRK8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BRK8/entry","name":"Prkaa2","description":"5'-AMP-activated protein kinase catalytic subunit alpha-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2366148","identifier":"Q91WG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q91WG5/entry","name":"Prkag2","description":"5'-AMP-activated protein kinase subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8328017","identifier":"Q6PAM0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PAM0/entry","name":"Prkab2","description":"5'-AMP-activated protein kinase subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5860","complexName":"AMPK complex, alpha1-beta2-gamma2 variant","organismName":"Mus musculus; 10090","description":"Energy sensor serine/threonine kinase that plays a key role in regulating cellular energy metabolism. Energy stress manifests as a drop in the ratio of adenosine triphosphate (ATP) to AMP/ADP, which activates AMPK's kinase activity, allowing it to upregulate ATP-generating catabolic pathways and to reduce energy-consuming catabolic pathways and cellular programs: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators.","predictedComplex":false,"interactors":[{"ac":"EBI-2366148","identifier":"Q91WG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q91WG5/entry","name":"Prkag2","description":"5'-AMP-activated protein kinase subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7282395","identifier":"Q5EG47","identifierLink":"https://www.uniprot.org/uniprotkb/Q5EG47/entry","name":"Prkaa1","description":"5'-AMP-activated protein kinase catalytic subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8328017","identifier":"Q6PAM0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PAM0/entry","name":"Prkab2","description":"5'-AMP-activated protein kinase subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5861","complexName":"SF1-U2AF65 splicing factor complex","organismName":"Mus musculus; 10090","description":"Spliceosome complexes that recognizes consensus sequences at the 3-prime splice sites of pre-mRNAs. Once bound to the pre-mRNA, U2af2 recruits the U2 small nuclear ribonucleoprotein particle (snRNP) to the assembling spliceosome. Phosphorylation of SF1 by Uhmk1 (P97343) enhances Sf1-U2af2 interactions and promotes assembly of the ternary complex of Sf1, U2af2, and the 3-prime splice site.","predictedComplex":false,"interactors":[{"ac":"EBI-8312835","identifier":"Q64213","identifierLink":"https://www.uniprot.org/uniprotkb/Q64213/entry","name":"Sf1","description":"Splicing factor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11208","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8321355","identifier":"P26369","identifierLink":"https://www.uniprot.org/uniprotkb/P26369/entry","name":"U2af2","description":"Splicing factor U2AF 65 kDa subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5862","complexName":"Eukaryotic translation initiation factor 4F, EIF4A2 and EIF4G1 variant","organismName":"Mus musculus; 10090","description":"Eukaryotic translation initiation factor 4F (eIF4F) consists of three subunits, eIF4A, eIF4E, and eIF4G. Cap-dependent translation initiation commences with the binding of the cap structure (m7GTP) found at the 5 prime end of mRNA to eIF4E subunit. The eIF4F complex then loads mRNAs onto the 40S ribosomal subunit together with eIF3.\r\nSubunit eIF4A is an ATP-dependent RNA helicase involved in cap recognition and is required for mRNA binding to ribosome. eIF4G subunit serves as a scaffold for eIF4A and eIF4E subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-1634890","identifier":"P10630","identifierLink":"https://www.uniprot.org/uniprotkb/P10630/entry","name":"Eif4a2","description":"Eukaryotic initiation factor 4A-II","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2000006","identifier":"P63073","identifierLink":"https://www.uniprot.org/uniprotkb/P63073/entry","name":"Eif4e","description":"Eukaryotic translation initiation factor 4E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8175606","identifier":"Q6NZJ6","identifierLink":"https://www.uniprot.org/uniprotkb/Q6NZJ6/entry","name":"Eif4g1","description":"Eukaryotic translation initiation factor 4 gamma 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23253","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5863","complexName":"Eukaryotic translation initiation factor 4F, EIF4A1 and EIF4G1 variant","organismName":"Mus musculus; 10090","description":"Eukaryotic translation initiation factor 4F (eIF4F) consists of three subunits, eIF4A, eIF4E, and eIF4G. Cap-dependent translation initiation commences with the binding of the cap structure (m7GTP) found at the 5 prime end of mRNA to eIF4E subunit. The eIF4F complex then loads mRNAs onto the 40S ribosomal subunit together with eIF3.\r\nSubunit eIF4A is an ATP-dependent RNA helicase involved in cap recognition and is required for mRNA binding to ribosome. eIF4G subunit serves as a scaffold for eIF4A and eIF4E subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-2000006","identifier":"P63073","identifierLink":"https://www.uniprot.org/uniprotkb/P63073/entry","name":"Eif4e","description":"Eukaryotic translation initiation factor 4E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6665935","identifier":"P60843","identifierLink":"https://www.uniprot.org/uniprotkb/P60843/entry","name":"Eif4a1","description":"Eukaryotic initiation factor 4A-I","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8175606","identifier":"Q6NZJ6","identifierLink":"https://www.uniprot.org/uniprotkb/Q6NZJ6/entry","name":"Eif4g1","description":"Eukaryotic translation initiation factor 4 gamma 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23253","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5864","complexName":"Eukaryotic translation initiation factor 4F, EIF4A2 and EIF4G3 variant","organismName":"Mus musculus; 10090","description":"Eukaryotic translation initiation factor 4F (eIF4F) consists of three subunits, eIF4A, eIF4E, and eIF4G. Cap-dependent translation initiation commences with the binding of the cap structure (m7GTP) found at the 5 prime end of mRNA to eIF4E subunit. The eIF4F complex then loads mRNAs onto the 40S ribosomal subunit together with eIF3.\r\nSubunit eIF4A is an ATP-dependent RNA helicase involved in cap recognition and is required for mRNA binding to ribosome. eIF4G subunit serves as a scaffold for eIF4A and eIF4E subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-11664146","identifier":"Q80XI3","identifierLink":"https://www.uniprot.org/uniprotkb/Q80XI3/entry","name":"Eif4g3","description":"Eukaryotic translation initiation factor 4 gamma 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23253","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1634890","identifier":"P10630","identifierLink":"https://www.uniprot.org/uniprotkb/P10630/entry","name":"Eif4a2","description":"Eukaryotic initiation factor 4A-II","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2000006","identifier":"P63073","identifierLink":"https://www.uniprot.org/uniprotkb/P63073/entry","name":"Eif4e","description":"Eukaryotic translation initiation factor 4E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5865","complexName":"Eukaryotic translation initiation factor 4F, EIF4A1 and EIF4G3 variant","organismName":"Mus musculus; 10090","description":"Eukaryotic translation initiation factor 4F (eIF4F) consists of three subunits, eIF4A, eIF4E, and eIF4G. 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The eIF4F complex then loads mRNAs onto the 40S ribosomal subunit together with eIF3.\r\nSubunit eIF4A is an ATP-dependent RNA helicase involved in cap recognition and is required for mRNA binding to ribosome. eIF4G subunit serves as a scaffold for eIF4A and eIF4E subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-11664146","identifier":"Q80XI3","identifierLink":"https://www.uniprot.org/uniprotkb/Q80XI3/entry","name":"Eif4g3","description":"Eukaryotic translation initiation factor 4 gamma 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23253","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2000006","identifier":"P63073","identifierLink":"https://www.uniprot.org/uniprotkb/P63073/entry","name":"Eif4e","description":"Eukaryotic translation initiation factor 4E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6665935","identifier":"P60843","identifierLink":"https://www.uniprot.org/uniprotkb/P60843/entry","name":"Eif4a1","description":"Eukaryotic initiation factor 4A-I","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5866","complexName":"Keratin-80- Keratin-82 dimer complex","organismName":"Mus musculus; 10090","description":"Part of the intermediate filaments of the cytoskeleton. Mostly found in hair.","predictedComplex":false,"interactors":[{"ac":"EBI-25622211","identifier":"Q99M74","identifierLink":"https://www.uniprot.org/uniprotkb/Q99M74/entry","name":"Krt82","description":"Keratin, type II cuticular Hb2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45616","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6877415","identifier":"Q0VBK2","identifierLink":"https://www.uniprot.org/uniprotkb/Q0VBK2/entry","name":"Krt80","description":"Keratin, type II cytoskeletal 80","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45616","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5867","complexName":"Keratin-5 - Keratin-14 dimer complex","organismName":"Mus musculus; 10090","description":"Part of the intermediate filaments of the cytoskeleton. Mostly found in skin.","predictedComplex":false,"interactors":[{"ac":"EBI-1544062","identifier":"Q61781","identifierLink":"https://www.uniprot.org/uniprotkb/Q61781/entry","name":"Krt14","description":"Keratin, type I cytoskeletal 14","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-774204","identifier":"Q922U2","identifierLink":"https://www.uniprot.org/uniprotkb/Q922U2/entry","name":"Krt5","description":"Keratin, type II cytoskeletal 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45616","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5868","complexName":"Keratin-8 - Keratin-18 dimer complex","organismName":"Mus musculus; 10090","description":"Part of the intermediate filaments of the cytoskeleton. Mostly found in skin.","predictedComplex":false,"interactors":[{"ac":"EBI-6932294","identifier":"P11679","identifierLink":"https://www.uniprot.org/uniprotkb/P11679/entry","name":"Krt8","description":"Keratin, type II cytoskeletal 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45616","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8180964","identifier":"P05784","identifierLink":"https://www.uniprot.org/uniprotkb/P05784/entry","name":"Krt18","description":"Keratin, type I cytoskeletal 18","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5869","complexName":"Keratin-25 - Keratin-71 dimer complex","organismName":"Mus musculus; 10090","description":"Part of the intermediate filaments of the cytoskeleton. Mostly found in hair.","predictedComplex":false,"interactors":[{"ac":"EBI-25622298","identifier":"Q8VCW2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VCW2/entry","name":"Krt25","description":"Keratin, type I cytoskeletal 25","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8319391","identifier":"Q9R0H5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R0H5/entry","name":"Krt71","description":"Keratin, type II cytoskeletal 71","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45616","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5870","complexName":"Keratin-36 - Keratin-86 dimer complex","organismName":"Mus musculus; 10090","description":"Part of the intermediate filaments of the cytoskeleton. Mostly found in hair.","predictedComplex":false,"interactors":[{"ac":"EBI-25622340","identifier":"B1AQ75","identifierLink":"https://www.uniprot.org/uniprotkb/B1AQ75/entry","name":"Krt36","description":"Keratin, type I cuticular Ha6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25622363","identifier":"P97861","identifierLink":"https://www.uniprot.org/uniprotkb/P97861/entry","name":"Krt86","description":"Keratin, type II cuticular Hb6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45616","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5871","complexName":"Keratin-1 - Keratin-10 dimer complex","organismName":"Mus musculus; 10090","description":"Part of the intermediate filaments of the cytoskeleton. Mostly found in skin.","predictedComplex":false,"interactors":[{"ac":"EBI-646288","identifier":"P02535","identifierLink":"https://www.uniprot.org/uniprotkb/P02535/entry","name":"Krt10","description":"Keratin, type I cytoskeletal 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-646772","identifier":"P04104","identifierLink":"https://www.uniprot.org/uniprotkb/P04104/entry","name":"Krt1","description":"Keratin, type II cytoskeletal 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45616","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5881","complexName":"Endoplasmic reticulum membrane complex, EMC9 variant","organismName":"Homo sapiens; 9606","description":"Insertase complex required for the post-translational integration of tail-anchored proteins and co-translational insertion of some multi-pass membrane proteins into the endoplasmic reticulum membrane. The complex reduces the energetic cost of insertion by inducing a local thinning of the membrane by approximately 10A, thus decreasing the distance that a substrate's soluble lumenal domain must travel through the hydrophobic bilayer, and also by creating a positively charged patch in the bilayer.","predictedComplex":false,"interactors":[{"ac":"EBI-1044442","identifier":"Q8N766","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N766/entry","name":"EMC1","description":"ER membrane protein complex subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21573","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1054670","identifier":"Q9P0I2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P0I2/entry","name":"EMC3","description":"ER membrane protein complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13116","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11284388","identifier":"Q5UCC4","identifierLink":"https://www.uniprot.org/uniprotkb/Q5UCC4/entry","name":"EMC10","description":"ER membrane protein complex subunit 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21397","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2814031","identifier":"Q5J8M3","identifierLink":"https://www.uniprot.org/uniprotkb/Q5J8M3/entry","name":"EMC4","description":"ER membrane protein complex subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19315","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2820492","identifier":"Q9BV81","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BV81/entry","name":"EMC6","description":"ER membrane protein complex subunit 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20994","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359031","identifier":"Q15006","identifierLink":"https://www.uniprot.org/uniprotkb/Q15006/entry","name":"EMC2","description":"ER membrane protein complex subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12760","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6163737","identifier":"Q8N4V1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N4V1/entry","name":"MMGT1","description":"ER membrane protein complex subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21181","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6309137","identifier":"Q9NPA0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPA0/entry","name":"EMC7","description":"Endoplasmic reticulum membrane protein complex subunit 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13605","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-748366","identifier":"Q9Y3B6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3B6/entry","name":"EMC9","description":"ER membrane protein complex subunit 9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12941","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5882","complexName":"Endoplasmic reticulum membrane complex, EMC8 variant","organismName":"Mus musculus; 10090","description":"Insertase complex required for the post-translational integration of tail-anchored proteins and co-translational insertion of some multi-pass membrane proteins into the endoplasmic reticulum membrane. The complex reduces the energetic cost of insertion by inducing a local thinning of the membrane by approximately 10A, thus decreasing the distance that a substrate's soluble lumenal domain must travel through the hydrophobic bilayer, and also by creating a positively charged patch in the bilayer.","predictedComplex":false,"interactors":[{"ac":"EBI-11121115","identifier":"Q9CQW0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQW0/entry","name":"Emc6","description":"ER membrane protein complex subunit 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR20994","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11516104","identifier":"Q9CZX9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CZX9/entry","name":"Emc4","description":"ER membrane protein complex subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR19315","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25638630","identifier":"Q3TAS6","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TAS6/entry","name":"Emc10","description":"ER membrane protein complex subunit 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21397","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25638656","identifier":"O70378","identifierLink":"https://www.uniprot.org/uniprotkb/O70378/entry","name":"Emc8","description":"ER membrane protein complex subunit 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12941","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-776290","identifier":"Q8C7X2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C7X2/entry","name":"Emc1","description":"ER membrane protein complex subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21573","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-776295","identifier":"Q9CRD2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CRD2/entry","name":"Emc2","description":"ER membrane protein complex subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12760","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8369868","identifier":"Q99KI3","identifierLink":"https://www.uniprot.org/uniprotkb/Q99KI3/entry","name":"Emc3","description":"ER membrane protein complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13116","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8429427","identifier":"Q9EP72","identifierLink":"https://www.uniprot.org/uniprotkb/Q9EP72/entry","name":"Emc7","description":"Endoplasmic reticulum membrane protein complex subunit 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13605","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8587133","identifier":"Q8K273","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K273/entry","name":"Mmgt1","description":"ER membrane protein complex subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21181","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5883","complexName":"Endoplasmic reticulum membrane complex, EMC9 variant","organismName":"Mus musculus; 10090","description":"Insertase complex required for the post-translational integration of tail-anchored proteins and co-translational insertion of some multi-pass membrane proteins into the endoplasmic reticulum membrane. The complex reduces the energetic cost of insertion by inducing a local thinning of the membrane by approximately 10A, thus decreasing the distance that a substrate's soluble lumenal domain must travel through the hydrophobic bilayer, and also by creating  a positively charged patch in the bilayer.","predictedComplex":false,"interactors":[{"ac":"EBI-11121115","identifier":"Q9CQW0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQW0/entry","name":"Emc6","description":"ER membrane protein complex subunit 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR20994","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11516104","identifier":"Q9CZX9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CZX9/entry","name":"Emc4","description":"ER membrane protein complex subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR19315","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25638630","identifier":"Q3TAS6","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TAS6/entry","name":"Emc10","description":"ER membrane protein complex subunit 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21397","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-776290","identifier":"Q8C7X2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C7X2/entry","name":"Emc1","description":"ER membrane protein complex subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21573","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-776295","identifier":"Q9CRD2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CRD2/entry","name":"Emc2","description":"ER membrane protein complex subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12760","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8366432","identifier":"Q9DB76","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DB76/entry","name":"Emc9","description":"ER membrane protein complex subunit 9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12941","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8369868","identifier":"Q99KI3","identifierLink":"https://www.uniprot.org/uniprotkb/Q99KI3/entry","name":"Emc3","description":"ER membrane protein complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13116","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8429427","identifier":"Q9EP72","identifierLink":"https://www.uniprot.org/uniprotkb/Q9EP72/entry","name":"Emc7","description":"Endoplasmic reticulum membrane protein complex subunit 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13605","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8587133","identifier":"Q8K273","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K273/entry","name":"Mmgt1","description":"ER membrane protein complex subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21181","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5884","complexName":"Flagellar motor stator complex","organismName":"Escherichia coli (strain K12); 83333","description":"Transmembrane unit of the flagellar motor which conducts protons and exerts force on the rotor. Each core rotor complex (CPX-1082/CPX-1085) is typically surrounded by 10 stator complexes, each of which can independently produce torque for flagellar rotation.","predictedComplex":false,"interactors":[{"ac":"EBI-1117399","identifier":"P0AF06","identifierLink":"https://www.uniprot.org/uniprotkb/P0AF06/entry","name":"motB","description":"Motility protein B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30329","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-557926","identifier":"P09348","identifierLink":"https://www.uniprot.org/uniprotkb/P09348/entry","name":"motA","description":"Motility protein A","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30433","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5885","complexName":"Flagellar export complex","organismName":"Escherichia coli (strain K12); 83333","description":"A type III protein export apparatus that transports the rod, hook and filament axial component proteins from the cytoplasm to the distal end of the growing flagellar structure. The transmembrane export gate (flhA, flhB, fliP, fliQ and fliR) acts as a proton-protein antiporter to couple an inward-directed proton translocation with an outward-directed protein export. fliH, fliI and fliJ form a cytoplasmic ATPase ring which hydrolyzes ATP to activate the export gate.","predictedComplex":false,"interactors":[{"ac":"EBI-1118363","identifier":"P52612","identifierLink":"https://www.uniprot.org/uniprotkb/P52612/entry","name":"fliI","description":"Flagellum-specific ATP synthase","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR15184","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1126536","identifier":"P31068","identifierLink":"https://www.uniprot.org/uniprotkb/P31068/entry","name":"fliH","description":"Flagellar assembly protein FliH","stochiometry":"minValue: 12, maxValue: 12","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34982","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1130699","identifier":"P76298","identifierLink":"https://www.uniprot.org/uniprotkb/P76298/entry","name":"flhA","description":"Flagellar biosynthesis protein FlhA","stochiometry":"minValue: 9, maxValue: 9","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30161","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2369483","identifier":"P0AC07","identifierLink":"https://www.uniprot.org/uniprotkb/P0AC07/entry","name":"fliQ","description":"Flagellar biosynthetic protein FliQ","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2369538","identifier":"P76299","identifierLink":"https://www.uniprot.org/uniprotkb/P76299/entry","name":"flhB","description":"Flagellar biosynthetic protein FlhB","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30531","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2370160","identifier":"P22586","identifierLink":"https://www.uniprot.org/uniprotkb/P22586/entry","name":"fliO","description":"Flagellar protein FliO","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR38766","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2370407","identifier":"P33135","identifierLink":"https://www.uniprot.org/uniprotkb/P33135/entry","name":"fliR","description":"Flagellar biosynthetic protein FliR","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30065","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25640564","identifier":"P0AC05","identifierLink":"https://www.uniprot.org/uniprotkb/P0AC05/entry","name":"fliP","description":"Flagellar biosynthetic protein FliP","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30587","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-554036","identifier":"P52613","identifierLink":"https://www.uniprot.org/uniprotkb/P52613/entry","name":"fliJ","description":"Flagellar FliJ protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR38786","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5887","complexName":"Flagellar basal-body rod complex","organismName":"Escherichia coli (strain K12); 83333","description":"Acts as a drive shaft to transmit torque to the hook which then allows the synchronous rotation of multiple flagellar filaments. The 7nm diameter proximal rod penetrates into the MS-ring formed by fliF (P25798). The distal rod, with a diameter of 13 nm, is surrounded by the lipoprotein L and P rings, formed by lipoprotein flgH (P0A6S0) and periplasmic protein flgI (P0A6S3), respectively. The L and P rings may protect the structure from shearing forces during rotation.","predictedComplex":false,"interactors":[{"ac":"EBI-1113873","identifier":"P0ABX2","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABX2/entry","name":"flgC","description":"Flagellar basal-body rod protein FlgC","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30435","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1121976","identifier":"P0ABW9","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABW9/entry","name":"flgB","description":"Flagellar basal body rod protein FlgB","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30435","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1122044","identifier":"P75938","identifierLink":"https://www.uniprot.org/uniprotkb/P75938/entry","name":"flgF","description":"Flagellar basal-body rod protein FlgF","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30435","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1122074","identifier":"P0ABX5","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABX5/entry","name":"flgG","description":"Flagellar basal-body rod protein FlgG","stochiometry":"minValue: 24, maxValue: 24","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30435","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2370099","identifier":"P0A8T5","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8T5/entry","name":"fliE","description":"Flagellar hook-basal body complex protein FliE","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34653","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5888","complexName":"ygaZH putative valine exporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"Putative transmembrane exporter of branched chain amino acids, such as L-valine ( 2-amino-3-methylbutanoic acid) .","predictedComplex":false,"interactors":[{"ac":"EBI-25640940","identifier":"P76630","identifierLink":"https://www.uniprot.org/uniprotkb/P76630/entry","name":"ygaZ","description":"Inner membrane protein YgaZ","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34979","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25640955","identifier":"P43667","identifierLink":"https://www.uniprot.org/uniprotkb/P43667/entry","name":"ygaH","description":"Uncharacterized protein YgaH","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]}]},{"complexAC":"CPX-5890","complexName":"Translocation and assembly module complex","organismName":"Escherichia coli (strain K12); 83333","description":"A two-membrane spanning complex required for the proper assembly of a subset of autotransporters, outer membrane proteins which either expose on the cell surface or release into the extracellular space an effector passenger domain which is responsible for an associated virulence function.","predictedComplex":false,"interactors":[{"ac":"EBI-1114298","identifier":"P0ADE4","identifierLink":"https://www.uniprot.org/uniprotkb/P0ADE4/entry","name":"tamA","description":"Translocation and assembly module subunit TamA","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR12815","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1117885","identifier":"P39321","identifierLink":"https://www.uniprot.org/uniprotkb/P39321/entry","name":"tamB","description":"Translocation and assembly module subunit TamB","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR36985","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5892","complexName":"PspBC inner membrane stress response complex","organismName":"Escherichia coli (strain K12); 83333","description":"Stress-responsive regulatory switch, which responds to membrane stresses, such as the mislocalisation of proteins to the inner membrane. Stress-induced alteration in its properties appears to lead to recruitment of pspA (P0AFM6), enabling at least a partial release of pspA from pspF (P37344) in the pspAF transcription regulation complex (CPX-5745). This allows transcription of the Psp membrane-stabilizing system through binding of pspF to the sigma factor rpoN (P24255).","predictedComplex":false,"interactors":[{"ac":"EBI-1134561","identifier":"P0AFN2","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFN2/entry","name":"pspC","description":"Phage shock protein C","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33885","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6408513","identifier":"P0AFM9","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFM9/entry","name":"pspB","description":"Phage shock protein B","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]}]},{"complexAC":"CPX-5893","complexName":"Alternative pathway fluid-phase C3 convertase complex C3(H2O)Bb","organismName":"Mus musculus; 10090","description":"A serine-type endopeptidase complex of the alternative pathway of complement activation of the innate immune system. Cleaves Complement C3 precurser (P01027) into anaphylatoxin C3A (P01027-PRO_0000005920) and nascent convertase core-component C3b (CPX-988). Restricted to the fluid-phase. \r\n\r\nC3(H2O)Bb convertase is very unstable and readily inactivated by Factor H (P06909) thus regulating the amount of spontaneously available C3 convertase initiating the alternative pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-12739639","identifier":"P01027-PRO_0000005918","identifierLink":"https://www.uniprot.org/uniprotkb/P01027-PRO_0000005918/entry","name":"C3","description":"Complement C3 beta chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-25642947","identifier":"P04186-PRO_0000027550","identifierLink":"https://www.uniprot.org/uniprotkb/P04186-PRO_0000027550/entry","name":"Cfb","description":"Complement factor B Bb","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-25642954","identifier":"P01027-PRO_0000005919","identifierLink":"https://www.uniprot.org/uniprotkb/P01027-PRO_0000005919/entry","name":"C3","description":"Complement C3 alpha chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-5894","complexName":"Alternative pathway C3 convertase complex C3bBb","organismName":"Mus musculus; 10090","description":"A serine-type endopeptidase complex of the alternative pathway of complement activation of the innate immune system. Cleaves Complement C3 precurser (P01027) into anaphylatoxin C3A (P01027-PRO_0000005920) and nascent core-convertase component C3b (CPX-988). Occurs in the fluid-phase and binds host and pathogen cells. \r\n\r\nC3bBb convertase is unstable. In fluid-phase or when bound to the host cell it is readily inactivated by Factor H (P06909) thus preventing autoimmune activation.","predictedComplex":false,"interactors":[{"ac":"EBI-12739605","identifier":"CPX-988","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-988","name":"Complement C3b complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-25642947","identifier":"P04186-PRO_0000027550","identifierLink":"https://www.uniprot.org/uniprotkb/P04186-PRO_0000027550/entry","name":"Cfb","description":"Complement factor B Bb","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-5895","complexName":"Alternative pathway solid-phase C5 convertase complex C3bBbC3b","organismName":"Mus musculus; 10090","description":"A serine-type endopeptidase complex of the alternative pathway of complement activation of the innate immune system. Cleaves Complement C5 precurser (P06684) into anaphylatoxin C5a (P06684-PRO_0000005994) and Complement C5b (P06684-PRO_0000005991, P06684-PRO_0000005995). Binds host and pathogen cells via its reactive thioester moiety. \r\n\r\nC3bBbC3b convertase is more stable than C3bBb convertase (CPX-5894). When bound to the host cell it is readily inactivated by Factor H (P06909) thus preventing autoimmune activation. \r\n\r\nCombines with C5b, C6 (E9Q6D8), C7 (D3YXF5), C8A (Q8K182), C8B (Q8BH35) & C8G (Q8VCG4) and C9 (P06683) to form the Membrane Attack Complex (CPX-6159).","predictedComplex":false,"interactors":[{"ac":"EBI-12739605","identifier":"CPX-988","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-988","name":"Complement C3b complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-25642960","identifier":"CPX-5894","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-5894","name":"Alternative pathway C3 convertase complex C3bBb","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-5896","complexName":"Alternative pathway pathogen cell-bound C3 convertase complex C3bBbP","organismName":"Mus musculus; 10090","description":"A serine-type endopeptidase complex of the alternative pathway of complement activation of the innate immune system. Cleaves Complement C3 precurser (P01027) into anaphylatoxin C3A (P01027-PRO_0000005920) and nascent convertase core-component C3b (CPX-988). Only occurs bound to pathogen cells and binds to target cells via its reactive thioester moiety. \r\n\r\nProperdin-binding stablises C3bBb convertase (CPX-5894) and prevents its inactivation by Factor H (P06909).","predictedComplex":false,"interactors":[{"ac":"EBI-15183907","identifier":"P11680","identifierLink":"https://www.uniprot.org/uniprotkb/P11680/entry","name":"Cfp","description":"Properdin","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22906","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25642960","identifier":"CPX-5894","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-5894","name":"Alternative pathway C3 convertase complex C3bBb","description":null,"stochiometry":"minValue: 1, maxValue: 5","interactorType":"stable complex","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-5897","complexName":"Alternative pathway pathogen cell-bound C5 convertase complex C3bBbC3bP","organismName":"Mus musculus; 10090","description":"A serine-type endopeptidase complex of the alternative pathway of complement activation of the innate immune system. Cleaves Complement C5 precurser (P06684) into anaphylatoxin C5a (P06684-PRO_0000005994) and Complement C5b (P06684-PRO_0000005991, P06684-PRO_0000005995). Only occurs bound to pathogen cells and to target cells via its reactive thioester moiety. \r\n\r\nProperdin-binding stablises C3bBbC3b convertase (CPX-5895) and prevents its inactivation by Factor H (P06909). \r\n\r\nFollowing properdin dissociation the complex combines with C5b, C6 (E9Q6D8), C7 (D3YXF5), C8A (Q8K182), C8B (Q8BH35) & C8G (Q8VCG4) and C9 (P06683) to form the Membrane Attack Complex (CPX-6159).","predictedComplex":false,"interactors":[{"ac":"EBI-12739605","identifier":"CPX-988","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-988","name":"Complement C3b complex","description":null,"stochiometry":"minValue: 1, maxValue: 5","interactorType":"stable complex","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-15183907","identifier":"P11680","identifierLink":"https://www.uniprot.org/uniprotkb/P11680/entry","name":"Cfp","description":"Properdin","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22906","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25642960","identifier":"CPX-5894","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-5894","name":"Alternative pathway C3 convertase complex C3bBb","description":null,"stochiometry":"minValue: 1, maxValue: 5","interactorType":"stable complex","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-5898","complexName":"bolA-grxD iron-sulfur cluster assembly complex","organismName":"Escherichia coli (strain K12); 83333","description":"Reversibly bind Fe-S clusters and appear to play a role in Fe-S cluster assembly and trafficking, and in transferring an intact Fe-S cluster to an apo acceptor protein.","predictedComplex":false,"interactors":[{"ac":"EBI-10824516","identifier":"CHEBI:16856","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16856","name":"glutathione","description":"glutathione","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-25647592","identifier":"CHEBI:33737","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:33737","name":"di-mu-sulfido-diiron(2+)","description":"di-mu-sulfido-diiron(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-545774","identifier":"P0ABE2","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABE2/entry","name":"bolA","description":"DNA-binding transcriptional regulator BolA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR46229","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-545828","identifier":"P0AC69","identifierLink":"https://www.uniprot.org/uniprotkb/P0AC69/entry","name":"grxD","description":"Glutaredoxin 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10293","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5899","complexName":"ibaG-grxD iron-sulfur cluster assembly complex","organismName":"Escherichia coli (strain K12); 83333","description":"Implicated in Fe-S cluster assembly and trafficking, transferring an intact Fe-S cluster to an apo acceptor protein. CGFS-type Grxs form [2Fe-2S]-bridged homodimers with the active site cysteines and two GSH molecules ligating the Fe-S cluster.","predictedComplex":false,"interactors":[{"ac":"EBI-10824516","identifier":"CHEBI:16856","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16856","name":"glutathione","description":"glutathione","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1131877","identifier":"P0A9W6","identifierLink":"https://www.uniprot.org/uniprotkb/P0A9W6/entry","name":"ibaG","description":"Acid stress protein IbaG","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR46229","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25647592","identifier":"CHEBI:33737","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:33737","name":"di-mu-sulfido-diiron(2+)","description":"di-mu-sulfido-diiron(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-545828","identifier":"P0AC69","identifierLink":"https://www.uniprot.org/uniprotkb/P0AC69/entry","name":"grxD","description":"Glutaredoxin 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10293","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5900","complexName":"CD94-NKG2A natural killer receptor complex","organismName":"Mus musculus; 10090","description":"C-type lectin inhibitory receptor present on natural killer (NK) cells and a subset of T cells. Binds the HLA-E class I histocompatibility antigen molecule, specifically the peptide-bound HLA-E-B2M heterotrimeric complex, resulting in a suppression of the activation of signaling processes and the inhibition of NK cell-mediated cytolysis. The interaction of CD94-NKG2A with HLA-E is a central mechanism by which NK cells indirectly monitor the expression of other MHC class I molecules within a target cell.","predictedComplex":false,"interactors":[{"ac":"EBI-25647975","identifier":"O54707","identifierLink":"https://www.uniprot.org/uniprotkb/O54707/entry","name":"Klrd1","description":"Natural killer cells antigen CD94","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25648001","identifier":"Q9Z202","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z202/entry","name":"Klrc1","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5901","complexName":"CD94-NKG2C natural killer receptor complex","organismName":"Homo sapiens; 9606","description":"C-type lectin inhibitory receptor present on natural killer (NK) cells and a subset of T cells. Binds the HLA-E class I histocompatibility antigen molecule,specifically the peptide-bound HLA-E-B2M heterotrimeric complex with relatively low affinity, potentially resulting in activation of signaling processes and the activation of NK cell-mediated cytolysis.","predictedComplex":false,"interactors":[{"ac":"EBI-3862171","identifier":"P26717","identifierLink":"https://www.uniprot.org/uniprotkb/P26717/entry","name":"KLRC2","description":"NKG2-C type II integral membrane protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9018174","identifier":"Q13241","identifierLink":"https://www.uniprot.org/uniprotkb/Q13241/entry","name":"KLRD1","description":"Natural killer cells antigen CD94","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5902","complexName":"CD94-NKG2C natural killer receptor complex","organismName":"Mus musculus; 10090","description":"C-type lectin inhibitory receptor present on natural killer (NK) cells and a subset of T cells. Binds the HLA-E class I histocompatibility antigen molecule,specifically the peptide-bound HLA-E-B2M heterotrimeric complex with relatively low affinity, potentially resulting in activation of signaling processes and the activation of NK cell-mediated cytolysis.","predictedComplex":false,"interactors":[{"ac":"EBI-25647975","identifier":"O54707","identifierLink":"https://www.uniprot.org/uniprotkb/O54707/entry","name":"Klrd1","description":"Natural killer cells antigen CD94","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25648102","identifier":"Q9WTJ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WTJ9/entry","name":"Klrc2","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5903","complexName":"CD94-NKG2E natural killer receptor complex","organismName":"Homo sapiens; 9606","description":"C-type lectin inhibitory receptor present on natural killer (NK) cells and a subset of T cells. Binds the HLA-E class I histocompatibility antigen molecule,specifically the peptide-bound HLA-E-B2M heterotrimeric complex potentially resulting in activation of signaling processes and the activation of NK cell-mediated cytolysis.","predictedComplex":false,"interactors":[{"ac":"EBI-2862730","identifier":"Q07444","identifierLink":"https://www.uniprot.org/uniprotkb/Q07444/entry","name":"KLRC3","description":"NKG2-E type II integral membrane protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9018174","identifier":"Q13241","identifierLink":"https://www.uniprot.org/uniprotkb/Q13241/entry","name":"KLRD1","description":"Natural killer cells antigen CD94","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5904","complexName":"CD94-NKG2E natural killer receptor complex","organismName":"Mus musculus; 10090","description":"C-type lectin inhibitory receptor present on natural killer (NK) cells and a subset of T cells. Binds the HLA-E class I histocompatibility antigen molecule,specifically the peptide-bound HLA-E-B2M heterotrimeric complex potentially resulting in activation of signaling processes and the activation of NK cell-mediated cytolysis.","predictedComplex":false,"interactors":[{"ac":"EBI-25647975","identifier":"O54707","identifierLink":"https://www.uniprot.org/uniprotkb/O54707/entry","name":"Klrd1","description":"Natural killer cells antigen CD94","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25648185","identifier":"Q9QXN7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9QXN7/entry","name":"Klrc3","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5906","complexName":"CcdB-poisoned gyrase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Prevents the formation of the GyrA-GyrB DNA Gyrase complex (CPX-2177) by both inhibiting free gyrase and stabilizing covalent gyrase:DNA intermediates in a conformation such that the gyrase A subunit is covalently closed to the cleaved DNA. This results in DNA strand breakage, inhibition of cell proliferation and cell death.","predictedComplex":false,"interactors":[{"ac":"EBI-25647730","identifier":"P62554","identifierLink":"https://www.uniprot.org/uniprotkb/P62554/entry","name":"ccdB","description":"Toxin CcdB","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-547129","identifier":"P0AES4","identifierLink":"https://www.uniprot.org/uniprotkb/P0AES4/entry","name":"gyrA","description":"DNA gyrase subunit A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43493","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5908","complexName":"CcdAB toxin-antitoxin complex","organismName":"Escherichia coli (strain K12); 83333","description":"Type II toxin-antitoxin (TA) system formed by the toxin (ccdB), and the antitoxin (ccdA). TA systems act as effectors of dormancy and persistence, with the toxin causing growth arrest by interfering with a vital cellular process, such as transcription, translation or DNA replication, and the cognate antitoxin neutralizing the toxin activity during normal growth conditions. Formation of this complex dissociates the CcdB-poisoned gyrase complex (CPX-5906) in a process called rejuvenation. The CcdAB complex also acts as a repressor of the ccd operon.","predictedComplex":false,"interactors":[{"ac":"EBI-25647704","identifier":"P62552","identifierLink":"https://www.uniprot.org/uniprotkb/P62552/entry","name":"ccdA","description":"Antitoxin CcdA","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-25647730","identifier":"P62554","identifierLink":"https://www.uniprot.org/uniprotkb/P62554/entry","name":"ccdB","description":"Toxin CcdB","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]}]},{"complexAC":"CPX-5909","complexName":"Replication restart primosome complex, priAC variant","organismName":"Escherichia coli (strain K12); 83333","description":"Required for the restart of replication at sites of premature termination of DNA replication which leaves collapsed/abandoned replication forks that would otherwise create double-strand DNA breaks (DSBs) on the next round of replication. Serves to reload the replicative helicase dnaB on sites far removed from the origin of replication in a DNA structure-dependent manner. priA binds single-stranded, double-stranded and forked DNA with high affinity. priC binds ssDNA, preferentially associating with replication forks that include at least 7 nucleotide gaps between the nascent leading strand and replication fork. The dnaB-dnaC complex (CPX-1934) is recruited to the primosome, possibly through direct contacts with dnaT and the dnaB is loaded from dnaB-dnaC onto ssDNA on the lagging strand template. Recruitment of dnaG allows RNA primer synthesis from which the polymerase III holoenzyme can synthesize a nascent lagging strand.","predictedComplex":false,"interactors":[{"ac":"EBI-1117383","identifier":"P23862","identifierLink":"https://www.uniprot.org/uniprotkb/P23862/entry","name":"priC","description":"Replication restart protein PriC","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-548978","identifier":"P0ACB0","identifierLink":"https://www.uniprot.org/uniprotkb/P0ACB0/entry","name":"dnaB","description":"Replicative DNA helicase DnaB","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30153","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549012","identifier":"P0AEF0","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEF0/entry","name":"dnaC","description":"Replicative helicase loader DnaC","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549259","identifier":"P0ABS5","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABS5/entry","name":"dnaG","description":"DNA primase","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30313","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549621","identifier":"P0A8J2","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8J2/entry","name":"dnaT","description":"Replication restart protein DnaT","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-552050","identifier":"P17888","identifierLink":"https://www.uniprot.org/uniprotkb/P17888/entry","name":"priA","description":"Replication restart protein PriA","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30580","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5910","complexName":"Replication restart primosome complex, priAB variant","organismName":"Escherichia coli (strain K12); 83333","description":"Required for the restart of replication at sites of premature termination of DNA replication which leaves collapsed/abandoned replication forks that would otherwise create double-strand DNA breaks (DSBs) on the next round of replication. Serves to reload the replicative helicase dnaB on sites far removed from the origin of replication in a DNA structure-dependent manner.The PriA-PriB variant appears to be the dominant restart mechanism in E.coli, with priA binding single-stranded, double-stranded and forked DNA with high affinity. PriB appears to be important for restart following DNA recombination. On binding, priA undergoes a conformational change, exposing the priB binding site. The priA:priB:DNA ternary interaction stabilizes priA on the DNA and enhances its helicase activity, facilitating unwinding of the nascent lagging strand if one is present. dnaT is recruited to the priA:priB:DNA ternary complex which leads to release of ssDNA by priB. The dnaB-dnaC complex (CPX-1934) is recruited to the primosome, possibly through direct contacts with dnaT and the dnaB is loaded from dnaB-dnaC onto ssDNA on the lagging strand template. Recruitment of dnaG allows RNA primer synthesis from which the polymerase III holoenzyme can synthesize a nascent lagging strand.","predictedComplex":false,"interactors":[{"ac":"EBI-1125223","identifier":"P07013","identifierLink":"https://www.uniprot.org/uniprotkb/P07013/entry","name":"priB","description":"Replication restart protein PriB","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-548978","identifier":"P0ACB0","identifierLink":"https://www.uniprot.org/uniprotkb/P0ACB0/entry","name":"dnaB","description":"Replicative DNA helicase DnaB","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30153","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549012","identifier":"P0AEF0","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEF0/entry","name":"dnaC","description":"Replicative helicase loader DnaC","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549259","identifier":"P0ABS5","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABS5/entry","name":"dnaG","description":"DNA primase","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30313","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549621","identifier":"P0A8J2","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8J2/entry","name":"dnaT","description":"Replication restart protein DnaT","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-552050","identifier":"P17888","identifierLink":"https://www.uniprot.org/uniprotkb/P17888/entry","name":"priA","description":"Replication restart protein PriA","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30580","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5911","complexName":"Replication restart primosome complex, priC-rep variant","organismName":"Escherichia coli (strain K12); 83333","description":"Required for the restart of replication at sites of premature termination of DNA replication which leaves collapsed/abandoned replication forks that would otherwise create double-strand DNA breaks (DSBs) on the next round of replication. Serves to reload the replicative helicase dnaB on sites far removed from the origin of replication in a DNA structure-dependent manner. On replication forks lacking nascent leading and lagging strands priC is sufficient to load dnaB from the DnaB-DnaC complex (CPX-1934) in the absence of any other restart proteins but appears to require the rep helicase to create single-stranded DNA on the lagging strand for restart pathway progression or to remove nascent lagging strand DNA to enable priC-mediated loading of dnaB. Recruitment of dnaG allows RNA primer synthesis from which the polymerase III holoenzyme can synthesize a nascent lagging strand.","predictedComplex":false,"interactors":[{"ac":"EBI-1117383","identifier":"P23862","identifierLink":"https://www.uniprot.org/uniprotkb/P23862/entry","name":"priC","description":"Replication restart protein PriC","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-548978","identifier":"P0ACB0","identifierLink":"https://www.uniprot.org/uniprotkb/P0ACB0/entry","name":"dnaB","description":"Replicative DNA helicase DnaB","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30153","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549012","identifier":"P0AEF0","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEF0/entry","name":"dnaC","description":"Replicative helicase loader DnaC","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549259","identifier":"P0ABS5","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABS5/entry","name":"dnaG","description":"DNA primase","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30313","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6558011","identifier":"P09980","identifierLink":"https://www.uniprot.org/uniprotkb/P09980/entry","name":"rep","description":"ATP-dependent DNA helicase Rep","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11070","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5912","complexName":"L-tartrate dehydratase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Oxygen-labile stereospecific enzyme which participates in glyoxylate and dicarboxylate metabolism by catalysing the breakdown of (R,R)-tartrate to oxaloacetate and H2O.","predictedComplex":false,"interactors":[{"ac":"EBI-1113137","identifier":"P05847","identifierLink":"https://www.uniprot.org/uniprotkb/P05847/entry","name":"ttdA","description":"L(+)-tartrate dehydratase subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30389","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1129625","identifier":"P0AC35","identifierLink":"https://www.uniprot.org/uniprotkb/P0AC35/entry","name":"ttdB","description":"L(+)-tartrate dehydratase subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880384","identifier":"CHEBI:30408","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30408","name":"fe-s cluster","description":"iron-sulfur cluster","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1945","complexName":"Regulatory inactivation of dnaA (RIDA) complex","organismName":"Escherichia coli (strain K12); 83333","description":"Regulatory role in DNA replication. dnaA-ATP-hydrolysis at oriC results in replication initiation. Formation of the RIDA complex promotes the hydrolysis of ATP bound to dnaA. The resultant ADP–dnaA is inactive in initiation.","predictedComplex":false,"interactors":[{"ac":"EBI-1108845","identifier":"CHEBI:15422","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15422","name":"atp","description":"ATP","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-542385","identifier":"P0A988","identifierLink":"https://www.uniprot.org/uniprotkb/P0A988/entry","name":"dnaN","description":"Beta sliding clamp","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30478","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-545453","identifier":"P69931","identifierLink":"https://www.uniprot.org/uniprotkb/P69931/entry","name":"hda","description":"DnaA regulatory inactivator Hda","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-548951","identifier":"P03004","identifierLink":"https://www.uniprot.org/uniprotkb/P03004/entry","name":"dnaA","description":"Chromosomal replication initiator protein DnaA","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5941","complexName":"Fructose-specific enzyme II complex","organismName":"Escherichia coli (strain K12); 83333","description":"Involved in the transport of fructose across the cell membrane as part of the phosphoenolpyruvate:sugar phosphotransferase system (PTS). The fructose-specific PTS has no requirement for hpr/ptsH (P0AA04), fruB combines a IIA domain with a HPr domain. fruA contains a duplicated EIIB domain (EIIB' domain) in the N-terminal which lacks the active site and functions to facilitate phosphoryl transfer between the EIIA domain of diphosphoryl transfer protein (DTP) and the EIIB domain.","predictedComplex":false,"interactors":[{"ac":"EBI-1124430","identifier":"P20966","identifierLink":"https://www.uniprot.org/uniprotkb/P20966/entry","name":"fruA","description":"PTS system fructose-specific EIIB'BC component","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30505","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-557233","identifier":"P69811","identifierLink":"https://www.uniprot.org/uniprotkb/P69811/entry","name":"fruB","description":"Multiphosphoryl transfer protein","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30181","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5942","complexName":"Galactitol-specific enzyme II complex","organismName":"Escherichia coli (strain K12); 83333","description":"Involved in the transport of galactitol and D-glucitol across the cell membrane as part of the phosphoenolpyruvate:sugar phosphotransferase system (PTS). A phosphoryl group is transferred from hpr (P0AA04) to gatA (IIA), from gatA to chbgatB (IIB) and finally from gatB onto the incoming sugar bound to membrane-embedded gatC (IIC).","predictedComplex":false,"interactors":[{"ac":"EBI-25691684","identifier":"P69831","identifierLink":"https://www.uniprot.org/uniprotkb/P69831/entry","name":"gatC","description":"PTS system galactitol-specific EIIC component","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR37324","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-550961","identifier":"P37188","identifierLink":"https://www.uniprot.org/uniprotkb/P37188/entry","name":"gatB","description":"PTS system galactitol-specific EIIB component","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-552766","identifier":"P69828","identifierLink":"https://www.uniprot.org/uniprotkb/P69828/entry","name":"gatA","description":"PTS system galactitol-specific EIIA component","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR47738","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5943","complexName":"Glucose-specific enzyme II complex","organismName":"Escherichia coli (strain K12); 83333","description":"Involved in the transport of glucose across the cell membrane as part of the phosphoenolpyruvate:sugar phosphotransferase system (PTS). A phosphoryl group is transferred from hpr (P0AA04) to ptsG (IIAGlc) and thence from IIAGlc to the C-terminal cytoplasmic domain of the glucose transporter crr/IICBGlc","predictedComplex":false,"interactors":[{"ac":"EBI-369856","identifier":"P69783","identifierLink":"https://www.uniprot.org/uniprotkb/P69783/entry","name":"crr","description":"PTS system glucose-specific EIIA component","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR45008","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-903497","identifier":"P69786","identifierLink":"https://www.uniprot.org/uniprotkb/P69786/entry","name":"ptsG","description":"PTS system glucose-specific EIICB component","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30009","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5961","complexName":"Mitochondrial calcium uniporter complex, MICU1-MICU2 variant","organismName":"Homo sapiens; 9606","description":"Highly selective, inward-rectifying Ca2+ channel located on the inner mitochondrial membrane. The uniporter is quiescent in resting cellular conditions and becomes activated only when local Ca2+ levels rise above approximately 1 microM with the MCU tetramer forming a calcium-conducting pore. Ca2+ uptake is driven by the large negative inner mitochondrial membrane potential generated by proton pumping into the intermembrane space by the electron transport chain. The stoichiometric ratio of MICU1/MCU/SMDT1 can vary between tissues, resulting in a tissue-specific activity profile that matches metabolic requirements.","predictedComplex":false,"interactors":[{"ac":"EBI-11908005","identifier":"Q9H4I9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H4I9/entry","name":"SMDT1","description":"Essential MCU regulator, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR33904","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2371996","identifier":"Q9BPX6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BPX6/entry","name":"MICU1","description":"Calcium uptake protein 1, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3197790","identifier":"Q8IYU8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IYU8/entry","name":"MICU2","description":"Calcium uptake protein 2, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6552124","identifier":"Q8NE86","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NE86/entry","name":"MCU","description":"Calcium uniporter protein, mitochondrial","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5963","complexName":"Mitochondrial calcium uniporter complex, MICU1 variant","organismName":"Homo sapiens; 9606","description":"Highly selective, inward-rectifying Ca2+ channel located on the inner mitochondrial membrane. The uniporter is quiescent in resting cellular conditions and becomes activated only when local Ca2+ levels rise above approximately 1 microM with the MCU tetramer forming a calcium-conducting pore. Ca2+ uptake is driven by the large negative inner mitochondrial membrane potential generated by proton pumping into the intermembrane space by the electron transport chain. The stoichiometric ratio of MICU1/MCU/SMDT1 can vary between tissues, resulting in a tissue-specific activity profile that matches metabolic requirements.","predictedComplex":false,"interactors":[{"ac":"EBI-11908005","identifier":"Q9H4I9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H4I9/entry","name":"SMDT1","description":"Essential MCU regulator, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR33904","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2371996","identifier":"Q9BPX6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BPX6/entry","name":"MICU1","description":"Calcium uptake protein 1, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6552124","identifier":"Q8NE86","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NE86/entry","name":"MCU","description":"Calcium uniporter protein, mitochondrial","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5965","complexName":"Mitochondrial calcium uniporter complex, MICU1-MICU3 variant","organismName":"Homo sapiens; 9606","description":"Highly selective, inward-rectifying Ca2+ channel located on the inner mitochondrial membrane. The uniporter is quiescent in resting cellular conditions and becomes activated only when local Ca2+ levels rise above approximately 1 microM with the MCU tetramer forming a calcium-conducting pore. Ca2+ uptake is driven by the large negative inner mitochondrial membrane potential generated by proton pumping into the intermembrane space by the electron transport chain. The stoichiometric ratio of MICU1/MCU/SMDT1 can vary between tissues, resulting in a tissue-specific activity profile that matches metabolic requirements. Neuron-specific MICU3 lowers the threshold of Ca2+-driven MCU activation enabling axonal mitochondria to respond to small elevations in cytoplasmic Ca2+ levels.","predictedComplex":false,"interactors":[{"ac":"EBI-11908005","identifier":"Q9H4I9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H4I9/entry","name":"SMDT1","description":"Essential MCU regulator, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR33904","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21798316","identifier":"Q86XE3","identifierLink":"https://www.uniprot.org/uniprotkb/Q86XE3/entry","name":"MICU3","description":"Calcium uptake protein 3, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2371996","identifier":"Q9BPX6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BPX6/entry","name":"MICU1","description":"Calcium uptake protein 1, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6552124","identifier":"Q8NE86","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NE86/entry","name":"MCU","description":"Calcium uniporter protein, mitochondrial","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3388","complexName":"Synaptonemal complex","organismName":"Caenorhabditis elegans; 6239","description":"Liquid crystalline structure that forms a large scaffold connecting homologous chromosomes from end to end during meiotic prophase I. Required for stabilising chromosome pairing and alignment, and for crossover events and chiasmata formation between homologous chromosome pairs.\r\n\r\nOnce assembly of the complex has been initiated, the ZHP heterodimers zhp-1-zhp-2 (CPX-5801) and zhp-3-zhp-4 (CPX-5802) are recruited to the complex to promote the accumulation of pro-crossover factors at a single recombination intermediate to drive accurate chromosome segregation.","predictedComplex":false,"interactors":[{"ac":"EBI-16011890","identifier":"Q95XC8","identifierLink":"https://www.uniprot.org/uniprotkb/Q95XC8/entry","name":"htp-2","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-16876660","identifier":"G5EGS8","identifierLink":"https://www.uniprot.org/uniprotkb/G5EGS8/entry","name":"syp-1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-16876674","identifier":"Q9N5K3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9N5K3/entry","name":"syp-4","description":"Synaptonemal complex protein 4","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-2413860","identifier":"O76388","identifierLink":"https://www.uniprot.org/uniprotkb/O76388/entry","name":"syp-2","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-25612337","identifier":"Q9N3E8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9N3E8/entry","name":"syp-5","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-314667","identifier":"G5EBG0","identifierLink":"https://www.uniprot.org/uniprotkb/G5EBG0/entry","name":"him-3","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-321572","identifier":"O62238","identifierLink":"https://www.uniprot.org/uniprotkb/O62238/entry","name":"syp-3","description":"Synaptonemal complex protein 3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-321751","identifier":"Q20305","identifierLink":"https://www.uniprot.org/uniprotkb/Q20305/entry","name":"htp-1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-322898","identifier":"O44741","identifierLink":"https://www.uniprot.org/uniprotkb/O44741/entry","name":"syp-6","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-323265","identifier":"O01820","identifierLink":"https://www.uniprot.org/uniprotkb/O01820/entry","name":"htp-3","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]}]},{"complexAC":"CPX-3401","complexName":"Interleukin-17-like receptor complex","organismName":"Caenorhabditis elegans; 6239","description":"Interleukin-17 (IL-17) related receptor complex, which upon activation acts as a modulator of neuronal activity. Binding of the ligand ilc-17.1 (Q22687) to the receptor complex triggers a signalling cascade that increases neuronal activity in RGM interneurons in response to input from oxygen-sensing neurons, and leads to increased animal movement and aggregation behaviour. Actl-1 (Q18008) may function as an adaptor for the complex to allow for further downstream signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-16877763","identifier":"Q9NA64","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NA64/entry","name":"ilcr-1","description":"Interleukin cytokine receptor-related protein 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR15583","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-327172","identifier":"Q10128","identifierLink":"https://www.uniprot.org/uniprotkb/Q10128/entry","name":"ilcr-2","description":"Interleukin cytokine receptor-related protein 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR15583","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3403","complexName":"DNA-dependent protein kinase complex","organismName":"Homo sapiens; 9606","description":"Serine/threonine-protein kinase complex, central to the nonhomologous end joining (NHEJ) DNA-repair pathway, which rejoins double-strand breaks. It is also required for V(D)J recombination, a process that utilizes NHEJ to promote immune system diversity. Directly impacts transcriptional regulation, in part potentially by phosphorylating the C-terminal domain of RNA polymerse II. The XRCC5/6 heterodimer binds ends of dsDNA and both recruits PRKDC to DNA double strand breaks and stimulates its kinase activity.","predictedComplex":false,"interactors":[{"ac":"EBI-352053","identifier":"P78527","identifierLink":"https://www.uniprot.org/uniprotkb/P78527/entry","name":"PRKDC","description":"DNA-dependent protein kinase catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-761759","identifier":"CPX-1993","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-1993","name":"Ku70:Ku80 complex","description":"Ku70:Ku80 heterodimer","stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-3424","complexName":"DNA-dependent protein kinase complex","organismName":"Mus musculus; 10090","description":"Serine/threonine-protein kinase complex, central to the nonhomologous end joining (NHEJ) DNA-repair pathway, which rejoins double-strand breaks. It is also required for V(D)J recombination, a process that utilizes NHEJ to promote immune system diversity. Directly impacts transcriptional regulation, in part potentially by phosphorylating the C-terminal domain of RNA polymerse II. The XRCC5/6 heterodimer binds ends of dsDNA and both recruits PRKDC to DNA double strand breaks and stimulates its kinase activity.","predictedComplex":false,"interactors":[{"ac":"EBI-2272005","identifier":"P97313","identifierLink":"https://www.uniprot.org/uniprotkb/P97313/entry","name":"Prkdc","description":"DNA-dependent protein kinase catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-822783","identifier":"CPX-2047","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-2047","name":"Ku70:Ku80 complex","description":"Ku70:Ku80 heterodimer","stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-3445","complexName":"Twin-arginine translocation complex","organismName":"Escherichia coli (strain K12); 83333","description":"Proton motive force dependent transporter of folded precursor proteins containing a SRRxFLK (TAT) sequence motif in the N-terminal part of their signal sequences across the cytoplasmic membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-1112947","identifier":"P0A843","identifierLink":"https://www.uniprot.org/uniprotkb/P0A843/entry","name":"tatE","description":"Sec-independent protein translocase protein TatE","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42982","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4411542","identifier":"P69428","identifierLink":"https://www.uniprot.org/uniprotkb/P69428/entry","name":"tatA","description":"Sec-independent protein translocase protein TatA","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42982","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4411577","identifier":"P69425","identifierLink":"https://www.uniprot.org/uniprotkb/P69425/entry","name":"tatB","description":"Sec-independent protein translocase protein TatB","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33162","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4411641","identifier":"P69423","identifierLink":"https://www.uniprot.org/uniprotkb/P69423/entry","name":"tatC","description":"Sec-independent protein translocase protein TatC","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30371","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3446","complexName":"TrpAB tryptophan synthase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the final two steps in the biosynthesis of L-tryptophan. Complex formation stimulates the separate enzymatic activities of the alpha and beta subunit by one to two orders of magnitude, due to conformational changes of the subunits on binding. The alpha-subunit catalyses the cleavage of indole-glycerol-phosphate to indole and glyceraldehyde-3-phosphate. In the beta-subunit, indole is condensed with l-serine to l-tryptophan and water in a pyridoxal-5-prime-phosphate dependent reaction. Indole diffuses from the alpha to the beta-active site through a tunnel formed by the subunits, preventing its loss through absorption by the cell membranes","predictedComplex":false,"interactors":[{"ac":"EBI-1120833","identifier":"P0A877","identifierLink":"https://www.uniprot.org/uniprotkb/P0A877/entry","name":"trpA","description":"Tryptophan synthase alpha chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43406","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1123130","identifier":"P0A879","identifierLink":"https://www.uniprot.org/uniprotkb/P0A879/entry","name":"trpB","description":"Tryptophan synthase beta chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR48077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8852014","identifier":"CHEBI:597326","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:597326","name":"pyridoxal 5'-phosphate(2-)","description":"pyridoxal 5'-phosphate(2-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3447","complexName":"NapAB nitrate reductase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Periplasmic molybdoenzyme that catalyzes the two-electron reduction of nitrate to nitrite. napB receives electrons from the membrane-anchored tetraheme c-type napC protein and transfers these to napA subunit, thus allowing electron flow between membrane and periplasm.","predictedComplex":false,"interactors":[{"ac":"EBI-11426020","identifier":"CHEBI:60539","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60539","name":"mo(=o)-bis(molybdopterin guanine dinucleotide)(4-)","description":"Mo(=O)-bis(molybdopterin guanine dinucleotide)(4-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-17171907","identifier":"P0ABL3","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABL3/entry","name":"napB","description":"Periplasmic nitrate reductase, electron transfer subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR38604","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17171967","identifier":"CHEBI:60562","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60562","name":"ferroheme c","description":"ferroheme c","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-554952","identifier":"P33937","identifierLink":"https://www.uniprot.org/uniprotkb/P33937/entry","name":"napA","description":"Periplasmic nitrate reductase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3461","complexName":"Chromosomal passenger complex","organismName":"Caenorhabditis elegans; 6239","description":"Serine/threonine kinase complex which ensures chromosome bi-orientation on the mitotic spindle during metaphase by phosphorylating multiple kinetochore components. It destabilizes monopolar attachments by phosphorylating key proteins at the kinetophore. The opposing Chromosomal Passenger complex and gsp-1 (Q27497) activities ensure that chromosomes achieve a bipolar attachment to the spindle. Monopolar attachments do not produce tension across sister kinetochores (and the complex may act by sensing this absence of tension). The Chromosome passenger complex is conserved from yeast to man and is an essential regulator of diverse aspects of mitosis that ensure faithful chromosome segregation. The complex undergoes changes in its localization throughout mitosis: in early mitosis it presumably localizes to chromosome arms while later in metaphase it is found at the centromere. At anaphase onset it re-localizes to mitotic spindle microtubules accumulating in the midbody in late anaphase where it promotes spindle disassembly and cytokinesis. It also plays a role in contractile ring formation and regulation of abscission in cytokinesis. air-2 (O01427), bir-1 (G5EFA2), and icp-1 (G5EE37) require csc-1 (O45952) to localize to meiotic chromatin, mitotic chromosomes and the spindle mid zone in meiosis and mitosis. In turn, bir-1 (G5EFA2), csc-1 (O45952) and icp-1 (G5EE37) localization to chromosomes is mutually interdependent.","predictedComplex":false,"interactors":[{"ac":"EBI-312947","identifier":"O01427","identifierLink":"https://www.uniprot.org/uniprotkb/O01427/entry","name":"air-2","description":"Aurora/IPL1-related protein kinase 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24350","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-312981","identifier":"G5EE37","identifierLink":"https://www.uniprot.org/uniprotkb/G5EE37/entry","name":"icp-1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-328435","identifier":"G5EFA2","identifierLink":"https://www.uniprot.org/uniprotkb/G5EFA2/entry","name":"bir-1","description":"Chromosomal passenger complex protein bir-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR46771","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-328477","identifier":"O45952","identifierLink":"https://www.uniprot.org/uniprotkb/O45952/entry","name":"csc-1","description":"Chromosome segregation and cytokinesis defective protein 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3462","complexName":"CLA4-BEM1-CDC24 polarity complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for the establishment of cell polarity during the cell division cycle, and essential for bud emergence. Binds directly to activated CDC42 GTPase and is required for orchestrating a cellular gradient of CDC42. The complex assembles in late G1 and BEM1 directly augments the guanine exchange factor (GEF) activity of CDC24, promoting the exchange of CDC42-bound GDP with GTP. BEM1 also increases CDC24 phosphorylation by CLA4. Phosphorylation inhibits scaffold-dependent stimulation of CDC24 GEF activity, thus BEM1 stimulates GEF activity in a reversible fashion, controlling the flux of cellular signalling through CDC42. The core circuit appears to be a positive feedback loop with GTP-CDC42 at the membrane recruiting the complex from the cytoplasm to promote activation of neighbouring CDC42. A corresponding negative feedback loop appears to ensure only one bud forms.","predictedComplex":false,"interactors":[{"ac":"EBI-3508","identifier":"P29366","identifierLink":"https://www.uniprot.org/uniprotkb/P29366/entry","name":"BEM1","description":"Bud emergence protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15706","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4220","identifier":"P11433","identifierLink":"https://www.uniprot.org/uniprotkb/P11433/entry","name":"CDC24","description":"Cell division control protein 24","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47339","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4750","identifier":"P48562","identifierLink":"https://www.uniprot.org/uniprotkb/P48562/entry","name":"CLA4","description":"Serine/threonine-protein kinase CLA4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR48015","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3463","complexName":"Central spindlin complex","organismName":"Caenorhabditis elegans; 6239","description":"Microtubule-dependent and Rho-mediated signaling complex. Plays a key role in the formation of the central spindle (a set of microtubule bundles that forms between the separating chromosomes) during late anaphase and contractile ring formation during cytokinesis. \r\n\r\nDuring anaphase, activates and targets the guanine nucleotide exchange factor (GEF) ect-2 (Q9U364) to the central spindle, where it can activate the guanosine triphosphatase (GTPase) Rho family member rho-1 (Q22038).  rho-1 signalling is controlled by the central spindle. The complex promotes the formation of microtubule bundles acting cooperatively with several other protein complexes to bundle antiparallel microtubules during anaphase. Localization at the central spindle requires the Chromosome passenger complex (CPX-3461). \r\n\r\nFurthermore, the complex is directly phosphorylated by the Chromosome passenger complex. Phosphorylation of the complex regulates its activity during cytokinesis.\r\n\r\nThe complex may also stimulate rho-1 activation at the cell membrane, which in turn orchestrates contractile ring assembly and constriction during cytokinesis.","predictedComplex":false,"interactors":[{"ac":"EBI-315948","identifier":"Q9XUS9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XUS9/entry","name":"cyk-4","description":null,"stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR46199","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9634015","identifier":"Q8MQ03","identifierLink":"https://www.uniprot.org/uniprotkb/Q8MQ03/entry","name":"zen-4","description":"Kinesin-like protein","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3464","complexName":"MlaFEDB lipid transport complex","organismName":"Escherichia coli (strain K12); 83333","description":"Required for the maintenance of asymmetery of the outer membrane, with an outer leaflet rich in lipopolysaccharide and an inner leaflet composed of phospholipids. MlaC (P0ADV7) shuttles phospholipid substrates between the inner membrane MlaFEDB transporter and an outer membrane complex, diffusing across the periplasm to the MlaFEDB complex in the inner membrane, where ATP hydrolysis may facilitate extraction of the lipid from MlaC and/or the translocation of the lipid into the inner membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-20198988","identifier":"P64606","identifierLink":"https://www.uniprot.org/uniprotkb/P64606/entry","name":"mlaE","description":"Intermembrane phospholipid transport system permease protein MlaE","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30188","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-561408","identifier":"P63386","identifierLink":"https://www.uniprot.org/uniprotkb/P63386/entry","name":"mlaF","description":"Intermembrane phospholipid transport system ATP-binding protein MlaF","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7869311","identifier":"P64604","identifierLink":"https://www.uniprot.org/uniprotkb/P64604/entry","name":"mlaD","description":"Intermembrane phospholipid transport system binding protein MlaD","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33371","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9151937","identifier":"P64602","identifierLink":"https://www.uniprot.org/uniprotkb/P64602/entry","name":"mlaB","description":"Intermembrane phospholipid transport system binding protein MlaB","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR35849","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3481","complexName":"Shieldin complex","organismName":"Homo sapiens; 9606","description":"Promotes the repair of DNA double-stranded breaks (DSBs). Functions as a downstream effector of 53BP1-RIF1 during the G1 and S phases of the cell cycle to promote non-homologous end joining (NHEJ) and suppress DNA end resection. Also plays a role in NHEJ-dependent fusion of unprotected telomeres and is required for immunoglobulin class-switch recombination.","predictedComplex":false,"interactors":[{"ac":"EBI-20209073","identifier":"Q6ZNX1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6ZNX1/entry","name":"SHLD3","description":"Shieldin complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR41404","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2560414","identifier":"Q86V20","identifierLink":"https://www.uniprot.org/uniprotkb/Q86V20/entry","name":"SHLD2","description":"Shieldin complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14495","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2560428","identifier":"Q8IYI0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IYI0/entry","name":"SHLD1","description":"Shieldin complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR36863","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-77889","identifier":"Q9UI95","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UI95/entry","name":"MAD2L2","description":"Mitotic spindle assembly checkpoint protein MAD2B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3482","complexName":"Eukaryotic translation initiation factor 4E-Mxt complex","organismName":"Caenorhabditis elegans; 6239","description":"Plays a role in translation initiation. The 4E-BP protein mxt-1 competes with eIF4G/ifg-1 (Q7JMF0) for binding to eIF4E/ife-3 when this protein is bound to the 7-methylguanosine-containing 5-prime cap of messenger RNAs. However, in contrast to other 4E-BPs, formation of this complex appears to promote cap-dependent translation initiation.","predictedComplex":false,"interactors":[{"ac":"EBI-330111","identifier":"Q9XW13","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XW13/entry","name":"mxt-1","description":"Eukaryotic translation initiation factor 4E-binding protein Mextli homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR20849","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-330119","identifier":"O61955","identifierLink":"https://www.uniprot.org/uniprotkb/O61955/entry","name":"ife-3","description":"Eukaryotic translation initiation factor 4E-3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3483","complexName":"Shieldin complex","organismName":"Mus musculus; 10090","description":"Promotes the repair of DNA double-stranded breaks (DSBs). Functions as a downstream effector of 53BP1-RIF1 during the G1 and S phases of the cell cycle to promote non-homologous end joining (NHEJ) and suppress DNA end resection. Also plays a role in NHEJ-dependent fusion of unprotected telomeres and is required for immunoglobulin class-switch recombination.","predictedComplex":false,"interactors":[{"ac":"EBI-20557767","identifier":"Q3UEN2","identifierLink":"https://www.uniprot.org/uniprotkb/Q3UEN2/entry","name":"Shld2","description":"Shieldin complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14495","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20557805","identifier":"Q9D112","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D112/entry","name":"Shld1","description":"Shieldin complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR36863","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20557820","identifier":"Q9CZV2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CZV2/entry","name":"Shld3","description":"Shieldin complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR41404","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2552856","identifier":"Q9D752","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D752/entry","name":"Mad2l2","description":"Mitotic spindle assembly checkpoint protein MAD2B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3503","complexName":"MIH complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Role in cytokinesis. May bridge actomyosin ring contraction and septum synthesis, resulting in the coordination of these processes, and leading to plasma membrane ingression and fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-10988","identifier":"P53141","identifierLink":"https://www.uniprot.org/uniprotkb/P53141/entry","name":"MLC1","description":"Myosin light chain 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-35351","identifier":"Q12280","identifierLink":"https://www.uniprot.org/uniprotkb/Q12280/entry","name":"IQG1","description":"Ras GTPase-activating-like protein IQG1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14149","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5412","identifier":"Q05080","identifierLink":"https://www.uniprot.org/uniprotkb/Q05080/entry","name":"HOF1","description":"Cytokinesis protein 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23065","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3521","complexName":"myrf-1-myrf-2 complex","organismName":"Caenorhabditis elegans; 6239","description":"Plays a role in the synaptic rewiring of the GABAergic motor neurons (known as dorsal D (DD) neurons) during the early stages of larval development. The complex forms between full length proteins, both of which are subsequently processed in the endoplasmic reticulum and undergo serine-483-dependent auto-cleavage through the intramolecular chaperone auto-processing domain (IPR030392). This results in the translocation of the N-termini complex to the nucleus where it binds to DNA to regulate synaptic rewiring. The C-termini are retained in the endoplasmic reticulum. Synaptic rewiring occurs during the L1 stage and  is completed by the late L2 stage of larval development. Early in larval development, DD neurons form new processes onto dorsal muscles whilst the existing ventral synapses are disassembled. At the same time, new ventral motor neurons are generated and are incorporated into the motor circuitry.","predictedComplex":false,"interactors":[{"ac":"EBI-6727439","identifier":"D9PTN5","identifierLink":"https://www.uniprot.org/uniprotkb/D9PTN5/entry","name":"myrf-2","description":"Myelin regulatory factor homolog 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13029","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6731843","identifier":"G5EFI7","identifierLink":"https://www.uniprot.org/uniprotkb/G5EFI7/entry","name":"myrf-1","description":"Myelin regulatory factor homolog 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13029","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3523","complexName":"Glycogen synthase-glycogenin complex","organismName":"Caenorhabditis elegans; 6239","description":"Glycogen synthase complex which  extends the oligosaccharide chain formed by homodimeric glycogenin (gyg-1) glycosyltransferase. gyg-1 initiates glucose polymerization by catalyzing the formation of a short alpha (1,4)-glucosyl chain which it covalently attaches via auto-glucosylation to form a glucose 1-O-tyrosyl linkage to Tyr-194  This primer glucose chain of 8-12 residues is then further elongated by the GYG-GYS complex, successive adding alpha-1,4-linked glucose residues to the nonreducing end of the polysaccharide chain, using UDP-glucose as the sugar donor with the release of UDP after which, gyg-1 and gsy-1 dissociate.","predictedComplex":false,"interactors":[{"ac":"EBI-2418492","identifier":"H2KYQ5","identifierLink":"https://www.uniprot.org/uniprotkb/H2KYQ5/entry","name":"gyg-1","description":"Glycogenin-1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11183","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-313125","identifier":"Q9U2D9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9U2D9/entry","name":"gsy-1","description":"Glycogen [starch] synthase","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10176","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3541","complexName":"AIM21-TDA2 actin assembly regulator complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Localizes to actin cortical patches at sites of endocytosis and negatively regulates barbed end F-actin assembly, resulting in the generation of free actin pools. Necessary for efficient endocytosis and balancing the distribution of actin between patches and cables. Interacts with, and may regulate the activity of, the F-actin capping protein complex (CPX-1637).","predictedComplex":false,"interactors":[{"ac":"EBI-22573","identifier":"P40045","identifierLink":"https://www.uniprot.org/uniprotkb/P40045/entry","name":"TDA2","description":"Topoisomerase I damage affected protein 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-25376","identifier":"P40563","identifierLink":"https://www.uniprot.org/uniprotkb/P40563/entry","name":"AIM21","description":"Altered inheritance of mitochondria protein 21","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-3561","complexName":"PYL1 ABA receptor complex","organismName":"Arabidopsis thaliana; 3702","description":"Abscisic acid (ABA) receptor that inhibits group-A protein phosphatases type 2C (PP2Cs), e.g. HAB1 (Q9CAJ0), in the presence of ABA. Leads to phosphorylation and activation of SnRK2 kinases which in turn activate transcription factors that are required for ABA-mediated responses such as stomatal closure, germination inhibition and adaption to environmental stress.","predictedComplex":false,"interactors":[{"ac":"EBI-2363104","identifier":"Q8VZS8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VZS8/entry","name":"PYL1","description":"Abscisic acid receptor PYL1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR31213","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3562","complexName":"PYL2 ABA receptor complex","organismName":"Arabidopsis thaliana; 3702","description":"Abscisic acid (ABA) receptor that inhibits group-A protein phosphatases type 2C (PP2Cs), e.g. HAB1 (Q9CAJ0), in the presence of ABA. Leads to phosphorylation and activation of SnRK2 kinases which in turn activate transcription factors that are required for ABA-mediated responses such as stomatal closure, germination inhibition and adaption to environmental stress.","predictedComplex":false,"interactors":[{"ac":"EBI-2363125","identifier":"O80992","identifierLink":"https://www.uniprot.org/uniprotkb/O80992/entry","name":"PYL2","description":"Abscisic acid receptor PYL2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR31213","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3563","complexName":"PYL3 ABA receptor complex","organismName":"Arabidopsis thaliana; 3702","description":"Abscisic acid (ABA) receptor that inhibits group-A protein phosphatases type 2C (PP2Cs), e.g. HAB1 (Q9CAJ0), in the presence of ABA. Leads to phosphorylation and activation of SnRK2 kinases which in turn activate transcription factors that are required for ABA-mediated responses such as stomatal closure, germination inhibition and adaption to environmental stress.","predictedComplex":false,"interactors":[{"ac":"EBI-2363144","identifier":"Q9SSM7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9SSM7/entry","name":"PYL3","description":"Abscisic acid receptor PYL3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR31213","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3564","complexName":"KdpFABC potassium import complex","organismName":"Escherichia coli (strain K12); 83333","description":"A potassium pump that maintains intracellular homeostasis as well as cell shape and turgor under conditions where potassium is limiting. The complex exhibits high selectivity and binding-affinity (Kd = 2uM)4 and is able to maintain cytoplasmic K+ concentrations against gradients up to 10,000-fold. Mutagenesis has been used to establish that K+ is transported through KdpA and that the energy of ATP is harnessed by KdpB.  During catalysis, the KdpFABC complex cycles between two main conformational states, each of which comprises different structural properties together with different binding affinities for both ATP and the transport substrate.","predictedComplex":false,"interactors":[{"ac":"EBI-1116956","identifier":"P03960","identifierLink":"https://www.uniprot.org/uniprotkb/P03960/entry","name":"kdpB","description":"Potassium-transporting ATPase ATP-binding subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43743","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20568427","identifier":"P36937","identifierLink":"https://www.uniprot.org/uniprotkb/P36937/entry","name":"kdpF","description":"Potassium-transporting ATPase KdpF subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-20568442","identifier":"P03959","identifierLink":"https://www.uniprot.org/uniprotkb/P03959/entry","name":"kdpA","description":"Potassium-transporting ATPase potassium-binding subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6997216","identifier":"P03961","identifierLink":"https://www.uniprot.org/uniprotkb/P03961/entry","name":"kdpC","description":"Potassium-transporting ATPase KdpC subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30042","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3568","complexName":"CcmABCDE system I cytochrome c biogenesis complex","organismName":"Escherichia coli (strain K12); 83333","description":"Required for the covalent ligation of heme to a C1XXC2H heme-binding site in an apo-cytochome C. CcmABCD is homologous to the eukaryotic-type ABC transporters and are responsible for conveying heme b to the periplasm and loading it to the heme-chaperone CcmE ccmC binds heme b non-covalently via its two transmembrane His residues. Once heme b reaches the periplasm, it is thought to interact with the WWD domain of ccmC and the hydrophobic heme-binding region of ccmE. ATP hydrolysis by ccmAB may be required for the release of heme-bound ccmE from the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-1128007","identifier":"P69490","identifierLink":"https://www.uniprot.org/uniprotkb/P69490/entry","name":"ccmE","description":"Cytochrome c-type biogenesis protein CcmE","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34128","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2123469","identifier":"P0ABM1","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABM1/entry","name":"ccmC","description":"Heme exporter protein C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30071","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3894922","identifier":"P0ABM5","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABM5/entry","name":"ccmD","description":"Heme exporter protein D","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR37531","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-546936","identifier":"P0ABL8","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABL8/entry","name":"ccmB","description":"Heme exporter protein B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30070","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6402796","identifier":"P33931","identifierLink":"https://www.uniprot.org/uniprotkb/P33931/entry","name":"ccmA","description":"Cytochrome c biogenesis ATP-binding export protein CcmA","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43499","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3569","complexName":"CcmFH system I cytochrome c biogenesis complex","organismName":"Escherichia coli (strain K12); 83333","description":"Required for the covalent ligation of heme to a C1XXC2H heme-binding site in an apo-cytochome C. Acts as a Cytochrome C synthetase that accepts heme from the ccmE (P69490) chaperone for attachment to apo-cytochrome c via the formation of a thioether. Thioreduction is mediated by dsbE/ccmG (P0AA86) which appears to bind to this complex.","predictedComplex":false,"interactors":[{"ac":"EBI-560309","identifier":"P0ABM9","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABM9/entry","name":"ccmH","description":"Cytochrome c-type biogenesis protein CcmH","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR47870","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-763370","identifier":"P33927","identifierLink":"https://www.uniprot.org/uniprotkb/P33927/entry","name":"ccmF","description":"Cytochrome c-type biogenesis protein CcmF","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43653","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3570","complexName":"Acetolactate synthase II complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the first step that is common to the biosynthesis of  branched-chain amino acids. The reaction involves the irreversible decarboxylation of pyruvate to a bound hydroxyethyl group that then condenses with either a second pyruvate molecule to form 2-acetolactate as the first step in the biosynthesis of valine and leucine or with 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate as the initial  step in the biosynthesis of isoleucine.\r\nThe AHAS I (CPX-3573) and AHAS III (CPX-3575) complexes are both sensitive to feedback inhibition by valine, whereas the AHAS II complex is not, enabling bacteria expressing this complex to grow in valine-rich conditions.","predictedComplex":false,"interactors":[{"ac":"EBI-1133701","identifier":"P0DP90","identifierLink":"https://www.uniprot.org/uniprotkb/P0DP90/entry","name":"ilvG","description":"Acetolactate synthase isozyme 2 large subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-1133722","identifier":"P0ADG1","identifierLink":"https://www.uniprot.org/uniprotkb/P0ADG1/entry","name":"ilvM","description":"Acetolactate synthase isozyme 2 small subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9691551","identifier":"CHEBI:58937","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58937","name":"thiamine(1+) diphosphate(3-)","description":"thiamine(1+) diphosphate(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3572","complexName":"TGA2-NPR1 complex","organismName":"Arabidopsis thaliana; 3702","description":"Transcriptional co-activator required for the systemic acquired resistance (SAR) via the regulation of pathogenesis-related genes (e.g. PR-1) under induction of salicylic acid (SA). May bind to promotor region via TGA2 subunit. Functions in plant defence against pathogens.","predictedComplex":false,"interactors":[{"ac":"EBI-1392127","identifier":"P93002","identifierLink":"https://www.uniprot.org/uniprotkb/P93002/entry","name":"NPR1","description":"Regulatory protein NPR1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR46475","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-541307","identifier":"P43273","identifierLink":"https://www.uniprot.org/uniprotkb/P43273/entry","name":"TGA2","description":"Transcription factor TGA2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR45693","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3573","complexName":"Acetolactate synthase I complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the first step that is common to the biosynthesis of  branched-chain amino acids. The reaction involves the irreversible decarboxylation of pyruvate to a bound hydroxyethyl group that then condenses with either a second pyruvate molecule to form 2-acetolactate as the first step in the biosynthesis of valine and leucine. or with 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate as  the  initial  step in the biosynthesis of isoleucine. \r\nThe AHAS I and AHAS III (CPX-3575) complexes are both sensitive to feedback inhibition by valine, whereas the AHAS II complex (CPX-3570) is not, enabling bacteria expressing this complex to grow in valine-rich conditions.","predictedComplex":false,"interactors":[{"ac":"EBI-1133508","identifier":"P0ADF8","identifierLink":"https://www.uniprot.org/uniprotkb/P0ADF8/entry","name":"ilvN","description":"Acetolactate synthase isozyme 1 small subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-552948","identifier":"P08142","identifierLink":"https://www.uniprot.org/uniprotkb/P08142/entry","name":"ilvB","description":"Acetolactate synthase isozyme 1 large subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR18968","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9691551","identifier":"CHEBI:58937","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58937","name":"thiamine(1+) diphosphate(3-)","description":"thiamine(1+) diphosphate(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3575","complexName":"Acetolactate synthase III complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the first step that is common to the biosynthesis of  branched-chain amino acids. The reaction involves the irreversible decarboxylation of pyruvate to a bound hydroxyethyl group that then condenses with either a second pyruvate molecule to form 2-acetolactate as the first step in the biosynthesis of valine and leucine. or with 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate as  the  initial  step  in  the biosynthesis of isoleucine. \r\nThe AHAS I (CPX-3573) and AHAS III complexes are both sensitive to feedback inhibition by valine, whereas the AHAS II complex (CPX-3570) is not, enabling bacteria expressing this complex to grow in valine-rich conditions.","predictedComplex":false,"interactors":[{"ac":"EBI-1113638","identifier":"P00893","identifierLink":"https://www.uniprot.org/uniprotkb/P00893/entry","name":"ilvI","description":"Acetolactate synthase isozyme 3 large subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR18968","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9120528","identifier":"P00894","identifierLink":"https://www.uniprot.org/uniprotkb/P00894/entry","name":"ilvH","description":"Acetolactate synthase isozyme 3 small subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9691551","identifier":"CHEBI:58937","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58937","name":"thiamine(1+) diphosphate(3-)","description":"thiamine(1+) diphosphate(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3576","complexName":"Ferric-citrate outer membrane transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"A member of the TonB-dependent transporter family (TBDTs) which binds and then transports ferric citrate across the outer membrane. Catecholate transport requires an outer membrane receptor (fecA), which is relatively specific for its ligand. The ligand-bound receptor then physically interacts with the TonB protein. TBDTs are energy-dependent gated channels that usually transport large metal complexes which cannot fit through porins, and are too scarce to enter by mass-action-driven transport. Energy-dependent uptake through TBDTs requires interaction with TonB in complex with exbB and exbD in the inner membrane, ExbBD. TonB undergoes rapid energized movement driven by ExbBD which harvests the electrochemical force from the electrochemical proton gradient created by the proton gradient across the inner membrane and convert it into rotational motion. Hence, tonB may pull or twist the N-termini of TBDTs to promote transport of substrates into the periplasm. ATP-binding-cassette (ABC) transporters subsequently move the ferric citrate (Fe3+) through the periplasm and inner membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-1131517","identifier":"P13036","identifierLink":"https://www.uniprot.org/uniprotkb/P13036/entry","name":"fecA","description":"Fe(3+) dicitrate transport protein FecA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6399986","identifier":"P0ABU7","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABU7/entry","name":"exbB","description":"Biopolymer transport protein ExbB","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6399993","identifier":"P02929","identifierLink":"https://www.uniprot.org/uniprotkb/P02929/entry","name":"tonB","description":"Protein TonB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33446","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6417016","identifier":"P0ABV2","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABV2/entry","name":"exbD","description":"Biopolymer transport protein ExbD","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3577","complexName":"Ferric-catecholate outer membrane transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"A member of the TonB-dependent transporter family (TBDTs) which binds and then transports Fe3+ complexed to linear catecholates, such as dihydroxybenzoyl, across the outer membrane.  Catecholate transport requires an outer membrane receptor (cirA), which is relatively specific for its ligand. The ligand-bound receptor then physically interacts with the TonB protein. TBDTs are energy-dependent gated channels that usually transport large metal complexes which cannot fit through porins, and are too scarce to enter by mass-action-driven transport. Energy-dependent uptake through TBDTs requires interaction with TonB in complex with exbB and exbD in the inner membrane, ExbBD. TonB undergoes rapid energized movement driven by ExbBD which harvests the electrochemical force from the electrochemical proton gradient created by the proton gradient across the inner membrane and convert it into rotational motion. Hence, tonB may pull or twist the N-termini of TBDTs to promote transport of substrates into the periplasm. ATP-binding-cassette (ABC) transporters subsequently move the ferric-catecholate (Fe3+) through the periplasm and inner membrane. The complex has also implicated in the uptake of catechol‐substituted cephalosporins and is used by Group B colicins  (E. coli‐specific bacteriocins) to bind and cross the outer membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-1124042","identifier":"P17315","identifierLink":"https://www.uniprot.org/uniprotkb/P17315/entry","name":"cirA","description":"Colicin I receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30069","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6399986","identifier":"P0ABU7","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABU7/entry","name":"exbB","description":"Biopolymer transport protein ExbB","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6399993","identifier":"P02929","identifierLink":"https://www.uniprot.org/uniprotkb/P02929/entry","name":"tonB","description":"Protein TonB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33446","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6417016","identifier":"P0ABV2","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABV2/entry","name":"exbD","description":"Biopolymer transport protein ExbD","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3578","complexName":"Ferric-enterobactin outer membrane transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"A member of the TonB-dependent transporter family (TBDTs) which binds and then transports Fe3+ complexed to the catecholate ferric enterobactin (CHEBI:28199) across the outer membrane. Catecholate transport requires an outer membrane receptor (fepA), which is relatively specific for its ligand. The ligand-bound receptor then physically interacts with the TonB protein. TBDTs are energy-dependent gated channels that usually transport large metal complexes which cannot fit through porins, and are too scarce to enter by mass-action-driven transport. Energy-dependent uptake through TBDTs requires interaction with TonB in complex with exbB and exbD in the inner membrane, ExbBD. TonB undergoes rapid energized movement driven by ExbBD which harvest the electrochemical force from the electrochemical proton gradient created by the proton gradient across the inner membrane and convert it into rotational motion. Hence, tonB may pull or twist the N-termini of TBDTs to promote transport of substrates into the periplasm. ATP-binding-cassette (ABC) transporters subsequently move the ferric-catecholate (Fe3+) through the periplasm and inner membrane. The complex is used by Group B colicins (E. coli‐specific bacteriocins) to bind and cross the outer membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-6399986","identifier":"P0ABU7","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABU7/entry","name":"exbB","description":"Biopolymer transport protein ExbB","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6399993","identifier":"P02929","identifierLink":"https://www.uniprot.org/uniprotkb/P02929/entry","name":"tonB","description":"Protein TonB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33446","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6400027","identifier":"P05825","identifierLink":"https://www.uniprot.org/uniprotkb/P05825/entry","name":"fepA","description":"Ferrienterobactin receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30069","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6417016","identifier":"P0ABV2","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABV2/entry","name":"exbD","description":"Biopolymer transport protein ExbD","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3579","complexName":"Ferric-coprogen outer membrane transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"A member of the TonB-dependent transporter family (TBDTs) which binds and then transports Fe3+ complexed to sideraphores such as coprogen, ferrioxamine B, and rhodotorulic acid across the outer membrane. Sideraphore transport requires an outer membrane receptor (fhuE), which is relatively specific for its ligand. The ligand-bound receptor then physically interacts with the TonB protein. TBDTs are energy-dependent gated channels that usually transport large metal complexes which cannot fit through porins, and are too scarce to enter by mass-action-driven transport. Energy-dependent uptake through TBDTs requires interaction with TonB in complex with exbB and exbD in the inner membrane, ExbBD. TonB undergoes rapid energized movement driven by ExbBD which harvests the electrochemical force from the electrochemical proton gradient created by the proton gradient across the inner membrane and convert it into rotational motion. Hence, tonB may pull or twist the N-termini of TBDTs to promote transport of substrates into the periplasm. ATP-binding-cassette (ABC) transporters subsequently move the ferric-siderophore (Fe3+) through the periplasm and inner membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-20593008","identifier":"P16869","identifierLink":"https://www.uniprot.org/uniprotkb/P16869/entry","name":"fhuE","description":"Hydroxamate siderophore receptor FhuE","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32552","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6399986","identifier":"P0ABU7","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABU7/entry","name":"exbB","description":"Biopolymer transport protein ExbB","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6399993","identifier":"P02929","identifierLink":"https://www.uniprot.org/uniprotkb/P02929/entry","name":"tonB","description":"Protein TonB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33446","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6417016","identifier":"P0ABV2","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABV2/entry","name":"exbD","description":"Biopolymer transport protein ExbD","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3580","complexName":"fiu outer membrane transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"A member of the TonB-dependent transporter family (TBDTs) which binds and then transports ions (probably ferric) complexed to sideraphores across the outer membrane. Sideraphore transport requires an outer membrane receptor (fiu), which is relatively specific for its ligand. The ligand-bound receptor then physically interacts with the TonB protein. TBDTs are energy-dependent gated channels that usually transport large metal complexes which cannot fit through porins, and are too scarce to enter by mass-action-driven transport. Energy-dependent uptake through TBDTs requires interaction with tonB in complex with exbB and exbD in the inner membrane, ExbBD. TonB undergoes rapid energized movement driven by ExbBD which harvests the electrochemical force from the electrochemical proton gradient created by the proton gradient across the inner membrane and convert it into rotational motion. Hence, TonB may pull or twist the N-termini of TBDTs to promote transport of substrates into the periplasm. ATP-binding-cassette (ABC) transporters subsequently move the ion-siderophore through the periplasm and inner membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-1120371","identifier":"P75780","identifierLink":"https://www.uniprot.org/uniprotkb/P75780/entry","name":"fiu","description":"Catecholate siderophore receptor Fiu","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32552","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6399986","identifier":"P0ABU7","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABU7/entry","name":"exbB","description":"Biopolymer transport protein ExbB","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6399993","identifier":"P02929","identifierLink":"https://www.uniprot.org/uniprotkb/P02929/entry","name":"tonB","description":"Protein TonB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33446","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6417016","identifier":"P0ABV2","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABV2/entry","name":"exbD","description":"Biopolymer transport protein ExbD","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3581","complexName":"AMT1-3 homotrimer","organismName":"Arabidopsis thaliana; 3702","description":"High affinity ammonium transporter complex that enables the transfer of ammonium across the plasma membrane into the cell under nitrogen-deficient growth conditions. Critical for allosteric regulation of transport activity which enables plant roots to repress ammonium uptake at elevated ammonium supplies.","predictedComplex":false,"interactors":[{"ac":"EBI-16716530","identifier":"Q9SQH9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9SQH9/entry","name":"AMT1-3","description":"Ammonium transporter 1 member 3","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11730","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3582","complexName":"AMT1-1 - AMT1-3 heterotrimer, variant 1","organismName":"Arabidopsis thaliana; 3702","description":"High affinity ammonium transporter complex that enables the transfer of ammonium across the plasma membrane into the cell under nitrogen-deficient growth conditions. Critical for allosteric regulation of transport activity which enables plant roots to repress ammonium uptake at elevated ammonium supplies.","predictedComplex":false,"interactors":[{"ac":"EBI-16426081","identifier":"P54144","identifierLink":"https://www.uniprot.org/uniprotkb/P54144/entry","name":"AMT1-1","description":"Ammonium transporter 1 member 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11730","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16716530","identifier":"Q9SQH9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9SQH9/entry","name":"AMT1-3","description":"Ammonium transporter 1 member 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11730","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3583","complexName":"AMT1-1 - AMT1-3 heterotrimer, variant 2","organismName":"Arabidopsis thaliana; 3702","description":"High affinity ammonium transporter complex that enables the transfer of ammonium across the plasma membrane into the cell under nitrogen-deficient growth conditions. Critical for allosteric regulation of transport activity which enables plant roots to repress ammonium uptake at elevated ammonium supplies.","predictedComplex":false,"interactors":[{"ac":"EBI-16426081","identifier":"P54144","identifierLink":"https://www.uniprot.org/uniprotkb/P54144/entry","name":"AMT1-1","description":"Ammonium transporter 1 member 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11730","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16716530","identifier":"Q9SQH9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9SQH9/entry","name":"AMT1-3","description":"Ammonium transporter 1 member 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11730","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3584","complexName":"WHY2 complex","organismName":"Arabidopsis thaliana; 3702","description":"Modulates DNA repair in plant mitochondria by binding single-stranded DNA in a non-sequence-specific manner.","predictedComplex":false,"interactors":[{"ac":"EBI-15219982","identifier":"Q8VYF7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VYF7/entry","name":"WHY2","description":"Single-stranded DNA-binding protein WHY2, mitochondrial","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR31745","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3585","complexName":"Uncharacterized yncD-DHBS outer membrane transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"A putative member of the TonB-dependent transporter family (TBDTs) which may bind and then transport Fe3+ complexed to sideraphores such as 2,3-dihydroxybenzoylserine (DHBS) across the outer membrane. Sideraphore transport requires an outer membrane receptor (yncD), which is relatively specific for its ligand. The ligand-bound receptor then physically interacts with the TonB protein. TBDTs are energy-dependent gated channels that usually transport large metal complexes which cannot fit through porins, and are too scarce to enter by mass-action-driven transport. Energy-dependent uptake through TBDTs requires interaction with TonB in complex with exbB and exbD in the inner membrane, ExbBD. TonB undergoes rapid energized movement driven by ExbBD which harvest the electrochemical force from the electrochemical proton gradient created by the proton gradient across the inner membrane and convert it into rotational motion. Hence, tonB may pull or twist the N-termini of TBDTs to promote transport of substrates into the periplasm. ATP-binding-cassette (ABC) transporters subsequently move the ferric-siderophore (Fe3+) through the periplasm and inner membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-562418","identifier":"P76115","identifierLink":"https://www.uniprot.org/uniprotkb/P76115/entry","name":"pqqU","description":"Pyrroloquinoline quinone transporter","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30069","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6399986","identifier":"P0ABU7","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABU7/entry","name":"exbB","description":"Biopolymer transport protein ExbB","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6399993","identifier":"P02929","identifierLink":"https://www.uniprot.org/uniprotkb/P02929/entry","name":"tonB","description":"Protein TonB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33446","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6417016","identifier":"P0ABV2","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABV2/entry","name":"exbD","description":"Biopolymer transport protein ExbD","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3586","complexName":"WHY3 complex","organismName":"Arabidopsis thaliana; 3702","description":"Modulates DNA repair in plant chloroplasts by binding single-stranded DNA in a non-sequence-specific manner. Contributes to both basal and specific defense responses. Transcription can be induced by salicylic acid (SA).","predictedComplex":false,"interactors":[{"ac":"EBI-15215764","identifier":"Q66GR6","identifierLink":"https://www.uniprot.org/uniprotkb/Q66GR6/entry","name":"WHY3","description":"Single-stranded DNA-binding protein WHY3, chloroplastic","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR31745","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3601","complexName":"TGA2 complex","organismName":"Arabidopsis thaliana; 3702","description":"Transcriptional repressor complex binding to the cognate DNA sequence TGACG of the promoter region of the PR-1 gene and represses its expression both in the absence and in the presence of salicylic acid (SA).","predictedComplex":false,"interactors":[{"ac":"EBI-541307","identifier":"P43273","identifierLink":"https://www.uniprot.org/uniprotkb/P43273/entry","name":"TGA2","description":"Transcription factor TGA2","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR45693","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3621","complexName":"ATR-ATRIP DNA damage-sensing kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Master regulator of the DNA damage response controlling a signaling cascade required for the maintenance of genomic integrity. Activated by RPA complex (CPX-21)-coated single-stranded DNA at the site of DNA double-strand breaks and stalled replication forks. Appears to control the production of an adequate and balanced pool of deoxyribonucleotides and maintain replication fork stability.","predictedComplex":false,"interactors":[{"ac":"EBI-35652","identifier":"Q04377","identifierLink":"https://www.uniprot.org/uniprotkb/Q04377/entry","name":"LCD1","description":"DNA damage checkpoint protein LCD1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-6668","identifier":"P38111","identifierLink":"https://www.uniprot.org/uniprotkb/P38111/entry","name":"MEC1","description":"Serine/threonine-protein kinase MEC1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3622","complexName":"ATR-ATRIP DNA damage-sensing kinase complex","organismName":"Homo sapiens; 9606","description":"Master regulator of the DNA damage response controlling a signaling cascade required for the maintenance of genomic integrity. Activated by RPA complex-coated single-stranded DNA at the site of DNA double-strand breaks and stalled replication forks. Appears to control the production of an adequate and balanced pool of deoxyribonucleotides and maintain replication fork stability.","predictedComplex":false,"interactors":[{"ac":"EBI-747353","identifier":"Q8WXE1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WXE1/entry","name":"ATRIP","description":"ATR-interacting protein","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28594","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968983","identifier":"Q13535","identifierLink":"https://www.uniprot.org/uniprotkb/Q13535/entry","name":"ATR","description":"Serine/threonine-protein kinase ATR","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3623","complexName":"ATR-ATRIP DNA damage-sensing kinase complex","organismName":"Mus musculus; 10090","description":"Master regulator of the DNA damage response controlling a signaling cascade required for the maintenance of genomic integrity. Activated by RPA complex-coated single-stranded DNA at the site of DNA double-strand breaks and stalled replication forks. Appears to control the production of an adequate and balanced pool of deoxyribonucleotides and maintain replication fork stability.","predictedComplex":false,"interactors":[{"ac":"EBI-1202426","identifier":"Q9JKK8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JKK8/entry","name":"Atr","description":"Serine/threonine-protein kinase ATR","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5235246","identifier":"Q8BMG1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BMG1/entry","name":"Atrip","description":"ATR-interacting protein","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR28594","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3624","complexName":"Alternative nuclear cap-binding complex","organismName":"Homo sapiens; 9606","description":"Binds co-transcriptionally to the 5-prime, m7GpppG-cap (m7G-cap) structures of RNA polymerase II transcripts (mainly pre-mRNAs and some asRNAs and lincRNAs). Required for mRNA export from the nucleus (by way of binding to TREX complex).  \r\n\r\nPossibly required for RNA interference (by way of binding asRNAs and lincRNAs) and splicing (by way of binding to exon-junction complex). Also binds serrate (SRRT/ARS2, Q9BXP5) which is associated with suppression of poly-A tail formation in histone 3-prime end pre-mRNA processing (by comparison with classic CBC, CPX-1427). Does not appear to bind snRNAs. \r\n\r\nBy way of comparison with classic CBC, alternative CBC is probably replaced by the cytoplasmic cap-binding complex eIF4F by binding to importin complex. Importin-complex-bound CBC gets reimported into the nucleus for reuse.","predictedComplex":false,"interactors":[{"ac":"EBI-464743","identifier":"Q09161","identifierLink":"https://www.uniprot.org/uniprotkb/Q09161/entry","name":"NCBP1","description":"Nuclear cap-binding protein subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6657994","identifier":"Q53F19","identifierLink":"https://www.uniprot.org/uniprotkb/Q53F19/entry","name":"NCBP3","description":"Nuclear cap-binding protein subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16291","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1605","complexName":"WMM N6-adenosine-methyltransferase complex","organismName":"Homo sapiens; 9606","description":"An N6-methyltransferase complex that methylates adenosine residues (m6A) at the 5'-[AG]GAC-3' consensus sites of some mRNAs. M6A acts as a key regulator of mRNA stability, methylation is completed upon the release of mRNA into the nucleoplasm and promotes mRNA destabilization and degradation. See also related METT3-METTL14 sub-complex (CPX-21210).\r\n\r\nRegulates various processes such as the circadian clock, differentiation of embryonic, haematopoietic and spermatogonial stem cells as well as T-cells, cortical neurogenesis, response to DNA damage, and primary miRNA processing.\r\n\r\nTRIM28 (Q13263), HNRNPH proteins (P31943/P55795/P31942) and RBM15/RBM15B (Q96T37/Q8NDT2) have also been postulated to be members of or are associated with this complex.","predictedComplex":false,"interactors":[{"ac":"EBI-2679720","identifier":"Q5T200","identifierLink":"https://www.uniprot.org/uniprotkb/Q5T200/entry","name":"ZC3H13","description":"Zinc finger CCCH domain-containing protein 13","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13585","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2819293","identifier":"Q69YN4","identifierLink":"https://www.uniprot.org/uniprotkb/Q69YN4/entry","name":"VIRMA","description":"Protein virilizer homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23185","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2832762","identifier":"Q75N03","identifierLink":"https://www.uniprot.org/uniprotkb/Q75N03/entry","name":"CBLL1","description":"E3 ubiquitin-protein ligase Hakai","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13480","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-58912060","identifier":"CPX-21210","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-21210","name":"Methyltransferase complex, METTL3-METTL14","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-751647","identifier":"Q15007","identifierLink":"https://www.uniprot.org/uniprotkb/Q15007/entry","name":"WTAP","description":"Pre-mRNA-splicing regulator WTAP","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15217","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1609","complexName":"WMM N6-adenosine-methyltransferase complex","organismName":"Mus musculus; 10090","description":"An N6-methyltransferase complex that methylates adenosine residues (m6A) at the 5'-[AG]GAC-3' consensus sites of some mRNAs. M6A acts as a key regulator of mRNA stability, methylation is completed upon the release of mRNA into the nucleoplasm and promotes mRNA destabilization and degradation.\r\n\r\nRegulates various processes such as the circadian clock, differentiation of embryonic, haematopoietic and spermatogonial stem cells as well as T-cells, cortical neurogenesis, response to DNA damage, and primary miRNA processing.\r\n\r\nTrim28 (Q62318), Hnrnph proteins (P31942/P70333/P70333) and Rbm15/Rbm15b (Q0VBL3/Q6PHZ5) have also been postulated to be members of or are associated with this complex.","predictedComplex":false,"interactors":[{"ac":"EBI-11664268","identifier":"A2AIV2","identifierLink":"https://www.uniprot.org/uniprotkb/A2AIV2/entry","name":"Virma","description":"Protein virilizer homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23185","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15893911","identifier":"E9Q784","identifierLink":"https://www.uniprot.org/uniprotkb/E9Q784/entry","name":"Zc3h13","description":"Zinc finger CCCH domain-containing protein 13","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13585","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16089028","identifier":"Q3UIK4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3UIK4/entry","name":"Mettl14","description":"N(6)-adenosine-methyltransferase non-catalytic subunit METTL14","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13107","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7644904","identifier":"Q9JIY2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JIY2/entry","name":"Cbll1","description":"E3 ubiquitin-protein ligase Hakai","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13480","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8311763","identifier":"Q8C3P7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C3P7/entry","name":"Mettl3","description":"N(6)-adenosine-methyltransferase catalytic subunit METTL3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9987670","identifier":"Q9ER69","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ER69/entry","name":"Wtap","description":"Pre-mRNA-splicing regulator WTAP","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15217","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3642","complexName":"CoQ biosynthetic complex","organismName":"Homo sapiens; 9606","description":"Required for the synthesis of Coenzyme Q (CoQ), an isoprenylated benzoquinone which functions as an electron carrier from complex I or II to complex III in the inner mitochondrial membrane and which also acts as an antioxidant  preventing the oxidation of lipoproteins and the plasma membrane. Assembly of the complex appears to be triggered by 4-hydroxyl-3-hexaprenyl benzoate (HHB) which is a precursor of CoQ.","predictedComplex":false,"interactors":[{"ac":"EBI-10897372","identifier":"Q9NZJ6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZJ6/entry","name":"COQ3","description":"Ubiquinone biosynthesis O-methyltransferase, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43464","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11017131","identifier":"Q99807","identifierLink":"https://www.uniprot.org/uniprotkb/Q99807/entry","name":"COQ7","description":"NADPH-dependent 3-demethoxyubiquinone 3-hydroxylase, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11237","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11472102","identifier":"CHEBI:24875","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:24875","name":"iron cation","description":"iron cation","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-12284865","identifier":"Q9Y3A0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3A0/entry","name":"COQ4","description":"Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12922","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12577722","identifier":"Q5HYK3","identifierLink":"https://www.uniprot.org/uniprotkb/Q5HYK3/entry","name":"COQ5","description":"2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43591","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-718148","identifier":"Q9Y2Z9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2Z9/entry","name":"COQ6","description":"Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43876","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724524","identifier":"O75208","identifierLink":"https://www.uniprot.org/uniprotkb/O75208/entry","name":"COQ9","description":"Ubiquinone biosynthesis protein COQ9, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21427","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3661","complexName":"Alternative nuclear cap-binding complex","organismName":"Mus musculus; 10090","description":"Binds co-transcriptionally to the 5-prime, m7GpppG-cap (m7G-cap) structures of RNA polymerase II transcripts (mainly pre-mRNAs and some asRNAs and lincRNAs). Required for mRNA export from the nucleus (by way of binding to TREX complex).  \r\n\r\nPossibly required for RNA interference (by way of binding asRNAs and lincRNAs) and splicing (by way of binding to exon-junction complex). Also binds serrate (Srrt/Ars2, Q99MR6) which is associated with suppression of poly-A tail formation in histone 3-prime end pre-mRNA processing (by comparison with classic CBC, CPX-923). Does not appear to bind snRNAs. \r\n\r\nBy way of comparison with classic CBC, alternative CBC is probably replaced by the cytoplasmic cap-binding complex eIF4F by binding to importin complex. Importin-complex-bound CBC gets reimported into the nucleus for reuse.","predictedComplex":false,"interactors":[{"ac":"EBI-11519402","identifier":"Q8BZR9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BZR9/entry","name":"Ncbp3","description":"Nuclear cap-binding protein subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16291","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16747696","identifier":"Q3UYV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q3UYV9/entry","name":"Ncbp1","description":"Nuclear cap-binding protein subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3662","complexName":"CoQ biosynthetic complex","organismName":"Mus musculus; 10090","description":"Required for the synthesis of Coenzyme Q (CoQ), an isoprenylated benzoquinone which functions as an electron carrier from complex I or II to complex III in the inner mitochondrial membrane and which also acts as an antioxidant  preventing the oxidation of lipoproteins and the plasma membrane. Assembly of the complex appears to be triggered by 4-hydroxyl-3-hexaprenyl benzoate (HHB) which is a precursor of CoQ.","predictedComplex":false,"interactors":[{"ac":"EBI-11472102","identifier":"CHEBI:24875","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:24875","name":"iron cation","description":"iron cation","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-20639727","identifier":"P97478","identifierLink":"https://www.uniprot.org/uniprotkb/P97478/entry","name":"Coq7","description":"NADPH-dependent 3-demethoxyubiquinone 3-hydroxylase, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11237","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20639758","identifier":"Q8BGB8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BGB8/entry","name":"Coq4","description":"Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12922","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8345854","identifier":"Q9CXI0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CXI0/entry","name":"Coq5","description":"2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR43591","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8350154","identifier":"Q8R1S0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R1S0/entry","name":"Coq6","description":"Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR43876","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8351371","identifier":"Q8BMS4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BMS4/entry","name":"Coq3","description":"Ubiquinone biosynthesis O-methyltransferase, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR43464","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8354092","identifier":"Q8K1Z0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K1Z0/entry","name":"Coq9","description":"Ubiquinone biosynthesis protein COQ9, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21427","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3663","complexName":"Caspase-8 complex","organismName":"Mus musculus; 10090","description":"Cysteine protease that specifically cleaves substrates with an aspartic acid residue at the P(1) position and has an optimal recognition motif that incorporates four amino acid residues N-terminal to the cleavage site. Caspase-8 is an initiator enzyme in death receptors induced pathways of which the downstream executioner Caspase-3 (CPX-3803) is a physiological target. It is activated via proteolytic cleavage by the DISC complex. Once activated Caspase-8 cleaves and activates Caspase-3, Caspase-4 (P70343), Caspase-6 (CPX-3944), Caspase-7 (CPX-3947) and Caspase-9 (CPX-3801 and CPX-3824).","predictedComplex":false,"interactors":[{"ac":"EBI-20651125","identifier":"O89110-PRO_0000004633","identifierLink":"https://www.uniprot.org/uniprotkb/O89110-PRO_0000004633/entry","name":"Casp8","description":"Caspase-8 subunit p18","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-20651130","identifier":"O89110-PRO_0000004635","identifierLink":"https://www.uniprot.org/uniprotkb/O89110-PRO_0000004635/entry","name":"Casp8","description":"Caspase-8 subunit p10","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-3681","complexName":"SCF-Ydr131c ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SCF-Ydr131c is a member of the SCF (Skp1-Cullin-F-box) E3 ubiquitin ligase family, in which the F-box protein, YDR131C (Q03899), forms the substrate recognition subunit. The complex may form a homodimer.","predictedComplex":false,"interactors":[{"ac":"EBI-19730","identifier":"P14682","identifierLink":"https://www.uniprot.org/uniprotkb/P14682/entry","name":"CDC34","description":"Ubiquitin-conjugating enzyme E2-34 kDa","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31686","identifier":"Q08273","identifierLink":"https://www.uniprot.org/uniprotkb/Q08273/entry","name":"HRT1","description":"RING-box protein HRT1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-36201","identifier":"Q03899","identifierLink":"https://www.uniprot.org/uniprotkb/Q03899/entry","name":"yd131","description":"F-box protein YDR131C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-4090","identifier":"P52286","identifierLink":"https://www.uniprot.org/uniprotkb/P52286/entry","name":"SKP1","description":"Suppressor of kinetochore protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4321","identifier":"Q12018","identifierLink":"https://www.uniprot.org/uniprotkb/Q12018/entry","name":"CDC53","description":"Cell division control protein 53","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3721","complexName":"PCNA homotrimer","organismName":"Caenorhabditis elegans; 6239","description":"Role in DNA replication, repair, cell-cycle control, and chromatin remodeling. Exists as a double back-to-back homotrimeric ring which encircles double-stranded DNA and slides spontaneously across it. Loaded onto at template-primer junctions synthesized on unwound DNA during S phase in an ATP-dependent process by replication factor C , where it recruits replicative DNA polymerases and stimulates their activity. The process of chromatin assembly is tightly coupled to DNA replication or repair and the double homotrimer allows DNA polymerase delta to binds to one homotrimer whilst the chromatin assembly factor-1 CNOT7 (Q17345)  binds to the other.","predictedComplex":false,"interactors":[{"ac":"EBI-318162","identifier":"O02115","identifierLink":"https://www.uniprot.org/uniprotkb/O02115/entry","name":"pcn-1","description":"Proliferating cell nuclear antigen","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11352","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3742","complexName":"cysEK cysteine synthase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the final steps in cysteine biosynthesis. The complex is comprised of the two enzymes that catalyze the final steps in cysteine biosynthesis. Serine acetyltransferase (CysE) catalyzes an acyl transfer from acetyl-CoA to L-Ser using a random-order kinetic mechanism to form O-acetyl-l-serine (OAS). OAS allosterically regulates CysB (P0A9F3), a transcriptional activator of the cysteine regulon, up-regulating CysB expression by binding to and preventing CysB from binding to its own promoter, where it inhibits transcription. OAS also regulates the balance of the bound and free forms of CysE and CysK by binding to and dissociating the complex. CysK a pyridoxal 5′-phosphate (PLP)-dependent enzyme, appears to be inactive in the complex, but when active, displaces the acetoxy group from OAS with bisulfide to yield L-Cys. Dissociation therefore stimulates both OAS consumption and cysteine synthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-1133237","identifier":"P0A9D4","identifierLink":"https://www.uniprot.org/uniprotkb/P0A9D4/entry","name":"cysE","description":"Serine acetyltransferase","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42811","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-553933","identifier":"P0ABK5","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABK5/entry","name":"cysK","description":"Cysteine synthase A","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10314","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8852014","identifier":"CHEBI:597326","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:597326","name":"pyridoxal 5'-phosphate(2-)","description":"pyridoxal 5'-phosphate(2-)","stochiometry":"minValue: 6, maxValue: 6","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3743","complexName":"pgaCD beta-glycosyltransferase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Required for the synthesis of poly-beta-1,6-N-acetylglucosamine (poly‐GlcNAc), catalyzing the polymerization of single monomer units of UDP-N-acetylglucosamine to produce the linear homopolymer. Poly-GlcNAc is required for the formation of an extracellular polymeric matrix produced when cells switch to growth in surface-associated multicellular communities or biofilms. The activity of the complex is allosterically regulated by the secondary messenger bis-(3'-5')-cyclic dimeric GMP (c‐di‐GMP) which binds to both proteins, stabilizing and activating the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-1784723","identifier":"CHEBI:49537","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49537","name":"c-di-gmp","description":"c-di-GMP","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-561450","identifier":"P75905","identifierLink":"https://www.uniprot.org/uniprotkb/P75905/entry","name":"pgaC","description":"Poly-beta-1,6-N-acetyl-D-glucosamine synthase","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43630","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-562069","identifier":"P69432","identifierLink":"https://www.uniprot.org/uniprotkb/P69432/entry","name":"pgaD","description":"Biofilm PGA synthesis protein PgaD","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]}]},{"complexAC":"CPX-3762","complexName":"Apoptosome","organismName":"Homo sapiens; 9606","description":"A protease complex that cleaves loops in pro-Caspase-3 (P42574) and pro-Caspase-7 (P55210) in an ATP-dependent manner to create active caspases (CPX-970 and CPX-2862) that execute the death program.\r\n\r\nIts formation is triggered by the release of Cytochrome c (P99999) from the mitochondria in response to intrinsic cell death stimuli. \r\n\r\nWhen released, Cytochrome c binds to APAF1 in a 1:1 stoichiometry to trigger nucleotide exchange and stepwise assembly of a heptameric structure. Pro-Caspase-9 is then recruited to form a multimeric Apaf1-Cytochrome c - pro-Caspase-9 complex. Once recruited, pro-Caspase-9 undergoes auto-cleavage resulting in two subunits: p35 and a p10. This step leads to the formation of a proteolytically active Apoptosome.","predictedComplex":false,"interactors":[{"ac":"EBI-1252632","identifier":"CHEBI:18248","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18248","name":"iron","description":"iron","stochiometry":"minValue: 7, maxValue: 7","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-13635286","identifier":"P55211-PRO_0000004643","identifierLink":"https://www.uniprot.org/uniprotkb/P55211-PRO_0000004643/entry","name":"CASP9","description":"Caspase-9 subunit p10","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-446479","identifier":"P99999","identifierLink":"https://www.uniprot.org/uniprotkb/P99999/entry","name":"CYCS","description":"Cytochrome c","stochiometry":"minValue: 7, maxValue: 7","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11961","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-446492","identifier":"O14727","identifierLink":"https://www.uniprot.org/uniprotkb/O14727/entry","name":"APAF1","description":"Apoptotic protease-activating factor 1","stochiometry":"minValue: 7, maxValue: 7","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22845","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-516799","identifier":"P55211","identifierLink":"https://www.uniprot.org/uniprotkb/P55211/entry","name":"CASP9","description":"Caspase-9","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10454","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 7, maxValue: 7","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3785","complexName":"Tryptase alpha/beta-1 complex","organismName":"Homo sapiens; 9606","description":"A trypsin-like serine protease predominantly found in mast cells from which it is secreted as a complex with proteoglycans upon its coupled activation-degranulation response. Active only after proteolytic removal of the pro-domain and functions both, as tetramer and monomer. Both forms are activated allosterically: The teramer is activated by insertion of the n-terminus of each protomer into its neighbour’s “activation pocket” while the monomer requires acidic conditions and heparin binding. While heparin binding in the tetramer is not required for its activity it both stabilizes the tetramer and allosterically conditions its active site. Substrates are diverse and include VIP, PAR2, pro-stromelysin, pro-urokinase, fibrinogen, cathelicidin, and kininogen. The active cleft of the tetramer faces towards the centre of the pore thus restricting accessibility for large substrates while the heparin-activated monomer processes large substrates like fibrinogen. Substrate catalysis leads to activation or inhibition of downstream biological pathways depending on context. \r\n\r\nTryptase is an important mediator of the allergic inflammatory responses in asthma. \r\n\r\nThe deletion in isoform-2 prevents tetramer formation. Tryptase alpha-1 is an inactive allele of beta-1.","predictedComplex":false,"interactors":[{"ac":"EBI-20764158","identifier":"Q15661-PRO_0000027480","identifierLink":"https://www.uniprot.org/uniprotkb/Q15661-PRO_0000027480/entry","name":"TPSAB1","description":"Tryptase alpha/beta-1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-3801","complexName":"Caspase-9 complex","organismName":"Mus musculus; 10090","description":"A cysteine protease complex that is an apical protease of the intrinsic apoptosis pathway. Generates the active forms of Caspases-3 (CPX-3803) and Caspase-7 (CPX-3947) by limited proteolysis, and thereby transmit the apoptotic signal to the execution phase. \r\n\r\nCaspase-9 is mostly active as part of a multicomponent complex known as the apoptosome (CPX-3824), however it has residual catalytic activity on its own.","predictedComplex":false,"interactors":[{"ac":"EBI-20767226","identifier":"Q8C3Q9-PRO_0000421173","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C3Q9-PRO_0000421173/entry","name":"Casp9","description":"Caspase-9 subunit p35","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-20767234","identifier":"Q8C3Q9-PRO_0000421175","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C3Q9-PRO_0000421175/entry","name":"Casp9","description":"Caspase-9 subunit p10","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-3802","complexName":"30S small ribosomal subunit","organismName":"Escherichia coli (strain K12); 83333","description":"Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). \r\n\r\nA ribosome is made two subunits - a smaller 30S subunit which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit (CPX-3807) which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 50S subunit acts as the decoding centre of the ribosome which brings mRNA and aminoacylated transfer (t)RNAs together, with the 16S ribosomal (r)RNA being required for the selection of the cognate tRNA. Guides the initiating start codon AUG of mRNA into position by recognizing the Shine-Dalgarno sequence, a complementary binding site about 8 base pairs upstream from the start codon. In order to form the translation complex with the 50S subunit, the 30S subunit must bind the Translation Initiation factor complex (CPX-2244), mRNA, and f-met-tRNA.","predictedComplex":false,"interactors":[{"ac":"EBI-1127032","identifier":"P0AG63","identifierLink":"https://www.uniprot.org/uniprotkb/P0AG63/entry","name":"rpsQ","description":"Small ribosomal subunit protein uS17","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10744","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20767452","identifier":"URS00005CADE5_83333","identifierLink":"http://rnacentral.org/rna/URS00005CADE5_83333","name":"16s_rrna_ecoli","description":"Ribosomal RNA 16S Escherichia coli","stochiometry":"minValue: 1, maxValue: 1","interactorType":"ribosomal rna","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-543068","identifier":"P02358","identifierLink":"https://www.uniprot.org/uniprotkb/P02358/entry","name":"rpsF","description":"Small ribosomal subunit protein bS6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR21011","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-543074","identifier":"P02359","identifierLink":"https://www.uniprot.org/uniprotkb/P02359/entry","name":"rpsG","description":"Small ribosomal subunit protein uS7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11205","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-543081","identifier":"P0A7W7","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7W7/entry","name":"rpsH","description":"Small ribosomal subunit protein uS8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11758","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-543165","identifier":"P0A7S9","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7S9/entry","name":"rpsM","description":"Small ribosomal subunit protein uS13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10871","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-543439","identifier":"P0A7V0","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7V0/entry","name":"rpsB","description":"Small ribosomal subunit protein uS2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR12534","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-543939","identifier":"P0A7V8","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7V8/entry","name":"rpsD","description":"Small ribosomal subunit protein uS4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11831","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-543949","identifier":"P0A7W1","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7W1/entry","name":"rpsE","description":"Small ribosomal subunit protein uS5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR13718","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-543960","identifier":"P0A7S3","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7S3/entry","name":"rpsL","description":"Small ribosomal subunit protein uS12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11652","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-543971","identifier":"P0AG59","identifierLink":"https://www.uniprot.org/uniprotkb/P0AG59/entry","name":"rpsN","description":"Small ribosomal subunit protein uS14","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR19836","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544015","identifier":"P0A7U3","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7U3/entry","name":"rpsS","description":"Small ribosomal subunit protein uS19","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11880","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544023","identifier":"P0A7U7","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7U7/entry","name":"rpsT","description":"Small ribosomal subunit protein bS20","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33398","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544602","identifier":"P0A7R5","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7R5/entry","name":"rpsJ","description":"Small ribosomal subunit protein uS10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11700","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544851","identifier":"P0A7V3","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7V3/entry","name":"rpsC","description":"Small ribosomal subunit protein uS3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11760","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-545119","identifier":"P0ADZ4","identifierLink":"https://www.uniprot.org/uniprotkb/P0ADZ4/entry","name":"rpsO","description":"Small ribosomal subunit protein uS15","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR23321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-546072","identifier":"P0A7X3","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7X3/entry","name":"rpsI","description":"Small ribosomal subunit protein uS9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR21569","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-546099","identifier":"P68679","identifierLink":"https://www.uniprot.org/uniprotkb/P68679/entry","name":"rpsU","description":"Small ribosomal subunit protein bS21","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR21109","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-546520","identifier":"P0AG67","identifierLink":"https://www.uniprot.org/uniprotkb/P0AG67/entry","name":"rpsA","description":"Small ribosomal subunit protein bS1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10724","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-546580","identifier":"P0A7T3","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7T3/entry","name":"rpsP","description":"Small ribosomal subunit protein bS16","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR12919","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-548800","identifier":"P0A7R9","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7R9/entry","name":"rpsK","description":"Small ribosomal subunit protein uS11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11759","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-548844","identifier":"P0A7T7","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7T7/entry","name":"rpsR","description":"Small ribosomal subunit protein bS18","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR13479","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3803","complexName":"Caspase-3 complex","organismName":"Mus musculus; 10090","description":"A thiol protease complex that is activated by Caspase-9 (CPX-3801 and CPX-3824) and is one of the main effector caspases in mammalian cells. Cleaves and activates Caspase-6 (CPX-3944), Caspase-7 (CPX-3947) and Caspase-9. \r\nAt the onset of apoptosis it proteolytically cleaves poly[ADP-ribose] polymerase 1 (PARP1, P11103) at a '214-Asp-|-Gly-215' bond. It is also the primary activator of apoptotic DNA fragmentation through inactivation of DNA fragmentation factor subunit alpha (DFFA - O54786).","predictedComplex":false,"interactors":[{"ac":"EBI-20767314","identifier":"P70677-PRO_0000004575","identifierLink":"https://www.uniprot.org/uniprotkb/P70677-PRO_0000004575/entry","name":"Casp3","description":"Caspase-3 subunit p17","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-20767320","identifier":"P70677-PRO_0000004576","identifierLink":"https://www.uniprot.org/uniprotkb/P70677-PRO_0000004576/entry","name":"Casp3","description":"Caspase-3 subunit p12","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-3804","complexName":"Tryptase alpha/beta-1 complex","organismName":"Mus musculus; 10090","description":"A trypsin-like serine protease predominantly found in mast cells from which it is secreted as a complex with proteoglycans upon its coupled activation-degranulation response. Active only after proteolytic removal of the pro-domain and functions both, as tetramer and monomer. Both forms are activated allosterically: the teramer is activated by insertion of the n-terminus of each protomer into its neighbour’s “activation pocket” while the monomer requires acidic conditions and heparin binding. While heparin binding in the tetramer is not required for its activity it both stabilizes the tetramer and allosterically conditions its active site. Substrates are diverse and include VIP, PAR2, pro-stromelysin, pro-urokinase, fibrinogen, cathelicidin, and kininogen. The active cleft of the tetramer faces towards the centre of the pore thus restricting accessibility for large substrates while the heparin-activated monomer processes large substrates like fibrinogen. Substrate catalysis leads to activation or inhibition of downstream biological pathways depending on context. \r\n\r\nThe deletion in isoform-2 prevents tetramer formation. Tryptase alpha-1 is an inactive allele of beta-1 (by similarity from human).","predictedComplex":false,"interactors":[{"ac":"EBI-20767391","identifier":"Q02844-PRO_0000027495","identifierLink":"https://www.uniprot.org/uniprotkb/Q02844-PRO_0000027495/entry","name":"Tpsab1","description":"Tryptase","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-3805","complexName":"Tryptase beta-2 complex","organismName":"Homo sapiens; 9606","description":"A trypsin-like serine protease predominantly found in mast cells from which it is secreted as a complex with proteoglycans upon its coupled activation-degranulation response. Active only after proteolytic removal of the pro-domain and functions both, as tetramer and monomer. Both forms are activated allosterically: The teramer is activated by insertion of the n-terminus of each protomer into its neighbour’s “activation pocket” while the monomer requires acidic conditions and heparin binding. While heparin binding in the tetramer is not required for its activity it both stabilizes the tetramer and allosterically conditions its active site. Substrates are diverse and include VIP, PAR2, pro-stromelysin, pro-urokinase, fibrinogen, cathelicidin, and kininogen. The active cleft of the tetramer faces towards the centre of the pore thus restricting accessibility for large substrates while the heparin-activated monomer processes large substrates like fibrinogen. Substrate catalysis leads to activation or inhibition of downstream biological pathways depending on context. \r\n\r\nTryptase is an important mediator of the allergic inflammatory responses in asthma. \r\n\r\nTryptase beta-3 is an inactive allele of beta-2.","predictedComplex":false,"interactors":[{"ac":"EBI-20767437","identifier":"P20231-PRO_0000027482","identifierLink":"https://www.uniprot.org/uniprotkb/P20231-PRO_0000027482/entry","name":"TPSB2","description":"Tryptase beta-2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-3806","complexName":"Tryptase beta-2 complex","organismName":"Mus musculus; 10090","description":"A trypsin-like serine protease predominantly found in mast cells from which it is secreted as a complex with proteoglycans upon its coupled activation-degranulation response. Active only after proteolytic removal of the pro-domain and functions both, as tetramer and monomer. Both forms are activated allosterically: The teramer is activated by insertion of the n-terminus of each protomer into its neighbour’s “activation pocket” while the monomer requires acidic conditions and heparin binding. While heparin binding in the tetramer is not required for its activity it both stabilizes the tetramer and allosterically conditions its active site. Substrates are diverse and include VIP, PAR2, pro-stromelysin, pro-urokinase, fibrinogen, cathelicidin, and kininogen. The active cleft of the tetramer faces towards the centre of the pore thus restricting accessibility for large substrates while the heparin-activated monomer processes large substrates like fibrinogen. Substrate catalysis leads to activation or inhibition of downstream biological pathways depending on context. \r\n\r\nTryptase beta-3 is an inactive allele of beta-2.","predictedComplex":false,"interactors":[{"ac":"EBI-20767599","identifier":"P21845-PRO_0000027491","identifierLink":"https://www.uniprot.org/uniprotkb/P21845-PRO_0000027491/entry","name":"Tpsb2","description":"Tryptase beta-2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-3807","complexName":"50S large ribosomal subunit","organismName":"Escherichia coli (strain K12); 83333","description":"Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). \r\n\r\nA ribosome is made two subunits - a smaller 30S subunit (CPX-3802) which binds to a larger subunit and the mRNA pattern, and a larger 50S subunit which binds to the tRNA, the amino acids, and the smaller subunit. When a ribosome finishes reading an mRNA molecule, these two subunits split apart. The 30S subunit is responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation.","predictedComplex":false,"interactors":[{"ac":"EBI-1112692","identifier":"P0A7Q6","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7Q6/entry","name":"rpmJ","description":"Large ribosomal subunit protein bL36A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1112732","identifier":"P0A7N4","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7N4/entry","name":"rpmF","description":"Large ribosomal subunit protein bL32","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR35534","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1113805","identifier":"P0A7P5","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7P5/entry","name":"rpmH","description":"Large ribosomal subunit protein bL34","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR14503","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1115812","identifier":"P0A7M9","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7M9/entry","name":"rpmE","description":"Large ribosomal subunit protein bL31","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33280","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1133348","identifier":"P0AG51","identifierLink":"https://www.uniprot.org/uniprotkb/P0AG51/entry","name":"rpmD","description":"Large ribosomal subunit protein uL30","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR15892","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1134774","identifier":"P0A7Q1","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7Q1/entry","name":"rpmI","description":"Large ribosomal subunit protein bL35","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20767693","identifier":"URS00005B2216_83333","identifierLink":"http://rnacentral.org/rna/URS00005B2216_83333","name":"23s_ecoli","description":"23S ribosomal RNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"ribosomal rna","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-20767698","identifier":"URS000002D309_83333","identifierLink":"http://rnacentral.org/rna/URS000002D309_83333","name":"5s_ecoli","description":"5S ribosomal RNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"ribosomal rna","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-542200","identifier":"P60438","identifierLink":"https://www.uniprot.org/uniprotkb/P60438/entry","name":"rplC","description":"Large ribosomal subunit protein uL3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11229","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-542207","identifier":"P0C018","identifierLink":"https://www.uniprot.org/uniprotkb/P0C018/entry","name":"rplR","description":"Large ribosomal subunit protein uL18","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR12899","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-542255","identifier":"P61175","identifierLink":"https://www.uniprot.org/uniprotkb/P61175/entry","name":"rplV","description":"Large ribosomal subunit protein uL22","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR13501","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-542264","identifier":"P0ADZ0","identifierLink":"https://www.uniprot.org/uniprotkb/P0ADZ0/entry","name":"rplW","description":"Large ribosomal subunit protein uL23","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11620","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-542445","identifier":"P0AG48","identifierLink":"https://www.uniprot.org/uniprotkb/P0AG48/entry","name":"rplU","description":"Large ribosomal subunit protein bL21","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR21349","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-542475","identifier":"P0A7N9","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7N9/entry","name":"rpmG","description":"Large ribosomal subunit protein bL33","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR15238","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-543017","identifier":"P02413","identifierLink":"https://www.uniprot.org/uniprotkb/P02413/entry","name":"rplO","description":"Large ribosomal subunit protein uL15","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR12934","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-543024","identifier":"P0A7M2","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7M2/entry","name":"rpmB","description":"Large ribosomal subunit protein bL28","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR13528","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-543515","identifier":"P60422","identifierLink":"https://www.uniprot.org/uniprotkb/P60422/entry","name":"rplB","description":"Large ribosomal subunit protein uL2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR13691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-543702","identifier":"P0A7K2","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7K2/entry","name":"rplL","description":"Large ribosomal subunit protein bL12","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR45987","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-543771","identifier":"P0A7L0","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7L0/entry","name":"rplA","description":"Large ribosomal subunit protein uL1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR36427","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-543801","identifier":"P0AA10","identifierLink":"https://www.uniprot.org/uniprotkb/P0AA10/entry","name":"rplM","description":"Large ribosomal subunit protein uL13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11545","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-543891","identifier":"P0A7K6","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7K6/entry","name":"rplS","description":"Large ribosomal subunit protein bL19","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR15680","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544558","identifier":"P0AG44","identifierLink":"https://www.uniprot.org/uniprotkb/P0AG44/entry","name":"rplQ","description":"Large ribosomal subunit protein bL17","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR14413","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544699","identifier":"P0A7L3","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7L3/entry","name":"rplT","description":"Large ribosomal subunit protein bL20","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10986","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-545597","identifier":"P60723","identifierLink":"https://www.uniprot.org/uniprotkb/P60723/entry","name":"rplD","description":"Large ribosomal subunit protein uL4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10746","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-545605","identifier":"P0ADY3","identifierLink":"https://www.uniprot.org/uniprotkb/P0ADY3/entry","name":"rplN","description":"Large ribosomal subunit protein uL14","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-545956","identifier":"P62399","identifierLink":"https://www.uniprot.org/uniprotkb/P62399/entry","name":"rplE","description":"Large ribosomal subunit protein uL5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11994","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-546389","identifier":"P0AG55","identifierLink":"https://www.uniprot.org/uniprotkb/P0AG55/entry","name":"rplF","description":"Large ribosomal subunit protein uL6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11655","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-546437","identifier":"P0A7R1","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7R1/entry","name":"rplI","description":"Large ribosomal subunit protein bL9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR21368","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-546481","identifier":"P60624","identifierLink":"https://www.uniprot.org/uniprotkb/P60624/entry","name":"rplX","description":"Large ribosomal subunit protein uL24","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR12903","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-546493","identifier":"P0A7M6","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7M6/entry","name":"rpmC","description":"Large ribosomal subunit protein uL29","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10916","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-546827","identifier":"P0A7J3","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7J3/entry","name":"rplJ","description":"Large ribosomal subunit protein uL10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11560","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-546875","identifier":"P0A7L8","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7L8/entry","name":"rpmA","description":"Large ribosomal subunit protein bL27","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR15893","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-547288","identifier":"P0A7J7","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7J7/entry","name":"rplK","description":"Large ribosomal subunit protein uL11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11661","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-548773","identifier":"P0ADY7","identifierLink":"https://www.uniprot.org/uniprotkb/P0ADY7/entry","name":"rplP","description":"Large ribosomal subunit protein uL16","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR12220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-553087","identifier":"P68919","identifierLink":"https://www.uniprot.org/uniprotkb/P68919/entry","name":"rplY","description":"Large ribosomal subunit protein bL25","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33284","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9136181","identifier":"P0A7N1","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7N1/entry","name":"ykgM","description":"Large ribosomal subunit protein bL31B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33280","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3821","complexName":"nrdDG class III anaerobic ribonucleotide reductase activation complex","organismName":"Escherichia coli (strain K12); 83333","description":"Formation of this complex leads to the activation of the nrdD glycyl radical homodimer (CPX-3822) which catalyzes the conversion of ribonucleotides into the deoxyribonucleotides required for DNA synthesis and repair. nrdG generates an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine, nrdG then dissociates from the complex to leave the activated homodimer.","predictedComplex":false,"interactors":[{"ac":"EBI-1135026","identifier":"P0A9N8","identifierLink":"https://www.uniprot.org/uniprotkb/P0A9N8/entry","name":"nrdG","description":"Anaerobic ribonucleoside-triphosphate reductase-activating protein","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30352","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12520674","identifier":"CHEBI:67040","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:67040","name":"s-adenosyl-l-methioninate","description":"S-adenosyl-L-methioninate","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-370011","identifier":"P28903","identifierLink":"https://www.uniprot.org/uniprotkb/P28903/entry","name":"nrdD","description":"Anaerobic ribonucleoside-triphosphate reductase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR21075","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3822","complexName":"nrdD class III anaerobic ribonucleotide reductase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Glycyl radical deoxyribonucleotides reductase required for DNA synthesis and repair. The formation of the nrdDG class III anaerobic ribonucleotide reductase activation complex (CPX-3821) leads to activation of the NRD homodimer. This then dissociates and catalyzes several rounds of NTP reduction in the presence of formate as an electron donor, with ATP as the allosteric effector and requiring Mg2+ and K+ to stimulate the reaction. \r\n\r\nExposure of the activated reductase to oxygen leads to C-terminal truncation and inactivation of the protein, by cleavage at the N-terminal side of Gly-681.","predictedComplex":false,"interactors":[{"ac":"EBI-370011","identifier":"P28903","identifierLink":"https://www.uniprot.org/uniprotkb/P28903/entry","name":"nrdD","description":"Anaerobic ribonucleoside-triphosphate reductase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR21075","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3823","complexName":"epg-6-atg-2 complex","organismName":"Caenorhabditis elegans; 6239","description":"Essential for autophagy, a catabolic process that sequesters undesired cellular material into autophagosomes for delivery to lysosomes for degradation. Functions at a late step of autophagosome formation where it regulates the distribution of autophagy proteins such as atg-9 (Q3T903) and atg-13 (P34379). Within the complex itself, epg-6 binds to phosphatidylinositols on early autophagic structures to promote autophagosome formation. In particular, epg-6 binds with high affinity to phosphatidylinositols including phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 5-phosphate (PtdIns(5)P), but more weakly to phosphatidylinositol 4-phosphate (PtdIns(4)P) and phosphatidylinositol 3,5-biphosphate (PtdIns(3,5)P2).","predictedComplex":false,"interactors":[{"ac":"EBI-20768589","identifier":"Q21480","identifierLink":"https://www.uniprot.org/uniprotkb/Q21480/entry","name":"atg-2","description":"Autophagy-related protein 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13190","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7684889","identifier":"Q86MP3","identifierLink":"https://www.uniprot.org/uniprotkb/Q86MP3/entry","name":"epg-6","description":"Ectopic P granules protein 6","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11227","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3824","complexName":"Apoptosome","organismName":"Mus musculus; 10090","description":"A protease complex that cleaves loops in pro-Caspase-3 (P70677) and pro-Caspase-7 (P97864) in an ATP-dependent manner to create active caspases (CPX-3803 and CPX-3947) that execute the death program.\r\n\r\nIts formation is triggered by the release of Cytochrome c (P62897) from the mitochondria in response to intrinsic cell death stimuli. \r\n\r\nWhen released, Cytochrome c binds to APAF1 in a 1:1 stoichiometry to trigger nucleotide exchange and stepwise assembly of a heptameric structure. Pro-Caspase-9 is then recruited to form a multimeric Apaf1-Cytochrome c - pro-Caspase-9 complex. Once recruited, pro-Caspase-9 undergoes auto-cleavage resulting in two subunits: p35 and a p10. This step leads to the formation of a proteolytically active Apoptosome.","predictedComplex":false,"interactors":[{"ac":"EBI-1202386","identifier":"O88879","identifierLink":"https://www.uniprot.org/uniprotkb/O88879/entry","name":"Apaf1","description":"Apoptotic protease-activating factor 1","stochiometry":"minValue: 7, maxValue: 7","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22845","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1252632","identifier":"CHEBI:18248","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18248","name":"iron","description":"iron","stochiometry":"minValue: 7, maxValue: 7","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-20767226","identifier":"Q8C3Q9-PRO_0000421173","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C3Q9-PRO_0000421173/entry","name":"Casp9","description":"Caspase-9 subunit p35","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-20767234","identifier":"Q8C3Q9-PRO_0000421175","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C3Q9-PRO_0000421175/entry","name":"Casp9","description":"Caspase-9 subunit p10","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-2308573","identifier":"P62897","identifierLink":"https://www.uniprot.org/uniprotkb/P62897/entry","name":"Cycs","description":"Cytochrome c, somatic","stochiometry":"minValue: 7, maxValue: 7","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11961","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 7, maxValue: 7","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3861","complexName":"lptBFG LPS ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"Required for the assembly of the dense outer membrane coating of lipopolysaccharides (LPS) required by Gram-negative bacteria to protect themselves from chemical stressors. \r\n\r\nPart of a seven-subunit assembly that spans the cellular envelope. \r\nExtracts LPS from the outer leaflet of the inner membrane and provides the energy to drive its transport across the inner membrane, periplasm and into the outer membrane through an ATPase-dependent mechanism. The cytoplasmic nucleotide-binding domain of the lptB dimer hydrolyzes ATP to switch the substrate cavity of the transmembrane domains of the lptF/G dimer between inward- and outward-facing conformations. LPS then crosses the periplasm along a continuous hydrophobic groove formed by lptC (P0ADV9), lptA (P0ADV1) and lptD (P31554). The lptDE complex (CPX-1093) subsequently sorts LPS to the outer leaflet of the outer membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-371195","identifier":"P0A9V1","identifierLink":"https://www.uniprot.org/uniprotkb/P0A9V1/entry","name":"lptB","description":"Lipopolysaccharide export system ATP-binding protein LptB","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR45772","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7041027","identifier":"P0AF98","identifierLink":"https://www.uniprot.org/uniprotkb/P0AF98/entry","name":"lptF","description":"Lipopolysaccharide export system permease protein LptF","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7041050","identifier":"P0ADC6","identifierLink":"https://www.uniprot.org/uniprotkb/P0ADC6/entry","name":"lptG","description":"Lipopolysaccharide export system permease protein LptG","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3863","complexName":"atg-5-atg-12-atg-16.1-atg-16.2 complex","organismName":"Caenorhabditis elegans; 6239","description":"Essential for autophagy during nutrient deprivation, a catabolic process that sequesters undesired cellular material into autophagosomes for delivery to lysosomes for degradation. May promote autophagosome formation. Functions as an E3-like enzyme in the lgg-1 (Q09490) conjugation system. The atg-5-atg-12-atg-16.1 (CPX-3865), atg-5-atg-12-atg-16.2 (CPX-3866) and atg-5-atg-12-atg-16.1-atg-16.2 (CPX-3863) complexes target the autophagic membrane via the atg-5-atg-16.1 and/or atg-5-atg-16.2 complex moieties and then recruits an atg-3:lgg-1 thioester intermediate via the interaction between atg-3 (Q9N369) and atg-12/lgg-3 (Q10931). The ATG12-ATG5 complex (CPX-3864) conjugate facilitates the transfer reaction of lgg-1 from atg-3 to phosphatidylethanolamine (PE) through a reorganization of the catalytic centre of the E2-like enzyme atg-3. The C-terminal glycine of lgg-1 is then conjugated to the amine moiety of PE. The roles of atg-16.1 (Q19124) and atg-16.2 (Q09406), which have no E3-like activity appears to be to target the ATG12-ATG5 conjugate to the autophagic membranes. lgg-1-PE/ATG12-ATG5 complexes form homogeneous oligomers, comprising two to four subunits. Atg-16.1 and/or atg-16.2 may then act to reorganize lgg-1-PE/ATG12-ATG5 oligomers to form a continuous, flat protein layer with meshwork-like architecture on membranes.","predictedComplex":false,"interactors":[{"ac":"EBI-20797856","identifier":"Q19124","identifierLink":"https://www.uniprot.org/uniprotkb/Q19124/entry","name":"atg-16.1","description":"Autophagic-related protein 16.1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR19878","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20797904","identifier":"Q3V5I7","identifierLink":"https://www.uniprot.org/uniprotkb/Q3V5I7/entry","name":"atg-5","description":"Autophagy-related protein 5","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20797923","identifier":"Q10931","identifierLink":"https://www.uniprot.org/uniprotkb/Q10931/entry","name":"lgg-3","description":"Ubiquitin-like protein atg-12","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13385","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-324230","identifier":"Q09406","identifierLink":"https://www.uniprot.org/uniprotkb/Q09406/entry","name":"atg-16.2","description":"Autophagic-related protein 16.2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR19878","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3864","complexName":"ATG12-ATG5 complex","organismName":"Caenorhabditis elegans; 6239","description":"Essential for autophagy during nutrient deprivation, a catabolic process that sequesters undesired cellular material into autophagosomes for delivery to lysosomes for degradation. Contributes to nutrition homeostasis and damage control in eukaryotic cells. Acts as an E3-like ligase dependent on ATP and two enzymes, atg-7 (G5EBK4) as an E1-like activating enzyme and atg-10 (Q18991) as an E2-like conjugating enzyme. Required for lipidation of lgg-1 (Q09490), for example by phosphatidylethanolamine, and associates to the vesicle membranes once bound to atg-16.1 (Q19124) in the atg-5-atg-12-atg-16.1 complex (CPX-3865), atg-16.2 (Q09406) in the atg-5-atg-12-atg-16.2 complex (CPX-3866), and atg-16.1/atg-16.2 in the complex atg-5-atg-12-atg-16.1-atg-16.2 complex (CPX-3863).","predictedComplex":false,"interactors":[{"ac":"EBI-20797904","identifier":"Q3V5I7","identifierLink":"https://www.uniprot.org/uniprotkb/Q3V5I7/entry","name":"atg-5","description":"Autophagy-related protein 5","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20797923","identifier":"Q10931","identifierLink":"https://www.uniprot.org/uniprotkb/Q10931/entry","name":"lgg-3","description":"Ubiquitin-like protein atg-12","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13385","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3865","complexName":"atg-5-atg-12-atg-16.1 complex","organismName":"Caenorhabditis elegans; 6239","description":"Essential for autophagy during nutrient deprivation, a catabolic process that sequesters undesired cellular material into autophagosomes for delivery to lysosomes for degradation. May promote autophagosome formation. Functions as an E3-like enzyme in the lgg-1 (Q09490) conjugation system. The atg-5-atg-12-atg-16.1 (CPX-3865), atg-5-atg-12-atg-16.2 (CPX-3866) and atg-5-atg-12-atg-16.1-atg-16.2 (CPX-3863) complexes target the autophagic membrane via the atg-5-atg-16.1 and/or atg-5-atg-16.2 complex moieties and then recruits an atg-3:lgg-1 thioester intermediate via the interaction between atg-3 (Q9N369) and atg-12/lgg-3 (Q10931). The ATG12-ATG5 complex (CPX-3864) conjugate facilitates the transfer reaction of lgg-1 (Q09490) from atg-3  to phosphatidylethanolamine (PE) through a reorganization of the catalytic centre of the E2-like enzyme atg-3 (Q9N369). The C-terminal glycine of lgg-1is then conjugated to the amine moiety of PE. The roles of atg-16.1 (Q19124) and atg-16.2 (Q09406), which have no E3-like activity appears to be to target the ATG12-ATG5 conjugate to the autophagic membranes. lgg-1-PE/ATG12-ATG5 complexes form homogeneous oligomers, comprising two to four subunits. Atg-16.1 and/or atg-16.2 may then act to reorganize lgg-1-PE/ATG12-ATG5 oligomers to form a continuous, flat protein layer with meshwork-like architecture on membranes.","predictedComplex":false,"interactors":[{"ac":"EBI-20797856","identifier":"Q19124","identifierLink":"https://www.uniprot.org/uniprotkb/Q19124/entry","name":"atg-16.1","description":"Autophagic-related protein 16.1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR19878","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20797904","identifier":"Q3V5I7","identifierLink":"https://www.uniprot.org/uniprotkb/Q3V5I7/entry","name":"atg-5","description":"Autophagy-related protein 5","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20797923","identifier":"Q10931","identifierLink":"https://www.uniprot.org/uniprotkb/Q10931/entry","name":"lgg-3","description":"Ubiquitin-like protein atg-12","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13385","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3866","complexName":"atg-5-atg-12-atg-16.2 complex","organismName":"Caenorhabditis elegans; 6239","description":"Essential for autophagy during nutrient deprivation, a catabolic process that sequesters undesired cellular material into autophagosomes for delivery to lysosomes for degradation. Promotes autophagosome formation playing a role in the recruitment of lipidated lgg-1 (Q09490) to the autophagosome membrane. Also required for the nucleation of lgg-1 positive autophagosomes. Essential for autophagy during nutrient deprivation, a catabolic process that sequesters undesired cellular material into autophagosomes for delivery to lysosomes for degradation. May promote autophagosome formation. Specifically, functions as an E3-like enzyme in the lgg-1 conjugation system. The atg-5-atg-12-atg-16.1 (CPX-3865), atg-5-atg-12-atg-16.2 (CPX-3866) and atg-5-atg-12-atg-16.1-atg-16.2 (CPX-3863) complexes target the autophagic membrane via the atg-5-atg-16.1 and/or atg-5-atg-16.2 complex moieties and then recruits an atg-3:lgg-1 thioester intermediate via the interaction between atg-3 (Q9N369) and atg-12/lgg-3 (Q10931). The ATG12-ATG5 complex (CPX-3864) conjugate facilitates the transfer reaction of lgg-1 (Q09490) from atg-3 to phosphatidylethanolamine (PE) through a reorganization of the catalytic centre of the E2-like enzyme atg-3 (Q9N369). The C-terminal glycine of lgg-1 is then conjugated to the amine moiety of PE. The roles of atg-16.1 (Q19124) and atg-16.2 (Q09406), which have no E3-like activity appears to be to target the ATG12-ATG5 conjugate to the autophagic membranes. lgg-1-PE/ATG12-ATG5 complexes form homogeneous oligomers, comprising two to four subunits. Atg-16.1 and/or atg-16.2 may then act to reorganize lgg-1-PE/ATG12-ATG5 oligomers to form a continuous, flat protein layer with meshwork-like architecture on membranes.","predictedComplex":false,"interactors":[{"ac":"EBI-20797904","identifier":"Q3V5I7","identifierLink":"https://www.uniprot.org/uniprotkb/Q3V5I7/entry","name":"atg-5","description":"Autophagy-related protein 5","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20797923","identifier":"Q10931","identifierLink":"https://www.uniprot.org/uniprotkb/Q10931/entry","name":"lgg-3","description":"Ubiquitin-like protein atg-12","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13385","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-324230","identifier":"Q09406","identifierLink":"https://www.uniprot.org/uniprotkb/Q09406/entry","name":"atg-16.2","description":"Autophagic-related protein 16.2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR19878","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3881","complexName":"arr-1-mpz-1-daf-18 complex","organismName":"Caenorhabditis elegans; 6239","description":"Signalling complex that positively regulates the insulin-like daf-2 (Q968Y9) signaling pathway to control the phosphorylation and intracellular localisation of the forkhead transcription factor FOXO/daf-16 (O16850). Formation of the complex probably inhibits the phosphatase activity of PTEN/daf-18 (G5EE01). The complex may play a role in the regulation of lifespan.","predictedComplex":false,"interactors":[{"ac":"EBI-20798434","identifier":"P51485","identifierLink":"https://www.uniprot.org/uniprotkb/P51485/entry","name":"arr-1","description":"Beta-arrestin arr-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11792","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2914422","identifier":"G5EE01","identifierLink":"https://www.uniprot.org/uniprotkb/G5EE01/entry","name":"daf-18","description":"Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase daf-18","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2915667","identifier":"G5ECZ8","identifierLink":"https://www.uniprot.org/uniprotkb/G5ECZ8/entry","name":"mpz-1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR19964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3882","complexName":"daf-16-ftt-2 complex","organismName":"Caenorhabditis elegans; 6239","description":"The complex functions in the insulin-like daf-2 (Q968Y9) signaling pathway to negatively regulate the transcriptional activity of the forkhead transcription factor FOXO/daf-16 (O16850). Binding of fft-2 (Q20655) to daf-16 sequesters daf-16  to the cytoplasm. This negatively regulates the expression of daf-16 target genes which are involved in a range of processes including apoptosis, the oxidative stress response, DNA repair and metabolism.","predictedComplex":false,"interactors":[{"ac":"EBI-324028","identifier":"O16850","identifierLink":"https://www.uniprot.org/uniprotkb/O16850/entry","name":"daf-16","description":"Forkhead box protein O","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-966073","identifier":"Q20655","identifierLink":"https://www.uniprot.org/uniprotkb/Q20655/entry","name":"ftt-2","description":"14-3-3-like protein 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR18860","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3883","complexName":"daf-16-sir-2.1 complex","organismName":"Caenorhabditis elegans; 6239","description":"Functions to regulate gene expression and promote longevity in the stress response pathway. Complex most likely sequesters the forkhead transcription factor FOXO/daf-16 (O16850) to the nucleus and thus serves to promote the transcriptional activity of FOXO/daf-16 in response to stress. The 14-3-3 proteins par-5 (P41932) or ftt-2 (P41932) may be required as scaffolding proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-324028","identifier":"O16850","identifierLink":"https://www.uniprot.org/uniprotkb/O16850/entry","name":"daf-16","description":"Forkhead box protein O","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-966082","identifier":"Q21921","identifierLink":"https://www.uniprot.org/uniprotkb/Q21921/entry","name":"sir-2.1","description":"NAD-dependent protein deacetylase sir-2.1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11085","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3884","complexName":"daf-16-par-5 complex","organismName":"Caenorhabditis elegans; 6239","description":"The complex may function in the insulin-like daf-2 (Q968Y9) signaling pathway to negatively regulate the transcriptional activity of the forkhead transcription factor FOXO/daf-16 (O16850). Binding of par-5 (P41932) to daf-16 may sequester daf-16 to the cytoplasm.","predictedComplex":false,"interactors":[{"ac":"EBI-318108","identifier":"P41932","identifierLink":"https://www.uniprot.org/uniprotkb/P41932/entry","name":"par-5","description":"14-3-3-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR18860","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-324028","identifier":"O16850","identifierLink":"https://www.uniprot.org/uniprotkb/O16850/entry","name":"daf-16","description":"Forkhead box protein O","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3885","complexName":"sir-2.1-ftt-2 complex","organismName":"Caenorhabditis elegans; 6239","description":"Complex may function in the nucleus to regulate the transcriptional activities of transcription factors such as the forkhead transcription factor FOXO/daf-16 (O16850).","predictedComplex":false,"interactors":[{"ac":"EBI-966073","identifier":"Q20655","identifierLink":"https://www.uniprot.org/uniprotkb/Q20655/entry","name":"ftt-2","description":"14-3-3-like protein 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR18860","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-966082","identifier":"Q21921","identifierLink":"https://www.uniprot.org/uniprotkb/Q21921/entry","name":"sir-2.1","description":"NAD-dependent protein deacetylase sir-2.1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11085","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3886","complexName":"sir-2.1-par-5 complex","organismName":"Caenorhabditis elegans; 6239","description":"Complex may function in the nucleus to regulate the transcriptional activities of transcription factors such as the forkhead transcription factor FOXO/daf-16 (O16850).","predictedComplex":false,"interactors":[{"ac":"EBI-318108","identifier":"P41932","identifierLink":"https://www.uniprot.org/uniprotkb/P41932/entry","name":"par-5","description":"14-3-3-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR18860","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-966082","identifier":"Q21921","identifierLink":"https://www.uniprot.org/uniprotkb/Q21921/entry","name":"sir-2.1","description":"NAD-dependent protein deacetylase sir-2.1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11085","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3887","complexName":"TRPP complex","organismName":"Caenorhabditis elegans; 6239","description":"Probable sensory receptor that localizes to sensory cilia of male-specific sensory neurons and is involved in several aspects of male mating behaviour. Is thus required for male reproduction. The localisation of the complex is regulated by the inositol polyphosphate 5-phosphatase cil-1 (P34370).","predictedComplex":false,"interactors":[{"ac":"EBI-2529627","identifier":"Q09624","identifierLink":"https://www.uniprot.org/uniprotkb/Q09624/entry","name":"lov-1","description":"Location of vulva defective 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10877","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3890911","identifier":"Q9U1S7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9U1S7/entry","name":"pkd-2","description":"Polycystin-2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10877","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3888","complexName":"SDC complex","organismName":"Caenorhabditis elegans; 6239","description":"Sex-determination complex involved in hermaphrodite sexual development by modulating chromosome and sex-specific gene expression. sdc-2, within the complex, recruits the Condensin I-like dosage compensation complex (CPX-1273) to hermaphrodite X-chromosomes to repress the transcription of male sex-determining genes, such as the male sex-determination gene her-1 (P34704), and promote hermaphrodite differentiation. Association with diverse DNA targets results in different degrees of repression.","predictedComplex":false,"interactors":[{"ac":"EBI-20798952","identifier":"P24349","identifierLink":"https://www.uniprot.org/uniprotkb/P24349/entry","name":"sdc-1","description":"Zinc finger protein sdc-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24408","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20798975","identifier":"G5EBL3","identifierLink":"https://www.uniprot.org/uniprotkb/G5EBL3/entry","name":"sdc-2","description":"Sex determination and dosage compensation protein sdc-2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13270","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20798990","identifier":"P34706","identifierLink":"https://www.uniprot.org/uniprotkb/P34706/entry","name":"sdc-3","description":"Zinc finger protein sdc-3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]}]},{"complexAC":"CPX-3889","complexName":"Katanin complex","organismName":"Caenorhabditis elegans; 6239","description":"Microtubule severing complex involved in establishing the meiotic spindle. Specifically mediates the disassembly of microtubles of the meiotic spindle in order to promote the rapid reorganisation of cellular microtubule arrays. Mei-1 (P34808) is the catalytic subunit of the complex which severs microtubules in an ATP-dependent manner, whilst mei-2 (O44740) may serve as a targeting subunit.","predictedComplex":false,"interactors":[{"ac":"EBI-323243","identifier":"O44740","identifierLink":"https://www.uniprot.org/uniprotkb/O44740/entry","name":"mei-2","description":"Meiotic spindle formation protein 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-323248","identifier":"P34808","identifierLink":"https://www.uniprot.org/uniprotkb/P34808/entry","name":"mei-1","description":"Meiotic spindle formation protein mei-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR23074","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3890","complexName":"FACT complex hmg-3 variant","organismName":"Caenorhabditis elegans; 6239","description":"FACT is an H2A-H2B histone chaperon complex that helps reorganize nucleosomes in an ATP-independent fashion. It is involved in various processes related to chromatin dynamics: DNA replication, DNA damage and repair, transcription initiation and elongation. Binds histone H2A-H2B dimers and possibly small amounts of H3H4. Facilitates RNAPol II driven transcription through chromatin by destabilizing nucleosomal structure so that one of the H2A-H2B dimers is removed upon RNA Pol II passage. Subsequently brings back the histones and thereby maintains nucleosome integrity after RNA Pol II passage. Involved in cell cycle progression and chromosomal segregation in embryos. Plays a role in the development of the anterior pharynx. The FACT complex may also include hmg-4 (P41848) instead of hmg-3 (O01683) in the FACT complex hmg-4 variant (CPX-3891). There may be some redundancy between the roles of hmg-3 and hmg-4, however, hmg-3 expression seems to be germline specific.","predictedComplex":false,"interactors":[{"ac":"EBI-2004633","identifier":"O01683","identifierLink":"https://www.uniprot.org/uniprotkb/O01683/entry","name":"hmg-3","description":"FACT complex subunit ssrp1-B","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45849","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20799273","identifier":"Q9N5R9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9N5R9/entry","name":"spt-16","description":"FACT complex subunit spt-16","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13980","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3891","complexName":"FACT complex hmg-4 variant","organismName":"Caenorhabditis elegans; 6239","description":"FACT is an H2A-H2B histone chaperon complex that helps reorganize nucleosomes in an ATP-independent fashion. It is involved in various processes related to chromatin dynamics: DNA replication, DNA damage and repair, transcription initiation and elongation. Binds histone H2A-H2B dimers and possibly small amounts of H3H4. Facilitates RNAPol II driven transcription through chromatin by destabilizing nucleosomal structure so that one of the H2A-H2B dimers is removed upon RNA Pol II passage. Subsequently brings back the histones and thereby maintains nucleosome integrity after RNA Pol II passage. Involved in cell cycle progression and chromosomal segregation in embryos. Plays a role in the development of the anterior pharynx. The FACT complex may also include hmg-3 (O01683) instead of hmg-4 (P41848) in the FACT complex hmg-3 variant (CPX-3890). There may be some redundancy between the roles of hmg-3 and hmg-4, However, hmg-4 is expressed in both somatic tissues and the germline.","predictedComplex":false,"interactors":[{"ac":"EBI-20799273","identifier":"Q9N5R9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9N5R9/entry","name":"spt-16","description":"FACT complex subunit spt-16","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13980","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-328030","identifier":"P41848","identifierLink":"https://www.uniprot.org/uniprotkb/P41848/entry","name":"hmg-4","description":"FACT complex subunit SSRP1-A","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45849","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3901","complexName":"Caspase-2 complex","organismName":"Mus musculus; 10090","description":"Thiol-dependent aspartate-specific protease complex possessing features of both initiator and executioner caspases and required in stress-induced apoptosis. Genotoxic stress, mitotic catastrophe, heat shock, ER stress or bacterial toxins can stimulate Caspase-2 activation. It is activated by autocatalytic cleavage in the Caspase-2-PIDDosome (CPX-3963). Once activated, it is released from the PIDDosome and induces BID (P70444) cleavage, BAX (Q07813) translocation to mitochondria, subsequent cytochrome c (P62897) release and consequent activation of the apoptotic process. Specifically cleaves substrates with an aspartic acid residue at position P1 and has a preferred cleavage sequence of Val-Asp-Val-Ala-Asp-|-. \r\n\r\nIn addition, Caspase-2 has been reported to be a negative regulator of necroptosis and to be indispensable for correct cell proliferation and genomic stability acting as a potential tumor suppressor factor. \r\n\r\nCaspase-2 is negatively regulated by phosphorylation at distinct sites (Ser157 and Ser340) during cell division and in nutrient abundance conditions. Also, in response to heat shock, Caspase-2 activity is suppressed by the chaperone HSP90AA1(P07901).","predictedComplex":false,"interactors":[{"ac":"EBI-20818887","identifier":"P29594-PRO_0000004547","identifierLink":"https://www.uniprot.org/uniprotkb/P29594-PRO_0000004547/entry","name":"Casp2","description":"Caspase-2 subunit p18","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-20818914","identifier":"P29594-PRO_0000004549","identifierLink":"https://www.uniprot.org/uniprotkb/P29594-PRO_0000004549/entry","name":"Casp2","description":"Caspase-2 subunit p12","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-3905","complexName":"Caspase-2 PIDDosome","organismName":"Homo sapiens; 9606","description":"Cysteine-type endopeptidase complex that assembles in response to genotoxic stress, mitotic catastrophe, heat shock, ER stress or bacterial toxins and is considered to be the primary activating platform for Caspase-2 (CPX-969). Facilitates Caspase-2 autocatalytic cleavage. Once activated, Caspase-2 is released and induces BID (P55957) cleavage, BAX (Q07812) translocation to mitochondria, subsequent cytochrome c (P99999) release and consequent activation of the apoptotic process.\r\n\r\nAltered Caspase-2 and CRADD expressions were observed in mantle cell lymphoma tumor samples.","predictedComplex":false,"interactors":[{"ac":"EBI-520342","identifier":"P42575","identifierLink":"https://www.uniprot.org/uniprotkb/P42575/entry","name":"CASP2","description":"Caspase-2","stochiometry":"minValue: 7, maxValue: 7","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10454","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-520375","identifier":"P78560","identifierLink":"https://www.uniprot.org/uniprotkb/P78560/entry","name":"CRADD","description":"Death domain-containing protein CRADD","stochiometry":"minValue: 7, maxValue: 7","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15034","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-520427","identifier":"Q9HB75","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HB75/entry","name":"PIDD1","description":"p53-induced death domain-containing protein 1","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45752","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3921","complexName":"2-oxoglutarate dehydrogenase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Multi-enzyme complex that catalyzes the conversion of 2-oxoglutarate (2-ketoglutarate) to succinyl-CoA and CO2, with the production of NADH, during the citric acid cycle. \r\n\r\nIt contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3). \r\n\r\n2-oxoglutarate is bound and decarboxylated by sucA, sucB catalyzes the transfer of a succinyl group from the S-succinyldihydrolipoyl moiety to coenzyme A, forming succinyl-CoA and lpdA catalyzes the transfer of electrons to the ultimate acceptor, NAD.","predictedComplex":false,"interactors":[{"ac":"EBI-16416616","identifier":"CHEBI:83088","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:83088","name":"(r)-lipoate","description":"(R)-lipoate","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-542856","identifier":"P0A9P0","identifierLink":"https://www.uniprot.org/uniprotkb/P0A9P0/entry","name":"lpdA","description":"Dihydrolipoyl dehydrogenase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR22912","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-543523","identifier":"P0AFG3","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFG3/entry","name":"sucA","description":"2-oxoglutarate dehydrogenase E1 component","stochiometry":"minValue: 12, maxValue: 12","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR23152","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-558621","identifier":"P0AFG6","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFG6/entry","name":"sucB","description":"Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex","stochiometry":"minValue: 24, maxValue: 24","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9691551","identifier":"CHEBI:58937","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58937","name":"thiamine(1+) diphosphate(3-)","description":"thiamine(1+) diphosphate(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3924","complexName":"Mitotic Checkpoint Complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Acts as a crucial surveillance mechanism to ensure faithful chromosome segregation. MCC prevents the onset of anaphase until all chromosomes are properly attached with the spindle microtubules. The checkpoint can be considered as a signal transduction pathway. The activation of the checkpoint is initiated when unoccupied kinetochores or kinetochores lacking tension are detected in the cell. The MCC prevents premature chromosome segregation by inhibiting the APC/C-CDC20 holoenzyme, an E3 ubiquitin ligase responsible for targeting securin (P21135) and cyclin B for degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-1252744","identifier":"P78972","identifierLink":"https://www.uniprot.org/uniprotkb/P78972/entry","name":"slp1","description":"WD repeat-containing protein slp1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR19918","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1269284","identifier":"O59767","identifierLink":"https://www.uniprot.org/uniprotkb/O59767/entry","name":"mad3","description":"Mitotic spindle checkpoint component mad3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-1269310","identifier":"O14417","identifierLink":"https://www.uniprot.org/uniprotkb/O14417/entry","name":"mad2","description":"Mitotic spindle checkpoint component mad2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3943","complexName":"Pyruvate dehydrogenase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Converts pyruvate to acetyl-CoA and CO2, thus providing a metabolic connection between glycolysis, whose end product is pyruvate, and the tricarboxylic acid cycle, which starts with acetyl-CoA. \r\n\r\nIt contains multiple copies of three enzymatic components, that are encoded by a single operon: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). \r\n\r\nIn anaerobic Escherichia coli, the complex is normally inactive due to inhibition of ldpA by NADH. During aerobic growth, the NADH generated in glycolysis is oxidized and the complex becomes active.","predictedComplex":false,"interactors":[{"ac":"EBI-16416616","identifier":"CHEBI:83088","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:83088","name":"(r)-lipoate","description":"(R)-lipoate","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-542683","identifier":"P0AFG8","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFG8/entry","name":"aceE","description":"Pyruvate dehydrogenase E1 component","stochiometry":"minValue: 24, maxValue: 24","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43825","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-542707","identifier":"P06959","identifierLink":"https://www.uniprot.org/uniprotkb/P06959/entry","name":"aceF","description":"Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex","stochiometry":"minValue: 24, maxValue: 24","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43178","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-542856","identifier":"P0A9P0","identifierLink":"https://www.uniprot.org/uniprotkb/P0A9P0/entry","name":"lpdA","description":"Dihydrolipoyl dehydrogenase","stochiometry":"minValue: 12, maxValue: 12","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR22912","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":"minValue: 12, maxValue: 12","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9691551","identifier":"CHEBI:58937","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58937","name":"thiamine(1+) diphosphate(3-)","description":"thiamine(1+) diphosphate(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3944","complexName":"Caspase-6 complex","organismName":"Mus musculus; 10090","description":"A cysteine protease complex that specifically cleaves substrates with an aspartic acid residue at position P1 and has a preferred cleavage sequence of Val-Glu-His-Asp-|-. Caspase-6 is an initiator enzyme involved in the activation cascade of caspases responsible for apoptosis execution. \r\n\r\nCaspase-6 is capable of autoactivation and/or may be activated via proteolytic cleavage by Caspase-3 (CPX-3803) or Caspase-8 (CPX-3663). Once activated it cleaves pro-Caspase-2 (P29594) and pro-Caspase-8 (O89110) allowing their oligomerization into active Caspase-2 (CPX-3901) and Caspase-8. Caspase-6 induces mitochondrial permeabilisation, which leads to cytochrome c (P62897) release and activation of the Apotosome (CPX-3824).","predictedComplex":false,"interactors":[{"ac":"EBI-20827582","identifier":"O08738-PRO_0000004613","identifierLink":"https://www.uniprot.org/uniprotkb/O08738-PRO_0000004613/entry","name":"Casp6","description":"Caspase-6 subunit p18","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-20827589","identifier":"O08738-PRO_0000004615","identifierLink":"https://www.uniprot.org/uniprotkb/O08738-PRO_0000004615/entry","name":"Casp6","description":"Caspase-6 subunit p11","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-3946","complexName":"Mitotic Checkpoint Complex","organismName":"Homo sapiens; 9606","description":"Acts as a crucial surveillance mechanism to ensure faithful chromosome segregation. MCC prevents the onset of anaphase until all chromosomes are properly attached with the spindle microtubules. The checkpoint can be considered as a signal transduction pathway. The activation of the checkpoint is initiated when unoccupied kinetochores or kinetochores lacking tension are detected in the cell. The MCC prevents premature chromosome segregation by inhibiting the APC/C-CDC20 holoenzyme, an E3 ubiquitin ligase responsible for targeting securin (O95997/Q9NZH5) and cyclin B for degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-1001438","identifier":"O60566","identifierLink":"https://www.uniprot.org/uniprotkb/O60566/entry","name":"BUB1B","description":"Mitotic checkpoint serine/threonine-protein kinase BUB1 beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14030","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1050987","identifier":"O43684","identifierLink":"https://www.uniprot.org/uniprotkb/O43684/entry","name":"BUB3","description":"Mitotic checkpoint protein BUB3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-367462","identifier":"Q12834","identifierLink":"https://www.uniprot.org/uniprotkb/Q12834/entry","name":"CDC20","description":"Cell division cycle protein 20 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19918","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-78203","identifier":"Q13257","identifierLink":"https://www.uniprot.org/uniprotkb/Q13257/entry","name":"MAD2L1","description":"Mitotic spindle assembly checkpoint protein MAD2A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3947","complexName":"Caspase-7 complex","organismName":"Mus musculus; 10090","description":"A cysteine protease complex of the executioner Caspase group that specifically cleaves substrates with an aspartic acid residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-. \r\n\r\nOnce activated by Caspase-8 (CPX-3663) or Caspase-9 (CPX-3801 or CPX-3824), Caspase-7 leads to apoptosis and inflammation by cleaving sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly[ADP-ribose] polymerase 1 (Parp1, P11103) at a '214-Asp-|-Gly-215' bond.","predictedComplex":false,"interactors":[{"ac":"EBI-20827692","identifier":"P97864-PRO_0000004625","identifierLink":"https://www.uniprot.org/uniprotkb/P97864-PRO_0000004625/entry","name":"Casp7","description":"Caspase-7 subunit p20","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-20827702","identifier":"P97864-PRO_0000004627","identifierLink":"https://www.uniprot.org/uniprotkb/P97864-PRO_0000004627/entry","name":"Casp7","description":"Caspase-7 subunit p11","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-3949","complexName":"Glycine cleavage system complex","organismName":"Escherichia coli (strain K12); 83333","description":"Multienzyme complex that catalyses the reversible oxidation of glycine, yielding carbon dioxide (CO), ammonia (NH3), 5,10-methylenetetrahydrofolate and a reduced pyridine nucleotide.  The 1-carbon units thus generated are used in the synthesis of purines, histidine, thymine, pantothenate, and methionine and in the formylation of the aminoacylated initiator fMet-TRNAfMet required for translation initiation. \r\n\r\ngcvP binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO2 is released and the remaining methylamine moiety is transferred to the lipoamide cofactor of gcvH,  which is bound to the P protein prior to decarboxylation of glycine. gcvT catalyzes the release of NH3 from the methylamine group and transfers the remaining C1 unit to tetrahydrofolate, forming 5,10-methylenetetrahydrofolate. lpdA then oxidizes the lipoic acid component of the H protein and transfers the electrons to NAD+, to form NADH .","predictedComplex":false,"interactors":[{"ac":"EBI-1130796","identifier":"P27248","identifierLink":"https://www.uniprot.org/uniprotkb/P27248/entry","name":"gcvT","description":"Aminomethyltransferase","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43757","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16416616","identifier":"CHEBI:83088","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:83088","name":"(r)-lipoate","description":"(R)-lipoate","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-542856","identifier":"P0A9P0","identifierLink":"https://www.uniprot.org/uniprotkb/P0A9P0/entry","name":"lpdA","description":"Dihydrolipoyl dehydrogenase","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR22912","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-551489","identifier":"P33195","identifierLink":"https://www.uniprot.org/uniprotkb/P33195/entry","name":"gcvP","description":"Glycine dehydrogenase (decarboxylating)","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11773","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8852014","identifier":"CHEBI:597326","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:597326","name":"pyridoxal 5'-phosphate(2-)","description":"pyridoxal 5'-phosphate(2-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9134702","identifier":"P0A6T9","identifierLink":"https://www.uniprot.org/uniprotkb/P0A6T9/entry","name":"gcvH","description":"Glycine cleavage system H protein","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11715","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3961","complexName":"C9orf72-SMCR8 complex","organismName":"Homo sapiens; 9606","description":"Potential GDP-GTP exchange factor (GEF) for Rab GTPases and may therefore regulate vesicular trafficking. May act as a negative regulator of autoimmunity, through negative regulation of lysosomal exocytosis. May also function in the autolysosomal pathway through interactions with the autophagy initiation complex (CPX-373).","predictedComplex":false,"interactors":[{"ac":"EBI-16693635","identifier":"Q96LT7-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q96LT7-1/entry","name":"C9orf72","description":"Guanine nucleotide exchange factor C9orf72","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2819137","identifier":"Q9HAD4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HAD4/entry","name":"WDR41","description":"WD repeat-containing protein 41","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22805","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2961718","identifier":"Q8TEV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TEV9/entry","name":"SMCR8","description":"Guanine nucleotide exchange protein SMCR8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3962","complexName":"C9orf72-SMCR8 complex","organismName":"Mus musculus; 10090","description":"Potential GDP-GTP exchange factor (GEF) for Rab GTPases and may therefore regulate vesicular trafficking. May act as a negative regulator of autoimmunity, through negative regulation of lysosomal exocytosis. May also function in the autolysosomal pathway through interactions with the autophagy initiation complex (CPX-380).","predictedComplex":false,"interactors":[{"ac":"EBI-20938904","identifier":"Q6DFW0-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6DFW0-1/entry","name":"C9orf72","description":"Guanine nucleotide exchange factor C9orf72 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-20938909","identifier":"Q3UMB5","identifierLink":"https://www.uniprot.org/uniprotkb/Q3UMB5/entry","name":"Smcr8","description":"Guanine nucleotide exchange protein SMCR8","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR31334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20938942","identifier":"Q3UDP0","identifierLink":"https://www.uniprot.org/uniprotkb/Q3UDP0/entry","name":"Wdr41","description":"WD repeat-containing protein 41","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22805","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3963","complexName":"Caspase-2 PIDDosome","organismName":"Mus musculus; 10090","description":"Cysteine-type endopeptidase complex that assembles in response to genotoxic stress, mitotic catastrophe, heat shock, ER stress or bacterial toxins and is considered to be the primary activating platform for Caspase-2 (CPX-3901). Facilitates Caspase-2 autocatalytic cleavage. Once activated, Caspase-2 is released and induces Bid (P70444) cleavage, Bax (Q07813) translocation to mitochondria, subsequent cytochrome c (P62897) release and consequent activation of the apoptotic process.","predictedComplex":false,"interactors":[{"ac":"EBI-20818835","identifier":"P29594","identifierLink":"https://www.uniprot.org/uniprotkb/P29594/entry","name":"Casp2","description":"Caspase-2","stochiometry":"minValue: 7, maxValue: 7","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10454","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20939530","identifier":"Q9ERV7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ERV7/entry","name":"Pidd1","description":"p53-induced death domain-containing protein 1","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45752","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8391259","identifier":"O88843","identifierLink":"https://www.uniprot.org/uniprotkb/O88843/entry","name":"Cradd","description":"Death domain-containing protein CRADD","stochiometry":"minValue: 7, maxValue: 7","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15034","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3964","complexName":"fadBA fatty acid oxidation complex, aerobic conditions","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the final step of fatty acid oxidation in the beta-oxidation pathway. The beta-oxidation pathway acts in a cyclic fashion, in which each cycle results in shortening the input acyl-CoA by two carbon atoms to give acetyl-CoA. Produced acetyl-CoA molecules enter the citric acid cycle (Krebs cycle) to be oxidized for energy production. \r\n\r\nThis complex has five separate enzymatic activities including hydration, oxidation and thiolytic cleavage functions. Escherichia coli uses fatty acids as a sole carbon and energy source during aerobic growth.","predictedComplex":false,"interactors":[{"ac":"EBI-20944681","identifier":"P21151","identifierLink":"https://www.uniprot.org/uniprotkb/P21151/entry","name":"fadA","description":"3-ketoacyl-CoA thiolase FadA","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43853","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-370062","identifier":"P21177","identifierLink":"https://www.uniprot.org/uniprotkb/P21177/entry","name":"fadB","description":"Fatty acid oxidation complex subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43612","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3966","complexName":"fadJI fatty acid oxidation complex, anaerobic conditions","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the oxidiation of fatty acids under anaerobic conditions using a terminal respiratory electron acceptor such as nitrate. \r\n\r\nThe beta-oxidation pathway acts in a cyclic fashion, in which each cycle results in shortening the input acyl-CoA by two carbon atoms to give acetyl-CoA. Produces acetyl-CoA molecules enter the citric acid cycle (Krebs cycle) to be oxidized for energy production.\r\n \r\nThis complex has multiple enzymatic activities including hydration, oxidation and thiolytic cleavage functions and is capable of oxidising fatty acids such as octanoate and decanoate, that cannot be used by Escherichia coli under aerobic conditions. The complex may be partially functional redundant with FadBA (CPX-3964) and be active under aerobic conditions, increasing the efficiency of beta-oxidation under these circumstances by favouring substrates of different chain length.","predictedComplex":false,"interactors":[{"ac":"EBI-545361","identifier":"P77399","identifierLink":"https://www.uniprot.org/uniprotkb/P77399/entry","name":"fadJ","description":"Fatty acid oxidation complex subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43612","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-545371","identifier":"P76503","identifierLink":"https://www.uniprot.org/uniprotkb/P76503/entry","name":"fadI","description":"3-ketoacyl-CoA thiolase FadI","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR18919","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3968","complexName":"Mitotic Checkpoint Complex","organismName":"Mus musculus; 10090","description":"Acts as a crucial surveillance mechanism to ensure faithful chromosome segregation. MCC prevents the onset of anaphase until all chromosomes are properly attached with the spindle microtubules. The checkpoint can be considered as a signal transduction pathway. The activation of the checkpoint is initiated when unoccupied kinetochores or kinetochores lacking tension are detected in the cell. The MCC prevents premature chromosome segregation by inhibiting the APC/C-CDC20 holoenzyme, an E3 ubiquitin ligase responsible for targeting securin (Q9CQJ7/Q3Y5K5) and cyclin B for degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-1781718","identifier":"Q9WVA3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WVA3/entry","name":"Bub3","description":"Mitotic checkpoint protein BUB3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2551389","identifier":"Q9JJ66","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JJ66/entry","name":"Cdc20","description":"Cell division cycle protein 20 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR19918","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2552918","identifier":"Q9Z1B5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z1B5/entry","name":"Mad2l1","description":"Mitotic spindle assembly checkpoint protein MAD2A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2553777","identifier":"Q9Z1S0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z1S0/entry","name":"Bub1b","description":"Mitotic checkpoint serine/threonine-protein kinase BUB1 beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14030","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3982","complexName":"dosPC diguanylate cyclase/c-di-GMP phosphodiesterase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Oxygen sensor complex that controls the production and removal of cyclic diguanylate (c-di-GMP), a second messenger which is important in the regulation of biofilm production and changes in motility and virulence. \r\n\r\nThe dosCP operon encodes two oxygen sensors that have antagonistic enzyme properties, with dosP being a heme-based c-di-GMP phosphodiesterase and dosC displaying diguanylate cyclase (DGC) activity in response to oxygen availability. dosC contains an N-terminal sensory globin domain that binds heme in an apolar binding pocket and catalyzes the synthesis of c-di-GMP via the condensation of 2 GTP molecules. Binding of O2 to the reduced heme in dosP enhances c-di-GMP phosphodiesterase activity, possibly die to a conformational change which releases catalytic suppression caused by the heme sensor domain. The complex may also be part of a larger ribonucleoprotein assembly which performs oxygen-dependent RNA processing.","predictedComplex":false,"interactors":[{"ac":"EBI-1124248","identifier":"P76129","identifierLink":"https://www.uniprot.org/uniprotkb/P76129/entry","name":"dosP","description":"Oxygen sensor protein DosP","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33121","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20986988","identifier":"P0AA89","identifierLink":"https://www.uniprot.org/uniprotkb/P0AA89/entry","name":"dosC","description":"Diguanylate cyclase DosC","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR45138","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3983","complexName":"Hsp90-cdc-37-pph-5 phosphatase complex","organismName":"Caenorhabditis elegans; 6239","description":"Serine-threonine phosphatase complex that most likely dephosphorylates a myriad of proteins involved in different signaling pathways. The complex may also act as a chaperone complex that is required for the proper folding, maturation and stabilization of target protein. Implicated in wide ranging cellular processes, including apoptosis, differentiation, DNA damage response, cell survival, regulation of ion channels or circadian rhythms, in response to steroid and thyroid hormones, calcium, fatty acids, TGF-beta as well as oxidative and genotoxic stresses. Dephosphorylates cdc-37-Ser14 within the complex. pph-5 resides in an autoinhibited state, in which its TPR domain interacts with the catalytic region and prevents substrate access to the catalytic pocket. Binding of pph-5 to daf-21/Hsp90 releases the autoinhibition of pph-5 to promote phosphatase activity of the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-313329","identifier":"Q18688","identifierLink":"https://www.uniprot.org/uniprotkb/Q18688/entry","name":"hsp-90","description":"Heat shock protein 90","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11528","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-316460","identifier":"Q9NES8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NES8/entry","name":"pph-5","description":"Serine/threonine-protein phosphatase 5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45668","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-329675","identifier":"O02108","identifierLink":"https://www.uniprot.org/uniprotkb/O02108/entry","name":"cdc-37","description":"Probable Hsp90 co-chaperone cdc37","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12800","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1528","complexName":"SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK15","organismName":"Arabidopsis thaliana; 3702","description":"SCF-TIR1 is a member of the SCF (Skp1-Cullin-F-box) E3 ubiquitin ligase family, which catalyse the last step of ubiquitination cascade, promoting transfer of ubiquitin from an E2 enzyme to form a covalent bond with a substrate lysine. 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In response to genotoxic damage, the complex is loaded around DNA.","predictedComplex":false,"interactors":[{"ac":"EBI-323706","identifier":"G5EFI9","identifierLink":"https://www.uniprot.org/uniprotkb/G5EFI9/entry","name":"hus-1","description":"Checkpoint protein","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12900","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-323732","identifier":"G5EC44","identifierLink":"https://www.uniprot.org/uniprotkb/G5EC44/entry","name":"mrt-2","description":"Cell cycle checkpoint protein RAD1 homolog mrt-2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10870","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-330330","identifier":"Q95Q27","identifierLink":"https://www.uniprot.org/uniprotkb/Q95Q27/entry","name":"hpr-9","description":"Cell cycle checkpoint protein hpr-9","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR15237","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1616","complexName":"Clathrin complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Building block of the polyhedral coat of coated pits and vesicles, forming a polymeric mechanical scaffold on the vesicle surface. 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EDS1-PAD4-SAG101 complexes (CPX-1325 & CPX-1619) are required for resistance signalling against turnip crinkle virus.","predictedComplex":false,"interactors":[{"ac":"EBI-16422562","identifier":"Q4F883","identifierLink":"https://www.uniprot.org/uniprotkb/Q4F883/entry","name":"SAG101","description":"Senescence-associated carboxylesterase 101","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR46898","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16748660","identifier":"Q9SU71","identifierLink":"https://www.uniprot.org/uniprotkb/Q9SU71/entry","name":"EDS1B","description":"Protein EDS1B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR47090","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1618","complexName":"EDS1-PAD4 complex, variant EDS1B","organismName":"Arabidopsis thaliana; 3702","description":"Functions in basal disease resistance and resistance (R) gene-mediated effector triggered immunity (ETI), regulates accumulation of the hormone salicylic acid (SA) which is a necessary component of systemic immunity. 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EDS1-PAD4-SAG101 complexes (CPX-1325 & CPX-1619) are required for resistance signalling against turnip crinkle virus.","predictedComplex":false,"interactors":[{"ac":"EBI-1390441","identifier":"Q9S745","identifierLink":"https://www.uniprot.org/uniprotkb/Q9S745/entry","name":"PAD4","description":"Lipase-like PAD4","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR47413","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16748660","identifier":"Q9SU71","identifierLink":"https://www.uniprot.org/uniprotkb/Q9SU71/entry","name":"EDS1B","description":"Protein EDS1B","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR47090","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1619","complexName":"EDS1-PAD4-SAG101 complex, variant EDS1B","organismName":"Arabidopsis thaliana; 3702","description":"Functions in basal disease resistance and resistance (R) gene-mediated effector triggered immunity (ETI), regulates accumulation of the hormone salicylic acid (SA) which is a necessary component of systemic immunity. 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Unwinds D-loops to promote the formation of non-crossover recombinants through the synthesis-dependent strand annealing pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-2555534","identifier":"Q96E14","identifierLink":"https://www.uniprot.org/uniprotkb/Q96E14/entry","name":"RMI2","description":"RecQ-mediated genome instability protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR33962","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-621339","identifier":"Q9H9A7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H9A7/entry","name":"RMI1","description":"RecQ-mediated genome instability protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14790","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-621345","identifier":"Q13472","identifierLink":"https://www.uniprot.org/uniprotkb/Q13472/entry","name":"TOP3A","description":"DNA topoisomerase 3-alpha","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11390","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-621372","identifier":"P54132","identifierLink":"https://www.uniprot.org/uniprotkb/P54132/entry","name":"BLM","description":"RecQ-like DNA helicase BLM","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13710","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3302","complexName":"TDRD3-TOP3B type IA topoisomerase complex","organismName":"Mus musculus; 10090","description":"DNA/RNA type IA topoisomerase family, which transiently cleaves and rejoins one strand of the DNA duplex, relaxing  supercoiled DNA and torsional tension of DNA introduced during DNA replication and transcription, resolving recombination intermediates during meiosis and DNA repair. Transiently traps the 5-prime end of the cleaved DNA by covalent bonding via catalytic tyrosine residues.","predictedComplex":false,"interactors":[{"ac":"EBI-16728364","identifier":"Q9Z321","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z321/entry","name":"Top3b","description":"DNA topoisomerase 3-beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11390","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16767508","identifier":"Q91W18-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q91W18-1/entry","name":"Tdrd3","description":"Tudor domain-containing protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-3303","complexName":"BTR double Holliday Junction dissolution complex","organismName":"Mus musculus; 10090","description":"Processes the double Holliday Junction, a DNA intermediate formed during homologous recombination, by convergent DNA branch migration of the two Holliday junctions in the structure and DNA strand decatenation, to yield non-crossover recombinants. Unwinds D-loops to promote the formation of non-crossover recombinants through the synthesis-dependent strand annealing pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-16767576","identifier":"O88700","identifierLink":"https://www.uniprot.org/uniprotkb/O88700/entry","name":"Blm","description":"RecQ-like DNA helicase BLM","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13710","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16767679","identifier":"Q3UPE3","identifierLink":"https://www.uniprot.org/uniprotkb/Q3UPE3/entry","name":"Rmi2","description":"RecQ-mediated genome instability protein 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR33962","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2551265","identifier":"O70157","identifierLink":"https://www.uniprot.org/uniprotkb/O70157/entry","name":"Top3a","description":"DNA topoisomerase 3-alpha","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11390","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2553444","identifier":"Q9D4G9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D4G9/entry","name":"Rmi1","description":"RecQ-mediated genome instability protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14790","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3342","complexName":"Seipin complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for resulating the size, morphology and content of lipid droplets. Acts to stabilize the contact points between the endoplasmic reticulum and lipid droplet, preventing the equilibration of the two membrane systems and establishing a diffusion barrier. The complex modulates the balance between neutral lipid and phospholipid synthesis and appears to affect the distribution of enzymes involved in phosphatidic acid to diacyl glycerol conversion. Mutations in human seipin cause lipodystrophy.","predictedComplex":false,"interactors":[{"ac":"EBI-21668","identifier":"P25587","identifierLink":"https://www.uniprot.org/uniprotkb/P25587/entry","name":"LDB16","description":"Protein LDB16","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-35851","identifier":"Q06058","identifierLink":"https://www.uniprot.org/uniprotkb/Q06058/entry","name":"SEI1","description":"Seipin","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-3361","complexName":"bZIP transcription factor complex, CEBPB-CEBPB","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. The DNA recognition sequence depends on the composition of the bZIP dimer with the complex either binding to the preferred region of one of the partners or to a novel bZIP cognate site. This complex regulates the expression of genes involved in immune and inflammatory responses, binding to the regulatory regions of several acute-phase and cytokines genes and probably playing a role in the regulation of acute-phase reaction, inflammation and hemopoiesis.","predictedComplex":false,"interactors":[{"ac":"EBI-969696","identifier":"P17676","identifierLink":"https://www.uniprot.org/uniprotkb/P17676/entry","name":"CEBPB","description":"CCAAT/enhancer-binding protein beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3381","complexName":"Egg-3/4/5 MBK-2 complex","organismName":"Caenorhabditis elegans; 6239","description":"Pseudophosphatase complex required for oocyte-to-zygote transition. Components of the complex sequester and modulate the kinase activity of mbk-2 before and during the early phases of meiosis to regulate oocyte maturation and egg activation. The complex localises to the cortex of the oocyte before the meiotic divisions and it is retained there during the early meiotic divisions. The inactive phosphatases egg-3, egg-4 and egg-5 are required for the cortical localisation of mbk-2. In particular, egg-3 acts as scaffold to tether mbk-2, egg-4 and egg-5 to the oocyte cortex, and thus restricts mbk-2 activity to the cortex during meiosis I. egg-4 and egg-5 bind to mbk-2 and inhibit its kinase activity. egg-3 does not affect mbk-2 activity. During anaphase of meiosis I, egg-3 relocalises to the cytoplasm and is targeted for degradation by the Anaphase Promoting Complex/Cyclosome (CPX-3382). This releases mbk-2 from the complex to modify the oocyte proteins required after meiosis.","predictedComplex":false,"interactors":[{"ac":"EBI-2005616","identifier":"Q9XTF3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XTF3/entry","name":"mbk-2","description":"Dual specificity tyrosine-phosphorylation-regulated kinase mbk-2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24058","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2476895","identifier":"Q20402","identifierLink":"https://www.uniprot.org/uniprotkb/Q20402/entry","name":"egg-3","description":"Protein tyrosine phosphatase-like protein egg-3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR46163","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2476926","identifier":"O01767","identifierLink":"https://www.uniprot.org/uniprotkb/O01767/entry","name":"egg-4","description":"Inactive protein-tyrosine phosphatase egg-4","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR19134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2476960","identifier":"O61789","identifierLink":"https://www.uniprot.org/uniprotkb/O61789/entry","name":"egg-5","description":"Inactive protein-tyrosine phosphatase egg-5","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR19134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3382","complexName":"Anaphase-promoting complex","organismName":"Caenorhabditis elegans; 6239","description":"APC, a key regulator of cell cycle progression, is a conserved E3 ubiqutin ligase which facilitates multiubiqutination of cell cycle proteins, including cyclins, so marking them for proteasomal destruction. Generally believed that APC acts as a scaffold that brings E2 enzymes and substrates into close proximity. APC activity is required for metaphase-anaphase transition, mitotic exit, G1 phase and DNA replication. Acts by mediating the ubiquitination and subsequent degradation of target proteins. Has a developmental role in early embryogenesis and the metaphase to anaphase transition in oocyte and spermatocyte meiosis and mitosis in germ cells. Required for embryonic anterior-posterior axis formation. Involved in regulating GABA neurotransmitter release at neuromuscular junctions in GABA motor neurons.\r\n\r\nIn particular, targets the inactive phosphatase egg-3, a component of the Egg-3/4/5 MBK-2 complex (CPX-3381), which is involved in oocyte-to-zygote transition, for degradation by the proteasome during meiotic divisions.","predictedComplex":false,"interactors":[{"ac":"EBI-11464923","identifier":"Q93903","identifierLink":"https://www.uniprot.org/uniprotkb/Q93903/entry","name":"gfi-3","description":"Protein gfi-3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12830","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16826226","identifier":"Q95Q00","identifierLink":"https://www.uniprot.org/uniprotkb/Q95Q00/entry","name":"such-1","description":"Suppressor of spindle checkpoint defect 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12830","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16826239","identifier":"H2L2B8","identifierLink":"https://www.uniprot.org/uniprotkb/H2L2B8/entry","name":"apc-10","description":"Anaphase-promoting complex subunit 10","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12936","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16851340","identifier":"Q17883","identifierLink":"https://www.uniprot.org/uniprotkb/Q17883/entry","name":"apc-17","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-2004414","identifier":"Q09410","identifierLink":"https://www.uniprot.org/uniprotkb/Q09410/entry","name":"emb-1","description":"Anaphase-promoting complex subunit emb-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-311807","identifier":"G5EG38","identifierLink":"https://www.uniprot.org/uniprotkb/G5EG38/entry","name":"emb-27","description":"Cell division cycle protein 16 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-311903","identifier":"P34441","identifierLink":"https://www.uniprot.org/uniprotkb/P34441/entry","name":"emb-30","description":"Abnormal embryogenesis protein 30","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13260","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-312218","identifier":"Q19294","identifierLink":"https://www.uniprot.org/uniprotkb/Q19294/entry","name":"mat-3","description":"Cell division cycle protein 23 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-314913","identifier":"Q20052","identifierLink":"https://www.uniprot.org/uniprotkb/Q20052/entry","name":"apc-11","description":"Anaphase-promoting complex subunit 11","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-317316","identifier":"O01902","identifierLink":"https://www.uniprot.org/uniprotkb/O01902/entry","name":"sam-4","description":"BLOC-1-related complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR31634","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-321211","identifier":"P34514","identifierLink":"https://www.uniprot.org/uniprotkb/P34514/entry","name":"apc-2","description":"Anaphase-promoting complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-329825","identifier":"O18191","identifierLink":"https://www.uniprot.org/uniprotkb/O18191/entry","name":"mat-2","description":"Anaphase-promoting complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12827","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-329972","identifier":"Q9N593","identifierLink":"https://www.uniprot.org/uniprotkb/Q9N593/entry","name":"mat-1","description":"Cell division cycle protein 27 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12558","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6458195","identifier":"G4RT11","identifierLink":"https://www.uniprot.org/uniprotkb/G4RT11/entry","name":"cdc-26","description":"Anaphase-promoting complex subunit CDC26","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]}]},{"complexAC":"CPX-3383","complexName":"CBC-fem-1 Ubiquitin Ligase complex","organismName":"Caenorhabditis elegans; 6239","description":"Member of the CBC (Cullin-2-Elongin-B-Elongin-C) E3 ubiquitin ligase family. Complexes within this family mediate the ubiquitination and subsequent proteasomal degradation of target proteins involved in cell cycle progression, signal transduction, transcription and transcription-coupled nucleotide excision repair. The substrate recognition subunit binds substrates, positioning them for ubiquitination by ubiquitin-conjugating enzymes (E2s) that bind to the complex through the E3 ubiquitin ligase rbx-1 (Q23457). The complex plays a role in sex-determination, specifically regulating male sexual development. Promotes the proteasomal-mediated degradation of tra-1 (P34708), a transcription repressor of male-specific genes.","predictedComplex":false,"interactors":[{"ac":"EBI-16843383","identifier":"CPX-3385","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-3385","name":"Fem-2 phosphatase complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-1811231","identifier":"Q17390","identifierLink":"https://www.uniprot.org/uniprotkb/Q17390/entry","name":"cul-2","description":"Cullin-2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1998112","identifier":"Q23457","identifierLink":"https://www.uniprot.org/uniprotkb/Q23457/entry","name":"rbx-1","description":"RING-box protein 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-300574","identifier":"Q9BKS1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BKS1/entry","name":"elc-1","description":"Elongin-C","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR20648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-330567","identifier":"G5ECR7","identifierLink":"https://www.uniprot.org/uniprotkb/G5ECR7/entry","name":"elb-1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13248","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3384","complexName":"LAS1 RNA processome complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Endonuclease responsible for the removal of the second internal transcribed spacer region (ITS2) from 35S pre-ribosomal RNA, located  between the 5.8S and 25S rRNA. LAS1 within this complex functions as RNA endonuclease, which cleaves at site C2, yielding a 2′,3′ cyclic phosphate at the 7S pre-rRNA and a hydroxyl group at the 5′ end of the 26S pre-rRNA. Subsequently, GRC3, phosphorylates 26S pre-rRNA at its free 5′-OH group, allowing the associated RAT1 5′ to 3′ exonuclease and its co-factor RAI1 to trim 26S pre-rRNA to 25′S pre-rRNA.","predictedComplex":false,"interactors":[{"ac":"EBI-10053","identifier":"P36146","identifierLink":"https://www.uniprot.org/uniprotkb/P36146/entry","name":"LAS1","description":"Protein LAS1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15002","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16426399","identifier":"CPX-1332","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-1332","name":"RAT1-RAI1 RNA polymerase II termination complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-3741923","identifier":"Q07845","identifierLink":"https://www.uniprot.org/uniprotkb/Q07845/entry","name":"GRC3","description":"Polynucleotide 5'-hydroxyl-kinase GRC3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12755","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3385","complexName":"Fem-2 phosphatase complex","organismName":"Caenorhabditis elegans; 6239","description":"Ca(2+)/Calmodulin-dependent protein phosphatase complex that mediates the degradation of target proteins. Required for sex determination, specifically male sexual development. Promotes the degradation of tra-1 (P34708), a transcriptional repressor of male-specific genes.","predictedComplex":false,"interactors":[{"ac":"EBI-1998155","identifier":"P17221","identifierLink":"https://www.uniprot.org/uniprotkb/P17221/entry","name":"fem-1","description":"Sex-determining protein fem-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24173","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1998402","identifier":"P49594","identifierLink":"https://www.uniprot.org/uniprotkb/P49594/entry","name":"fem-2","description":"Protein phosphatase fem-2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13832","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-445465","identifier":"P34691","identifierLink":"https://www.uniprot.org/uniprotkb/P34691/entry","name":"fem-3","description":"Sex-determination protein fem-3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3386","complexName":"COP9 signalosome complex","organismName":"Caenorhabditis elegans; 6239","description":"Essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes. This leads to decreased Ubl ligase activity of SCF-type complexes. Mediates the deneddylation of the cullin cul-3 (Q17391), which leads to the targeting of mei-3/katanin (P34808) for degradation at the meiosis to mitosis transition. Plays an essential role in embryogenesis and oogenesis and is required to regulate microtubule stability in the early embryo. The complex localises to the cytoplasm during mitosis, and to the nucleus during interphase of early embryos.","predictedComplex":false,"interactors":[{"ac":"EBI-313007","identifier":"P91001","identifierLink":"https://www.uniprot.org/uniprotkb/P91001/entry","name":"csn-5","description":"COP9 signalosome complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10410","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-314047","identifier":"Q95PZ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q95PZ0/entry","name":"csn-6","description":"COP9 signalosome complex subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10540","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-318834","identifier":"Q94261","identifierLink":"https://www.uniprot.org/uniprotkb/Q94261/entry","name":"cif-1","description":"COP9/Signalosome and eIF3 complex-shared subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR15350","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-331347","identifier":"Q9N359","identifierLink":"https://www.uniprot.org/uniprotkb/Q9N359/entry","name":"csn-4","description":"COP9 signalosome complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10855","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-331408","identifier":"Q9GS00","identifierLink":"https://www.uniprot.org/uniprotkb/Q9GS00/entry","name":"csn-1","description":"COP9 signalosome complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR14145","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-331413","identifier":"O01422","identifierLink":"https://www.uniprot.org/uniprotkb/O01422/entry","name":"csn-2","description":"COP9 signalosome complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-331420","identifier":"Q9N425","identifierLink":"https://www.uniprot.org/uniprotkb/Q9N425/entry","name":"csn-3","description":"COP9 signalosome complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10758","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-6155","complexName":"Mitochondrial ribonuclease P complex","organismName":"Homo sapiens; 9606","description":"Catalytically active H1 RNA responsible for cleaving the 5′ leader sequence from long pre-mitochondrial (mt)tRNAs polycistronic transcripts by phosphodiester bond hydrolysis to generate tRNAs with mature 5′-ends\r\nThe complex only forms in the presence of the pre-(mt)tRNA substrate. May methylate (mt)tRNA independently of the related mitochondrial tRNA:m(1)R9 methyltransferase complex (CPX-6161).","predictedComplex":false,"interactors":[{"ac":"EBI-2107046","identifier":"Q7L0Y3","identifierLink":"https://www.uniprot.org/uniprotkb/Q7L0Y3/entry","name":"TRMT10C","description":"tRNA methyltransferase 10 homolog C","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13563","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2107070","identifier":"O15091","identifierLink":"https://www.uniprot.org/uniprotkb/O15091/entry","name":"PRORP","description":"Mitochondrial ribonuclease P catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13547","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25827394","identifier":"CHEBI:10668","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:10668","name":"trna precursor","description":"tRNA precursor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-79964","identifier":"Q99714","identifierLink":"https://www.uniprot.org/uniprotkb/Q99714/entry","name":"HSD17B10","description":"3-hydroxyacyl-CoA dehydrogenase type-2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43658","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-6156","complexName":"Classical and lectin pathway C3 convertase complex C4b2a-B","organismName":"Homo sapiens; 9606","description":"A serine-type endopeptidase complex of the classical and lectin pathway of complement activation of the innate immune system. Cleaves Complement C3 precurser (P01024) into anaphylatoxin C3A (P01024-PRO_0000005910) and nascent convertase core-component C3b (CPX-973). Components are cleaved by the C1s component of Complement C1 complex (CPX-1920) of the classical pathway or lectins of the lectin pathway. Occurs in the fluid-phase and binds to pathogen cells via its reactive thioester moiety. \r\n\r\nIf bound to another C4b molecule it can also act as C5 convertase by cleaving Complement C5 precurser (P01031) into anaphylatoxin C5A (P01031-PRO_0000005988) and C5b (P01031-PRO_0000005985, P01031-PRO_0000005989) but with low efficiency. \r\n\r\nActs as an opsonin and interacts with glycoproteins and carbohydrates on pathogenic or apoptotic target cell surfaces through its reactive thioester moiety. Opsonization of target cells leads to enhanced phagocytosis, lysis of target cells via membrane attack complex assembly, clearance of antibody-antigen complexes and up-regulation of the adaptive response.","predictedComplex":false,"interactors":[{"ac":"EBI-25474394","identifier":"P06681-PRO_0000027612","identifierLink":"https://www.uniprot.org/uniprotkb/P06681-PRO_0000027612/entry","name":"C2","description":"Complement C2a fragment","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25827115","identifier":"P0C0L5-PRO_0000042706","identifierLink":"https://www.uniprot.org/uniprotkb/P0C0L5-PRO_0000042706/entry","name":"C4B","description":"Complement C4 gamma chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25827142","identifier":"P0C0L5-PRO_0000042699","identifierLink":"https://www.uniprot.org/uniprotkb/P0C0L5-PRO_0000042699/entry","name":"C4B","description":"Complement C4 beta chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25827150","identifier":"P0C0L5-PRO_0000042703","identifierLink":"https://www.uniprot.org/uniprotkb/P0C0L5-PRO_0000042703/entry","name":"C4B","description":"Complement C4b-B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6157","complexName":"Classical and lectin pathway C5 convertase complex C4b2a3b-A","organismName":"Homo sapiens; 9606","description":"A serine-type endopeptidase complex of the classical and lectin pathway of complement activation of the innate immune system. Cleaves Complement C5 precurser (P01031) into anaphylatoxin C5a (P01031-PRO_0000005988) and Complement C5b (P01031-PRO_0000005985, P01031-PRO_0000005989). Binds to pathogen cells via its reactive thioester moiety. \r\n\r\nActs as an opsonin and interacts with glycoproteins and carbohydrates on pathogenic or apoptotic target cell surfaces through its reactive thioester moiety. Opsonization of target cells leads to enhanced phagocytosis, lysis of target cells via membrane attack complex (CPX-6159) assembly, clearance of antibody-antigen complexes and up-regulation of the adaptive response.","predictedComplex":false,"interactors":[{"ac":"EBI-12735745","identifier":"CPX-973","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-973","name":"Complement C3b complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25474378","identifier":"CPX-5675","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-5675","name":"Classical and lectin pathway C3 convertase complex C4b2a-A","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6158","complexName":"Classical and lectin pathway C5 convertase complex C4b2a3b-B","organismName":"Homo sapiens; 9606","description":"A serine-type endopeptidase complex of the classical and lectin pathway of complement activation of the innate immune system. Cleaves Complement C5 precurser (P01031) into anaphylatoxin C5a (P01031-PRO_0000005988) and Complement C5b (P01031-PRO_0000005985, P01031-PRO_0000005989). Binds to pathogen cells via its reactive thioester moiety. \r\n\r\nActs as an opsonin and interacts with glycoproteins and carbohydrates on pathogenic or apoptotic target cell surfaces through its reactive thioester moiety. Opsonization of target cells leads to enhanced phagocytosis, lysis of target cells via membrane attack complex assembly, clearance of antibody-antigen complexes and up-regulation of the adaptive response.","predictedComplex":false,"interactors":[{"ac":"EBI-12735745","identifier":"CPX-973","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-973","name":"Complement C3b complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25827077","identifier":"CPX-6156","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-6156","name":"Classical and lectin pathway C3 convertase complex C4b2a-B","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6159","complexName":"Membrane attack complex","organismName":"Homo sapiens; 9606","description":"Transmembrane complex of the terminal pathway of complement activation that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells due for destruction. Sublytic MAC modulates inflammation and proliferation when formed on self-cells; host cells are protected from bystander damage by the GPI-anchored receptor CD59 (P13987).","predictedComplex":false,"interactors":[{"ac":"EBI-12523855","identifier":"P07358","identifierLink":"https://www.uniprot.org/uniprotkb/P07358/entry","name":"C8B","description":"Complement component C8 beta chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1753221","identifier":"P13671","identifierLink":"https://www.uniprot.org/uniprotkb/P13671/entry","name":"C6","description":"Complement component C6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25468097","identifier":"P01031-PRO_0000005985","identifierLink":"https://www.uniprot.org/uniprotkb/P01031-PRO_0000005985/entry","name":"C5","description":"Complement C5 beta chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25468103","identifier":"P01031-PRO_0000005989","identifierLink":"https://www.uniprot.org/uniprotkb/P01031-PRO_0000005989/entry","name":"C5","description":"Complement C5b","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2872846","identifier":"P10643","identifierLink":"https://www.uniprot.org/uniprotkb/P10643/entry","name":"C7","description":"Complement component C7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6677628","identifier":"P02748","identifierLink":"https://www.uniprot.org/uniprotkb/P02748/entry","name":"C9","description":"Complement component C9","stochiometry":"minValue: 18, maxValue: 18","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9021639","identifier":"P07357","identifierLink":"https://www.uniprot.org/uniprotkb/P07357/entry","name":"C8A","description":"Complement component C8 alpha chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9021652","identifier":"P07360","identifierLink":"https://www.uniprot.org/uniprotkb/P07360/entry","name":"C8G","description":"Complement component C8 gamma chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6161","complexName":"Mitochondrial tRNA:m(1)R9 methyltransferase complex","organismName":"Homo sapiens; 9606","description":"Responsible for the methylation of the nitrogen-1 (N1) atom of purine bases at position 9 to form 1-methyladenosine (m1A9) or 1-methylguanosine (m1G9). N1-methylation promotes the folding of human (mt)tRNALys into the conventional tRNA L-shape.","predictedComplex":false,"interactors":[{"ac":"EBI-2107046","identifier":"Q7L0Y3","identifierLink":"https://www.uniprot.org/uniprotkb/Q7L0Y3/entry","name":"TRMT10C","description":"tRNA methyltransferase 10 homolog C","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13563","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-79964","identifier":"Q99714","identifierLink":"https://www.uniprot.org/uniprotkb/Q99714/entry","name":"HSD17B10","description":"3-hydroxyacyl-CoA dehydrogenase type-2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43658","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6163","complexName":"Complement factor H complex","organismName":"Homo sapiens; 9606","description":"Glycoprotein complex of the alternative pathway (AP) of complement activation that discriminate between self-structures and foreign structures to maintain a well-balanced immune response by modulating complement activation. Downregulates the AP by enhancing dissociation of the C3bBb (CPX-5601) complexes and by acting as a cofactor for factor I (P05156) in proteolytic inactivation of already-deposited C3b (CPX-973). It inactivates C3b by competitively binding it thereby reducing available C3b molecules for the next factor, factor B (P00751), of the cascade. Binds to self markers such as glycan structures to prevent complement activation and amplification on self-surfaces.","predictedComplex":false,"interactors":[{"ac":"EBI-1223708","identifier":"P08603","identifierLink":"https://www.uniprot.org/uniprotkb/P08603/entry","name":"CFH","description":"Complement factor H","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45785","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6164","complexName":"Complement factor I-H-C3b complex","organismName":"Homo sapiens; 9606","description":"Serine-type endopeptidase complex of the alternative pathway (AP) of complement activation that maintains a well-balanced immune response by modulating complement activation. Downregulates the AP by proteolytically inactivating fluid-phase and already-deposited C3b (CPX-973).","predictedComplex":false,"interactors":[{"ac":"EBI-1223708","identifier":"P08603","identifierLink":"https://www.uniprot.org/uniprotkb/P08603/entry","name":"CFH","description":"Complement factor H","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45785","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12735745","identifier":"CPX-973","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-973","name":"Complement C3b complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25827771","identifier":"CPX-6165","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-6165","name":"Complement factor I complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6165","complexName":"Complement factor I complex","organismName":"Homo sapiens; 9606","description":"Serine-type endopeptidase complex of the alternative pathway (AP) of complement activation that maintains a well-balanced immune response by modulating complement activation. Downregulates the AP by proteolytically inactivating fluid-phase and already-deposited C3b (CPX-973), iC3b and C4b (P0C0L4/P0C0L5) in the presence of cofactors such as C4b binding protein (P04003 & P20851), Complement receptor 1 (CR1, P17927) or MCP (CD46, P15529) and as part of I-H-C3b complex (CPX-6164).","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-21196599","identifier":"P05156-PRO_0000027569","identifierLink":"https://www.uniprot.org/uniprotkb/P05156-PRO_0000027569/entry","name":"CFI","description":"Complement factor I heavy chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-21196605","identifier":"P05156-PRO_0000027570","identifierLink":"https://www.uniprot.org/uniprotkb/P05156-PRO_0000027570/entry","name":"CFI","description":"Complement factor I light chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6166","complexName":"CRUMBS3-PALS1-PATJ cell polarity complex","organismName":"Homo sapiens; 9606","description":"Evolutionarily conserved complex that acts as a key regulator of cell polarity and cell shape. It localizes at the subapical region (SAR) above the adherens junction of epithelial cells where it plays a major role in establishment, regulation, and maintenance of apical polarity and acts as an apical component of tight junctions. In addition to the core components (which are always found together), other proteins can associate with the complex, depending on the type and developmental stage of the cell, thus providing it with functional diversity and flexibility.\r\nMutations in its components are associated with a variety of retinal degenerations.","predictedComplex":false,"interactors":[{"ac":"EBI-2513978","identifier":"Q8N3R9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N3R9/entry","name":"PALS1","description":"Protein PALS1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23122","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724390","identifier":"Q8NI35","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NI35/entry","name":"PATJ","description":"InaD-like protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9844372","identifier":"Q9BUF7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BUF7/entry","name":"CRB3","description":"Protein crumbs homolog 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6167","complexName":"CRUMBS1-PALS1-PATJ cell polarity complex","organismName":"Homo sapiens; 9606","description":"Evolutionarily conserved complex that acts as a key regulator of cell polarity and cell shape. It localizes at the subapical region (SAR) above the adherens junction of epithelial cells where it plays a major role in establishment, regulation, and maintenance of apical polarity and acts as an apical component of tight junctions. In addition to the core components (which are always found together), other proteins can associate with the complex, depending on the type and developmental stage of the cell, thus providing it with functional diversity and flexibility.\r\nMutations in its components are associated with a variety of retinal degenerations.","predictedComplex":false,"interactors":[{"ac":"EBI-1048648","identifier":"P82279","identifierLink":"https://www.uniprot.org/uniprotkb/P82279/entry","name":"CRB1","description":"Protein crumbs homolog 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24049","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2513978","identifier":"Q8N3R9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N3R9/entry","name":"PALS1","description":"Protein PALS1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23122","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724390","identifier":"Q8NI35","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NI35/entry","name":"PATJ","description":"InaD-like protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6168","complexName":"Scribble cell polarity complex, DLG1-LLGL2-SCRIB variant","organismName":"Homo sapiens; 9606","description":"Evolutionarily conserved complex that acts as a key regulator of cell polarity and cell shape. It plays a major role in establishment, regulation, and maintenance of apicobasal polarity in epithelial cells.\r\nIt localizes to the basolateral membrane in epithelial cells and is required for proper localization of the other PDZ protein complexes involved in apicobasal polarity: CRUMBS (CPX-6166, CPX-6167 and CPX-6180) and PAR.","predictedComplex":false,"interactors":[{"ac":"EBI-2434001","identifier":"Q6P1M3","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P1M3/entry","name":"LLGL2","description":"LLGL scribble cell polarity complex component 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10241","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357345","identifier":"Q14160","identifierLink":"https://www.uniprot.org/uniprotkb/Q14160/entry","name":"SCRIB","description":"Protein scribble homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357481","identifier":"Q12959","identifierLink":"https://www.uniprot.org/uniprotkb/Q12959/entry","name":"DLG1","description":"Disks large homolog 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6169","complexName":"Mitochondrial propionyl-CoA carboxylase complex","organismName":"Homo sapiens; 9606","description":"Biotin-dependent propionyl-CoA carboxylase which catalyzes the carboxylation of propionyl-CoA to produce D-methylmalonyl-CoA. Methylmalonyl-CoA is subsequently converted to succinyl-CoA, an intermediate in the tricarboxylic acid cycle The enzyme complex is required for the metabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and also cholesterol.","predictedComplex":false,"interactors":[{"ac":"EBI-1371908","identifier":"P05166","identifierLink":"https://www.uniprot.org/uniprotkb/P05166/entry","name":"PCCB","description":"Propionyl-CoA carboxylase beta chain, mitochondrial","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2211679","identifier":"P05165","identifierLink":"https://www.uniprot.org/uniprotkb/P05165/entry","name":"PCCA","description":"Propionyl-CoA carboxylase alpha chain, mitochondrial","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18866","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25829468","identifier":"CHEBI:57586","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57586","name":"biotinate","description":"biotinate","stochiometry":"minValue: 6, maxValue: 6","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 12, maxValue: 12","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-6170","complexName":"MBL2-MASP1 lectin-protease complex","organismName":"Homo sapiens; 9606","description":"Calcium-dependent pattern-recognition receptor and serine protease complex of the lectin pathway (LP) of complement activation. Activates the LP by binding sugar moieties of pathogen-associated molecular patterns (PAMPs) displayed on microbes via the lectin MBL2 subcomplex. Binds preferentially to mannose, fucose and N-acetylglucosamine. Also binds to late, but not early, apoptotic cells, as well as to apoptotic blebs and to necrotic cells facilitating their uptake by macrophages. MASP1 protease is probably activated by cleavage by a MASP1 from a neighbouring MBL2-MASP1 complex and in turn cleaves and activates MASP2 protease in MLB2-MASP2 complex (CPX-6203) and complement precursor C4 (P0C0L4).","predictedComplex":false,"interactors":[{"ac":"EBI-25828811","identifier":"P48740-PRO_0000027593","identifierLink":"https://www.uniprot.org/uniprotkb/P48740-PRO_0000027593/entry","name":"MASP1","description":"Mannan-binding lectin serine protease 1 heavy chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25828820","identifier":"P48740-PRO_0000027594","identifierLink":"https://www.uniprot.org/uniprotkb/P48740-PRO_0000027594/entry","name":"MASP1","description":"Mannan-binding lectin serine protease 1 light chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-5325353","identifier":"P11226","identifierLink":"https://www.uniprot.org/uniprotkb/P11226/entry","name":"MBL2","description":"Mannose-binding protein C","stochiometry":"minValue: 12, maxValue: 12","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24024","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6172","complexName":"FCN1-MASP1 lectin-protease complex","organismName":"Homo sapiens; 9606","description":"Calcium-dependent pattern-recognition receptor and serine protease complex of the lectin pathway (LP) of complement activation. Activates the LP by binding sugar moieties and acetyl groups of pathogen-associated molecular patterns (PAMPs) displayed on microbes via the lectin FCN1 subcomplex. Binds preferentially to 9-O-acetylated 2-6-linked sialic acid derivatives and to various glycans containing sialic acid engaged in a 2-3 linkage. May also activate monocytes. Mainly present in peripheral blood leukocytes, monocytes and granulocytes. MASP1 protease is probably activated by cleavage by a MASP1 from a neighbouring FCN1-MASP1 complex and in turn cleaves and activates MASP2 protease in FCN1-MASP2 complex (CPX-6237) and complement precursor C4 (P0C0L4).","predictedComplex":false,"interactors":[{"ac":"EBI-25828811","identifier":"P48740-PRO_0000027593","identifierLink":"https://www.uniprot.org/uniprotkb/P48740-PRO_0000027593/entry","name":"MASP1","description":"Mannan-binding lectin serine protease 1 heavy chain","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25828820","identifier":"P48740-PRO_0000027594","identifierLink":"https://www.uniprot.org/uniprotkb/P48740-PRO_0000027594/entry","name":"MASP1","description":"Mannan-binding lectin serine protease 1 light chain","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-5282479","identifier":"O00602","identifierLink":"https://www.uniprot.org/uniprotkb/O00602/entry","name":"FCN1","description":"Ficolin-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19143","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6174","complexName":"Mitochondrial glutamyl-tRNA(Gln) amidotransferase complex","organismName":"Homo sapiens; 9606","description":"Transamidates Glu-mt-tRNA(Gln) into Gln-mt-tRNA(Gln), using free glutamine as an amide donor.","predictedComplex":false,"interactors":[{"ac":"EBI-2856796","identifier":"Q9H0R6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H0R6/entry","name":"QRSL1","description":"Glutamyl-tRNA(Gln) amidotransferase subunit A, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11895","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6137441","identifier":"O75879","identifierLink":"https://www.uniprot.org/uniprotkb/O75879/entry","name":"GATB","description":"Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11659","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6929453","identifier":"O43716","identifierLink":"https://www.uniprot.org/uniprotkb/O43716/entry","name":"GATC","description":"Glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15004","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6175","complexName":"Mitochondrial succinyl-CoA synthetase complex, GTP-specific variant","organismName":"Homo sapiens; 9606","description":"Catalyzes the reversible phosphorylation/dephosphorylation of Succinyl-CoA. Couples the hydrolysis of succinyl-CoA to the synthesis of GTP in the citric acid cycle (TCA) and thus represents the only step of substrate-level phosphorylation in the TCA .","predictedComplex":false,"interactors":[{"ac":"EBI-1237145","identifier":"P53597","identifierLink":"https://www.uniprot.org/uniprotkb/P53597/entry","name":"SUCLG1","description":"Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2511878","identifier":"Q96I99","identifierLink":"https://www.uniprot.org/uniprotkb/Q96I99/entry","name":"SUCLG2","description":"Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11815","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-6176","complexName":"Mitochondrial succinyl-CoA synthetase complex, ATP-specific variant","organismName":"Homo sapiens; 9606","description":"Catalyzes the reversible phosphorylation/dephosphorylation of Succinyl-CoA. Couples the hydrolysis of succinyl-CoA to the synthesis of ATP in the citric acid cycle (TCA) and thus represents the only step of substrate-level phosphorylation in the TCA .","predictedComplex":false,"interactors":[{"ac":"EBI-1237145","identifier":"P53597","identifierLink":"https://www.uniprot.org/uniprotkb/P53597/entry","name":"SUCLG1","description":"Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2269898","identifier":"Q9P2R7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P2R7/entry","name":"SUCLA2","description":"Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11815","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-6177","complexName":"Mitochondrial endopeptidase ClpXP complex","organismName":"Homo sapiens; 9606","description":"ATP-dependent serine protease which degrades proteins, potentially playing a central housekeeping function rather than targeting specific substrates. May contribute to mitochondrial protein quality control by degrading misfolded proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-1052667","identifier":"O76031","identifierLink":"https://www.uniprot.org/uniprotkb/O76031/entry","name":"CLPX","description":"ATP-dependent clpX-like chaperone, mitochondrial","stochiometry":"minValue: 12, maxValue: 12","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1056029","identifier":"Q16740","identifierLink":"https://www.uniprot.org/uniprotkb/Q16740/entry","name":"CLPP","description":"ATP-dependent Clp protease proteolytic subunit, mitochondrial","stochiometry":"minValue: 14, maxValue: 14","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10381","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6178","complexName":"FCN2-MASP1 lectin-protease complex","organismName":"Homo sapiens; 9606","description":"Calcium-dependent pattern-recognition receptor and serine protease complex of the lectin pathway (LP) of complement activation. Activates the LP by binding sugar moieties and acetyl groups of pathogen-associated molecular patterns (PAMPs) displayed on microbes via the lectin FCN2 subcomplex. Binds preferentially to heparin, N-acetylglucosamines (GlcNAc), sulfate and phosphate groups as well as DNA. Mainly expressed in liver. MASP1 protease is probably activated by cleavage by a MASP1 from a neighbouring FCN2-MASP1 complex and in turn cleaves and activates MASP2 protease in FCN2-MASP2 complex (CPX-6238) and complement precursor C4 (P0C0L4).","predictedComplex":false,"interactors":[{"ac":"EBI-25828811","identifier":"P48740-PRO_0000027593","identifierLink":"https://www.uniprot.org/uniprotkb/P48740-PRO_0000027593/entry","name":"MASP1","description":"Mannan-binding lectin serine protease 1 heavy chain","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25828820","identifier":"P48740-PRO_0000027594","identifierLink":"https://www.uniprot.org/uniprotkb/P48740-PRO_0000027594/entry","name":"MASP1","description":"Mannan-binding lectin serine protease 1 light chain","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-7468784","identifier":"Q15485","identifierLink":"https://www.uniprot.org/uniprotkb/Q15485/entry","name":"FCN2","description":"Ficolin-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19143","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6179","complexName":"FCN3-MASP1 lectin-protease complex","organismName":"Homo sapiens; 9606","description":"Calcium-dependent pattern-recognition receptor and serine protease complex of the lectin pathway (LP) of complement activation. Activates the LP by binding sugar moieties and acetyl groups of pathogen-associated molecular patterns (PAMPs) displayed on microbes via the lectin FCN3 subcomplex. Binds preferentially to N-acetylglucosamines (GlcNAc), GlcNAc, D-fucose, mono/oligosaccharide and lipopolysaccharides. Mainly expressed in liver and kidney. Mainly present in peripheral blood leukocytes, monocytes and granulocytes. MASP1 protease is probably activated by cleavage by a MASP1 from a neighbouring FCN3-MASP1 complex and in turn cleaves and activates MASP2 protease in FCN3-MASP2 complex (CPX-6239) and complement precursor C4 (P0C0L4).","predictedComplex":false,"interactors":[{"ac":"EBI-11786958","identifier":"O75636","identifierLink":"https://www.uniprot.org/uniprotkb/O75636/entry","name":"FCN3","description":"Ficolin-3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19143","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25828811","identifier":"P48740-PRO_0000027593","identifierLink":"https://www.uniprot.org/uniprotkb/P48740-PRO_0000027593/entry","name":"MASP1","description":"Mannan-binding lectin serine protease 1 heavy chain","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25828820","identifier":"P48740-PRO_0000027594","identifierLink":"https://www.uniprot.org/uniprotkb/P48740-PRO_0000027594/entry","name":"MASP1","description":"Mannan-binding lectin serine protease 1 light chain","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6180","complexName":"CRUMBS2-PALS1-PATJ cell polarity complex","organismName":"Homo sapiens; 9606","description":"Evolutionarily conserved complex that acts as a key regulator of cell polarity and cell shape. It localizes at the subapical region (SAR) above the adherens junction of epithelial cells where it plays a major role in establishment, regulation, and maintenance of apical polarity and acts as an apical component of tight junctions. In addition to the core components (which are always found together), other proteins can associate with the complex, depending on the type and developmental stage of the cell, thus providing it with functional diversity and flexibility.\r\nMutations in its components are associated with a variety of retinal degenerations.","predictedComplex":false,"interactors":[{"ac":"EBI-2513978","identifier":"Q8N3R9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N3R9/entry","name":"PALS1","description":"Protein PALS1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23122","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26302775","identifier":"Q5IJ48","identifierLink":"https://www.uniprot.org/uniprotkb/Q5IJ48/entry","name":"CRB2","description":"Protein crumbs homolog 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24049","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724390","identifier":"Q8NI35","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NI35/entry","name":"PATJ","description":"InaD-like protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6181","complexName":"CL-LK-MASP1 lectin-protease complex","organismName":"Homo sapiens; 9606","description":"Calcium-dependent pattern-recognition receptor and serine protease complex of the lectin pathway (LP) of complement activation. Activates the LP by binding sugar moieties of pathogen-associated molecular patterns (PAMPs) displayed on microbes via the lectin COLEC10-COLEC11 subcomplex. Binds preferentially to high-mannose oligosaccharides with at least one terminal alpha-1,2-linked mannose epitope, l-fucose, galactose, N-acetylglucosamine, N-acetylgalactosamine, fucosylated glycans and lipopolysaccharides. MASP1 protease is probably activated by cleavage by a MASP1 from a neighbouring CL-LK-MASP1 complex and in turn cleaves and activates MASP2 protease in CL-LK-MASP2 complex (CPX-6240) and complement precursor C4 (P0C0L4). \r\n\r\nAlso plays a role in apoptosis through its ability to bind in a calcium-independent manner the DNA present at the surface of apoptotic cells and to activate the complement in response to this binding.","predictedComplex":false,"interactors":[{"ac":"EBI-21859492","identifier":"Q9Y6Z7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6Z7/entry","name":"COLEC10","description":"Collectin-10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24024","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25809731","identifier":"Q9BWP8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BWP8/entry","name":"COLEC11","description":"Collectin-11","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24024","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25828811","identifier":"P48740-PRO_0000027593","identifierLink":"https://www.uniprot.org/uniprotkb/P48740-PRO_0000027593/entry","name":"MASP1","description":"Mannan-binding lectin serine protease 1 heavy chain","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25828820","identifier":"P48740-PRO_0000027594","identifierLink":"https://www.uniprot.org/uniprotkb/P48740-PRO_0000027594/entry","name":"MASP1","description":"Mannan-binding lectin serine protease 1 light chain","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6183","complexName":"PAR cell polarity complex, PARD6A-PRKCI variant","organismName":"Homo sapiens; 9606","description":"Conserved serine/threonine kinase complex that localises at tight junctions where it is required for the establishment of a cell polarity axis during the cell division cycle of epithelial cells.","predictedComplex":false,"interactors":[{"ac":"EBI-286199","identifier":"P41743","identifierLink":"https://www.uniprot.org/uniprotkb/P41743/entry","name":"PRKCI","description":"Protein kinase C iota type","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24356","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-81876","identifier":"Q9NPB6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPB6/entry","name":"PARD6A","description":"Partitioning defective 6 homolog alpha","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-81968","identifier":"Q8TEW0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TEW0/entry","name":"PARD3","description":"Partitioning defective 3 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16484","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6184","complexName":"Scribble cell polarity complex, DLG2-LLGL2-SCRIB variant","organismName":"Homo sapiens; 9606","description":"Evolutionarily conserved complex that acts as a key regulator of cell polarity and cell shape. It plays a major role in establishment, regulation, and maintenance of apicobasal polarity in epithelial cells.\r\nIt localizes to the basolateral membrane in epithelial cells and is required for proper localization of the other PDZ protein complexes involved in apicobasal polarity: CRUMBS (CPX-6166, CPX-6167 and CPX-6180) and PAR.","predictedComplex":false,"interactors":[{"ac":"EBI-2434001","identifier":"Q6P1M3","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P1M3/entry","name":"LLGL2","description":"LLGL scribble cell polarity complex component 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10241","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357345","identifier":"Q14160","identifierLink":"https://www.uniprot.org/uniprotkb/Q14160/entry","name":"SCRIB","description":"Protein scribble homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-80426","identifier":"Q15700","identifierLink":"https://www.uniprot.org/uniprotkb/Q15700/entry","name":"DLG2","description":"Disks large homolog 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6185","complexName":"Scribble cell polarity complex, DLG3-LLGL2-SCRIB variant","organismName":"Homo sapiens; 9606","description":"Evolutionarily conserved complex that acts as a key regulator of cell polarity and cell shape. It plays a major role in establishment, regulation, and maintenance of apicobasal polarity in epithelial cells.\r\nIt localizes to the basolateral membrane in epithelial cells and is required for proper localization of the other PDZ protein complexes involved in apicobasal polarity: CRUMBS (CPX-6166, CPX-6167 and CPX-6180) and PAR.","predictedComplex":false,"interactors":[{"ac":"EBI-2434001","identifier":"Q6P1M3","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P1M3/entry","name":"LLGL2","description":"LLGL scribble cell polarity complex component 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10241","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357345","identifier":"Q14160","identifierLink":"https://www.uniprot.org/uniprotkb/Q14160/entry","name":"SCRIB","description":"Protein scribble homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-80440","identifier":"Q92796","identifierLink":"https://www.uniprot.org/uniprotkb/Q92796/entry","name":"DLG3","description":"Disks large homolog 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6186","complexName":"Scribble cell polarity complex, DLG4-LLGL2-SCRIB variant","organismName":"Homo sapiens; 9606","description":"Evolutionarily conserved complex that acts as a key regulator of cell polarity and cell shape. It plays a major role in establishment, regulation, and maintenance of apicobasal polarity in epithelial cells.\r\nIt localizes to the basolateral membrane in epithelial cells and is required for proper localization of the other PDZ protein complexes involved in apicobasal polarity: CRUMBS (CPX-6166, CPX-6167 and CPX-6180) and PAR.","predictedComplex":false,"interactors":[{"ac":"EBI-2434001","identifier":"Q6P1M3","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P1M3/entry","name":"LLGL2","description":"LLGL scribble cell polarity complex component 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10241","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357345","identifier":"Q14160","identifierLink":"https://www.uniprot.org/uniprotkb/Q14160/entry","name":"SCRIB","description":"Protein scribble homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-80389","identifier":"P78352","identifierLink":"https://www.uniprot.org/uniprotkb/P78352/entry","name":"DLG4","description":"Disks large homolog 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6187","complexName":"Scribble cell polarity complex, DLG5-LLGL2-SCRIB variant","organismName":"Homo sapiens; 9606","description":"Evolutionarily conserved complex that acts as a key regulator of cell polarity and cell shape. It plays a major role in establishment, regulation, and maintenance of apicobasal polarity in epithelial cells.\r\nIt localizes to the basolateral membrane in epithelial cells and is required for proper localization of the other PDZ protein complexes involved in apicobasal polarity: CRUMBS (CPX-6166, CPX-6167 and CPX-6180) and PAR.","predictedComplex":false,"interactors":[{"ac":"EBI-2434001","identifier":"Q6P1M3","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P1M3/entry","name":"LLGL2","description":"LLGL scribble cell polarity complex component 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10241","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357345","identifier":"Q14160","identifierLink":"https://www.uniprot.org/uniprotkb/Q14160/entry","name":"SCRIB","description":"Protein scribble homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-715138","identifier":"Q8TDM6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TDM6/entry","name":"DLG5","description":"Disks large homolog 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46360","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6188","complexName":"Scribble cell polarity complex, DLG5-LLGL1-SCRIB variant","organismName":"Homo sapiens; 9606","description":"Evolutionarily conserved complex that acts as a key regulator of cell polarity and cell shape. It plays a major role in establishment, regulation, and maintenance of apicobasal polarity in epithelial cells.\r\nIt localizes to the basolateral membrane in epithelial cells and is required for proper localization of the other PDZ protein complexes involved in apicobasal polarity: CRUMBS (CPX-6166, CPX-6167 and CPX-6180) and PAR.","predictedComplex":false,"interactors":[{"ac":"EBI-299979","identifier":"Q15334","identifierLink":"https://www.uniprot.org/uniprotkb/Q15334/entry","name":"LLGL1","description":"Lethal(2) giant larvae protein homolog 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10241","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357345","identifier":"Q14160","identifierLink":"https://www.uniprot.org/uniprotkb/Q14160/entry","name":"SCRIB","description":"Protein scribble homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-715138","identifier":"Q8TDM6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TDM6/entry","name":"DLG5","description":"Disks large homolog 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46360","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6189","complexName":"Scribble cell polarity complex, DLG4-LLGL1-SCRIB variant","organismName":"Homo sapiens; 9606","description":"Evolutionarily conserved complex that acts as a key regulator of cell polarity and cell shape. It plays a major role in establishment, regulation, and maintenance of apicobasal polarity in epithelial cells.\r\nIt localizes to the basolateral membrane in epithelial cells and is required for proper localization of the other PDZ protein complexes involved in apicobasal polarity: CRUMBS (CPX-6166, CPX-6167 and CPX-6180) and PAR.","predictedComplex":false,"interactors":[{"ac":"EBI-299979","identifier":"Q15334","identifierLink":"https://www.uniprot.org/uniprotkb/Q15334/entry","name":"LLGL1","description":"Lethal(2) giant larvae protein homolog 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10241","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357345","identifier":"Q14160","identifierLink":"https://www.uniprot.org/uniprotkb/Q14160/entry","name":"SCRIB","description":"Protein scribble homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-80389","identifier":"P78352","identifierLink":"https://www.uniprot.org/uniprotkb/P78352/entry","name":"DLG4","description":"Disks large homolog 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6190","complexName":"Scribble cell polarity complex, DLG3-LLGL1-SCRIB variant","organismName":"Homo sapiens; 9606","description":"Evolutionarily conserved complex that acts as a key regulator of cell polarity and cell shape. It plays a major role in establishment, regulation, and maintenance of apicobasal polarity in epithelial cells.\r\nIt localizes to the basolateral membrane in epithelial cells and is required for proper localization of the other PDZ protein complexes involved in apicobasal polarity: CRUMBS (CPX-6166, CPX-6167 and CPX-6180) and PAR.","predictedComplex":false,"interactors":[{"ac":"EBI-299979","identifier":"Q15334","identifierLink":"https://www.uniprot.org/uniprotkb/Q15334/entry","name":"LLGL1","description":"Lethal(2) giant larvae protein homolog 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10241","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357345","identifier":"Q14160","identifierLink":"https://www.uniprot.org/uniprotkb/Q14160/entry","name":"SCRIB","description":"Protein scribble homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-80440","identifier":"Q92796","identifierLink":"https://www.uniprot.org/uniprotkb/Q92796/entry","name":"DLG3","description":"Disks large homolog 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6191","complexName":"Scribble cell polarity complex, DLG2-LLGL1-SCRIB variant","organismName":"Homo sapiens; 9606","description":"Evolutionarily conserved complex that acts as a key regulator of cell polarity and cell shape. It plays a major role in establishment, regulation, and maintenance of apicobasal polarity in epithelial cells.\r\nIt localizes to the basolateral membrane in epithelial cells and is required for proper localization of the other PDZ protein complexes involved in apicobasal polarity: CRUMBS (CPX-6166, CPX-6167 and CPX-6180) and PAR.","predictedComplex":false,"interactors":[{"ac":"EBI-299979","identifier":"Q15334","identifierLink":"https://www.uniprot.org/uniprotkb/Q15334/entry","name":"LLGL1","description":"Lethal(2) giant larvae protein homolog 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10241","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357345","identifier":"Q14160","identifierLink":"https://www.uniprot.org/uniprotkb/Q14160/entry","name":"SCRIB","description":"Protein scribble homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-80426","identifier":"Q15700","identifierLink":"https://www.uniprot.org/uniprotkb/Q15700/entry","name":"DLG2","description":"Disks large homolog 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6192","complexName":"Scribble cell polarity complex, DLG1-LLGL1-SCRIB variant","organismName":"Homo sapiens; 9606","description":"Evolutionarily conserved complex that acts as a key regulator of cell polarity and cell shape. It plays a major role in establishment, regulation, and maintenance of apicobasal polarity in epithelial cells.\r\nIt localizes to the basolateral membrane in epithelial cells and is required for proper localization of the other PDZ protein complexes involved in apicobasal polarity: CRUMBS (CPX-6166, CPX-6167 and CPX-6180) and PAR.","predictedComplex":false,"interactors":[{"ac":"EBI-299979","identifier":"Q15334","identifierLink":"https://www.uniprot.org/uniprotkb/Q15334/entry","name":"LLGL1","description":"Lethal(2) giant larvae protein homolog 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10241","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357345","identifier":"Q14160","identifierLink":"https://www.uniprot.org/uniprotkb/Q14160/entry","name":"SCRIB","description":"Protein scribble homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357481","identifier":"Q12959","identifierLink":"https://www.uniprot.org/uniprotkb/Q12959/entry","name":"DLG1","description":"Disks large homolog 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6193","complexName":"PAR cell polarity complex, PARD6B-PRKCI variant","organismName":"Homo sapiens; 9606","description":"Conserved serine/threonine kinase complex that localises at tight junctions where it is required for the establishment of a cell polarity axis during the cell division cycle of epithelial cells.","predictedComplex":false,"interactors":[{"ac":"EBI-286199","identifier":"P41743","identifierLink":"https://www.uniprot.org/uniprotkb/P41743/entry","name":"PRKCI","description":"Protein kinase C iota type","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24356","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-295391","identifier":"Q9BYG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BYG5/entry","name":"PARD6B","description":"Partitioning defective 6 homolog beta","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-81968","identifier":"Q8TEW0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TEW0/entry","name":"PARD3","description":"Partitioning defective 3 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16484","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6194","complexName":"PAR cell polarity complex, PARD6G-PRKCI variant","organismName":"Homo sapiens; 9606","description":"Conserved serine/threonine kinase complex that localises at tight junctions where it is required for the establishment of a cell polarity axis during the cell division cycle of epithelial cells.","predictedComplex":false,"interactors":[{"ac":"EBI-286199","identifier":"P41743","identifierLink":"https://www.uniprot.org/uniprotkb/P41743/entry","name":"PRKCI","description":"Protein kinase C iota type","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24356","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-295417","identifier":"Q9BYG4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BYG4/entry","name":"PARD6G","description":"Partitioning defective 6 homolog gamma","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-81968","identifier":"Q8TEW0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TEW0/entry","name":"PARD3","description":"Partitioning defective 3 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16484","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6195","complexName":"PAR cell polarity complex, PARD6G-PRKCZ variant","organismName":"Homo sapiens; 9606","description":"Conserved serine/threonine kinase complex that localises at tight junctions where it is required for the establishment of a cell polarity axis during the cell division cycle of epithelial cells.","predictedComplex":false,"interactors":[{"ac":"EBI-295351","identifier":"Q05513","identifierLink":"https://www.uniprot.org/uniprotkb/Q05513/entry","name":"PRKCZ","description":"Protein kinase C zeta type","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24356","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-295417","identifier":"Q9BYG4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BYG4/entry","name":"PARD6G","description":"Partitioning defective 6 homolog gamma","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-81968","identifier":"Q8TEW0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TEW0/entry","name":"PARD3","description":"Partitioning defective 3 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16484","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6196","complexName":"PAR cell polarity complex, PARD6B-PRKCZ variant","organismName":"Homo sapiens; 9606","description":"Conserved serine/threonine kinase complex that localises at tight junctions where it is required for the establishment of a cell polarity axis during the cell division cycle of epithelial cells.","predictedComplex":false,"interactors":[{"ac":"EBI-295351","identifier":"Q05513","identifierLink":"https://www.uniprot.org/uniprotkb/Q05513/entry","name":"PRKCZ","description":"Protein kinase C zeta type","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24356","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-295391","identifier":"Q9BYG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BYG5/entry","name":"PARD6B","description":"Partitioning defective 6 homolog beta","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-81968","identifier":"Q8TEW0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TEW0/entry","name":"PARD3","description":"Partitioning defective 3 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16484","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6197","complexName":"PAR cell polarity complex, PARD6A-PRKCZ variant","organismName":"Homo sapiens; 9606","description":"Conserved serine/threonine kinase complex that localises at tight junctions where it is required for the establishment of a cell polarity axis during the cell division cycle of epithelial cells.","predictedComplex":false,"interactors":[{"ac":"EBI-295351","identifier":"Q05513","identifierLink":"https://www.uniprot.org/uniprotkb/Q05513/entry","name":"PRKCZ","description":"Protein kinase C zeta type","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24356","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-81876","identifier":"Q9NPB6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPB6/entry","name":"PARD6A","description":"Partitioning defective 6 homolog alpha","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-81968","identifier":"Q8TEW0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TEW0/entry","name":"PARD3","description":"Partitioning defective 3 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16484","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6198","complexName":"Classical and lectin pathway C3 convertase complex C4b2a-B","organismName":"Mus musculus; 10090","description":"A serine-type endopeptidase complex of the lectin and classical pathway of complement activation of the innate immune system. Cleaves Complement C3 precursor (P01027) into anaphylatoxin C3A (P01027-PRO_0000005920) and nascent convertase core-component C3b (CPX-988). Components are cleaved by the C1s component of Complement C1 complex (CPX-4984, CPX-4985) of the classical pathway or lectins of the lectin pathway. Binds to pathogen cells via its reactive thioester moiety. \r\n\r\nCan also act as C5 convertase by cleaving Complement C5 precursor (P06684) into anaphylatoxin C5A (P06684-PRO_0000005994) and C5b (P06684-PRO_0000005991, P06684-PRO_0000005995) but with low efficiency. \r\n\r\nActs as an opsonin and interacts with glycoproteins and carbohydrates on pathogenic or apoptotic target cell surfaces through its reactive thioester moiety. Opsonization of target cells leads to enhanced phagocytosis, lysis of target cells via membrane attack complex (CPX-6159) assembly, clearance of antibody-antigen complexes and up-regulation of the adaptive response.","predictedComplex":false,"interactors":[{"ac":"EBI-26353792","identifier":"P21180-PRO_0000027615","identifierLink":"https://www.uniprot.org/uniprotkb/P21180-PRO_0000027615/entry","name":"C2","description":"Serine protease complement C2b","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-26353811","identifier":"P01029-PRO_0000005975","identifierLink":"https://www.uniprot.org/uniprotkb/P01029-PRO_0000005975/entry","name":"C4b","description":"Complement C4 alpha chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-26353817","identifier":"P01029-PRO_0000005973","identifierLink":"https://www.uniprot.org/uniprotkb/P01029-PRO_0000005973/entry","name":"C4b","description":"Complement C4 beta chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-26353823","identifier":"P01029-PRO_0000005978","identifierLink":"https://www.uniprot.org/uniprotkb/P01029-PRO_0000005978/entry","name":"C4b","description":"Complement C4 gamma chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-6199","complexName":"COG tethering complex","organismName":"Homo sapiens; 9606","description":"Peripheral membrane oligomeric protein complex which acts as a retrograde vesicle tethering factor in intra-Golgi protein trafficking, bringing cargo vesicles in close proximity to their target compartment. May play a role in protein glycosylation by directly or indirectly effecting transport, retention, or retrieval to appropriate cisternae of resident Golgi glycosylation enzymes.\r\n\r\nMutations in its subunits might result in type-II Congenital Disorders of Glycosylation.","predictedComplex":false,"interactors":[{"ac":"EBI-2807756","identifier":"Q96JB2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96JB2/entry","name":"COG3","description":"Conserved oligomeric Golgi complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13302","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-368371","identifier":"Q8WTW3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WTW3/entry","name":"COG1","description":"Conserved oligomeric Golgi complex subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31658","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-368382","identifier":"Q9H9E3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H9E3/entry","name":"COG4","description":"Conserved oligomeric Golgi complex subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24016","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3866319","identifier":"Q9Y2V7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2V7/entry","name":"COG6","description":"Conserved oligomeric Golgi complex subunit 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21506","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-389449","identifier":"Q14746","identifierLink":"https://www.uniprot.org/uniprotkb/Q14746/entry","name":"COG2","description":"Conserved oligomeric Golgi complex subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12961","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-389502","identifier":"Q9UP83","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UP83/entry","name":"COG5","description":"Conserved oligomeric Golgi complex subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13228","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-389534","identifier":"P83436","identifierLink":"https://www.uniprot.org/uniprotkb/P83436/entry","name":"COG7","description":"Conserved oligomeric Golgi complex subunit 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21443","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-720875","identifier":"Q96MW5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96MW5/entry","name":"COG8","description":"Conserved oligomeric Golgi complex subunit 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21311","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6200","complexName":"Classical and lectin pathway C5 convertase complex C4b2a3b-B","organismName":"Mus musculus; 10090","description":"A serine-type endopeptidase complex of the classical and lectin pathway of complement activation of the innate immune system. Cleaves Complement C5 precursor (P06684) into anaphylatoxin C5A (P06684-PRO_0000005994) and Complement C5b (P06684-PRO_0000005991, P06684-PRO_0000005995). Binds to pathogen cells via its reactive thioester moiety. \r\n\r\nActs as an opsonin and interacts with glycoproteins and carbohydrates on pathogenic or apoptotic target cell surfaces through its reactive thioester moiety. Opsonization of target cells leads to enhanced phagocytosis, lysis of target cells via membrane attack complex assembly, clearance of antibody-antigen complexes and up-regulation of the adaptive response.","predictedComplex":false,"interactors":[{"ac":"EBI-12739605","identifier":"CPX-988","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-988","name":"Complement C3b complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-26353742","identifier":"CPX-6198","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-6198","name":"Classical and lectin pathway C3 convertase complex C4b2a-B","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-6201","complexName":"NRZ tethering complex","organismName":"Homo sapiens; 9606","description":"Multisubunit tethering complex for retrograde trafficking of COPI vesicles from the Golgi to the endoplasmic reticulum.","predictedComplex":false,"interactors":[{"ac":"EBI-1001217","identifier":"O43264","identifierLink":"https://www.uniprot.org/uniprotkb/O43264/entry","name":"ZW10","description":"Centromere/kinetochore protein zw10 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12205","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2267264","identifier":"A2RRP1","identifierLink":"https://www.uniprot.org/uniprotkb/A2RRP1/entry","name":"NBAS","description":"NBAS subunit of NRZ tethering complex","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15922","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-726876","identifier":"Q6NUQ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6NUQ1/entry","name":"RINT1","description":"RAD50-interacting protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13520","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6202","complexName":"Membrane attack complex","organismName":"Mus musculus; 10090","description":"Transmembrane complex of the terminal pathway of complement activation that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells due for destruction. Sublytic MAC modulates inflammation and proliferation when formed on self-cells; host cells are protected from bystander damage by the GPI-anchored receptor CD59 (O55186/P58019).","predictedComplex":false,"interactors":[{"ac":"EBI-26354610","identifier":"E9Q6D8","identifierLink":"https://www.uniprot.org/uniprotkb/E9Q6D8/entry","name":"C6","description":"Complement component C6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26354641","identifier":"Q8K182","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K182/entry","name":"C8a","description":"Complement component C8 alpha chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26354920","identifier":"Q8VCG4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VCG4/entry","name":"C8g","description":"Complement component C8 gamma chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR47304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26354944","identifier":"P06683","identifierLink":"https://www.uniprot.org/uniprotkb/P06683/entry","name":"C9","description":"Complement component C9","stochiometry":"minValue: 18, maxValue: 18","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26354978","identifier":"P06684-PRO_0000005991","identifierLink":"https://www.uniprot.org/uniprotkb/P06684-PRO_0000005991/entry","name":"C5","description":"Complement C5 beta chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-26354984","identifier":"P06684-PRO_0000005995","identifierLink":"https://www.uniprot.org/uniprotkb/P06684-PRO_0000005995/entry","name":"C5","description":"Complement C5b","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-26354990","identifier":"D3YXF5","identifierLink":"https://www.uniprot.org/uniprotkb/D3YXF5/entry","name":"C7","description":"Complement component C7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26442502","identifier":"Q8BH35","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BH35/entry","name":"C8b","description":"Complement component C8 beta chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6203","complexName":"MBL2-MASP2 lectin-protease complex","organismName":"Homo sapiens; 9606","description":"Calcium-dependent pattern-recognition receptor and serine protease complex of the lectin pathway (LP) of complement activation. Activates the LP by binding sugar moieties of pathogen-associated molecular patterns (PAMPs) displayed on microbes via the lectin MBL2 subcomplex. Binds preferentially to mannose, fucose and N-acetylglucosamine. Also binds to late, but not early, apoptotic cells, as well as to apoptotic blebs and to necrotic cells facilitating their uptake by macrophages. MASP2 protease is activated by cleavage by a MASP1 from a neighbouring MBL2-MASP1 complex (CPX-6170) and in turn cleaves and activates complement precursors C4 (P0C0L4) and C2 (P06681) to form C3 convertase complexes C4b2a-A (CPX-5675) and C4b2a-B (CPX-6156).","predictedComplex":false,"interactors":[{"ac":"EBI-25828857","identifier":"O00187-PRO_0000027599","identifierLink":"https://www.uniprot.org/uniprotkb/O00187-PRO_0000027599/entry","name":"MASP2","description":"Mannan-binding lectin serine protease 2 A chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25828862","identifier":"O00187-PRO_0000027600","identifierLink":"https://www.uniprot.org/uniprotkb/O00187-PRO_0000027600/entry","name":"MASP2","description":"Mannan-binding lectin serine protease 2 B chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-5325353","identifier":"P11226","identifierLink":"https://www.uniprot.org/uniprotkb/P11226/entry","name":"MBL2","description":"Mannose-binding protein C","stochiometry":"minValue: 12, maxValue: 12","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24024","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6204","complexName":"Coagulation factor VIIIa-IXa complex","organismName":"Homo sapiens; 9606","description":"A serine-type endopeptidase complex of the intrinsic blood coagulation pathway (contact activation pathway). Cleaves Arg-|-Ile bonds of factor X (P00742) by limited proteolysis to form active factor Xa (CPX-6215) in the presence of vitamin K, Ca2+ ions, phospholipids and Factor VII (P08709). The coagulation pathway is terminated when fibrinogen is cleaved to fibrin which in turn polymerizes to produce a clot.","predictedComplex":false,"interactors":[{"ac":"EBI-12684022","identifier":"CPX-929","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-929","name":"Coagulation factor VIIIa complex, heavy chain variant 1","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-22185586","identifier":"CPX-4945","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-4945","name":"Coagulation factor IXa complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6205","complexName":"Coagulation factor XIa complex","organismName":"Homo sapiens; 9606","description":"A serine-type endopeptidase complex of the intrinsic blood coagulation pathway (contact activation pathway). Cleaves Arg-|-Ala and Arg-|-Val bonds of factor IX (P00740) by limited proteolysis to form active factor IXa (CPX-4945) and contributes to factor VIIa-TF complex (CPX-2808) activation. Also binds platelet glycoprotein Ib:IX:V complex. The coagulation pathway is terminated when fibrinogen is cleaved to fibrin which in turn polymerizes to produce a clot. \r\n\r\nIts zymogen form is activated by limited proteolysis by factor XIIa (CPX-6209) and thrombin (CPX-6222) to form active factor XIa. Inhibited by antithrombin (SERPINC1, P01008).","predictedComplex":false,"interactors":[{"ac":"EBI-25507318","identifier":"P03951-PRO_0000027825","identifierLink":"https://www.uniprot.org/uniprotkb/P03951-PRO_0000027825/entry","name":"F11","description":"Coagulation factor XIa heavy chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25507345","identifier":"P03951-PRO_0000027826","identifierLink":"https://www.uniprot.org/uniprotkb/P03951-PRO_0000027826/entry","name":"F11","description":"Coagulation factor XIa light chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6207","complexName":"EARP tethering complex","organismName":"Homo sapiens; 9606","description":"Multisubunit tethering complex that associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-11044388","identifier":"Q96JG6","identifierLink":"https://www.uniprot.org/uniprotkb/Q96JG6/entry","name":"VPS50","description":"Syndetin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13258","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2799833","identifier":"Q8N1B4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N1B4/entry","name":"VPS52","description":"Vacuolar protein sorting-associated protein 52 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14190","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2850511","identifier":"Q5VIR6","identifierLink":"https://www.uniprot.org/uniprotkb/Q5VIR6/entry","name":"VPS53","description":"Vacuolar protein sorting-associated protein 53 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12820","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2932923","identifier":"Q9UID3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UID3/entry","name":"VPS51","description":"Vacuolar protein sorting-associated protein 51 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15954","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6208","complexName":"GARP tethering complex","organismName":"Homo sapiens; 9606","description":"Multisubunit tethering complex involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN).","predictedComplex":false,"interactors":[{"ac":"EBI-2799833","identifier":"Q8N1B4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N1B4/entry","name":"VPS52","description":"Vacuolar protein sorting-associated protein 52 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14190","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2850511","identifier":"Q5VIR6","identifierLink":"https://www.uniprot.org/uniprotkb/Q5VIR6/entry","name":"VPS53","description":"Vacuolar protein sorting-associated protein 53 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12820","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2932923","identifier":"Q9UID3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UID3/entry","name":"VPS51","description":"Vacuolar protein sorting-associated protein 51 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15954","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5235744","identifier":"Q9P1Q0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P1Q0/entry","name":"VPS54","description":"Vacuolar protein sorting-associated protein 54","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12965","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6209","complexName":"Coagulation factor XIIa complex","organismName":"Homo sapiens; 9606","description":"A serine-type endopeptidase complex of the intrinsic blood coagulation pathway (contact activation pathway) whose formation in the plasma membrane initiates the blood coagulation process by initiating the cell-surface assembly and propagation of the coagulation protease cascade. Cleaves Arg-|-Ile bonds in factor VII (P08709) and factor XI (P03951) by limited proteolysis to form active factors VIIa (CPX-6211) and XIa (CPX-6205). Also activates prekallikrein (P03952) to form kallikrein (CPX-6234), angiotensinogins (P01019) to form angiotensins and kininogen (P01042) to form bradykinin (P01042-PRO_0000006688). The coagulation pathway is terminated when fibrinogen is cleaved to fibrin which in turn polymerizes to produce a clot. \r\n\r\nIts zymogen form is activated by damaged cell surface and by limited proteolysis by thrombin (CPX-6222) and kallikrein (CPX-6234) to form active factor XIIa. Inhibited by SERPING1 (P05155), SERPINA1 (P01009) and SERPINE1 (P05121). \r\n\r\nFactor XII and kallikrein activate each other in a reciprocal reaction.","predictedComplex":false,"interactors":[{"ac":"EBI-26356951","identifier":"P00748-PRO_0000027833","identifierLink":"https://www.uniprot.org/uniprotkb/P00748-PRO_0000027833/entry","name":"F12","description":"Coagulation factor XIIa heavy chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-26356956","identifier":"P00748-PRO_0000027835","identifierLink":"https://www.uniprot.org/uniprotkb/P00748-PRO_0000027835/entry","name":"F12","description":"Coagulation factor XIIa light chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6211","complexName":"Coagulation factor VIIa complex","organismName":"Homo sapiens; 9606","description":"Part of the extrinsic blood coagulation pathway (tissue factor pathway) whose formation in the plasma membrane initiates the blood coagulation process by initiating the cell-surface assembly and propagation of the coagulation protease cascade. Forms factor VIIa-TF complex (CPX-2808) that activates coagulation factors IX (P00740) and X (P00742) by limited proteolysis to form active factors IXa (CPX-4945) and Xa (CPX-6215). The coagulation pathway is terminated when fibrinogen is cleaved to fibrin which in turn polymerizes to produce a clot. \r\n\r\nIts zymogen form is activated by selective cleavage of Arg-|-Ile bonds to form active factor VIIa. Activation is triggered by trauma and minor proteolysis by thrombin (CPX-6222), factor Xa (CPX-6215), factor XIa (CPX-6205) and factor XIIa (CPX-6209). Also constitutively activated at very low levels. Inhibited by complex formation with TFPI (P10646/P48307) and factor Xa.","predictedComplex":false,"interactors":[{"ac":"EBI-11295626","identifier":"P08709-PRO_0000027730","identifierLink":"https://www.uniprot.org/uniprotkb/P08709-PRO_0000027730/entry","name":"F7","description":"Factor VII light chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-11295631","identifier":"P08709-PRO_0000027731","identifierLink":"https://www.uniprot.org/uniprotkb/P08709-PRO_0000027731/entry","name":"F7","description":"Factor VII heavy chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6212","complexName":"HOPS tethering complex","organismName":"Homo sapiens; 9606","description":"Multisubunit tethering complex involved in endo-lysosomal vesicle trafficking and lysosome biogenesis by cross-linking two membranes, and facilitating the formation of a SNARE complex during fusion. Required for the delivery of vacuolar proteins and homotypic fusion of vacuoles and controls the clearance of late endosomes and autophagosomes during heterophagy and autophagy through promoting fusion of these vesicles with the vacuole. Interacts with Rab GTPases RAB7 (P51149 and Q96AH8).  Possibly attaches endosomes to the cytoskeleton and required for the fusion of lysosomes with late endosomes and autophagosomes.","predictedComplex":false,"interactors":[{"ac":"EBI-1050197","identifier":"Q96JC1","identifierLink":"https://www.uniprot.org/uniprotkb/Q96JC1/entry","name":"VPS39","description":"Vam6/Vps39-like protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1053363","identifier":"Q9P253","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P253/entry","name":"VPS18","description":"Vacuolar protein sorting-associated protein 18 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23323","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2130459","identifier":"P49754","identifierLink":"https://www.uniprot.org/uniprotkb/P49754/entry","name":"VPS41","description":"Vacuolar protein sorting-associated protein 41 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12616","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2527283","identifier":"Q96AX1","identifierLink":"https://www.uniprot.org/uniprotkb/Q96AX1/entry","name":"VPS33A","description":"Vacuolar protein sorting-associated protein 33A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11679","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2655929","identifier":"Q9H269","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H269/entry","name":"VPS16","description":"Vacuolar protein sorting-associated protein 16 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12811","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373380","identifier":"Q9H270","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H270/entry","name":"VPS11","description":"Vacuolar protein sorting-associated protein 11 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23323","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6213","complexName":"CORVET tethering complex","organismName":"Homo sapiens; 9606","description":"Multisubunit tethering complex involved in early endosomal fusions by cross-linking two membranes, and facilitating the formation of a SNARE complex during fusion. Interacts with Rab GTPases RAB5  (P61020, P20339 and P51148) and activates and proof-reads SNARE assembly to drive membrane fusion. Possibly attaches early endosomes to the cytoskeleton.","predictedComplex":false,"interactors":[{"ac":"EBI-1053363","identifier":"Q9P253","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P253/entry","name":"VPS18","description":"Vacuolar protein sorting-associated protein 18 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23323","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2527283","identifier":"Q96AX1","identifierLink":"https://www.uniprot.org/uniprotkb/Q96AX1/entry","name":"VPS33A","description":"Vacuolar protein sorting-associated protein 33A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11679","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2655929","identifier":"Q9H269","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H269/entry","name":"VPS16","description":"Vacuolar protein sorting-associated protein 16 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12811","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2954829","identifier":"Q8WUH2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WUH2/entry","name":"TGFBRAP1","description":"Transforming growth factor-beta receptor-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373380","identifier":"Q9H270","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H270/entry","name":"VPS11","description":"Vacuolar protein sorting-associated protein 11 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23323","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7261494","identifier":"Q8N3P4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N3P4/entry","name":"VPS8","description":"Vacuolar protein sorting-associated protein 8 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12616","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6215","complexName":"Coagulation factor Xa complex","organismName":"Homo sapiens; 9606","description":"A serine-type endopeptidase complex of the common blood coagulation pathway. Cleaves Arg-|-Thr and then Arg-|-Ile bonds in prothrombin (P00734) by limited proteolysis to form thrombin (CPX-6222) and contributes to factor VIIa-TF complex (CPX-2808) activation. While factor Xa is constitutively active, it is 300,000-fold more active when bound to factor Va (CPX-6216). The coagulation pathway is terminated when fibrinogen is cleaved to fibrin which in turn polymerizes to produce a clot. \r\n\r\nIts zymogen form is activated by limited proteolysis by factor VIIa-TF complex and factor VIIIa-IXa complex (CPX-6204) to form active factor Xa. Inhibited by antithrombin (SERPINC1, P01008).","predictedComplex":false,"interactors":[{"ac":"EBI-26358766","identifier":"P00742-PRO_0000027788","identifierLink":"https://www.uniprot.org/uniprotkb/P00742-PRO_0000027788/entry","name":"F10","description":"Factor X light chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-26358771","identifier":"P00742-PRO_0000027789","identifierLink":"https://www.uniprot.org/uniprotkb/P00742-PRO_0000027789/entry","name":"F10","description":"Factor X heavy chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6216","complexName":"Coagulation factor Va complex","organismName":"Homo sapiens; 9606","description":"Part of the common blood coagulation pathway. Forms factor Va-Xa complex (CPX-6221) that cleaves prothrombin (P00734) by limited proteolysis to form thrombin (CPX-6222) and contributes to factor VIIa-TF complex (CPX-2808) activation. The coagulation pathway is terminated when fibrinogen is cleaved to fibrin which in turn polymerizes to produce a clot. \r\n\r\nIts zymogen form is activated by minor proteolysis by thrombin leading to a positive feedback cycle of factor Va and thrombin activation. Inhibited by Active Protein C (CPX-6224) and SERPINA5 (P05154).","predictedComplex":false,"interactors":[{"ac":"EBI-11700221","identifier":"P12259-PRO_0000002981","identifierLink":"https://www.uniprot.org/uniprotkb/P12259-PRO_0000002981/entry","name":"F5","description":"Coagulation factor V light chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-11700226","identifier":"P12259-PRO_0000002979","identifierLink":"https://www.uniprot.org/uniprotkb/P12259-PRO_0000002979/entry","name":"F5","description":"Coagulation factor V heavy chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6221","complexName":"Coagulation factor Va-Xa complex","organismName":"Homo sapiens; 9606","description":"A serine-type endopeptidase complex of the common blood coagulation pathway. In the presence of vitamin K cleaves Arg-|-Thr and then Arg-|-Ile bonds in prothrombin (P00734) by limited proteolysis to form thrombin and contributes to factor VIIa-TF complex (CPX-2808) activation. While factor Xa is constitutively active on its own it is 300,000-fold more active when in a complex with factor Va. The coagulation pathway is terminated when fibrinogen is cleaved to fibrin which in turn polymerizes to produce a clot.","predictedComplex":false,"interactors":[{"ac":"EBI-26358728","identifier":"CPX-6215","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-6215","name":"Coagulation factor Xa complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-26358896","identifier":"CPX-6216","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-6216","name":"Coagulation factor Va complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6222","complexName":"alpha-thrombin complex","organismName":"Homo sapiens; 9606","description":"A serine-type endopeptidase complex of the common blood coagulation pathway. Initiates the terminal stage when fibrinogen is cleaved to fibrin which in turn polymerizes to produce a clot. Cleaves Arg-|-Gly bonds in fibrinogen by limited proteolysis to form fibrin and contributes to the activation of factors Va (CPX-6216), VIIa (CPX-6211), VIIIa (CPX-929), XIa (CPX-6205), XIIa (CPX-4945), XIIIa (CPX-6231). May also activate itself at low levels before factor Xa (CPX-6215) is available. Forms a complex with thrombomodulin that negatively regulates its own activation. \r\n\r\nIts zymogen form is initially activated by minor proteolysis by factor Xa and then by factor Va-Xa complex (CPX-6221) leading to a positive feedback cycle of factor Va, Xa and thrombin activation. Inhibited by antithrombin (SERPINC1, P01008).","predictedComplex":false,"interactors":[{"ac":"EBI-21451889","identifier":"P00734-PRO_0000028164","identifierLink":"https://www.uniprot.org/uniprotkb/P00734-PRO_0000028164/entry","name":"F2","description":"Thrombin heavy chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-21451894","identifier":"P00734-PRO_0000028163","identifierLink":"https://www.uniprot.org/uniprotkb/P00734-PRO_0000028163/entry","name":"F2","description":"Thrombin light chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6223","complexName":"Thrombin-Thrombomodulin complex","organismName":"Homo sapiens; 9606","description":"A serine-type endopeptidase complex of the common blood coagulation pathway. Cleaves vitamin K-dependent protein C (P04070) by limited proteolysis to form activated protein C (APC, CPX-6224). APC negatively regulates blood coagulation by inactivating factors Va (CPX-6216) and VIIIa (CPX-929).","predictedComplex":false,"interactors":[{"ac":"EBI-26359573","identifier":"CPX-6222","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-6222","name":"alpha-thrombin complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-941422","identifier":"P07204","identifierLink":"https://www.uniprot.org/uniprotkb/P07204/entry","name":"THBD","description":"Thrombomodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6224","complexName":"Active Protein C complex","organismName":"Homo sapiens; 9606","description":"Vitamin K-dependent serine-type endopeptidase complex of the blood coagulation pathway that prevents coagulation and stimulates fibrinolysis by inactivating factors Va (CPX-6216) and VIIIa (CPX-929) in the presence of Vitamin K-dependent protein S (P07225) calcium ions and phospholipids. Also has cytoprotective effects that protects endothelial cell barrier function. \r\n\r\nIts zymogen form is activated by minor proteolysis by the thrombin-thrombomodulin complex (CPX-6223) to form active protein C.","predictedComplex":false,"interactors":[{"ac":"EBI-26361331","identifier":"P04070-PRO_0000028109","identifierLink":"https://www.uniprot.org/uniprotkb/P04070-PRO_0000028109/entry","name":"PROC","description":"Vitamin K-dependent protein C light chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-26361336","identifier":"P04070-PRO_0000028110","identifierLink":"https://www.uniprot.org/uniprotkb/P04070-PRO_0000028110/entry","name":"PROC","description":"Vitamin K-dependent protein C heavy chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6225","complexName":"Fibrin complex","organismName":"Homo sapiens; 9606","description":"Glycoprotein complex that forms fibrin clots as the last step of the coagulation pathway. Fibrinogen heterohexamers (CPX-1922) are activated by minor proteolysis of alpha and beta chains by alpha-thrombin complex (CPX-6222) to form so-called fibrin monomers (this complex). Fibrin clot (CPX-6230) formation is catalysed by factor XIIIa (CPX-6231). Clots are dissolved mainly by the proteolytic action of plasmin (P00747).","predictedComplex":false,"interactors":[{"ac":"EBI-26361754","identifier":"P02671-PRO_0000009022","identifierLink":"https://www.uniprot.org/uniprotkb/P02671-PRO_0000009022/entry","name":"FGA","description":"Fibrinogen alpha chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-26361759","identifier":"P02675-PRO_0000009071","identifierLink":"https://www.uniprot.org/uniprotkb/P02675-PRO_0000009071/entry","name":"FGB","description":"Fibrinogen beta chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-26361764","identifier":"P02679-PRO_0000009099","identifierLink":"https://www.uniprot.org/uniprotkb/P02679-PRO_0000009099/entry","name":"FGG","description":"Fibrinogen gamma chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6226","complexName":"GATOR1 complex","organismName":"Homo sapiens; 9606","description":"GTPase activating complex which functions as an inhibitor of the amino acid-sensing branch of the mTORC1 pathway. In response to amino acid depletion,  the complex strongly increases GTP hydrolysis by RRAGA or RRAGB within heterodimeric Rag complexes (CPX-2513, CPX-2514, CPX-2542, CPX-767) converting them to their inactive GDP-bound form. This releases mTORC1 (CPX-503) from the lysosomal surface and inhibits mTORC1 signaling The GATOR1 complex is negatively regulated by GATOR2 (CPX-6227).","predictedComplex":false,"interactors":[{"ac":"EBI-1043552","identifier":"Q8WTW4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WTW4/entry","name":"NPRL2","description":"GATOR1 complex protein NPRL2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12991","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11102814","identifier":"O75140","identifierLink":"https://www.uniprot.org/uniprotkb/O75140/entry","name":"DEPDC5","description":"GATOR1 complex protein DEPDC5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13179","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2650314","identifier":"Q12980","identifierLink":"https://www.uniprot.org/uniprotkb/Q12980/entry","name":"NPRL3","description":"GATOR1 complex protein NPRL3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13153","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6227","complexName":"GATOR2 complex","organismName":"Homo sapiens; 9606","description":"Functions as an activator of the amino acid-sensing branch of the mTORC1 pathway. Indirectly activates mTORC1 (CPX-503) through the inhibition of the GATOR1 complex (CPX-6226).","predictedComplex":false,"interactors":[{"ac":"EBI-1046596","identifier":"P55735","identifierLink":"https://www.uniprot.org/uniprotkb/P55735/entry","name":"SEC13","description":"Protein SEC13 homolog","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11024","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2515073","identifier":"Q6PJI9","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PJI9/entry","name":"WDR59","description":"GATOR2 complex protein WDR59","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46170","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2515122","identifier":"Q9NXC5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NXC5/entry","name":"MIOS","description":"GATOR2 complex protein MIOS","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16453","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-746424","identifier":"Q96S15","identifierLink":"https://www.uniprot.org/uniprotkb/Q96S15/entry","name":"WDR24","description":"GATOR2 complex protein WDR24","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46200","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-922818","identifier":"Q96EE3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96EE3/entry","name":"SEH1L","description":"Nucleoporin SEH1","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11024","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6229","complexName":"KICSTOR complex","organismName":"Homo sapiens; 9606","description":"Key regulator of the amino acid-sensing branch of the mTORC1 signaling pathway. It recruits the GATOR1 complex (CPX-6226) to the lysosomal membranes and allows its interaction with GATOR2 (CPX-6227) and the RAG GTPases. Negatively regulates mTORC1 (CPX-503) signaling in absence of amino acids. Probably also involved in the regulation of mTORC1 by glucose.","predictedComplex":false,"interactors":[{"ac":"EBI-1048252","identifier":"Q9Y664","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y664/entry","name":"KPTN","description":"KICSTOR complex protein kaptin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15435","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10749411","identifier":"Q5T011","identifierLink":"https://www.uniprot.org/uniprotkb/Q5T011/entry","name":"SZT2","description":"KICSTOR complex protein SZT2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14918","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20840475","identifier":"Q96MD2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96MD2/entry","name":"KICS2","description":"KICSTOR subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31581","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-723695","identifier":"Q969R8","identifierLink":"https://www.uniprot.org/uniprotkb/Q969R8/entry","name":"ITFG2","description":"KICSTOR complex protein ITFG2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16317","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6230","complexName":"Fibrin clot","organismName":"Homo sapiens; 9606","description":"Glycoprotein complex that forms fibrin clots as the last step of the coagulation pathway. Fibrinogen heterohexamers (CPX-1922) are activated by minor proteolysis of alpha and beta chains by alpha-thrombin complex (CPX-6222) to form so-called fibrin monomers (CPX-6225). Fibrin clot (this complex) formation is catalysed by factor XIIIa (CPX-6231). Clots are dissolved mainly by the proteolytic action of plasmin (P00747).","predictedComplex":false,"interactors":[{"ac":"EBI-26361358","identifier":"CPX-6225","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-6225","name":"Fibrin complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6231","complexName":"Coagulation factor XIIIa complex","organismName":"Homo sapiens; 9606","description":"A protein-glutamine gamma-glutamyltransferase complex that is part of the last step of the coagulation pathway. Catalyzes the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains of fibrin complexes (CPX-6225), thus stabilizing the fibrin clot (CPX-6230). Also cross-links Alpha-2-antiplasmin (SERPINF2 , P08697), or fibronectin (CPX-6232), to the alpha chains of fibrin. \r\n\r\nIts zymogen form is initially activated by minor proteolysis by alpha-thrombin complex (CPX-6222) and calcium ions.","predictedComplex":false,"interactors":[{"ac":"EBI-22196853","identifier":"P05160","identifierLink":"https://www.uniprot.org/uniprotkb/P05160/entry","name":"F13B","description":"Coagulation factor XIII B chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45785","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2565863","identifier":"P00488","identifierLink":"https://www.uniprot.org/uniprotkb/P00488/entry","name":"F13A1","description":"Coagulation factor XIII A chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11590","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6232","complexName":"Fibronectin complex","organismName":"Homo sapiens; 9606","description":"Extracellular matrix (ECM) complex that binds cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin. Involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. Participates in the regulation of type I collagen deposition by osteoblasts. \r\nAnastellin (a splice form of fibronectin) binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-1220319","identifier":"P02751","identifierLink":"https://www.uniprot.org/uniprotkb/P02751/entry","name":"FN1","description":"Fibronectin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46708","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6233","complexName":"Mitochondrial pyruvate dehydrogenase complex, somatic variant","organismName":"Homo sapiens; 9606","description":"Mitochondrial matrix enzyme that converts pyruvate to acetyl-CoA and CO2. This provides a metabolic connection between glycolysis, whose end product is pyruvate, and the tricarboxylic acid cycle, which starts with acetyl-CoA. Pyruvate dehydrogenase (PDH) activity is negatively regulated via phosphorylation of its PDHA1 subunit. \r\n\r\nIn the reaction mediated by the PDH complex, pyruvate becomes covalently linked to the thiamine diphosphate (TPP) cofactor of E1 (PDHA1 and PDHB), creating 2-alpha-hydroxy-ethyl-TPP. The alpha-hydroxy group of 2-alpha-hydroxy-ethyl-TPP is subsequently oxidized, creating an acetyl group that becomes bound to the dihydrolipoyllysine group of E2 (DLAT). DLAT transfers this acetyl group to CoA to generate acetyl-CoA.","predictedComplex":false,"interactors":[{"ac":"EBI-1035872","identifier":"P11177","identifierLink":"https://www.uniprot.org/uniprotkb/P11177/entry","name":"PDHB","description":"Pyruvate dehydrogenase E1 component subunit beta, mitochondrial","stochiometry":"minValue: 80, maxValue: 80","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11624","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1225105","identifier":"CHEBI:16238","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16238","name":"fad","description":"FAD - Flavin adenine dinucleotide","stochiometry":"minValue: 40, maxValue: 40","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-16416616","identifier":"CHEBI:83088","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:83088","name":"(r)-lipoate","description":"(R)-lipoate","stochiometry":"minValue: 80, maxValue: 80","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2959723","identifier":"P10515","identifierLink":"https://www.uniprot.org/uniprotkb/P10515/entry","name":"DLAT","description":"Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial","stochiometry":"minValue: 40, maxValue: 40","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23151","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353366","identifier":"P09622","identifierLink":"https://www.uniprot.org/uniprotkb/P09622/entry","name":"DLD","description":"Dihydrolipoyl dehydrogenase, mitochondrial","stochiometry":"minValue: 40, maxValue: 40","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22912","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-715747","identifier":"P08559","identifierLink":"https://www.uniprot.org/uniprotkb/P08559/entry","name":"PDHA1","description":"Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial","stochiometry":"minValue: 80, maxValue: 80","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11516","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-751566","identifier":"O00330","identifierLink":"https://www.uniprot.org/uniprotkb/O00330/entry","name":"PDHX","description":"Pyruvate dehydrogenase protein X component, mitochondrial","stochiometry":"minValue: 20, maxValue: 20","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23151","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9691551","identifier":"CHEBI:58937","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58937","name":"thiamine(1+) diphosphate(3-)","description":"thiamine(1+) diphosphate(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-6234","complexName":"Kallikrein complex","organismName":"Homo sapiens; 9606","description":"A serine-type endopeptidase complex of the intrinsic blood coagulation pathway (contact activation pathway). Activates factor XII (P00748) to form active factor XIIa (CPX-6209) after its binding to a negatively charged surface. Cleaves Arg-|-Xaa and Lys-|-Xaa bonds, including Lys-|-Arg and Arg-|-Ser bonds in HMW kininogen-1 (P01042) by limited proteolysis to release bradykinin (P01042-PRO_0000006688). May also play a role in the renin-angiotensin system by converting prorenin (P00797) into renin (P00797-PRO_0000026082). The coagulation pathway is terminated when fibrinogen is cleaved to fibrin which in turn polymerizes to produce a clot. \r\n\r\nIts zymogen form, prekallikrein, is activated, in a reciprocal reaction, by limited proteolysis by factor XIIa to form active kallikrein.","predictedComplex":false,"interactors":[{"ac":"EBI-10097117","identifier":"P03952-PRO_0000028021","identifierLink":"https://www.uniprot.org/uniprotkb/P03952-PRO_0000028021/entry","name":"KLKB1","description":"Plasma kallikrein heavy chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-26362033","identifier":"P03952-PRO_0000028022","identifierLink":"https://www.uniprot.org/uniprotkb/P03952-PRO_0000028022/entry","name":"KLKB1","description":"Plasma kallikrein light chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6235","complexName":"Coagulation factor VIIIa complex, heavy chain variant 2","organismName":"Homo sapiens; 9606","description":"Part of the intrinsic blood coagulation pathway (contact activation pathway). When bound to factor IXa (CPX-4945) forms the intrinsic tenase complex that cleaves Arg-|-Ile bonds of factor X (P00742) by limited proteolysis to form active factor Xa (CPX-6215) in the presence of vitamin K, Ca2+ ions, phospholipids and factor VII (P08709). The coagulation pathway is terminated when fibrinogen is cleaved to fibrin which in turn polymerizes to produce a clot. \r\n\r\nIts zymogen form is activated by limited proteolysis by thrombin (FIIa, P00734) to form active factor VIIIa. Inhibited by Active Protein C (APC, P04070). \r\n\r\nMutations in factor VIII gene lead to hemophilia A.","predictedComplex":false,"interactors":[{"ac":"EBI-11621603","identifier":"P00451-PRO_0000002968","identifierLink":"https://www.uniprot.org/uniprotkb/P00451-PRO_0000002968/entry","name":"F8","description":"Factor VIIIa heavy chain, 200 kDa isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-12684033","identifier":"P00451-PRO_0000002971","identifierLink":"https://www.uniprot.org/uniprotkb/P00451-PRO_0000002971/entry","name":"F8","description":"Factor VIIIa light chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6236","complexName":"Methylcrotonyl-CoA carboxylase complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the conversion of 3-methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for leucine and isovaleric acid catabolism. The biotin carboxylase component catalyzes the Mg-ATP-dependent carboxylation of the N1' atom of the biotin cofactor, using bicarbonate as the CO2 donor. The carboxyltransferase component then catalyzes the CO2 transfer from carboxybiotin to the gamma carbon of the alpha-beta unsaturated acid, 3-methylcrotonyl-CoA.","predictedComplex":false,"interactors":[{"ac":"EBI-2211296","identifier":"Q9HCC0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HCC0/entry","name":"MCCC2","description":"Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22855","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2211703","identifier":"Q96RQ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96RQ3/entry","name":"MCCC1","description":"Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18866","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25829468","identifier":"CHEBI:57586","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57586","name":"biotinate","description":"biotinate","stochiometry":"minValue: 6, maxValue: 6","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-6237","complexName":"FCN1-MASP2 lectin-protease complex","organismName":"Homo sapiens; 9606","description":"Calcium-dependent pattern-recognition receptor and serine protease complex of the lectin pathway (LP) of complement activation. Activates the LP by binding sugar moieties and acetyl groups of pathogen-associated molecular patterns (PAMPs) displayed on microbes via the lectin FCN1 subcomplex. Binds preferentially to 9-O-acetylated 2-6-linked sialic acid derivatives and to various glycans containing sialic acid engaged in a 2-3 linkage. May also activate monocytes. Mainly present in peripheral blood leukocytes, monocytes and granulocytes. MASP2 protease is probably activated by cleavage by a MASP1 from a neighbouring FCN1-MASP1 complex (CPX-6172) and in turn cleaves and activates complement precursors C4 (P0C0L4) and C2 (P06681) to form C3 convertase complexes C4b2a-A (CPX-5675) and C4b2a-B (CPX-6156).","predictedComplex":false,"interactors":[{"ac":"EBI-25828857","identifier":"O00187-PRO_0000027599","identifierLink":"https://www.uniprot.org/uniprotkb/O00187-PRO_0000027599/entry","name":"MASP2","description":"Mannan-binding lectin serine protease 2 A chain","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25828862","identifier":"O00187-PRO_0000027600","identifierLink":"https://www.uniprot.org/uniprotkb/O00187-PRO_0000027600/entry","name":"MASP2","description":"Mannan-binding lectin serine protease 2 B chain","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-5282479","identifier":"O00602","identifierLink":"https://www.uniprot.org/uniprotkb/O00602/entry","name":"FCN1","description":"Ficolin-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19143","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6238","complexName":"FCN2-MASP2 lectin-protease complex","organismName":"Homo sapiens; 9606","description":"Calcium-dependent pattern-recognition receptor and serine protease complex of the lectin pathway (LP) of complement activation. Activates the LP by binding sugar moieties and acetyl groups of pathogen-associated molecular patterns (PAMPs) displayed on microbes via the lectin FCN2 subcomplex. Binds preferentially to heparin, N-acetylglucosamines (GlcNAc), sulfate and phosphate groups as well as DNA. Mainly expressed in liver. MASP2 protease is probably activated by cleavage by a MASP1 from a neighbouring FCN2-MASP1 complex (CPX-6178) and in turn cleaves and activates complement precursors C4 (P0C0L4) and C2 (P06681) to form C3 convertase complexes C4b2a-A (CPX-5675) and C4b2a-B (CPX-6156).","predictedComplex":false,"interactors":[{"ac":"EBI-25828857","identifier":"O00187-PRO_0000027599","identifierLink":"https://www.uniprot.org/uniprotkb/O00187-PRO_0000027599/entry","name":"MASP2","description":"Mannan-binding lectin serine protease 2 A chain","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25828862","identifier":"O00187-PRO_0000027600","identifierLink":"https://www.uniprot.org/uniprotkb/O00187-PRO_0000027600/entry","name":"MASP2","description":"Mannan-binding lectin serine protease 2 B chain","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-7468784","identifier":"Q15485","identifierLink":"https://www.uniprot.org/uniprotkb/Q15485/entry","name":"FCN2","description":"Ficolin-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19143","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6239","complexName":"FCN3-MASP2 lectin-protease complex","organismName":"Homo sapiens; 9606","description":"Calcium-dependent pattern-recognition receptor and serine protease complex of the lectin pathway (LP) of complement activation. Activates the LP by binding sugar moieties and acetyl groups of pathogen-associated molecular patterns (PAMPs) displayed on microbes via the lectin FCN3 subcomplex. Binds preferentially to N-acetylglucosamines (GlcNAc), GlcNAc, D-fucose, mono/oligosaccharide and lipopolysaccharides. Mainly expressed in liver and kidney. Mainly present in peripheral blood leukocytes, monocytes and granulocytes. MASP2 protease is probably activated by cleavage by a MASP1 from a neighbouring FCN3-MASP1 complex (CPX-6179) and in turn cleaves and activates complement precursors C4 (P0C0L4) and C2 (P06681) to form C3 convertase complexes C4b2a-A (CPX-5675) and C4b2a-B (CPX-6156).","predictedComplex":false,"interactors":[{"ac":"EBI-11786958","identifier":"O75636","identifierLink":"https://www.uniprot.org/uniprotkb/O75636/entry","name":"FCN3","description":"Ficolin-3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19143","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25828857","identifier":"O00187-PRO_0000027599","identifierLink":"https://www.uniprot.org/uniprotkb/O00187-PRO_0000027599/entry","name":"MASP2","description":"Mannan-binding lectin serine protease 2 A chain","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25828862","identifier":"O00187-PRO_0000027600","identifierLink":"https://www.uniprot.org/uniprotkb/O00187-PRO_0000027600/entry","name":"MASP2","description":"Mannan-binding lectin serine protease 2 B chain","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6240","complexName":"CL-LK-MASP2 lectin-protease complex","organismName":"Homo sapiens; 9606","description":"Calcium-dependent pattern-recognition receptor and serine protease complex of the lectin pathway (LP) of complement activation. Activates the LP by binding sugar moieties of pathogen-associated molecular patterns (PAMPs) displayed on microbes via the lectin COLEC10-COLEC11 subcomplex. Binds preferentially to high-mannose oligosaccharides with at least one terminal alpha-1,2-linked mannose epitope, l-fucose, galactose, N-acetylglucosamine, N-acetylgalactosamine, fucosylated glycans and lipopolysaccharides. MASP2 protease is probably activated by cleavage by a MASP1 from a neighbouring CL-LK-MASP1 complex (CPX-6181) and in turn cleaves and activates complement precursors C4 (P0C0L4) and C2 (P06681) to form C3 convertase complexes C4b2a-A (CPX-5675) and C4b2a-B (CPX-6156). \r\n\r\nAlso plays a role in apoptosis through its ability to bind in a calcium-independent manner the DNA present at the surface of apoptotic cells and to activate the complement in response to this binding.","predictedComplex":false,"interactors":[{"ac":"EBI-21859492","identifier":"Q9Y6Z7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6Z7/entry","name":"COLEC10","description":"Collectin-10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24024","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25809731","identifier":"Q9BWP8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BWP8/entry","name":"COLEC11","description":"Collectin-11","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24024","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25828857","identifier":"O00187-PRO_0000027599","identifierLink":"https://www.uniprot.org/uniprotkb/O00187-PRO_0000027599/entry","name":"MASP2","description":"Mannan-binding lectin serine protease 2 A chain","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25828862","identifier":"O00187-PRO_0000027600","identifierLink":"https://www.uniprot.org/uniprotkb/O00187-PRO_0000027600/entry","name":"MASP2","description":"Mannan-binding lectin serine protease 2 B chain","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-6241","complexName":"CHEVI tethering complex","organismName":"Homo sapiens; 9606","description":"Multisubunit tethering complex that plays an essential role in in delivery of cargoes in several cell types. it is also implicated in phagosome-lysosome and in endosome-lysosome fusion.\r\n\r\nGenetic defects in its subunits lead to the arthrogryposis, renal dysfunction and cholestasis syndrome (ARC).","predictedComplex":false,"interactors":[{"ac":"EBI-749072","identifier":"Q9H267","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H267/entry","name":"VPS33B","description":"Vacuolar protein sorting-associated protein 33B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11679","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749080","identifier":"Q9H9C1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H9C1/entry","name":"VIPAS39","description":"Spermatogenesis-defective protein 39 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13364","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6242","complexName":"Mitochondrial pyruvate dehydrogenase complex, testis-specific variant","organismName":"Homo sapiens; 9606","description":"Mitochondrial matrix enzyme that converts pyruvate to acetyl-CoA and CO2. This provides a metabolic connection between glycolysis, whose end product is pyruvate, and the tricarboxylic acid cycle, which starts with acetyl-CoA. Pyruvate dehydrogenase (PDH) activity is negatively regulated via phosphorylation of its PDHA2 subunit. \r\n\r\nIn the reaction mediated by the PDH complex, pyruvate becomes covalently linked to the thiamine diphosphate (TPP) cofactor of E1 (PDHA2 and PDHB), creating 2-alpha-hydroxy-ethyl-TPP. The alpha-hydroxy group of 2-alpha-hydroxy-ethyl-TPP is subsequently oxidized, creating an acetyl group that becomes bound to the dihydrolipoyllysine group of E2 (DLAT). DLAT transfers this acetyl group to CoA to generate acetyl-CoA.","predictedComplex":false,"interactors":[{"ac":"EBI-1035872","identifier":"P11177","identifierLink":"https://www.uniprot.org/uniprotkb/P11177/entry","name":"PDHB","description":"Pyruvate dehydrogenase E1 component subunit beta, mitochondrial","stochiometry":"minValue: 80, maxValue: 80","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11624","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1225105","identifier":"CHEBI:16238","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16238","name":"fad","description":"FAD - Flavin adenine dinucleotide","stochiometry":"minValue: 40, maxValue: 40","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-16416616","identifier":"CHEBI:83088","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:83088","name":"(r)-lipoate","description":"(R)-lipoate","stochiometry":"minValue: 80, maxValue: 80","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2957428","identifier":"P29803","identifierLink":"https://www.uniprot.org/uniprotkb/P29803/entry","name":"PDHA2","description":"Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial","stochiometry":"minValue: 80, maxValue: 80","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11516","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2959723","identifier":"P10515","identifierLink":"https://www.uniprot.org/uniprotkb/P10515/entry","name":"DLAT","description":"Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial","stochiometry":"minValue: 40, maxValue: 40","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23151","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353366","identifier":"P09622","identifierLink":"https://www.uniprot.org/uniprotkb/P09622/entry","name":"DLD","description":"Dihydrolipoyl dehydrogenase, mitochondrial","stochiometry":"minValue: 40, maxValue: 40","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22912","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-751566","identifier":"O00330","identifierLink":"https://www.uniprot.org/uniprotkb/O00330/entry","name":"PDHX","description":"Pyruvate dehydrogenase protein X component, mitochondrial","stochiometry":"minValue: 20, maxValue: 20","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23151","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9691551","identifier":"CHEBI:58937","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58937","name":"thiamine(1+) diphosphate(3-)","description":"thiamine(1+) diphosphate(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-6243","complexName":"Mitochondrial processing peptidase complex","organismName":"Homo sapiens; 9606","description":"Metalloprotease which cleaves off the N-terminal presequence from nuclear encoded mitochondrial precursor proteins, such as the sequence that targets the proteins to the mitochondrial matrix.  Common features for cleavage of the extension peptides by MPP are a proximal basic amino acid residue, usually arginine at the P2 position, distal N-terminal basic residues generally 3-10 residues from the proximal arginine and an aromatic or less often another type of bulky hydrophobic residue at position P1'; MPP also prefers polar residues such as histidine, serine, and threonine at positions P2' and P3'.","predictedComplex":false,"interactors":[{"ac":"EBI-2514696","identifier":"Q10713","identifierLink":"https://www.uniprot.org/uniprotkb/Q10713/entry","name":"PMPCA","description":"Mitochondrial-processing peptidase subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11851","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-721199","identifier":"O75439","identifierLink":"https://www.uniprot.org/uniprotkb/O75439/entry","name":"PMPCB","description":"Mitochondrial-processing peptidase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11851","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-6244","complexName":"Mitochondrial inner membrane peptidase complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the removal of transit peptides required for the targeting of a range of nuclear encoded and most mitochondrial encoded precursor proteins from the mitochondrial matrix to the inner membrane or the inter-membrane space.","predictedComplex":false,"interactors":[{"ac":"EBI-20843876","identifier":"Q96T52","identifierLink":"https://www.uniprot.org/uniprotkb/Q96T52/entry","name":"IMMP2L","description":"Mitochondrial inner membrane protease subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46041","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21619007","identifier":"Q96LU5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96LU5/entry","name":"IMMP1L","description":"Mitochondrial inner membrane protease subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12383","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6245","complexName":"Mitochondrial trifunctional enzyme complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the last three of the four reactions in the fatty acid beta-oxidation process, adding water to the double bond of 2,3-enoyl-CoA, yielding 3-hydroxyacyl-CoA, dehydrogenating 3-hydroxyacyl-CoA to form 3-ketoacyl-CoA, and thiolyzing 3-ketoacyl-CoA between the alpha- and beta-carbons to remove a two-carbon unit which is released in the form of acetyl-CoA. These steps are repeated until all carbons in the fatty acyl-CoA are turned into acetyl-CoA, which enters the citric acid cycle. Exhibits specificity for long-chain fatty acids.","predictedComplex":false,"interactors":[{"ac":"EBI-356635","identifier":"P55084","identifierLink":"https://www.uniprot.org/uniprotkb/P55084/entry","name":"HADHB","description":"Trifunctional enzyme subunit beta, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18919","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356720","identifier":"P40939","identifierLink":"https://www.uniprot.org/uniprotkb/P40939/entry","name":"HADHA","description":"Trifunctional enzyme subunit alpha, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43612","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6261","complexName":"Mitochondrial pyruvate dehydrogenase serine/threonine phosphatase complex","organismName":"Homo sapiens; 9606","description":"Serine/threonine phosphatase complex believed to activate the pyruvate dehydrogenase (E1) subunit of the pyruvate dehydrogenase complex (CPX-6233/CPX-6242) by dephosphorylating PDHA1/PDHA2 (P08559/P29803).","predictedComplex":false,"interactors":[{"ac":"EBI-16769589","identifier":"Q8NCN5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NCN5/entry","name":"PDPR","description":"Pyruvate dehydrogenase phosphatase regulatory subunit, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2861634","identifier":"Q9P0J1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P0J1/entry","name":"PDP1","description":"[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13832","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-6263","complexName":"Fanconi anemia ubiquitin ligase complex","organismName":"Homo sapiens; 9606","description":"Ubiquitin ligase complex required for the repair of DNA interstrand crosslinks (ICL) and related lesions. The complex is activated when a replication fork stalls at an ICL and monoubiquitinates the Fanconi anemia ID complex (CPX-6264) in the presence of UBE2T (Q9NPD8), conjugating one ubiquitin molecule to each protein component. UBE2T acts as a specific E2 ubiquitin-conjugating enzyme for the complex. Monoubiquitination of ID is essential for ICL repair by excision, trans-lesion synthesis and homologous recombination.","predictedComplex":false,"interactors":[{"ac":"EBI-2339898","identifier":"Q9NW38","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NW38/entry","name":"FANCL","description":"E3 ubiquitin-protein ligase FANCL","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13206","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2557983","identifier":"Q8NB91","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NB91/entry","name":"FANCB","description":"Fanconi anemia group B protein","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28450","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2557990","identifier":"Q0VG06","identifierLink":"https://www.uniprot.org/uniprotkb/Q0VG06/entry","name":"FAAP100","description":"Fanconi anemia core complex-associated protein 100","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2817693","identifier":"Q6NZ36","identifierLink":"https://www.uniprot.org/uniprotkb/Q6NZ36/entry","name":"FAAP20","description":"Fanconi anemia core complex-associated protein 20","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR37862","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-396803","identifier":"Q9HB96","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HB96/entry","name":"FANCE","description":"Fanconi anemia group E protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32094","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-81570","identifier":"O15360","identifierLink":"https://www.uniprot.org/uniprotkb/O15360/entry","name":"FANCA","description":"Fanconi anemia group A protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12047","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-81589","identifier":"Q9NPI8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPI8/entry","name":"FANCF","description":"Fanconi anemia group F protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14449","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-81610","identifier":"O15287","identifierLink":"https://www.uniprot.org/uniprotkb/O15287/entry","name":"FANCG","description":"Fanconi anemia group G protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15254","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-81625","identifier":"Q00597","identifierLink":"https://www.uniprot.org/uniprotkb/Q00597/entry","name":"FANCC","description":"Fanconi anemia group C protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16798","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6264","complexName":"Fanconi anemia ID complex","organismName":"Homo sapiens; 9606","description":"Required for the repair of DNA interstrand crosslinks (ICL) and related lesions. Binds to DNA with a preference for branched structures, including Holliday-junctions, overhangs and replication-forks. ICL repair is activated when a replication fork stalls at an ICL, triggering monoubiquitination of the complex by the Fanconi Anemia ubiquitin ligase (CPX-6263), with one ubiquitin molecule being conjugated to each protein subunit. This may convert the ID complex into a clamp that can slide away from its initial location, potentially enabling downstream nucleases and other factors to act on the ICL.","predictedComplex":false,"interactors":[{"ac":"EBI-1013291","identifier":"Q9NVI1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NVI1/entry","name":"FANCI","description":"Fanconi anemia group I protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21818","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359343","identifier":"Q9BXW9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BXW9/entry","name":"FANCD2","description":"Fanconi anemia group D2 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32086","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6266","complexName":"Fanconi anemia FANCM-FAAP24-MHF anchoring complex","organismName":"Homo sapiens; 9606","description":"Required for the repair of DNA interstrand crosslinks (ICL) and related lesions. Recognizes different DNA structures, and recruits the Fanconi anemia ubiquitin ligase complex (CPX-6263) and other core Fanconi anemia pathway proteins to ICL sites. ICL repair is activated when a replication fork stalls at an ICL.","predictedComplex":false,"interactors":[{"ac":"EBI-1045650","identifier":"Q9BTP7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BTP7/entry","name":"FAAP24","description":"Fanconi anemia core complex-associated protein 24","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31786","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3957237","identifier":"Q8IYD8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IYD8/entry","name":"FANCM","description":"Fanconi anemia group M protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14025","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5529649","identifier":"Q8N2Z9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N2Z9/entry","name":"CENPS","description":"Centromere protein S","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22980","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5529694","identifier":"A8MT69","identifierLink":"https://www.uniprot.org/uniprotkb/A8MT69/entry","name":"CENPX","description":"Centromere protein X","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28680","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6267","complexName":"NELF negative elongation factor complex","organismName":"Homo sapiens; 9606","description":"Negatively regulates the elongation of transcription by RNA polymerase II. Required for promoter-proximal pausing when elongating Pol II pauses near the promoter, about 20-60 base pairs downstream of the transcription start site, a key event in post-initiation regulation of transcription. SUPT5H (O00267) docks the DSIF complex (CPX-891)  to Pol II near the RNA exit channel where it facilitates capping of the nascent RNA. NELF then recognizes the Pol II-SUPT5H interface and associates with the elongation complex as it transcribes through the promoter-proximal region. Binding of newly synthesized RNA by NELF may stabilize its interactions with elongating Pol II at specific loci. Phosphorylation of SUPT5H by P-TEFb (CPX-222/CPX-321/CPX-322) appears to trigger dissociation of NELF from Pol II, enabling Pol II reactivation and resumption of elongation.","predictedComplex":false,"interactors":[{"ac":"EBI-347721","identifier":"Q8WX92","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WX92/entry","name":"NELFB","description":"Negative elongation factor B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13503","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348444","identifier":"P18615","identifierLink":"https://www.uniprot.org/uniprotkb/P18615/entry","name":"NELFE","description":"Negative elongation factor E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR17250","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-536725","identifier":"Q8IXH7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IXH7/entry","name":"NELFCD","description":"Negative elongation factor C/D","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12144","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5461341","identifier":"Q9H3P2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H3P2/entry","name":"NELFA","description":"Negative elongation factor A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13328","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6268","complexName":"Dolichol-phosphate mannosyltransferase complex","organismName":"Homo sapiens; 9606","description":"Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man). Required for the biosynthesis of N-glycans which begins at the endoplasmic reticulum (ER) with the assembly of dolichol-linked tetra-decasaccharide (Glc3Man9GlcNAc2-PP-Dol). Dol-p-man is also a mannose donor for GPI anchor biosynthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-719526","identifier":"O60762","identifierLink":"https://www.uniprot.org/uniprotkb/O60762/entry","name":"DPM1","description":"Dolichol-phosphate mannosyltransferase subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43398","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9087337","identifier":"Q9P2X0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P2X0/entry","name":"DPM3","description":"Dolichol-phosphate mannosyltransferase subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16433","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9097061","identifier":"O94777","identifierLink":"https://www.uniprot.org/uniprotkb/O94777/entry","name":"DPM2","description":"Dolichol phosphate-mannose biosynthesis regulatory protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15039","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6269","complexName":"tRNA (adenine(58)-N(1))-methyltransferase complex","organismName":"Homo sapiens; 9606","description":"Methyltransferase complex which post-transcriptionally modifies initiator methionyl-tRNA by catalyzing the transfer of a methyl group from the cofactor S-adenosyl-l-methionine (CHEBI:67040) to N1 of adenine 58 to give 1-methyladenosine (m1A58). Also catalyses this modification at low levels in the tRNA-like T-loop-like structures of a small subset of mRNAs. This disrupts Watson–Crick base pairing at internal sites of mRNAs and may result in translational repression.","predictedComplex":false,"interactors":[{"ac":"EBI-934042","identifier":"Q96FX7","identifierLink":"https://www.uniprot.org/uniprotkb/Q96FX7/entry","name":"TRMT61A","description":"tRNA (adenine(58)-N(1))-methyltransferase catalytic subunit TRMT61A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12133","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-934061","identifier":"Q9UJA5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UJA5/entry","name":"TRMT6","description":"tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6270","complexName":"NatB N-alpha-acetyltransferase complex","organismName":"Homo sapiens; 9606","description":"N(alpha)-acetyltransferases responsible for the covalent attachment of an acetyl group (CH3CO) to the free alpha-amino group (NH3+) at the N-terminal end of a polypeptide, one of the most common co-translational modifications. This changes the electrostatic properties of proteins and therefore protein function, stability and localization. NatB is responsible for the acetylation of methionine-acidic/hydrophilic N-termini (Met-Asp-, Met-Asn-, Met-Glu-, and Met-Gln-). Required for normal cell cycle progression.","predictedComplex":false,"interactors":[{"ac":"EBI-1048503","identifier":"Q14CX7","identifierLink":"https://www.uniprot.org/uniprotkb/Q14CX7/entry","name":"NAA25","description":"N-alpha-acetyltransferase 25, NatB auxiliary subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1055023","identifier":"P61599","identifierLink":"https://www.uniprot.org/uniprotkb/P61599/entry","name":"NAA20","description":"N-alpha-acetyltransferase 20","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45910","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6271","complexName":"NatA N-alpha-acetyltransferase complex, NAA10-NAA15 variant","organismName":"Homo sapiens; 9606","description":"N(alpha)-acetyltransferases responsible for the covalent attachment of an acetyl group (CH3CO) to the free alpha-amino group (NH3+) at the N-terminal end of a polypeptide, one of the most common co-translational modifications. This changes the electrostatic properties of proteins and therefore protein function, stability and localization. NatA co-translationally acetylates N-termini that bear a small amino acid (Ala, Ser, Thr, Cys, and occasionally Val and Gly), which is exposed after methionine cleavage by methionine aminopeptidases.","predictedComplex":false,"interactors":[{"ac":"EBI-1042540","identifier":"Q9BXJ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BXJ9/entry","name":"NAA15","description":"N-alpha-acetyltransferase 15, NatA auxiliary subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-747693","identifier":"P41227","identifierLink":"https://www.uniprot.org/uniprotkb/P41227/entry","name":"NAA10","description":"N-alpha-acetyltransferase 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23091","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6272","complexName":"NatA N-alpha-acetyltransferase complex, NAA10-NAA16 variant","organismName":"Homo sapiens; 9606","description":"N(alpha)-acetyltransferases responsible for the covalent attachment of an acetyl group (CH3CO) to the free alpha-amino group (NH3+) at the N-terminal end of a polypeptide, one of the most common co-translational modifications. This changes the electrostatic properties of proteins and therefore protein function, stability and localization. NatA co-translationally acetylates N-termini that bear a small amino acid (Ala, Ser, Thr, Cys, and occasionally Val and Gly), which is exposed after methionine cleavage by methionine aminopeptidases.","predictedComplex":false,"interactors":[{"ac":"EBI-2561139","identifier":"Q6N069","identifierLink":"https://www.uniprot.org/uniprotkb/Q6N069/entry","name":"NAA16","description":"N-alpha-acetyltransferase 16, NatA auxiliary subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-747693","identifier":"P41227","identifierLink":"https://www.uniprot.org/uniprotkb/P41227/entry","name":"NAA10","description":"N-alpha-acetyltransferase 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23091","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6273","complexName":"NatA N-alpha-acetyltransferase complex, NAA11-NAA15 variant","organismName":"Homo sapiens; 9606","description":"N(alpha)-acetyltransferases responsible for the covalent attachment of an acetyl group (CH3CO) to the free alpha-amino group (NH3+) at the N-terminal end of a polypeptide, one of the most common co-translational modifications. This changes the electrostatic properties of proteins and therefore protein function, stability and localization. NatA co-translationally acetylates N-termini that bear a small amino acid (Ala, Ser, Thr, Cys, and occasionally Val and Gly), which is exposed after methionine cleavage by methionine aminopeptidases.","predictedComplex":false,"interactors":[{"ac":"EBI-1042540","identifier":"Q9BXJ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BXJ9/entry","name":"NAA15","description":"N-alpha-acetyltransferase 15, NatA auxiliary subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2585120","identifier":"Q9BSU3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BSU3/entry","name":"NAA11","description":"N-alpha-acetyltransferase 11","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23091","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6274","complexName":"NatA N-alpha-acetyltransferase complex, NAA11-NAA16 variant","organismName":"Homo sapiens; 9606","description":"N(alpha)-acetyltransferases responsible for the covalent attachment of an acetyl group (CH3CO) to the free alpha-amino group (NH3+) at the N-terminal end of a polypeptide, one of the most common co-translational modifications. This changes the electrostatic properties of proteins and therefore protein function, stability and localization. NatA co-translationally acetylates N-termini that bear a small amino acid (Ala, Ser, Thr, Cys, and occasionally Val and Gly), which is exposed after methionine cleavage by methionine aminopeptidases.","predictedComplex":false,"interactors":[{"ac":"EBI-2561139","identifier":"Q6N069","identifierLink":"https://www.uniprot.org/uniprotkb/Q6N069/entry","name":"NAA16","description":"N-alpha-acetyltransferase 16, NatA auxiliary subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2585120","identifier":"Q9BSU3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BSU3/entry","name":"NAA11","description":"N-alpha-acetyltransferase 11","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23091","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6275","complexName":"NatC N-alpha-acetyltransferase complex","organismName":"Homo sapiens; 9606","description":"N(alpha)-acetyltransferases responsible for the covalent attachment of an acetyl group (CH3CO) to the free alpha-amino group (NH3+) at the N-terminal end of a polypeptide, one of the most common co-translational modifications. This changes the electrostatic properties of proteins and therefore protein function, stability and localization. NatC acetylates N-terminal methionine of proteins with hydrophobic/amphipathic N-termini (Met-Leu- Met-Ile-, Met-Phe-, Met-Trp-, Mat-Val-, Met-Met-, Met-His-, and Met-Lys-) to varying degrees.","predictedComplex":false,"interactors":[{"ac":"EBI-9106461","identifier":"Q147X3","identifierLink":"https://www.uniprot.org/uniprotkb/Q147X3/entry","name":"NAA30","description":"N-alpha-acetyltransferase 30","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45896","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9106478","identifier":"Q5VZE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q5VZE5/entry","name":"NAA35","description":"N-alpha-acetyltransferase 35, NatC auxiliary subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21373","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9106509","identifier":"Q9BRA0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BRA0/entry","name":"NAA38","description":"N-alpha-acetyltransferase 38, NatC auxiliary subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6276","complexName":"DNA (cytosine-5)-methyltransferase 3B complex","organismName":"Homo sapiens; 9606","description":"DNA methyltransferase, which methylates DNA by a non-cooperative or processive mechanism. Required for genome-wide de novo methylation, a  major epigenetic mechanism that controls gene expression, genomic stability, and cell differentiation.  Predominantly occurs at the C-5 position of cytosine within the symmetric CpG dinucleotide, affecting approximately 70-80% of the CpG sites throughout the genome. Also responsible fornon-CpG methylation (mainly CpA ) in oocytes, embryonic stem cells, and neural cells DNA.  the DNMT3B–3L complex plays a role in early embryonic development and in minor satellite repeat methylation.  Methylates pericentric satellite repeats and actively transcribed genes within the gene body to prevent spurious transcription initiation.","predictedComplex":false,"interactors":[{"ac":"EBI-740967","identifier":"Q9UJW3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UJW3/entry","name":"DNMT3L","description":"DNA (cytosine-5)-methyltransferase 3-like","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-80125","identifier":"Q9UBC3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UBC3/entry","name":"DNMT3B","description":"DNA (cytosine-5)-methyltransferase 3B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6282","complexName":"ATP8B1-CDC50A P4-ATPase complex","organismName":"Homo sapiens; 9606","description":"A membrane pump which actively translocates, or flips, phospholipids across cell membranes from the exoplasmic to the cytoplasmic leaflet of the lipid bilayer. This generates and maintains membrane lipid asymmetry, a property essential for a wide variety of cellular processes such as vesicle budding and intracellular vesicle trafficking. Transport is accomplished by cyclic changes between two main enzyme conformations, during which the ATP8B1 ATPase is phosphorylated by ATP at a conserved aspartate residue (Asp-454) and subsequently dephosphorylated. CDC50 proteins are required for transport of P4‐ATPases from the endoplasmic reticulum to their final destinations and may also affect the catalytic cycle of the complex. Preferentially translocates phosphatidylcholine in the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-2836942","identifier":"Q9NV96","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NV96/entry","name":"TMEM30A","description":"Cell cycle control protein 50A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10926","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9524729","identifier":"O43520","identifierLink":"https://www.uniprot.org/uniprotkb/O43520/entry","name":"ATP8B1","description":"Phospholipid-transporting ATPase IC","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6283","complexName":"ATP8B1-CDC50B P4-ATPase complex","organismName":"Homo sapiens; 9606","description":"A membrane pump which actively translocates, or flips, phospholipids across cell membranes from the exoplasmic to the cytoplasmic leaflet of the lipid bilayer. This generates and maintains membrane lipid asymmetry, a property essential for a wide variety of cellular processes such as vesicle budding and intracellular vesicle trafficking. Transport is accomplished by cyclic changes between two main enzyme conformations, during which the ATP8B1 ATPase is phosphorylated by ATP at a conserved aspartate residue (Asp-454) and subsequently dephosphorylated. CDC50 proteins are required for transport of P4‐ATPases from the endoplasmic reticulum to their final destinations and may also affect the catalytic cycle of the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-9524729","identifier":"O43520","identifierLink":"https://www.uniprot.org/uniprotkb/O43520/entry","name":"ATP8B1","description":"Phospholipid-transporting ATPase IC","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9527107","identifier":"Q3MIR4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3MIR4/entry","name":"TMEM30B","description":"Cell cycle control protein 50B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10926","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6285","complexName":"ATP8A1-CDC50A P4-ATPase complex","organismName":"Homo sapiens; 9606","description":"A membrane pump which actively translocates, or flips, phospholipids across cell membranes from the exoplasmic to the cytoplasmic leaflet of the lipid bilayer. This generates and maintains membrane lipid asymmetry, a property essential for a wide variety of cellular processes such as vesicle budding and intracellular vesicle trafficking. Transport is accomplished by cyclic changes between two main enzyme conformations, during which the ATP8A1 ATPase is phosphorylated by ATP at a conserved aspartate residue (Asp-409) and subsequently dephosphorylated. CDC50 proteins are required for transport of P4‐ATPases from the endoplasmic reticulum to their final destinations and may also affect the catalytic cycle of the complex. Preferentially translocates phosphatidylserine in the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-2836942","identifier":"Q9NV96","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NV96/entry","name":"TMEM30A","description":"Cell cycle control protein 50A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10926","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9539324","identifier":"Q9Y2Q0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2Q0/entry","name":"ATP8A1","description":"Phospholipid-transporting ATPase IA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6286","complexName":"ATP8A1-CDC50B P4-ATPase complex","organismName":"Homo sapiens; 9606","description":"A membrane pump which actively translocates, or flips, phospholipids across cell membranes from the exoplasmic to the cytoplasmic leaflet of the lipid bilayer. This generates and maintains membrane lipid asymmetry, a property essential for a wide variety of cellular processes such as vesicle budding and intracellular vesicle trafficking. Transport is accomplished by cyclic changes between two main enzyme conformations, during which the ATP8A1 ATPase is phosphorylated by ATP at a conserved aspartate residue (Asp-409) and subsequently dephosphorylated. CDC50 proteins are required for transport of P4‐ATPases from the endoplasmic reticulum to their final destinations and may also affect the catalytic cycle of the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-9527107","identifier":"Q3MIR4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3MIR4/entry","name":"TMEM30B","description":"Cell cycle control protein 50B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10926","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9539324","identifier":"Q9Y2Q0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2Q0/entry","name":"ATP8A1","description":"Phospholipid-transporting ATPase IA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6301","complexName":"ATP8A2-CDC50A P4-ATPase complex","organismName":"Homo sapiens; 9606","description":"A membrane pump which actively translocates, or flips, phospholipids across cell membranes from the exoplasmic to the cytoplasmic leaflet of the lipid bilayer. This generates and maintains membrane lipid asymmetry, a property essential for a wide variety of cellular processes such as vesicle budding and intracellular vesicle trafficking. Transport is accomplished by cyclic changes between two main enzyme conformations, during which the ATP8A2 ATPase is phosphorylated by ATP at a conserved aspartate residue (Asp-428) and subsequently dephosphorylated. CDC50 proteins are required for transport of P4‐ATPases from the endoplasmic reticulum to their final destinations and may also affect the catalytic cycle of the complex. Preferentially translocates phosphatidylserine in the plasma membrane. Preferentially expressed in brain and testes.","predictedComplex":false,"interactors":[{"ac":"EBI-2836942","identifier":"Q9NV96","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NV96/entry","name":"TMEM30A","description":"Cell cycle control protein 50A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10926","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9539366","identifier":"Q9NTI2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NTI2/entry","name":"ATP8A2","description":"Phospholipid-transporting ATPase IB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6302","complexName":"ATP8B2-CDC50A P4-ATPase complex","organismName":"Homo sapiens; 9606","description":"A membrane pump which actively translocates, or flips, phospholipids across cell membranes from the exoplasmic to the cytoplasmic leaflet of the lipid bilayer. This generates and maintains membrane lipid asymmetry, a property essential for a wide variety of cellular processes such as vesicle budding and intracellular vesicle trafficking. Transport is accomplished by cyclic changes between two main enzyme conformations, during which the ATP8B2 ATPase is phosphorylated by ATP at a conserved aspartate residue (Asp-411) and subsequently dephosphorylated. CDC50 proteins are required for transport of P4‐ATPases from the endoplasmic reticulum to their final destinations and may also affect the catalytic cycle of the complex. Preferentially translocates phosphatidylcholine in the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-2836942","identifier":"Q9NV96","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NV96/entry","name":"TMEM30A","description":"Cell cycle control protein 50A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10926","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9539266","identifier":"P98198","identifierLink":"https://www.uniprot.org/uniprotkb/P98198/entry","name":"ATP8B2","description":"Phospholipid-transporting ATPase ID","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6303","complexName":"ATP8B2-CDC50B P4-ATPase complex","organismName":"Homo sapiens; 9606","description":"A membrane pump which actively translocates, or flips, phospholipids across cell membranes from the exoplasmic to the cytoplasmic leaflet of the lipid bilayer. This generates and maintains membrane lipid asymmetry, a property essential for a wide variety of cellular processes such as vesicle budding and intracellular vesicle trafficking. Transport is accomplished by cyclic changes between two main enzyme conformations, during which the ATP8B2 ATPase is phosphorylated by ATP at a conserved aspartate residue (Asp-411) and subsequently dephosphorylated. CDC50 proteins are required for transport of P4‐ATPases from the endoplasmic reticulum to their final destinations and may also affect the catalytic cycle of the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-9527107","identifier":"Q3MIR4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3MIR4/entry","name":"TMEM30B","description":"Cell cycle control protein 50B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10926","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9539266","identifier":"P98198","identifierLink":"https://www.uniprot.org/uniprotkb/P98198/entry","name":"ATP8B2","description":"Phospholipid-transporting ATPase ID","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6304","complexName":"ATP8B3-CDC50A P4-ATPase complex","organismName":"Homo sapiens; 9606","description":"A membrane pump which actively translocates, or flips, phospholipids across cell membranes from the exoplasmic to the cytoplasmic leaflet of the lipid bilayer. This generates and maintains membrane lipid asymmetry, a property essential for a wide variety of cellular processes such as vesicle budding and intracellular vesicle trafficking. Transport is accomplished by cyclic changes between two main enzyme conformations, during which the ATP8B3 ATPase is phosphorylated by ATP at a conserved aspartate residue (Asp-495) and subsequently dephosphorylated. CDC50 proteins are required for transport of P4‐ATPases from the endoplasmic reticulum to their final destinations and may also affect the catalytic cycle of the complex. Mainly found in testes.","predictedComplex":false,"interactors":[{"ac":"EBI-20856511","identifier":"O60423","identifierLink":"https://www.uniprot.org/uniprotkb/O60423/entry","name":"ATP8B3","description":"Phospholipid-transporting ATPase IK","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2836942","identifier":"Q9NV96","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NV96/entry","name":"TMEM30A","description":"Cell cycle control protein 50A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10926","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1320","complexName":"Peptide:N-glycanase-Rad23 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Role in the proteasomal degradation of a specific set of ER-associated protein degradation (ERAD) substrates, specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists proteasome-mediated glycoprotein degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-14668","identifier":"P32628","identifierLink":"https://www.uniprot.org/uniprotkb/P32628/entry","name":"RAD23","description":"UV excision repair protein RAD23","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10621","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-38139","identifier":"Q02890","identifierLink":"https://www.uniprot.org/uniprotkb/Q02890/entry","name":"PNG1","description":"Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1321","complexName":"EDS1-SAG101 complex, variant EDS1","organismName":"Arabidopsis thaliana; 3702","description":"Functions in basal disease resistance and resistance (R) gene-mediated effector triggered immunity (ETI), regulates accumulation of the hormone salicylic acid (SA) which is a necessary component of systemic immunity. Part of a family of systemic immunity complexes: EDS1-PAD4 complexes (CPX-1324 & CPX-1618) alone are sufficient for basal resistance, partly mediated via SA. EDS1-SAG101 complexes (this complex & CPX-1617) contribute to basal and TIR-NB-LRR-type R gene-triggered resistance in the absence of PAD4. Loss of SAG101 can be compensated for by the presence of PAD4 in both resistance responses. EDS1-PAD4-SAG101 complexes (CPX-1325 & CPX-1619) are required for resistance signalling against turnip crinkle virus.","predictedComplex":false,"interactors":[{"ac":"EBI-1390454","identifier":"Q9SU72","identifierLink":"https://www.uniprot.org/uniprotkb/Q9SU72/entry","name":"EDS1","description":"Protein EDS1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR47090","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16422562","identifier":"Q4F883","identifierLink":"https://www.uniprot.org/uniprotkb/Q4F883/entry","name":"SAG101","description":"Senescence-associated carboxylesterase 101","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR46898","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1322","complexName":"RAD53-ASF1 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Role in recovery from the DNA damage checkpoint. ASF1 binds most of the free and unmodified RAD53 in the cell and this is required for complete dephosphorylation of Rad53 when the upstream DNA damage checkpoint signaling is turned off. Phosphorylation of RAD53 following DNA damage causes dissociation and frees RAD53 to undergo autophosphorylation and activation and to participate in double-strand break repair.","predictedComplex":false,"interactors":[{"ac":"EBI-17843","identifier":"P22216","identifierLink":"https://www.uniprot.org/uniprotkb/P22216/entry","name":"RAD53","description":"Serine/threonine-protein kinase RAD53","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR44167","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3003","identifier":"P32447","identifierLink":"https://www.uniprot.org/uniprotkb/P32447/entry","name":"ASF1","description":"Histone chaperone ASF1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1323","complexName":"CDC48-RAD23-UFD2 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A type II AAA ATPase that is involved in the dislocation/extraction step of its substrate proteins from cellular structures or multiprotein complexes into the cytosol where they are largely degraded by the proteasome.. Role in the escort pathway of proteasomal protein degradation, linking the ubiquitylation of specific substrates directly to their delivery to the proteasome. Oligo-ubiquitylated substrates are recognized and extracted by CDC48. UFD2 modifies the client proteins with lys-48-linked chains of four to six ubiquitins. RAD23 is recruited to the ternary complex, in which its UBL domain associates with UFD2, and then CDC48 remodels the complex to release the RAD23-ubiquitylated substrate complex which binds to the proteasome and delivers the substrate for degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-14668","identifier":"P32628","identifierLink":"https://www.uniprot.org/uniprotkb/P32628/entry","name":"RAD23","description":"UV excision repair protein RAD23","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10621","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20003","identifier":"P54860","identifierLink":"https://www.uniprot.org/uniprotkb/P54860/entry","name":"UFD2","description":"E4 ubiquitin-protein ligase UFD2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13931","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4308","identifier":"P25694","identifierLink":"https://www.uniprot.org/uniprotkb/P25694/entry","name":"CDC48","description":"Cell division control protein 48","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1324","complexName":"EDS1-PAD4 complex, variant EDS1","organismName":"Arabidopsis thaliana; 3702","description":"Functions in basal disease resistance and resistance (R) gene-mediated effector triggered immunity (ETI), regulates accumulation of the hormone salicylic acid (SA) which is a necessary component of systemic immunity. Part of a family of systemic immunity complexes: EDS1-PAD4 complexes (this complex & CPX-1618) alone are sufficient for basal resistance, partly mediated via SA. EDS1-SAG101 complexes (CPX-1321 & CPX-1617) contribute to basal and TIR-NB-LRR-type R gene-triggered resistance in the absence of PAD4. Loss of SAG101 can be compensated for by the presence of PAD4 in both resistance responses. EDS1-PAD4-SAG101 complexes (CPX-1325 & CPX-1619) are required for resistance signalling against turnip crinkle virus.","predictedComplex":false,"interactors":[{"ac":"EBI-1390441","identifier":"Q9S745","identifierLink":"https://www.uniprot.org/uniprotkb/Q9S745/entry","name":"PAD4","description":"Lipase-like PAD4","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR47413","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1390454","identifier":"Q9SU72","identifierLink":"https://www.uniprot.org/uniprotkb/Q9SU72/entry","name":"EDS1","description":"Protein EDS1","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR47090","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1325","complexName":"EDS1-PAD4-SAG101 complex, variant EDS1","organismName":"Arabidopsis thaliana; 3702","description":"Functions in basal disease resistance and resistance (R) gene-mediated effector triggered immunity (ETI), regulates accumulation of the hormone salicylic acid (SA) which is a necessary component of systemic immunity. Part of a family of systemic immunity complexes: EDS1-PAD4 complexes (CPX-1324 & CPX-1618) alone are sufficient for basal resistance, partly mediated via SA. EDS1-SAG101 complexes (CPX-1321 & CPX-1617) contribute to basal and TIR-NB-LRR-type R gene-triggered resistance in the absence of PAD4. Loss of SAG101 can be compensated for by the presence of PAD4 in both resistance responses. EDS1-PAD4-SAG101 complexes (this complex & CPX-1619) are required for resistance signalling against turnip crinkle virus.","predictedComplex":false,"interactors":[{"ac":"EBI-1390441","identifier":"Q9S745","identifierLink":"https://www.uniprot.org/uniprotkb/Q9S745/entry","name":"PAD4","description":"Lipase-like PAD4","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR47413","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1390454","identifier":"Q9SU72","identifierLink":"https://www.uniprot.org/uniprotkb/Q9SU72/entry","name":"EDS1","description":"Protein EDS1","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR47090","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16422562","identifier":"Q4F883","identifierLink":"https://www.uniprot.org/uniprotkb/Q4F883/entry","name":"SAG101","description":"Senescence-associated carboxylesterase 101","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR46898","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1326","complexName":"CAX1-CAX3 complex","organismName":"Arabidopsis thaliana; 3702","description":"Cation antiporter complex that facilitates influx of cations, mainly Ca(2+) ions, into the cell and proton out of the cell. Required for normal growth, ion homeostasis and the functioning of stomata. Contribute to plant defense responses. Loss of CAX1 or CAX1 and CAX3 subunits results in severe reduction in growth, including leaf tip and flower necrosis and pronounced sensitivity to exogenous Ca(2+) and other ions. This effect is more pronounced if both subunits are missing.","predictedComplex":false,"interactors":[{"ac":"EBI-2292388","identifier":"Q39253","identifierLink":"https://www.uniprot.org/uniprotkb/Q39253/entry","name":"CAX1","description":"Vacuolar cation/proton exchanger 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR31503","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2292420","identifier":"Q93Z81","identifierLink":"https://www.uniprot.org/uniprotkb/Q93Z81/entry","name":"CAX3","description":"Vacuolar cation/proton exchanger 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR31503","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1330","complexName":"AMT1-1 homotrimer","organismName":"Arabidopsis thaliana; 3702","description":"High affinity ammonium transporter complex that enables the transfer of ammonium across the plasma membrane into the cell under nitrogen-deficient growth conditions. Critical for allosteric regulation of transport activity which enables plant roots to repress ammonium uptake at elevated ammonium supplies.","predictedComplex":false,"interactors":[{"ac":"EBI-16426081","identifier":"P54144","identifierLink":"https://www.uniprot.org/uniprotkb/P54144/entry","name":"AMT1-1","description":"Ammonium transporter 1 member 1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11730","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1331","complexName":"bI3 intron splicing factor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Self-splicing ribozymal RNA Group I intron splicing factor. A guanosine cofactor docks onto an active G-binding site and hydrolyses the phosphodiester bond at the splice site located in P1, resulting in a free hydroxyl group at the upstream exon and the guanosine cofactor being attached to the 5-prime end of the intron. The terminal guanosine of the intron then occupies the G-binding site to organize the second ester-transfer reaction leading to the ligation of the adjacent upstream and downstream exons and release of the catalytic intron.","predictedComplex":false,"interactors":[{"ac":"EBI-11278","identifier":"P07266","identifierLink":"https://www.uniprot.org/uniprotkb/P07266/entry","name":"MRS1","description":"Mitochondrial RNA-splicing protein MRS1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28072","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16423101","identifier":null,"identifierLink":null,"name":"bi3_intron_yeast_mrna","description":"bi3 intron mRNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"messenger rna","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-16423117","identifier":"Q9ZZW7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ZZW7/entry","name":"BI3","description":"Cytochrome b mRNA maturase bI3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19271","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1332","complexName":"RAT1-RAI1 RNA polymerase II termination complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"5-prime-3-prime exoribonuclease which promotes RNA polymerase II (RNAPII) termination by degrading RNA from the newly formed 5-prime phosphorylated end. RNAPII becomes catalytically disrupted when an NTP mis-incorporates and is more efficiently terminated by the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-14845","identifier":"Q02792","identifierLink":"https://www.uniprot.org/uniprotkb/Q02792/entry","name":"RAT1","description":"5'-3' exoribonuclease 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12341","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-24206","identifier":"P53063","identifierLink":"https://www.uniprot.org/uniprotkb/P53063/entry","name":"RAI1","description":"Decapping nuclease RAI1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12395","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1333","complexName":"RTT109-VPS75 histone acetyltransferase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Histone acetyltransferase complex that acetylates lysines-9, -27 and possibly  -56 on newly synthesized histone H3 during S-phase to mediate nucleosome assembly during DNA replication and DNA repair. Complex formation is required for full activity with VPS75, ensuring that RTT109 is efficiently localized in the nucleus,  and presenting histones to RTT109 for acetylation.","predictedComplex":false,"interactors":[{"ac":"EBI-2887026","identifier":"Q07794","identifierLink":"https://www.uniprot.org/uniprotkb/Q07794/entry","name":"RTT109","description":"Histone acetyltransferase RTT109","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31571","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29225","identifier":"P53853","identifierLink":"https://www.uniprot.org/uniprotkb/P53853/entry","name":"VPS75","description":"Vacuolar protein sorting-associated protein 75","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11875","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1334","complexName":"Nuclear cap-binding complex","organismName":"Arabidopsis thaliana; 3702","description":"Binds co-transcriptionally to the 5-prime, m7GpppG-cap (m7G-cap) structures of all RNA polymerase II transcripts (mRNAs and pre-miRNAs). Required for processes such as pre-mRNA splicing, export and degradation of nuclear mRNAs, primary miRNA processing and miRNA-mediated RNA interference. In the cytosol, importin-beta probably interacts with CBC-bound importin-alpha and promotes the dissociation of the RNA from CBC. Importin-complex-bound CBC gets reimported into the nucleus for reuse. \r\n\r\nModulates ABA signaling by altering transcript of early ABA signaling elements and function as negative regulators in guard cell ABA signaling. Mutations in either subunit result in slow growth, serrated leaf margins, ABA hypersensitivity and greater resistance to draught. Mutation of ABH1 results in early flowering by affecting the removal of the first intron of FLC (Q9S7Q7) which is a key flowering suppressor.","predictedComplex":false,"interactors":[{"ac":"EBI-2354070","identifier":"Q9XFD1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XFD1/entry","name":"CBP20","description":"Nuclear cap-binding protein subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR18847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2359412","identifier":"Q9SIU2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9SIU2/entry","name":"ABH1","description":"Nuclear cap-binding protein subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR12412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1335","complexName":"RVS161-RVS167 amphiphysin complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Binds to membranes and promote the membrane curvature required for endocytosis and also potentially membrane scission at the sites of endocytosis. The BAR domains present in both proteins form helical structures at the neck of the invaginating plasma membrane. Functions with INP52 (P50942) to promote scission of the vesicle. The complex appears to protect the PI(4,5)P2 in the vesicle neck resulting in differential hydrolysis by INP52 to generate a lipid phase boundary. This leads to a mechanochemical interfacial force, driving membrane scission. In growing yeast cells, the complexes localize to cortical actin patches, which are sites of endocytosis.","predictedComplex":false,"interactors":[{"ac":"EBI-14490","identifier":"P25343","identifierLink":"https://www.uniprot.org/uniprotkb/P25343/entry","name":"RVS161","description":"Reduced viability upon starvation protein 161","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47174","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14500","identifier":"P39743","identifierLink":"https://www.uniprot.org/uniprotkb/P39743/entry","name":"RVS167","description":"Reduced viability upon starvation protein 167","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47174","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1337","complexName":"WHY1 complex","organismName":"Arabidopsis thaliana; 3702","description":"Modulates DNA repair in plant chloroplasts by binding single-stranded DNA in a non-sequence-specific manner. Regulates telomere-length homeostasis by binding the telomere end. Contributes to both basal and specific defense responses. Transcription can be induced by salicylic acid (SA).","predictedComplex":false,"interactors":[{"ac":"EBI-16426969","identifier":"Q9M9S3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9M9S3/entry","name":"WHY1","description":"Single-stranded DNA-binding protein WHY1, chloroplastic","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR31745","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1339","complexName":"SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-SKP1A","organismName":"Arabidopsis thaliana; 3702","description":"SCF(COI1) is a member of the SCF (Skp1-Cullin-F-box) E3 ubiquitin ligase family, which catalyse the last step of ubiquitination cascade, promoting transfer of ubiquitin from an E2 enzyme to form a covalent bond with a substrate lysine. It perceives jasmonate signal and degrades Jasmonate ZIM Domain (JAZ) proteins, which repress the transcription factor MYC2 (Q39204) that binds to cis-acting elements of jasmonate response genes.","predictedComplex":false,"interactors":[{"ac":"EBI-16686500","identifier":"CHEBI:24937","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:24937","name":"jasmonates","description":"jasmonates","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-401159","identifier":"O04197","identifierLink":"https://www.uniprot.org/uniprotkb/O04197/entry","name":"COI1","description":"Coronatine-insensitive protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR16134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-532357","identifier":"Q39255","identifierLink":"https://www.uniprot.org/uniprotkb/Q39255/entry","name":"SKP1A","description":"SKP1-like protein 1A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-532404","identifier":"Q940X7","identifierLink":"https://www.uniprot.org/uniprotkb/Q940X7/entry","name":"RBX1A","description":"RING-box protein 1a","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-532411","identifier":"Q94AH6","identifierLink":"https://www.uniprot.org/uniprotkb/Q94AH6/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 3, maxValue: 3","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1340","complexName":"Separin-securin complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Regulates the metaphase-to-anaphase transition during cell cycle progression, playing a role in control of the metaphase-anaphase transition and anaphase onset. Complex formation both activates and inhibits the protease activity of separase which is responsible for cleaving the MCD1/SCC1 (Q12158) subunit of the cohesin ring that holds sister chromatids together during mitosis. Securin appears to ensure that separase adopts its proper fold required for proteolytic activity and also promotes subcellular localization of separase to the nucleus. Securin is degraded via ubiquitylation by the anaphase-promoting complex (APC, CPX-760, CPX-761, CPX-762, CPX-756) enabling separase to become fully active.","predictedComplex":false,"interactors":[{"ac":"EBI-16908","identifier":"P40316","identifierLink":"https://www.uniprot.org/uniprotkb/P40316/entry","name":"PDS1","description":"Securin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-6657","identifier":"Q03018","identifierLink":"https://www.uniprot.org/uniprotkb/Q03018/entry","name":"ESP1","description":"Separin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12792","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1341","complexName":"SEC23-LST1 COPII cargo recruitment complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Adapter complex which interacts with the COPII coat (CPX-2523) to recruit specific cargo proteins, such as PMA1 (P05030), the essential plasma membrane ATPase, into the membrane vesicles that export newly synthesised proteins from the endoplasmic reticulum. Requires the presence of SEC23/SEC24 in the COPII coat for activity. Required for the export of glycosylphosphatidylinositol-anchored proteins to the Golgi apparatus through interaction with the EMP24 complex (CPX-1698).","predictedComplex":false,"interactors":[{"ac":"EBI-16584","identifier":"P15303","identifierLink":"https://www.uniprot.org/uniprotkb/P15303/entry","name":"SEC23","description":"Protein transport protein SEC23","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11141","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17012","identifier":"P38810","identifierLink":"https://www.uniprot.org/uniprotkb/P38810/entry","name":"SFB3","description":"SED5-binding protein 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13803","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1342","complexName":"SET3C histone deacetylase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Histone deacetylase complex important in regulating gene induction during stress response, such as changes in carbon sources, nitrogen starvation and DNA damage. SET3C binds to the histone marker H3K4me2 either in the 5' region of the open reading frames or in the promoter regions of some genes, replacing H3K4me3","predictedComplex":false,"interactors":[{"ac":"EBI-16993","identifier":"P36124","identifierLink":"https://www.uniprot.org/uniprotkb/P36124/entry","name":"SET3","description":"SET domain-containing protein 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46462","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17136","identifier":"P38262","identifierLink":"https://www.uniprot.org/uniprotkb/P38262/entry","name":"SIF2","description":"SIR4-interacting protein SIF2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22846","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17596","identifier":"P25357","identifierLink":"https://www.uniprot.org/uniprotkb/P25357/entry","name":"SNT1","description":"Probable DNA-binding protein SNT1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13992","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32717409","identifier":"CHEBI:57540","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57540","name":"nad(1-)","description":"NAD(1-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-5463","identifier":"P14832","identifierLink":"https://www.uniprot.org/uniprotkb/P14832/entry","name":"CPR1","description":"Peptidyl-prolyl cis-trans isomerase","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11071","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8475","identifier":"P53096","identifierLink":"https://www.uniprot.org/uniprotkb/P53096/entry","name":"HOS2","description":"Probable histone deacetylase HOS2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8492","identifier":"P40480","identifierLink":"https://www.uniprot.org/uniprotkb/P40480/entry","name":"HOS4","description":"Protein HOS4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24123","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8691","identifier":"P53685","identifierLink":"https://www.uniprot.org/uniprotkb/P53685/entry","name":"HST1","description":"NAD-dependent protein deacetylase HST1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11085","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1343","complexName":"SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-SKP1A","organismName":"Arabidopsis thaliana; 3702","description":"SCF-TIR1 is a member of the SCF (Skp1-Cullin-F-box) E3 ubiquitin ligase family, which catalyse the last step of ubiquitination cascade, promoting transfer of ubiquitin from an E2 enzyme to form a covalent bond with a substrate lysine. 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In the U6 snRNP spliceosome machinery stabilises U6 small nuclear RNA (U6 snRNA) to ensure the efficiency and accuracy of constitutive and alternative splicing of selected pre-mRNAs depending on the environmental conditions. Loss of LMS8 leads to a range of severe developmental abnormalities.","predictedComplex":false,"interactors":[{"ac":"EBI-16419382","identifier":"Q9FKB0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9FKB0/entry","name":"LSM5","description":"Sm-like protein LSM5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR20971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16419411","identifier":"F4K4E3","identifierLink":"https://www.uniprot.org/uniprotkb/F4K4E3/entry","name":"LSM4","description":"Sm-like protein LSM4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16419650","identifier":"Q8VYI0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VYI0/entry","name":"LSM8","description":"Sm-like protein LSM8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR15588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4433669","identifier":"Q9SI54","identifierLink":"https://www.uniprot.org/uniprotkb/Q9SI54/entry","name":"LSM7","description":"Sm-like protein LSM7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9347287","identifier":"O22823","identifierLink":"https://www.uniprot.org/uniprotkb/O22823/entry","name":"LSM6B","description":"Sm-like protein LSM36B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9347299","identifier":"Q9C6K5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9C6K5/entry","name":"LSM3B","description":"Sm-like protein LSM3B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR13110","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9347308","identifier":"Q1H595","identifierLink":"https://www.uniprot.org/uniprotkb/Q1H595/entry","name":"LSM2","description":"Sm-like protein LSM2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR13829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1355","complexName":"RTT107-SLX4-SLX1 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for checkpoint dampening by reducing RAD53 checkpoint activation. Complex formation enables MEC1 (P38111) and CDK-mediated phosphorylation of SLX4 and RTT107 under replication stress and DNA damage situations. Upon phosphorylation of SLX4 on Ser-486, the complex becomes associated with DPB11 (P47027) and diminishes DPB11 interaction with RAD9, thus reducing RAD53 (P22216) phosphorylation and activation.","predictedComplex":false,"interactors":[{"ac":"EBI-21016","identifier":"P38324","identifierLink":"https://www.uniprot.org/uniprotkb/P38324/entry","name":"SLX1","description":"Structure-specific endonuclease subunit SLX1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR20208","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-24788","identifier":"P38850","identifierLink":"https://www.uniprot.org/uniprotkb/P38850/entry","name":"RTT107","description":"Regulator of Ty1 transposition protein 107","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47667","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-37788","identifier":"Q12098","identifierLink":"https://www.uniprot.org/uniprotkb/Q12098/entry","name":"SLX4","description":"Structure-specific endonuclease subunit SLX4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1357","complexName":"RSA centrosome-targeting complex","organismName":"Caenorhabditis elegans; 6239","description":"Serine/threonie phosphatase complex specifically localized to the centrosome. Required for the regulation of microtubule outgrowth from centrosomes and also for mitotic spindle assembly by ensuring the stability of kinetochore microtubules. May regulate microtubule outgrowth from centrosomes by restricting the levels of the microtubule destabilizer klp-7 (Q9XU12) at centrosomes and mitotic spindle assembly by targeting the Aurora kinase activator tpxl-1 (G5EDE7) to centrosomes.\r\n\r\nrsa-2 is required to recruit rsa-1 to the centrosome, but both regulatory subunits rsa-1 and rsa-2 are required for targeting let-92 to the centrosome. Furthermore, rsa-2 may act as a linker protein, connecting the core centrosomal protein spd-5 to let-92 via rsa-1.","predictedComplex":false,"interactors":[{"ac":"EBI-1187455","identifier":"O02217","identifierLink":"https://www.uniprot.org/uniprotkb/O02217/entry","name":"rsa-1","description":"Serine/threonine-protein phosphatase 2A regulatory subunit rsa-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12085","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1187461","identifier":"G5EFV3","identifierLink":"https://www.uniprot.org/uniprotkb/G5EFV3/entry","name":"rsa-2","description":"Regulator of spindle assembly protein 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-319655","identifier":"G5EGK8","identifierLink":"https://www.uniprot.org/uniprotkb/G5EGK8/entry","name":"let-92","description":"Serine/threonine-protein phosphatase 2A catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-322479","identifier":"P91349","identifierLink":"https://www.uniprot.org/uniprotkb/P91349/entry","name":"spd-5","description":"Spindle-defective protein 5","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR18861","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-322806","identifier":"Q09543","identifierLink":"https://www.uniprot.org/uniprotkb/Q09543/entry","name":"paa-1","description":"Probable serine/threonine-protein phosphatase PP2A regulatory subunit","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1358","complexName":"ced-3-ced-4-mac-1 complex","organismName":"Caenorhabditis elegans; 6239","description":"Complex plays a role in programmed cell death (apoptosis),  preventing ced-4 and caspase ced-3-mediated apoptosis.","predictedComplex":false,"interactors":[{"ac":"EBI-2005767","identifier":"Q9NAG4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NAG4/entry","name":"mac-1","description":"Protein mac-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-494118","identifier":"P30429","identifierLink":"https://www.uniprot.org/uniprotkb/P30429/entry","name":"ced-4","description":"Cell death protein 4","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-494247","identifier":"P42573","identifierLink":"https://www.uniprot.org/uniprotkb/P42573/entry","name":"ced-3","description":"Cell death protein 3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10454","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1359","complexName":"ced-4-ced-9-mac-1 complex","organismName":"Caenorhabditis elegans; 6239","description":"Complex plays a role in programmed cell death (apoptosis) preventing ced-4-mediated apoptosis.","predictedComplex":false,"interactors":[{"ac":"EBI-2005767","identifier":"Q9NAG4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NAG4/entry","name":"mac-1","description":"Protein mac-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-494110","identifier":"P41958","identifierLink":"https://www.uniprot.org/uniprotkb/P41958/entry","name":"ced-9","description":"Apoptosis regulator ced-9","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11256","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-494118","identifier":"P30429","identifierLink":"https://www.uniprot.org/uniprotkb/P30429/entry","name":"ced-4","description":"Cell death protein 4","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]}]},{"complexAC":"CPX-1360","complexName":"ced-3-ced-4 caspase complex","organismName":"Caenorhabditis elegans; 6239","description":"Cysteine protease complex that plays a major role in programmed cell death (apoptosis). In healthy cells, ced-4 is sequestered and inhibited within the ced-9-ced-4 complex (CPX-399). In response to cell death signals, egl-1 binds to and directly inhibits the activity of ced-9, releasing the cell death activator ced-4 from the ced-9-ced-4 complex (CPX-399). The released ced-4 dimer oligomerizes to form the ced-4 apoptosome and interacts with the ced-3 zymogen to form the ced-3-ced-4 complex. ced-4 interaction with ced-3  induces both the autoproteolytic cleavage of the ced-3 zymogen and caspase activity of the mature ced-3 caspase.","predictedComplex":false,"interactors":[{"ac":"EBI-494118","identifier":"P30429","identifierLink":"https://www.uniprot.org/uniprotkb/P30429/entry","name":"ced-4","description":"Cell death protein 4","stochiometry":"minValue: 8, maxValue: 8","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-494247","identifier":"P42573","identifierLink":"https://www.uniprot.org/uniprotkb/P42573/entry","name":"ced-3","description":"Cell death protein 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10454","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1361","complexName":"PP2A-RSA-1 phosphatase complex","organismName":"Caenorhabditis elegans; 6239","description":"Serine/threonine phosphatase complex which, when present in the larger RSA centrosome-targeting complex (CPX-1357) is required for the regulation of microtubule outgrowth from centrosomes and also for mitotic spindle assembly by ensuring the stability of kinetochore microtubules.\r\n\r\nThe complex is localized to the centrosome. In particular, the regulatory subunit rsa-1 recruits the core holoenzyme to the centrosome.","predictedComplex":false,"interactors":[{"ac":"EBI-1187455","identifier":"O02217","identifierLink":"https://www.uniprot.org/uniprotkb/O02217/entry","name":"rsa-1","description":"Serine/threonine-protein phosphatase 2A regulatory subunit rsa-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12085","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-319655","identifier":"G5EGK8","identifierLink":"https://www.uniprot.org/uniprotkb/G5EGK8/entry","name":"let-92","description":"Serine/threonine-protein phosphatase 2A catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-322806","identifier":"Q09543","identifierLink":"https://www.uniprot.org/uniprotkb/Q09543/entry","name":"paa-1","description":"Probable serine/threonine-protein phosphatase PP2A regulatory subunit","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1362","complexName":"SLX4-RAD1-RAD10 endonuclease complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Endonuclease, which cuts branched DNA structures at the transition between dsDNA and ssDNA. Required for the repair of double-stranded breaks flanked by direct repeat sequences (boxes) which can occur by single-strand annealing), if a 5-prime to 3-prime resection is allowed to progress past the repeats. The complementary single-stranded repeats can anneal, leaving heterologous flaps to be removed by the RAD1–RAD10 endonuclease, before gap-filling and ligation completes the repair thereby deleting one of the repeats and the intervening sequence. SLX4 functions as a scaffold, following phosphorylation by MEC1 (P38111) or TEL1 (P38110), and may participate in proper positioning of RAD1-RAD10 or directing proper assembly/disassembly of one or more tail removal proteins, such as SAW1 (P39735), at 3-prime tailed intermediates.","predictedComplex":false,"interactors":[{"ac":"EBI-14637","identifier":"P06838","identifierLink":"https://www.uniprot.org/uniprotkb/P06838/entry","name":"RAD10","description":"DNA repair protein RAD10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-14752","identifier":"P06777","identifierLink":"https://www.uniprot.org/uniprotkb/P06777/entry","name":"RAD1","description":"DNA repair protein RAD1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10150","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-37788","identifier":"Q12098","identifierLink":"https://www.uniprot.org/uniprotkb/Q12098/entry","name":"SLX4","description":"Structure-specific endonuclease subunit SLX4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1363","complexName":"SAW1-RAD1-RAD10 endonuclease complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Endonuclease, which cuts branched DNA structures at the transition between dsDNA and ssDNA. Required for the repair of double-stranded breaks flanked by direct repeat sequences (boxes) which can occur by single-strand annealing, if a 5-prime to 3-prime resection is allowed to progress past the repeats. The complementary single-stranded repeats can anneal, leaving heterologous flaps to be removed by the RAD1-RAD10 endonuclease catalyzing the 3-prime-non-homologous tail removal of the single-strand annealing recombination intermediates, before gap-filling and ligation completes the repair thereby deleting one of the repeats and the intervening sequence. SAW1 contributes to 3-prime tail removal as a mediator between a 3-prime DNA flap substrate and RAD1-RAD10.","predictedComplex":false,"interactors":[{"ac":"EBI-14637","identifier":"P06838","identifierLink":"https://www.uniprot.org/uniprotkb/P06838/entry","name":"RAD10","description":"DNA repair protein RAD10","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-14752","identifier":"P06777","identifierLink":"https://www.uniprot.org/uniprotkb/P06777/entry","name":"RAD1","description":"DNA repair protein RAD1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10150","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20627","identifier":"P39735","identifierLink":"https://www.uniprot.org/uniprotkb/P39735/entry","name":"SAW1","description":"Single-strand annealing weakened protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1364","complexName":"SMC5-SMC6 SUMO ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SUMO ligase complex with a role in homologous recombination (HR) and replication. Required for chromosome segregation at repetitive sequences.  Localizes to repetitive elements such as the rDNA and telomeres  where is is thought to promote and resolve HR-dependent intermediates using ATP-hydrolysis to symmetrically reel DNA into loops. Also required for telomere maintenance during replication and telomere elongation and for SUMOylating components of the replisome, such as MCM2 (P29469) and the POL2 (P21951) subunit of the DNA polymerase epsilon complex (CPX-2110), which is important for replication fork progression in the presence of DNA-damaging agents.","predictedComplex":false,"interactors":[{"ac":"EBI-11017","identifier":"P38632","identifierLink":"https://www.uniprot.org/uniprotkb/P38632/entry","name":"MMS21","description":"E3 SUMO-protein ligase MMS21","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21330","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14410","identifier":"P43124","identifierLink":"https://www.uniprot.org/uniprotkb/P43124/entry","name":"NSE4","description":"Non-structural maintenance of chromosome element 4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR16140","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15099","identifier":"Q12749","identifierLink":"https://www.uniprot.org/uniprotkb/Q12749/entry","name":"SMC6","description":"Structural maintenance of chromosomes protein 6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19306","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22506","identifier":"P40026","identifierLink":"https://www.uniprot.org/uniprotkb/P40026/entry","name":"KRE29","description":"DNA repair protein KRE29","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-27756","identifier":"Q03718","identifierLink":"https://www.uniprot.org/uniprotkb/Q03718/entry","name":"NSE5","description":"Non-structural maintenance of chromosome element 5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-30144","identifier":"Q07913","identifierLink":"https://www.uniprot.org/uniprotkb/Q07913/entry","name":"NSE1","description":"Non-structural maintenance of chromosomes element 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR20973","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34125","identifier":"Q08204","identifierLink":"https://www.uniprot.org/uniprotkb/Q08204/entry","name":"SMC5","description":"Structural maintenance of chromosomes protein 5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45916","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-36625","identifier":"Q05541","identifierLink":"https://www.uniprot.org/uniprotkb/Q05541/entry","name":"NSE3","description":"Non-structural maintenance of chromosome element 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11736","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1366","complexName":"PP2A-SUR-6 phosphatase complex","organismName":"Caenorhabditis elegans; 6239","description":"Serine/threonine phosphatase complex that acts as a regulator of centriole formation during mitosis. Associates with the SAS-5-SAS-6 complex (CPX-1374) and targets it to centrioles. The dephosphorylation of sas-5 by let-92 is required for the targeting of the SAS-5-SAS-6 complex (CPX-1374) to centrioles. Furthermore, the complex positively regulates centriole duplication during early embryonic cell divisions by preventing the degradation of sas-5 and kinase zyg-1 (Q9GT24).\r\n\r\nDuring vulva development, may play a role in the induction of vulva cell precursors by positively regulating let-60/Ras-MAP kinase signaling, probably by promoting lin-45 (Q07292) activation.\r\n\r\nIn intestinal epithelial cells, may play a role in the late secretory pathway probably by regulating the exocyst, a protein complex involved in targeting secretory vesicles to the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2003301","identifier":"G5EDR3","identifierLink":"https://www.uniprot.org/uniprotkb/G5EDR3/entry","name":"sur-6","description":"Serine/threonine-protein phosphatase 2A regulatory subunit sur-6","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11871","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-319655","identifier":"G5EGK8","identifierLink":"https://www.uniprot.org/uniprotkb/G5EGK8/entry","name":"let-92","description":"Serine/threonine-protein phosphatase 2A catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-322806","identifier":"Q09543","identifierLink":"https://www.uniprot.org/uniprotkb/Q09543/entry","name":"paa-1","description":"Probable serine/threonine-protein phosphatase PP2A regulatory subunit","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1367","complexName":"PP2A-PPTR-1 phosphatase complex","organismName":"Caenorhabditis elegans; 6239","description":"Serine/threonine phosphatase complex that negatively regulates the insulin receptor signaling cascade composed of daf-2 (Q968Y9), age-1 (Q94125), akt-1 (Q17941), akt-2 (Q9XTG7) and sgk-1 (Q2PJ68) by promoting the dephosphorylation of akt-1 on 'Thr-350'. Negatively regulates several functions controlled by the insulin pathway including dauer formation, lifespan, fat storage and stress resistance. \r\n\r\nIn addition, the complex may play a role in the asymmetric segregation of the P granule components during embryonic cell divisions but does not play an essential role in specifying germ cell fate.","predictedComplex":false,"interactors":[{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2298122","identifier":"O18178","identifierLink":"https://www.uniprot.org/uniprotkb/O18178/entry","name":"pptr-1","description":"Serine/threonine-protein phosphatase 2A regulatory subunit pptr-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10257","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-319655","identifier":"G5EGK8","identifierLink":"https://www.uniprot.org/uniprotkb/G5EGK8/entry","name":"let-92","description":"Serine/threonine-protein phosphatase 2A catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-322806","identifier":"Q09543","identifierLink":"https://www.uniprot.org/uniprotkb/Q09543/entry","name":"paa-1","description":"Probable serine/threonine-protein phosphatase PP2A regulatory subunit","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1368","complexName":"PP2A-PPTR-2 phosphatase complex","organismName":"Caenorhabditis elegans; 6239","description":"Predicted serine/threonine phosphatase complex with phosphatase activity driven by let-92.","predictedComplex":false,"interactors":[{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2413245","identifier":"A9UJN4","identifierLink":"https://www.uniprot.org/uniprotkb/A9UJN4/entry","name":"pptr-2","description":"Serine/threonine protein phosphatase 2A regulatory subunit","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10257","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-319655","identifier":"G5EGK8","identifierLink":"https://www.uniprot.org/uniprotkb/G5EGK8/entry","name":"let-92","description":"Serine/threonine-protein phosphatase 2A catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-322806","identifier":"Q09543","identifierLink":"https://www.uniprot.org/uniprotkb/Q09543/entry","name":"paa-1","description":"Probable serine/threonine-protein phosphatase PP2A regulatory subunit","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1370","complexName":"SNO1-SNZ1 pyridoxal 5'-phosphate synthase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the hydrolysis of glutamine to glutamate and ammonia, thus supplying ammonia as a source of the ring nitrogen of pyridoxine as part of the biosynthesis of pyridoxal 5'-phosphate. SNZ1 may act as a synthetase that mediates the coupling of ammonia  with an unknown acceptor substrate, possibly via a tunnel in the synthetase subunit.","predictedComplex":false,"interactors":[{"ac":"EBI-17618","identifier":"Q03148","identifierLink":"https://www.uniprot.org/uniprotkb/Q03148/entry","name":"SNZ1","description":"Pyridoxal 5'-phosphate synthase subunit SNZ1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28190","identifier":"Q03144","identifierLink":"https://www.uniprot.org/uniprotkb/Q03144/entry","name":"SNO1","description":"Pyridoxal 5'-phosphate synthase subunit SNO1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31559","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1371","complexName":"SNO2-SNZ1 pyridoxal 5'-phosphate synthase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the hydrolysis of glutamine to glutamate and ammonia, thus supplying ammonia as a source of the ring nitrogen of pyridoxine as part of the biosynthesis of pyridoxal 5'-phosphate. SNZ1 may act as a synthetase that mediates the coupling of ammonia  with an unknown acceptor substrate, possibly via a tunnel in the synthetase subunit.","predictedComplex":false,"interactors":[{"ac":"EBI-17618","identifier":"Q03148","identifierLink":"https://www.uniprot.org/uniprotkb/Q03148/entry","name":"SNZ1","description":"Pyridoxal 5'-phosphate synthase subunit SNZ1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28424","identifier":"P53823","identifierLink":"https://www.uniprot.org/uniprotkb/P53823/entry","name":"SNO2","description":"Probable pyridoxal 5'-phosphate synthase subunit SNO2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31559","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1372","complexName":"SNT2C histone deacetylase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Histone deacetylase complex which may play a role in transcriptional regulation in response tooxidative stress.","predictedComplex":false,"interactors":[{"ac":"EBI-15864","identifier":"P32561","identifierLink":"https://www.uniprot.org/uniprotkb/P32561/entry","name":"RPD3","description":"Histone deacetylase RPD3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23958","identifier":"P53127","identifierLink":"https://www.uniprot.org/uniprotkb/P53127/entry","name":"SNT2","description":"E3 ubiquitin-protein ligase SNT2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47672","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27382","identifier":"Q03214","identifierLink":"https://www.uniprot.org/uniprotkb/Q03214/entry","name":"ECM5","description":"Protein ECM5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10694","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1373","complexName":"PP2A-F43B10.1 phosphatase complex","organismName":"Caenorhabditis elegans; 6239","description":"Predicted serine/threonine phosphatase complex with phosphatase activity driven by let-92.","predictedComplex":false,"interactors":[{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2315966","identifier":"Q17744","identifierLink":"https://www.uniprot.org/uniprotkb/Q17744/entry","name":"q17744","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-319655","identifier":"G5EGK8","identifierLink":"https://www.uniprot.org/uniprotkb/G5EGK8/entry","name":"let-92","description":"Serine/threonine-protein phosphatase 2A catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-322806","identifier":"Q09543","identifierLink":"https://www.uniprot.org/uniprotkb/Q09543/entry","name":"paa-1","description":"Probable serine/threonine-protein phosphatase PP2A regulatory subunit","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1374","complexName":"SAS-5-SAS-6 complex","organismName":"Caenorhabditis elegans; 6239","description":"Forms the initial central tube of the centriole, to which other proteins may be recruited during centriole formation, assembly and duplication in mitosis. \r\n\r\nThe complex interacts with and is targeted to centrioles by the PP2A-SUR-6 phosphatase complex (CPX-1366) during centriole formation. sas-5 is dephosphorylated by the serine/threonine phosphatase let-92 (G5EGK8) within the PP2A-SUR-6 complex\r\n\r\nDuring centriole duplication, the complex may also be recruited to centrioles by the kinase zyg-1.","predictedComplex":false,"interactors":[{"ac":"EBI-327247","identifier":"O62479","identifierLink":"https://www.uniprot.org/uniprotkb/O62479/entry","name":"sas-6","description":"Spindle assembly abnormal protein 6","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR44281","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-327608","identifier":"Q20010","identifierLink":"https://www.uniprot.org/uniprotkb/Q20010/entry","name":"sas-5","description":"Spindle assembly abnormal protein 5","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]}]},{"complexAC":"CPX-1375","complexName":"PP2A-F47B8.3 phosphatase complex","organismName":"Caenorhabditis elegans; 6239","description":"Predicted serine/threonine phosphatase complex with phosphatase activity driven by let-92.","predictedComplex":false,"interactors":[{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2413592","identifier":"Q20519","identifierLink":"https://www.uniprot.org/uniprotkb/Q20519/entry","name":"q20519","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10293","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-319655","identifier":"G5EGK8","identifierLink":"https://www.uniprot.org/uniprotkb/G5EGK8/entry","name":"let-92","description":"Serine/threonine-protein phosphatase 2A catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-322806","identifier":"Q09543","identifierLink":"https://www.uniprot.org/uniprotkb/Q09543/entry","name":"paa-1","description":"Probable serine/threonine-protein phosphatase PP2A regulatory subunit","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1376","complexName":"PP2A-T22D1.5 phosphatase complex","organismName":"Caenorhabditis elegans; 6239","description":"Predicted serine/threonine phosphatase complex with phosphatase activity driven by let-92.","predictedComplex":false,"interactors":[{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2003817","identifier":"Q9GZH6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9GZH6/entry","name":"q9gzh6","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR14095","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-319655","identifier":"G5EGK8","identifierLink":"https://www.uniprot.org/uniprotkb/G5EGK8/entry","name":"let-92","description":"Serine/threonine-protein phosphatase 2A catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-322806","identifier":"Q09543","identifierLink":"https://www.uniprot.org/uniprotkb/Q09543/entry","name":"paa-1","description":"Probable serine/threonine-protein phosphatase PP2A regulatory subunit","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1377","complexName":"SNX4-ATG20 sorting nexin complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required on a maturing endosome to sort and export distinct cargo proteins. The heterodimers oligomerize and coat the membrane, driving a transition in topology from a  flat membrane to a form the tubular endosomal network thus generating transport vesicles for trafficking of retromer cargoes. SNX4-ATG20 functions on the SNC1 (P31109) v-SNARE recycling pathway to transport SNC1 to the Golgi","predictedComplex":false,"interactors":[{"ac":"EBI-17610","identifier":"P47057","identifierLink":"https://www.uniprot.org/uniprotkb/P47057/entry","name":"SNX4","description":"Sorting nexin-4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45949","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-36894","identifier":"Q07528","identifierLink":"https://www.uniprot.org/uniprotkb/Q07528/entry","name":"ATG20","description":"Autophagy-related protein 20","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46979","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1378","complexName":"SNX4-SNX41 sorting nexin complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required on a maturing endosome to sort and export distinct cargo proteins. The heterodimers oligomerize and coat the membrane, driving a transition in topology from a  flat membrane to a form the tubular endosomal network thus generating transport vesicles for trafficking of retromer cargoes . SNX4-SNX41 mediates retrograde sorting of ATG27(P46989), an integral membrane protein implicated in selective autophagy.","predictedComplex":false,"interactors":[{"ac":"EBI-17610","identifier":"P47057","identifierLink":"https://www.uniprot.org/uniprotkb/P47057/entry","name":"SNX4","description":"Sorting nexin-4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45949","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30464","identifier":"Q04053","identifierLink":"https://www.uniprot.org/uniprotkb/Q04053/entry","name":"SNX41","description":"Sorting nexin-41","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46979","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1379","complexName":"Mitochondrial succinyl-CoA synthetase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the nucleotide-dependent conversion of succinyl-CoA to succinate and ATP. This enzyme functions in the tricarboxylic acid (TCA) cycle","predictedComplex":false,"interactors":[{"ac":"EBI-18506","identifier":"P53598","identifierLink":"https://www.uniprot.org/uniprotkb/P53598/entry","name":"LSC1","description":"Succinate--CoA ligase [ADP-forming] subunit alpha, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18513","identifier":"P53312","identifierLink":"https://www.uniprot.org/uniprotkb/P53312/entry","name":"LSC2","description":"Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11815","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1380","complexName":"TAP42-RRD2-PPH21 phosphatase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A serine/threonine protein phosphatase complex that plays a major role in TOR1/2 (P35169/P32600)-mediated signaling and gene expression. Rapamycin causes release of the phosphatase-RRD dimer from TAP42.","predictedComplex":false,"interactors":[{"ac":"EBI-12745","identifier":"P23594","identifierLink":"https://www.uniprot.org/uniprotkb/P23594/entry","name":"PPH21","description":"Serine/threonine-protein phosphatase PP2A-1 catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-18926","identifier":"Q04372","identifierLink":"https://www.uniprot.org/uniprotkb/Q04372/entry","name":"TAP42","description":"Type 2A phosphatase-associated protein 42","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10933","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32784","identifier":"Q12461","identifierLink":"https://www.uniprot.org/uniprotkb/Q12461/entry","name":"RRD2","description":"Serine/threonine-protein phosphatase 2A activator 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10012","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1381","complexName":"NVJ1-VAC8 nucleus-vacuole junction complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Nucleus-vacuole junction complex, a membrane contact site formed between perinuclear and vacuolar membranes. Mediates essential cellular processes such as piecemeal microautophagy of the nucleus (PMN), a selective autophagic recycling process stimulated by carbon or nitrogen starvation through the target of rapamycin signaling pathway. Under these conditions, the region of the nucleus in the vicinity of NVJs invaginates into the vacuolar lumen and forms a bleb-like structure, which is released as a vesicle and eventually degraded by vacuolar hydrolases. NVJs are also involved in lipid metabolism by recruiting the two lipid-modifying enzymes, oxystereol-binding proteins homology OSH1 (P35845) involved in nonvesicular lipid trafficking and the enoyl-CoA reductase TSC13 (Q99190) that mediates the synthesis of very-long-chain fatty acids.","predictedComplex":false,"interactors":[{"ac":"EBI-20212","identifier":"P39968","identifierLink":"https://www.uniprot.org/uniprotkb/P39968/entry","name":"VAC8","description":"Vacuolar protein 8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47249","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-24885","identifier":"P38881","identifierLink":"https://www.uniprot.org/uniprotkb/P38881/entry","name":"NVJ1","description":"Nucleus-vacuole junction protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1382","complexName":"TAP42-RRD2-PPH22 phosphatase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A serine/threonine protein phosphatase complex that plays a major role in TOR1/2 (P35169/P32600)-mediated signaling and gene expression. Rapamycin causes release of the phosphatase-RRD dimer from TAP42.","predictedComplex":false,"interactors":[{"ac":"EBI-12752","identifier":"P23595","identifierLink":"https://www.uniprot.org/uniprotkb/P23595/entry","name":"PPH22","description":"Serine/threonine-protein phosphatase PP2A-2 catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-18926","identifier":"Q04372","identifierLink":"https://www.uniprot.org/uniprotkb/Q04372/entry","name":"TAP42","description":"Type 2A phosphatase-associated protein 42","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10933","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32784","identifier":"Q12461","identifierLink":"https://www.uniprot.org/uniprotkb/Q12461/entry","name":"RRD2","description":"Serine/threonine-protein phosphatase 2A activator 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10012","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1383","complexName":"TRAPPIII protein complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Tethering complexes which provide the initial recognition event that links a particular vesicle with its target membrane. It is an Autophagy-specific guanine nucleotide exchange factor for the Rab GTPase YPT1 (P01123) that is recruited to the phagophore assembly site (PAS) when macroautophagy is induced by the ATG1 kinase complex (CPX-1676). The TRAPPIII-specific subunit, TRS85, targets this complex to the PAS. BET3, BET5, TRS23, and TRS31 create a catalytic site for promoting GDP/GTP exchange in YPT1.","predictedComplex":false,"interactors":[{"ac":"EBI-19468","identifier":"P38334","identifierLink":"https://www.uniprot.org/uniprotkb/P38334/entry","name":"TRS20","description":"Trafficking protein particle complex subunit 20","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12403","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19474","identifier":"Q03784","identifierLink":"https://www.uniprot.org/uniprotkb/Q03784/entry","name":"TRS23","description":"Trafficking protein particle complex subunit 23","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23249","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19480","identifier":"Q99394","identifierLink":"https://www.uniprot.org/uniprotkb/Q99394/entry","name":"TRS33","description":"Trafficking protein particle complex subunit 33","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12817","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19492","identifier":"P46944","identifierLink":"https://www.uniprot.org/uniprotkb/P46944/entry","name":"TRS85","description":"Trafficking protein particle complex III-specific subunit 85","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-3567","identifier":"P36149","identifierLink":"https://www.uniprot.org/uniprotkb/P36149/entry","name":"BET3","description":"Trafficking protein particle complex subunit BET3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3580","identifier":"Q03630","identifierLink":"https://www.uniprot.org/uniprotkb/Q03630/entry","name":"BET5","description":"Trafficking protein particle complex subunit BET5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23249","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-38770","identifier":"Q03337","identifierLink":"https://www.uniprot.org/uniprotkb/Q03337/entry","name":"TRS31","description":"Trafficking protein particle complex subunit 31","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR20902","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1384","complexName":"SUM1-RFM1-HST1 histone deacetylase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Histone deacetylase complex which represses the expression of middle sporulation genes during vegetative growth. The histone H3 specific methyltransferase SET1 (P38827) promotes association of the locus-specific SUM1-RFM1-HST1 repressor complex with the middle sporulation element in the promoter region of a subset of genes. Once bound, the complex maintains histone H4 lys-5 in a deacetylated state. The complex is also required for full initiation capacity of ORC-mediated replication initiation at consensus sequence within origins of replication in the genome.","predictedComplex":false,"interactors":[{"ac":"EBI-15023","identifier":"Q12192","identifierLink":"https://www.uniprot.org/uniprotkb/Q12192/entry","name":"RFM1","description":"Repression factor of MSEs protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-18547","identifier":"P46676","identifierLink":"https://www.uniprot.org/uniprotkb/P46676/entry","name":"SUM1","description":"Suppressor of mar1-1 protein","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-8691","identifier":"P53685","identifierLink":"https://www.uniprot.org/uniprotkb/P53685/entry","name":"HST1","description":"NAD-dependent protein deacetylase HST1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11085","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1385","complexName":"unc-83-unc-84 LINC complex","organismName":"Caenorhabditis elegans; 6239","description":"Complex involved in nuclear migration throughout development, recruiting dynein and kinesin-1 to the nuclear surface.  The complex connects the nuclear envelope to the microtubule cytoskeleton to allow for nuclear transport along microtubules. unc-83 associates with and recruits the large microtubule-associated bicd-1-dlc-1-egal-1  (CPX-1388) and lis-1-nud-2 complexes (CPX-1389) and the Kinesin I motor complex (CPX-1390) to the nuclear envelope to regulate both the bidirectional migration of nuclei and the extent of nuclear migrations.","predictedComplex":false,"interactors":[{"ac":"EBI-2902228","identifier":"Q23064","identifierLink":"https://www.uniprot.org/uniprotkb/Q23064/entry","name":"unc-83","description":"Nuclear migration protein unc-83","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-313630","identifier":"Q20745","identifierLink":"https://www.uniprot.org/uniprotkb/Q20745/entry","name":"unc-84","description":"Nuclear migration and anchoring protein unc-84","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12911","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1386","complexName":"Synapsis initiation complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Forms at axial association sites, where the chromosomes are in close contact, and is required for polymerization of ZIP1 (P31111) along the lengths of chromosomes during synapsis, the pairing of two homologous chromosomes that occurs during meiosis.  ZIP1 polymerization into oligomeric arrays of transverse filaments leads to the formation of the synaptonemal complex, a proteinaceous connection between homologous chromosomes which forms during meiotic prophase. The accumulation of the  ZIP1 appears to require the SUMO E3 ligase activity  of CST9. The complex may also promote MSH4-MSH5 complex (CPX-1704)-mediated crossovers, the exchange of genetic material between homologous chromosomes during meiosis.","predictedComplex":false,"interactors":[{"ac":"EBI-2091833","identifier":"P40511","identifierLink":"https://www.uniprot.org/uniprotkb/P40511/entry","name":"SPO22","description":"Sporulation-specific protein 22","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR40375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-24222","identifier":"P53061","identifierLink":"https://www.uniprot.org/uniprotkb/P53061/entry","name":"ZIP2","description":"Protein ZIP2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-30044","identifier":"Q06032","identifierLink":"https://www.uniprot.org/uniprotkb/Q06032/entry","name":"CST9","description":"Chromosome stability protein 9","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22663","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3826035","identifier":"P17122","identifierLink":"https://www.uniprot.org/uniprotkb/P17122/entry","name":"SPO16","description":"Sporulation-specific protein 16","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1387","complexName":"Synaptonemal complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Liquid crystalline structure that forms a large scaffold connecting homologous chromosomes from end to end during meiotic prophase I. . Required for stabilising chromosome pairing and alignment, and for crossover events and chiasmata formation between homologous chromosome pairs. Mediates the lengthwise alignment of homologous chromsomes within 100 nm of each other with thread-like axial or lateral elements are paired together by transverse filaments formed by oligomerized ZIP1 proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-14909","identifier":"P14291","identifierLink":"https://www.uniprot.org/uniprotkb/P14291/entry","name":"RED1","description":"Protein RED1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-29645","identifier":"P31111","identifierLink":"https://www.uniprot.org/uniprotkb/P31111/entry","name":"ZIP1","description":"Synaptonemal complex protein ZIP1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-37150","identifier":"Q04110","identifierLink":"https://www.uniprot.org/uniprotkb/Q04110/entry","name":"ECM11","description":"Protein ECM11","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-3768303","identifier":"P20050","identifierLink":"https://www.uniprot.org/uniprotkb/P20050/entry","name":"HOP1","description":"Meiosis-specific protein HOP1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR48225","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3786338","identifier":"Q06201","identifierLink":"https://www.uniprot.org/uniprotkb/Q06201/entry","name":"GMC2","description":"Grand meiotic recombination cluster protein 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1388","complexName":"bicd-1-dlc-1-egal-1 microtubule-associated dynein motor complex","organismName":"Caenorhabditis elegans; 6239","description":"Motor complex that trafficks organelles, proteins and RNA towards the minus ends of microtubules. In particular, the complex plays a role in cellular processes including cell division, mitosis, meiosis, cell proliferation. \r\n\r\nIts role in organelle trafficking is through interactions with the nuclear migration protein unc-83. bicd-1 and dlc-1 interact with unc-83 within the unc-83-unc-84 complex (CPX-1385) and this recruits the motor complex to nuclear envelope where it is involved in the regulation of nuclear migrations in hypodermal precursor cells. \r\n\r\nIn addition, during cell division, the complex is involved in the pairing of homologous chromosomes, and also maintains germline development and homeostasis by inhibiting germ cell proliferation.\r\n\r\nThe complex is a component of a larger assembly that associates with microtubules through dynein.","predictedComplex":false,"interactors":[{"ac":"EBI-2006416","identifier":"V6CJ04","identifierLink":"https://www.uniprot.org/uniprotkb/V6CJ04/entry","name":"bicd-1","description":"Protein bicaudal D homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR31233","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-328324","identifier":"Q22799","identifierLink":"https://www.uniprot.org/uniprotkb/Q22799/entry","name":"dlc-1","description":"Dynein light chain 1, cytoplasmic","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-328330","identifier":"Q17902","identifierLink":"https://www.uniprot.org/uniprotkb/Q17902/entry","name":"egal-1","description":"Egalitarian protein homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR46628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1389","complexName":"lis-1-nud-2 microtubule-associated dynein motor complex","organismName":"Caenorhabditis elegans; 6239","description":"Motor complex that trafficks organelles, proteins and RNA towards the minus ends of microtubules. In particular, the complex plays a role in cellular processes including cell division, mitosis, meiosis, cell proliferation.  \r\n\r\nThe complex is recruited to the nuclear envelope to regulate nuclear migrations in hypodermal precursor cells. Its role in nuclear trafficking is through interactions with the nuclear migration protein unc-83. nud-2 interacts with unc-83 within the unc-83-unc-84 complex (CPX-1385) and this recruits the motor complex to nuclear envelope where it is involved in the regulation of nuclear migrations in hypodermal precursor cells. \r\n\r\nThe complex is a component of a larger assembly that associates with microtubules through dynein.","predictedComplex":false,"interactors":[{"ac":"EBI-2004982","identifier":"Q9NDC9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NDC9/entry","name":"lis-1","description":"Lissencephaly-1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR44129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-326083","identifier":"O45717","identifierLink":"https://www.uniprot.org/uniprotkb/O45717/entry","name":"nud-2","description":"Protein nud-2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10921","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1390","complexName":"Kinesin I motor complex, klc-2 variant","organismName":"Caenorhabditis elegans; 6239","description":"Motor complex that is involved in the trafficking of organelles and cellular components along microtubules. \r\n\r\nThe complex is recruited to the nuclear envelope to regulate nuclear migrations in hypodermal precursor cells. Its role in nuclear trafficking is through interactions with the nuclear migration protein unc-83. klc-2 interacts with unc-83 within the unc-83-unc-84 LINC complex (CPX-1385) and this recruits the motor complex to nuclear envelope where it is involved in the regulation of nuclear migrations in hypodermal precursor cells.\r\n\r\nThe complex plays a role in the localization and transport of components of synaptic vesicles through interactions with the cargo adaptor protein unc-16.\r\n\r\nThe complex is a component of a larger assembly that associates with microtubules through kinesin.","predictedComplex":false,"interactors":[{"ac":"EBI-315578","identifier":"P46822","identifierLink":"https://www.uniprot.org/uniprotkb/P46822/entry","name":"klc-2","description":"Kinesin light chain","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45783","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-315657","identifier":"P34540","identifierLink":"https://www.uniprot.org/uniprotkb/P34540/entry","name":"unc-116","description":"Kinesin heavy chain","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1391","complexName":"LSM1-7-PAT1 complex, variant LSM1A-LSM3A-LSM6A-PAT1H1","organismName":"Arabidopsis thaliana; 3702","description":"A cytoplasmic complex essential for P-body formation and deadenylation-dependent decapping of mRNA thereby regulating mRNA decay and subsequent degradation by the 5-to-3-prime pathway. Loss of LMS1 subunits leads to a range of severe developmental abnormalities.","predictedComplex":false,"interactors":[{"ac":"EBI-16419347","identifier":"Q945P8","identifierLink":"https://www.uniprot.org/uniprotkb/Q945P8/entry","name":"LSM1A","description":"Sm-like protein LSM1A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR15588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16419382","identifier":"Q9FKB0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9FKB0/entry","name":"LSM5","description":"Sm-like protein LSM5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR20971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16419411","identifier":"F4K4E3","identifierLink":"https://www.uniprot.org/uniprotkb/F4K4E3/entry","name":"LSM4","description":"Sm-like protein LSM4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16589519","identifier":"F4J077","identifierLink":"https://www.uniprot.org/uniprotkb/F4J077/entry","name":"PAT1H1","description":"Protein PAT1 homolog 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR21551","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4431531","identifier":"Q9M1Z3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9M1Z3/entry","name":"LSM6A","description":"Sm-like protein LSM6A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4433669","identifier":"Q9SI54","identifierLink":"https://www.uniprot.org/uniprotkb/Q9SI54/entry","name":"LSM7","description":"Sm-like protein LSM7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9347247","identifier":"Q9LMN4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9LMN4/entry","name":"LSM3A","description":"Sm-like protein LSM3A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR13110","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9347308","identifier":"Q1H595","identifierLink":"https://www.uniprot.org/uniprotkb/Q1H595/entry","name":"LSM2","description":"Sm-like protein LSM2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR13829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1392","complexName":"LSM1-7-PAT1 complex, variant LSM1A-LSM3A-LSM6B-PAT1H1","organismName":"Arabidopsis thaliana; 3702","description":"A cytoplasmic complex essential for P-body formation and deadenylation-dependent decapping of mRNA thereby regulating mRNA decay and subsequent degradation by the 5-to-3-prime pathway. Loss of LMS1 subunits leads to a range of severe developmental abnormalities.","predictedComplex":false,"interactors":[{"ac":"EBI-16419347","identifier":"Q945P8","identifierLink":"https://www.uniprot.org/uniprotkb/Q945P8/entry","name":"LSM1A","description":"Sm-like protein LSM1A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR15588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16419382","identifier":"Q9FKB0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9FKB0/entry","name":"LSM5","description":"Sm-like protein LSM5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR20971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16419411","identifier":"F4K4E3","identifierLink":"https://www.uniprot.org/uniprotkb/F4K4E3/entry","name":"LSM4","description":"Sm-like protein LSM4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16589519","identifier":"F4J077","identifierLink":"https://www.uniprot.org/uniprotkb/F4J077/entry","name":"PAT1H1","description":"Protein PAT1 homolog 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR21551","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4433669","identifier":"Q9SI54","identifierLink":"https://www.uniprot.org/uniprotkb/Q9SI54/entry","name":"LSM7","description":"Sm-like protein LSM7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9347247","identifier":"Q9LMN4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9LMN4/entry","name":"LSM3A","description":"Sm-like protein LSM3A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR13110","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9347287","identifier":"O22823","identifierLink":"https://www.uniprot.org/uniprotkb/O22823/entry","name":"LSM6B","description":"Sm-like protein LSM36B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9347308","identifier":"Q1H595","identifierLink":"https://www.uniprot.org/uniprotkb/Q1H595/entry","name":"LSM2","description":"Sm-like protein LSM2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR13829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1393","complexName":"LSM1-7-PAT1 complex, variant LSM1A-LSM3B-LSM6A-PAT1H1","organismName":"Arabidopsis thaliana; 3702","description":"A cytoplasmic complex essential for P-body formation and deadenylation-dependent decapping of mRNA thereby regulating mRNA decay and subsequent degradation by the 5-to-3-prime pathway. 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Loss of LMS1 subunits leads to a range of severe developmental abnormalities.","predictedComplex":false,"interactors":[{"ac":"EBI-16419382","identifier":"Q9FKB0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9FKB0/entry","name":"LSM5","description":"Sm-like protein LSM5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR20971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16419411","identifier":"F4K4E3","identifierLink":"https://www.uniprot.org/uniprotkb/F4K4E3/entry","name":"LSM4","description":"Sm-like protein LSM4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16589984","identifier":"Q94C98","identifierLink":"https://www.uniprot.org/uniprotkb/Q94C98/entry","name":"PAT1H2","description":"Protein PAT1 homolog 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR21551","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4431531","identifier":"Q9M1Z3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9M1Z3/entry","name":"LSM6A","description":"Sm-like protein LSM6A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4433669","identifier":"Q9SI54","identifierLink":"https://www.uniprot.org/uniprotkb/Q9SI54/entry","name":"LSM7","description":"Sm-like protein LSM7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4434198","identifier":"Q8LFL8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8LFL8/entry","name":"LSM1B","description":"Sm-like protein LSM1B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR15588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9347299","identifier":"Q9C6K5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9C6K5/entry","name":"LSM3B","description":"Sm-like protein LSM3B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR13110","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9347308","identifier":"Q1H595","identifierLink":"https://www.uniprot.org/uniprotkb/Q1H595/entry","name":"LSM2","description":"Sm-like protein LSM2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR13829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1406","complexName":"LSM1-7-PAT1 complex, variant LSM1B-LSM3B-LSM6B-PAT1H2","organismName":"Arabidopsis thaliana; 3702","description":"A cytoplasmic complex essential for P-body formation and deadenylation-dependent decapping of mRNA thereby regulating mRNA decay and subsequent degradation by the 5-to-3-prime pathway. Loss of LMS1 subunits leads to a range of severe developmental abnormalities.","predictedComplex":false,"interactors":[{"ac":"EBI-16419382","identifier":"Q9FKB0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9FKB0/entry","name":"LSM5","description":"Sm-like protein LSM5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR20971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16419411","identifier":"F4K4E3","identifierLink":"https://www.uniprot.org/uniprotkb/F4K4E3/entry","name":"LSM4","description":"Sm-like protein LSM4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16589984","identifier":"Q94C98","identifierLink":"https://www.uniprot.org/uniprotkb/Q94C98/entry","name":"PAT1H2","description":"Protein PAT1 homolog 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR21551","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4433669","identifier":"Q9SI54","identifierLink":"https://www.uniprot.org/uniprotkb/Q9SI54/entry","name":"LSM7","description":"Sm-like protein LSM7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4434198","identifier":"Q8LFL8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8LFL8/entry","name":"LSM1B","description":"Sm-like protein LSM1B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR15588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9347287","identifier":"O22823","identifierLink":"https://www.uniprot.org/uniprotkb/O22823/entry","name":"LSM6B","description":"Sm-like protein LSM36B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9347299","identifier":"Q9C6K5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9C6K5/entry","name":"LSM3B","description":"Sm-like protein LSM3B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR13110","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9347308","identifier":"Q1H595","identifierLink":"https://www.uniprot.org/uniprotkb/Q1H595/entry","name":"LSM2","description":"Sm-like protein LSM2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR13829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1407","complexName":"ECM11-GMC2 synaptonemal assembly activation factor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Facilitates the assembly of the transverse filament of the synaptonemal complex (CPX-1387) by promoting the oligomerisation of ZIP1 (P31111). Recruited to the site of synapsis initiation complex (CPX-1386) binding where it may act to stabilise the nascent ZIP1 oligomer. ECM11 SUMOylation promotes ZIP1 assembly whilst ZIP1 promotes ECM11 SUMOylation in a positive feedback loop leading to further assembly of ZIP1, loading of ECM11-GMC2 and SUMOylation of ECM11 until the Synaptonemal complex is fully established.","predictedComplex":false,"interactors":[{"ac":"EBI-37150","identifier":"Q04110","identifierLink":"https://www.uniprot.org/uniprotkb/Q04110/entry","name":"ECM11","description":"Protein ECM11","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-3786338","identifier":"Q06201","identifierLink":"https://www.uniprot.org/uniprotkb/Q06201/entry","name":"GMC2","description":"Grand meiotic recombination cluster protein 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1408","complexName":"Nuclear meiotic cohesin complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for sister chromatid cohesion during meiotic cell division, which enables cells to attach sister kinetochores  to microtubules with opposing polarity (bi-orientation) and subsequently resists the tendency of these microtubules to pull chromatids toward opposite spindle poles. Before the commencement of replication, the cohesin complex is loaded onto DNA. The arms of the SMC1/3 molecules embrace the DNA, thereby forming a ring of approx. 40 nm diameter. The head domains of SMC1 and SMC3 are locked together by REC8. Cohesion might be generated as the replication fork passes through the ring, entrapping both sister chromatids inside. At the metaphase to anaphase transition, REC8 is cleaved by separase, thereby opening the lock of the SMC1/3 head domains. The ring opens and sister chromatids can be pulled to opposite spindle poles. REC8 is required to efficiently recruit meiotic axis proteins such as RED1 and evenly distribute these along the meiotic chromosomes.","predictedComplex":false,"interactors":[{"ac":"EBI-16667","identifier":"P40541","identifierLink":"https://www.uniprot.org/uniprotkb/P40541/entry","name":"IRR1","description":"Cohesin subunit SCC3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11199","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17402","identifier":"P32908","identifierLink":"https://www.uniprot.org/uniprotkb/P32908/entry","name":"SMC1","description":"Structural maintenance of chromosomes protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR18937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17423","identifier":"P47037","identifierLink":"https://www.uniprot.org/uniprotkb/P47037/entry","name":"SMC3","description":"Structural maintenance of chromosomes protein 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43977","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2082885","identifier":"Q12188","identifierLink":"https://www.uniprot.org/uniprotkb/Q12188/entry","name":"REC8","description":"Meiotic recombination protein REC8","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12585","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1409","complexName":"UTP-A complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for early co-transcriptional events in ribosome biogenesis, acting as an RNA chaperone to initiate ribosome assembly. At the earliest stages of transcription, three subunits of UTPA (UTP8, UTP9 and UTP17) bind to nascent pre-rRNA at the very 5′ end  while the remaining four subunits (UTP10, UTP4, UTP5 and UTP15) interact with nucleotides further downstream in the 5'-external transcribed spacer (ETS). May also act to stimulate U3 snoRNP recruitment. A sub-unit of the small subunit (SSU) processome, a 2.2 MDa ribonucleoprotein complex involved in the processing, assembly and maturation of nascent pre-ribosomal RNA to form the small ribosomal subunit. The SSU processome is a giant particle composed of numerous ribosome assembly factors, including the UTP-A, UTP-B (CPX-1410), UTP-C (CPX-772/CPX-771/CPX-773) and MPP10 (CPX-1893) complexes, the U3 small nucleolar ribonucleoprotein (snoRNP) and many individual proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-1884","identifier":"P42945","identifierLink":"https://www.uniprot.org/uniprotkb/P42945/entry","name":"UTP10","description":"U3 small nucleolar RNA-associated protein 10","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13457","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23301","identifier":"P53276","identifierLink":"https://www.uniprot.org/uniprotkb/P53276/entry","name":"UTP8","description":"U3 small nucleolar RNA-associated protein 8","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-24892","identifier":"P38882","identifierLink":"https://www.uniprot.org/uniprotkb/P38882/entry","name":"UTP9","description":"U3 small nucleolar RNA-associated protein 9","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-28183","identifier":"Q04305","identifierLink":"https://www.uniprot.org/uniprotkb/Q04305/entry","name":"UTP15","description":"U3 small nucleolar RNA-associated protein 15","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19924","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-35712","identifier":"Q06679","identifierLink":"https://www.uniprot.org/uniprotkb/Q06679/entry","name":"UTP4","description":"U3 small nucleolar RNA-associated protein 4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR44163","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-35844","identifier":"Q04177","identifierLink":"https://www.uniprot.org/uniprotkb/Q04177/entry","name":"UTP5","description":"U3 small nucleolar RNA-associated protein 5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR44267","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-37773","identifier":"Q02931","identifierLink":"https://www.uniprot.org/uniprotkb/Q02931/entry","name":"NAN1","description":"NET1-associated nuclear protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR44215","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1410","complexName":"UTP-B complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for early co-transcriptional events in ribosome biogenesis, acting as an RNA chaperone to initiate ribosome assembly. May facilitate specific U3 snoRNA- 5'-external transcribed spacer (ETS) base-pairing with PWP2 bridging the interaction site. A sub-unit of the small subunit (SSU) processome, a 2.2 MDa ribonucleoprotein complex involved in the processing, assembly and maturation of nascent pre-ribosomal RNA to form the small ribosomal subunit. The SSU processome is a giant particle composed of numerous ribosome assembly factors, including the UTP-A (CPX-1409), UTP-B, UTP-C (CPX-772/CPX-771/CPX-773) and MPP10 (CPX-1893) complexes, the U3 small nucleolar ribonucleoprotein (snoRNP) and many individual proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-14332","identifier":"P25635","identifierLink":"https://www.uniprot.org/uniprotkb/P25635/entry","name":"PWP2","description":"Periodic tryptophan protein 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19858","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22119","identifier":"Q02354","identifierLink":"https://www.uniprot.org/uniprotkb/Q02354/entry","name":"UTP6","description":"U3 small nucleolar RNA-associated protein 6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23271","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34702","identifier":"Q05946","identifierLink":"https://www.uniprot.org/uniprotkb/Q05946/entry","name":"UTP13","description":"U3 small nucleolar RNA-associated protein 13","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19854","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359","identifier":"Q06078","identifierLink":"https://www.uniprot.org/uniprotkb/Q06078/entry","name":"UTP21","description":"U3 small nucleolar RNA-associated protein 21","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22840","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4534","identifier":"P40362","identifierLink":"https://www.uniprot.org/uniprotkb/P40362/entry","name":"UTP18","description":"U3 small nucleolar RNA-associated protein 18","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR18359","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5896","identifier":"Q12220","identifierLink":"https://www.uniprot.org/uniprotkb/Q12220/entry","name":"DIP2","description":"U3 small nucleolar RNA-associated protein 12","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19853","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1411","complexName":"Separase-Securin complex","organismName":"Caenorhabditis elegans; 6239","description":"Regulates the metaphase-to-anaphase transition during cell cycle progression, playing a role in control of the metaphase-anaphase transition and anaphase onset. Complex formation both activates and inhibits the protease activity of separase/sep-1 which is responsible for cleaving the scc-1 (Q19325) subunit of the cohesin ring that holds sister chromatids together during mitosis.  Securin/ify-1 appears to ensure that separase adopts its proper fold required for proteolytic activity and also promotes subcellular localization of separase to the nucleus. Securin is degraded via ubiquitylation by the anaphase-promoting complex enabling separase to become fully active.","predictedComplex":false,"interactors":[{"ac":"EBI-326265","identifier":"G5ED39","identifierLink":"https://www.uniprot.org/uniprotkb/G5ED39/entry","name":"sep-1","description":"Separin homolog sep-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12792","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-331643","identifier":"Q18235","identifierLink":"https://www.uniprot.org/uniprotkb/Q18235/entry","name":"ify-1","description":"Securin-like protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]}]},{"complexAC":"CPX-1412","complexName":"UBP3-BRE5 ubiquitin hydrolase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Specifically deubiquitylates and consequently controls the expression level of the SEC23 (P15303) and SEC27 (P41811) subunits of the COPII (CPX-2523) and COPI complexes that regulate anterograde and retrograde transport between the endoplasmic reticulum and the Golgi apparatus respectively. Also required for the assmbly of  nonmembranous ribonucleoprotein stress granules. Inhibits mitophagy but  promotes other types of autophagy, including ribophagy. The complex translocates dynamically from the cytosol to the mitochondria upon induction of mitophagy.","predictedComplex":false,"interactors":[{"ac":"EBI-19834","identifier":"Q01477","identifierLink":"https://www.uniprot.org/uniprotkb/Q01477/entry","name":"UBP3","description":"Ubiquitin carboxyl-terminal hydrolase 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24006","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28528","identifier":"P53741","identifierLink":"https://www.uniprot.org/uniprotkb/P53741/entry","name":"BRE5","description":"UBP3-associated protein BRE5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10693","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1413","complexName":"VPS55-VPS68 sorting complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Appears to act with or downstream of the ESCRT (Endosomal sorting complex required for transport) machinery to regulate trafficking at endosome and may also mediate a step in the endosomal maturation process.","predictedComplex":false,"interactors":[{"ac":"EBI-25497","identifier":"P47111","identifierLink":"https://www.uniprot.org/uniprotkb/P47111/entry","name":"VPS55","description":"Vacuolar protein sorting-associated protein 55","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29309","identifier":"Q12016","identifierLink":"https://www.uniprot.org/uniprotkb/Q12016/entry","name":"VPS68","description":"Vacuolar protein sorting-associated protein 68","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13180","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1414","complexName":"UBA3-ULA1 E1 enzyme","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"E1 enzyme complex that activates the Ubiquitin-like protein modifier RUB1 (Q03919) by adenylating its C-terminal glycine residue using ATP, then linking this residue to the side chain of the catalytic cysteine of UBA3 (Cys-168), yielding NEDD8-UBA3. This is conjugated by the E2 UBC12 (P52491) to a single site in the carboxyl termini of cullins, a family of hydrophobic proteins providing a scaffold for E3 ubiquitin ligases, thus modulating the E3 enzymatic activity.","predictedComplex":false,"interactors":[{"ac":"EBI-32882","identifier":"Q12059","identifierLink":"https://www.uniprot.org/uniprotkb/Q12059/entry","name":"ULA1","description":"NEDD8-activating enzyme E1 regulatory subunit","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-37997","identifier":"Q99344","identifierLink":"https://www.uniprot.org/uniprotkb/Q99344/entry","name":"UBA3","description":"NEDD8-activating enzyme E1 catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1415","complexName":"IME1-UME6 transcription activation complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Transcriptional activator that acts at promoters of early meiosis-specific genes and recruits the histone acetyl transferase Gcn5 to initiate transcription. Formation of the complex under meiotic induction conditions converts the URS1 element-binding protein, UME6, from a  repressor to an activator resulting in the formation of asci. Phosphorylation of IME1 by RIM11 (P38615) is required for complex formation.","predictedComplex":false,"interactors":[{"ac":"EBI-20086","identifier":"P39001","identifierLink":"https://www.uniprot.org/uniprotkb/P39001/entry","name":"UME6","description":"Transcriptional regulatory protein UME6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR37534","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9199","identifier":"P21190","identifierLink":"https://www.uniprot.org/uniprotkb/P21190/entry","name":"IME1","description":"Meiosis-inducing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1416","complexName":"Kinesin I motor complex, klc-1 variant","organismName":"Caenorhabditis elegans; 6239","description":"Probable motor complex that is involved in the trafficking of organelles and cellular components along microtubules. \r\n\r\nThe complex is recruited to the nuclear envelope to regulate nuclear migrations in hypodermal precursor cells. Its role in nuclear trafficking is through interactions with the nuclear migration protein unc-83. klc-1 interacts with unc-83 within the unc-83-unc-84 LINC complex (CPX-1385) and this recruits the motor complex to nuclear envelope where it is involved in the regulation of nuclear migrations in hypodermal precursor cells.\r\n\r\nThe complex plays a role in the localization and transport of components of synaptic vesicles through interactions with the cargo adaptor protein unc-16.\r\n\r\nThe complex is a component of a larger assembly that associates with microtubules through kinesin.","predictedComplex":false,"interactors":[{"ac":"EBI-315657","identifier":"P34540","identifierLink":"https://www.uniprot.org/uniprotkb/P34540/entry","name":"unc-116","description":"Kinesin heavy chain","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6455925","identifier":"H9G2T2","identifierLink":"https://www.uniprot.org/uniprotkb/H9G2T2/entry","name":"klc-1","description":"Kinesin light chain","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45783","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1417","complexName":"BBP-MUD2 branchpoint-binding complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Orchestrates spliceosome assembly by binding the intron branchpoint sequence 5-prime-UACUAAC and establishes cross intron-bridging interactions with the U1 snRNP (CPX-23) at the 5-prime splice site of an unspliced intron in an RNA transcript.","predictedComplex":false,"interactors":[{"ac":"EBI-11612","identifier":"P36084","identifierLink":"https://www.uniprot.org/uniprotkb/P36084/entry","name":"MUD2","description":"Splicing factor MUD2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34012","identifier":"Q12186","identifierLink":"https://www.uniprot.org/uniprotkb/Q12186/entry","name":"MSL5","description":"Branchpoint-bridging protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11208","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1418","complexName":"Spliceosomal commitment complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Formation of this complex is the first defined step in the yeast splicing pathway and is responsible for intron recognition, which targets pre-mRNA to the splicing pathway. Binding of the 5-prime end of U1 snRNP (CPX-23) to the 5-prime splice site through base-pairing forms first a basal complex only dependent on a 5-prime splice site (CC1) and then a more stable second complex dependent on a branchpoint as well as a 5-prime splice site region (CC2). Interactions between the BBP-MUD2 branchpoint-binding complex (CPX-1417) and the U1 snRNP protein PRP40 (P33203) defines a bridge between the two ends of the intron. PRP5 may interact with U1 snRNP and other proteins to bridge the 5' splice site and the UACUAACA box of the pre-mRNA's branchpoint region. It may also recruit U2 snRNP (CPX-26) which binds to the intron branch site of the commitment complex to form the pre-spliceosome in an ATP dependent step.","predictedComplex":false,"interactors":[{"ac":"EBI-10052014","identifier":"CPX-23","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-23","name":"U1 small nuclear ribonucleoprotein complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-13824","identifier":"P21372","identifierLink":"https://www.uniprot.org/uniprotkb/P21372/entry","name":"PRP5","description":"Pre-mRNA-processing ATP-dependent RNA helicase PRP5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16630464","identifier":"CPX-1417","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-1417","name":"BBP-MUD2 branchpoint-binding complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-16716764","identifier":null,"identifierLink":null,"name":"pre-mrna","description":"Precursor mRNA","stochiometry":null,"interactorType":"ribonucleic acid","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1419","complexName":"Spindle pole body central plaque complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Component of the spindle pole body, which is responsible for the nucleation and organisation of microtubules within the cell, thus playing a role in chromosome segregation in mitosis and meiosis and controlling cytoplasmic interphase microtubules.","predictedComplex":false,"interactors":[{"ac":"EBI-12041","identifier":"P33419","identifierLink":"https://www.uniprot.org/uniprotkb/P33419/entry","name":"SPC29","description":"Spindle pole component 29","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-12369","identifier":"P32380","identifierLink":"https://www.uniprot.org/uniprotkb/P32380/entry","name":"SPC110","description":"Spindle pole body component 110","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47357","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17777","identifier":"P36094","identifierLink":"https://www.uniprot.org/uniprotkb/P36094/entry","name":"SPC42","description":"Spindle pole body component SPC42","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-3976","identifier":"P06787","identifierLink":"https://www.uniprot.org/uniprotkb/P06787/entry","name":"CMD1","description":"Calmodulin","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1420","complexName":"Spindle pole body intermediate layer 2 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Component of the spindle pole body, which is responsible for the nucleation and organisation of microtubules within the cell, thus playing a role in chromosome segregation in mitosis and meiosis and controlling cytoplasmic interphase microtubules.","predictedComplex":false,"interactors":[{"ac":"EBI-17777","identifier":"P36094","identifierLink":"https://www.uniprot.org/uniprotkb/P36094/entry","name":"SPC42","description":"Spindle pole body component SPC42","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-29172","identifier":"P53865","identifierLink":"https://www.uniprot.org/uniprotkb/P53865/entry","name":"CNM67","description":"Chaotic nuclear migration protein 67","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1421","complexName":"NOP8 60s ribosome pre-assembly complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"May  function as a scaffold to mediate topological rearrangements by the RNA helicases and organize assembly of early pre-60S ribosomes.","predictedComplex":false,"interactors":[{"ac":"EBI-12135","identifier":"Q08287","identifierLink":"https://www.uniprot.org/uniprotkb/Q08287/entry","name":"NOP8","description":"60S ribosome subunit biogenesis protein NOP8","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-25492","identifier":"P47108","identifierLink":"https://www.uniprot.org/uniprotkb/P47108/entry","name":"URB2","description":"Nucleolar pre-ribosomal-associated protein 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15682","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26595","identifier":"P34241","identifierLink":"https://www.uniprot.org/uniprotkb/P34241/entry","name":"URB1","description":"Nucleolar pre-ribosomal-associated protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13500","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-33602","identifier":"Q05942","identifierLink":"https://www.uniprot.org/uniprotkb/Q05942/entry","name":"RSA3","description":"Ribosome assembly protein 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28127","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5625","identifier":"P53734","identifierLink":"https://www.uniprot.org/uniprotkb/P53734/entry","name":"DBP6","description":"ATP-dependent RNA helicase DBP6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1422","complexName":"TEL2-TTI1-TTI2 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Regulates the stability of phosphatidylinositol 3-kinase-related protein kinases (PIKKs) such as TEL1 (P38110) and MEC1 (P38111), which are required for checkpoint signaling. Newly synthesized PIKK interacts with TEL2, in the TEL2-TTI1-TTI2 complex assisted by HSP90 (P02829). Phosphorylated TEL2 then appears to mediate the interaction between PIKK and R2TP complex to eventually lead to the proper assembly of PIKK.","predictedComplex":false,"interactors":[{"ac":"EBI-19106","identifier":"P53038","identifierLink":"https://www.uniprot.org/uniprotkb/P53038/entry","name":"TEL2","description":"Telomere length regulation protein TEL2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15830","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25698","identifier":"P47168","identifierLink":"https://www.uniprot.org/uniprotkb/P47168/entry","name":"TTI2","description":"TEL2-interacting protein 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-26630","identifier":"P36097","identifierLink":"https://www.uniprot.org/uniprotkb/P36097/entry","name":"TTI1","description":"TEL2-interacting protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR18460","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1423","complexName":"COX1 pre-assembly complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Binds to and stabilizes COX1 (P00401) during the assembly of mitochondrial respiratory chain complex IV/cytochrome C oxidase (CPX-1721/CPX-1722). The process is probably catalyzed by assembly chaperones such as SHY1 (P53266) and COA1 (P40452). The complex also acts to trap the COX1-mRNA-specific translational activator, MSS51, thus rendering it incompetent to support translation of COX1. On further maturation of the assembly intermediate, MSS51 dissociates and can stimulate further rounds of COX1 mRNA translation.","predictedComplex":false,"interactors":[{"ac":"EBI-11318","identifier":"P32335","identifierLink":"https://www.uniprot.org/uniprotkb/P32335/entry","name":"MSS51","description":"Protein MSS51, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28069","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3680840","identifier":"Q3E7B2","identifierLink":"https://www.uniprot.org/uniprotkb/Q3E7B2/entry","name":"COA3","description":"Cytochrome c oxidase assembly factor 3, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15642","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5113","identifier":"P39103","identifierLink":"https://www.uniprot.org/uniprotkb/P39103/entry","name":"COX14","description":"Cytochrome c oxidase assembly protein COX14","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-8637","identifier":"P0CS90","identifierLink":"https://www.uniprot.org/uniprotkb/P0CS90/entry","name":"SSC1","description":"Import motor subunit, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1424","complexName":"Tubulin alpha-beta heterodimeric complex, TUB1 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Building block of the non-covalent cylindrical polymers that make up the hollow water-filled microtubule structures required for the migration and proper orientation of the nucleus, spindle pole body separation, spindle function, and nuclear division.","predictedComplex":false,"interactors":[{"ac":"EBI-18976","identifier":"P09733","identifierLink":"https://www.uniprot.org/uniprotkb/P09733/entry","name":"TUB1","description":"Tubulin alpha-1 chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18986","identifier":"P02557","identifierLink":"https://www.uniprot.org/uniprotkb/P02557/entry","name":"TUB2","description":"Tubulin beta chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25820308","identifier":"CHEBI:37565","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:37565","name":"gtp(4-)","description":"GTP(4-)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1425","complexName":"Tubulin alpha-beta heterodimeric complex, TUB3 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Building block of the non-covalent cylindrical polymers that make up the hollow water-filled microtubule structures required for the migration and proper orientation of the nucleus, spindle pole body separation, spindle function, and nuclear division.","predictedComplex":false,"interactors":[{"ac":"EBI-18981","identifier":"P09734","identifierLink":"https://www.uniprot.org/uniprotkb/P09734/entry","name":"TUB3","description":"Tubulin alpha-3 chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18986","identifier":"P02557","identifierLink":"https://www.uniprot.org/uniprotkb/P02557/entry","name":"TUB2","description":"Tubulin beta chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-989053","identifier":"CHEBI:15996","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15996","name":"gtp","description":"guanosine triphosphate - GTP","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1426","complexName":"Myosin class II complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Building block of the class II myosin bipolar filament, responsible for the anti-parallel sliding of actin filaments. Plays a role in cell separation, appearing to form thick filaments that scaffold the assembly of the division machinery. The myosin heavy chain motor domain mediates the ATP-dependent interaction with the F-actin cytoskeleton. The myosin neck region with the bound light chains acts as a rigid lever arm that amplifies movements within the myosin motor domain into a large mechanical stroke that directionally propels the myosin along the actin filament.","predictedComplex":false,"interactors":[{"ac":"EBI-10988","identifier":"P53141","identifierLink":"https://www.uniprot.org/uniprotkb/P53141/entry","name":"MLC1","description":"Myosin light chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10999","identifier":"Q06580","identifierLink":"https://www.uniprot.org/uniprotkb/Q06580/entry","name":"MLC2","description":"Myosin light chain 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23049","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11650","identifier":"P08964","identifierLink":"https://www.uniprot.org/uniprotkb/P08964/entry","name":"MYO1","description":"Myosin-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1427","complexName":"Nuclear cap-binding complex","organismName":"Homo sapiens; 9606","description":"Binds co-transcriptionally to the 5-prime, m7GpppG-cap (m7G-cap) structures of all RNA polymerase II transcripts (pre-mRNAs and pre-miRNAs). Required for processes such as transcription elongation, pre-mRNA splicing through commitment and NELF complexes and spliceosome formation, classic mRNA 3-prime end processing, suppression of poly-A tail formation in histone 3-prime end pre-mRNA processing in complex with serrate (SRRT/ARS2, Q9BXP5) and NELF complex, nuclear export of mRNAs and U snRNAs in complex with importin-alpha and either ALYREF (Q86V81) and TREX complex (mRNAs) or PHAX-XPO1/CRM1-RAN.GTP complex (U snRNAs), degradation of nuclear mRNAs via nonsense-mediated decay (NMD), primary miRNA processing in complex with serrate (SRRT/ARS2), miRNA-mediated RNA interference and the pioneer round of translation. During the pioneer round of translation it interacts with CTIF (O43310) which facilitates the eventual release of CBC from the transcript and its replacement by the cytoplasmic cap-binding complex eIF4F. In the cytosol, importin-beta interacts with CBC-bound importin-alpha and promotes the dissociation of the RNA from CBC. Importin-complex-bound CBC gets reimported into the nucleus for reuse. NCBP1 phosphorylation correlate with increased cap-dependent splicing activity. Histone pre-mRNA processing and the pioneer round of translation may be restricted to mammalian CBC.","predictedComplex":false,"interactors":[{"ac":"EBI-464729","identifier":"P52298","identifierLink":"https://www.uniprot.org/uniprotkb/P52298/entry","name":"NCBP2","description":"Nuclear cap-binding protein subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-464743","identifier":"Q09161","identifierLink":"https://www.uniprot.org/uniprotkb/Q09161/entry","name":"NCBP1","description":"Nuclear cap-binding protein subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5441","complexName":"SPO16:ZIP2","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Binds both single-stranded and double-stranded DNA; prefers nicked double-stranded DNA and Holliday Junction DNA. Lacks endonuclease activity and may act as a scaffolding complex stabilizing D-loop intermediates","predictedComplex":false,"interactors":[{"ac":"EBI-24222","identifier":"P53061","identifierLink":"https://www.uniprot.org/uniprotkb/P53061/entry","name":"ZIP2","description":"Protein ZIP2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-3826035","identifier":"P17122","identifierLink":"https://www.uniprot.org/uniprotkb/P17122/entry","name":"SPO16","description":"Sporulation-specific protein 16","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-5442","complexName":"ZZS complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Complex that preferentially binds double-strand break hot spots during meiosis; ZIP2 is critical for complex binding to chromosomes","predictedComplex":false,"interactors":[{"ac":"EBI-2091833","identifier":"P40511","identifierLink":"https://www.uniprot.org/uniprotkb/P40511/entry","name":"SPO22","description":"Sporulation-specific protein 22","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR40375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-24222","identifier":"P53061","identifierLink":"https://www.uniprot.org/uniprotkb/P53061/entry","name":"ZIP2","description":"Protein ZIP2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-3826035","identifier":"P17122","identifierLink":"https://www.uniprot.org/uniprotkb/P17122/entry","name":"SPO16","description":"Sporulation-specific protein 16","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-5461","complexName":"Endosomal SNARE complex PEP12-VTI1-SYN8-SNC2","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SNARE complex required for transport from the Golgi to endosomes. Mediates membrane fusion through the spontaneous assembly of four complementary SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) motifs. SNAREs bind to each other in-trans, that is, with SNAREs anchored in each apposed tethered membrane. The assembly process leads to a tight connection between the linked membranes and initiates membrane fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-13098","identifier":"P32854","identifierLink":"https://www.uniprot.org/uniprotkb/P32854/entry","name":"PEP12","description":"Syntaxin PEP12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17512","identifier":"P33328","identifierLink":"https://www.uniprot.org/uniprotkb/P33328/entry","name":"SNC2","description":"Synaptobrevin homolog 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18483","identifier":"P31377","identifierLink":"https://www.uniprot.org/uniprotkb/P31377/entry","name":"SYN8","description":"Syntaxin-8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20519","identifier":"Q04338","identifierLink":"https://www.uniprot.org/uniprotkb/Q04338/entry","name":"VTI1","description":"t-SNARE VTI1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21230","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5462","complexName":"Endosomal SNARE complex PEP12-VTI1-TLG1-SNC2","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SNARE complex required for transport from the Golgi to endosomes. Mediates membrane fusion through the spontaneous assembly of four complementary SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) motifs. SNAREs bind to each other in-trans, that is, with SNAREs anchored in each apposed tethered membrane. The assembly process leads to a tight connection between the linked membranes and initiates membrane fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-13098","identifier":"P32854","identifierLink":"https://www.uniprot.org/uniprotkb/P32854/entry","name":"PEP12","description":"Syntaxin PEP12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17512","identifier":"P33328","identifierLink":"https://www.uniprot.org/uniprotkb/P33328/entry","name":"SNC2","description":"Synaptobrevin homolog 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20519","identifier":"Q04338","identifierLink":"https://www.uniprot.org/uniprotkb/Q04338/entry","name":"VTI1","description":"t-SNARE VTI1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21230","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-38705","identifier":"Q03322","identifierLink":"https://www.uniprot.org/uniprotkb/Q03322/entry","name":"TLG1","description":"t-SNARE affecting a late Golgi compartment protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1365","complexName":"Vesicular SNARE complex SSO1-SEC9-SNC1","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"An exocytic SNARE complex required for the fusion of post-Golgi secretory vesicles with the plasma membrane and is active primarily in vegetative cells. Mediates membrane fusion through the spontaneous assembly of four complementary SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) motifs. SNAREs bind to each other in-trans, that is, with SNAREs anchored in each apposed tethered membrane. The assembly process leads to a tight connection between the linked membranes and initiates membrane fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-16904","identifier":"P40357","identifierLink":"https://www.uniprot.org/uniprotkb/P40357/entry","name":"SEC9","description":"Protein transport protein SEC9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2123541","identifier":"P31109","identifierLink":"https://www.uniprot.org/uniprotkb/P31109/entry","name":"SNC1","description":"Synaptobrevin homolog 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2206525","identifier":"P32867","identifierLink":"https://www.uniprot.org/uniprotkb/P32867/entry","name":"SSO1","description":"Protein SSO1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5463","complexName":"Vesicular SNARE complex SSO1-SEC9-SNC2","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"An exocytic SNARE complex required for the fusion of post-Golgi secretory vesicles with the plasma membrane and is active primarily in vegetative cells. Mediates membrane fusion through the spontaneous assembly of four complementary SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) motifs. SNAREs bind to each other in-trans, that is, with SNAREs anchored in each apposed tethered membrane. The assembly process leads to a tight connection between the linked membranes and initiates membrane fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-16904","identifier":"P40357","identifierLink":"https://www.uniprot.org/uniprotkb/P40357/entry","name":"SEC9","description":"Protein transport protein SEC9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17512","identifier":"P33328","identifierLink":"https://www.uniprot.org/uniprotkb/P33328/entry","name":"SNC2","description":"Synaptobrevin homolog 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2206525","identifier":"P32867","identifierLink":"https://www.uniprot.org/uniprotkb/P32867/entry","name":"SSO1","description":"Protein SSO1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5464","complexName":"Vesicular SNARE complex SSO1-SPO20-SNC1","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SNARE complex required for the fusion of post-Golgi secretory vesicles with the pre-spore membrane. Mediates membrane fusion through the spontaneous assembly of four complementary SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) motifs. SNAREs bind to each other in-trans, that is, with SNAREs anchored in each apposed tethered membrane. The assembly process leads to a tight connection between the linked membranes and initiates membrane fusion. SPO20 induction is sporolation-specific.","predictedComplex":false,"interactors":[{"ac":"EBI-2123541","identifier":"P31109","identifierLink":"https://www.uniprot.org/uniprotkb/P31109/entry","name":"SNC1","description":"Synaptobrevin homolog 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2206525","identifier":"P32867","identifierLink":"https://www.uniprot.org/uniprotkb/P32867/entry","name":"SSO1","description":"Protein SSO1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28034","identifier":"Q04359","identifierLink":"https://www.uniprot.org/uniprotkb/Q04359/entry","name":"SPO20","description":"Sporulation-specific protein 20","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5465","complexName":"Vesicular SNARE complex SSO2-SEC9-SNC2","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"An exocytic SNARE complex required for the fusion of post-Golgi secretory vesicles with the plasma membrane and is active primarily in vegetative cells. Mediates membrane fusion through the spontaneous assembly of four complementary SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) motifs. SNAREs bind to each other in-trans, that is, with SNAREs anchored in each apposed tethered membrane. The assembly process leads to a tight connection between the linked membranes and initiates membrane fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-16904","identifier":"P40357","identifierLink":"https://www.uniprot.org/uniprotkb/P40357/entry","name":"SEC9","description":"Protein transport protein SEC9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17512","identifier":"P33328","identifierLink":"https://www.uniprot.org/uniprotkb/P33328/entry","name":"SNC2","description":"Synaptobrevin homolog 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18227","identifier":"P39926","identifierLink":"https://www.uniprot.org/uniprotkb/P39926/entry","name":"SSO2","description":"Protein SSO2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5466","complexName":"Vesicular SNARE complex SSO1-SPO20-SNC2","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SNARE complex required for the fusion of post-Golgi secretory vesicles with the pre-spore membrane. Mediates membrane fusion through the spontaneous assembly of four complementary SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) motifs. SNAREs bind to each other in-trans, that is, with SNAREs anchored in each apposed tethered membrane. The assembly process leads to a tight connection between the linked membranes and initiates membrane fusion. SPO20 induction is sporulation-specific.","predictedComplex":false,"interactors":[{"ac":"EBI-17512","identifier":"P33328","identifierLink":"https://www.uniprot.org/uniprotkb/P33328/entry","name":"SNC2","description":"Synaptobrevin homolog 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2206525","identifier":"P32867","identifierLink":"https://www.uniprot.org/uniprotkb/P32867/entry","name":"SSO1","description":"Protein SSO1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28034","identifier":"Q04359","identifierLink":"https://www.uniprot.org/uniprotkb/Q04359/entry","name":"SPO20","description":"Sporulation-specific protein 20","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1369","complexName":"Vesicular SNARE complex SSO2-SEC9-SNC1","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"An exocytic SNARE complex required for the fusion of post-Golgi secretory vesicles with the plasma membrane and is active primarily in vegetative cells. 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The assembly process leads to a tight connection between the linked membranes and initiates membrane fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-16904","identifier":"P40357","identifierLink":"https://www.uniprot.org/uniprotkb/P40357/entry","name":"SEC9","description":"Protein transport protein SEC9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18227","identifier":"P39926","identifierLink":"https://www.uniprot.org/uniprotkb/P39926/entry","name":"SSO2","description":"Protein SSO2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2123541","identifier":"P31109","identifierLink":"https://www.uniprot.org/uniprotkb/P31109/entry","name":"SNC1","description":"Synaptobrevin homolog 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5521","complexName":"Vacuolar SNARE complex SSO1-SEC9-NYV1","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"SNARE complex required for the fusion of vacuoles with the plasma membrane and is active primarily in vegetative cells. Mediates membrane fusion through the spontaneous assembly of four complementary SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) motifs. SNAREs bind to each other in-trans, that is, with SNAREs anchored in each apposed tethered membrane. The assembly process leads to a tight connection between the linked membranes and initiates membrane fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-16904","identifier":"P40357","identifierLink":"https://www.uniprot.org/uniprotkb/P40357/entry","name":"SEC9","description":"Protein transport protein SEC9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2206525","identifier":"P32867","identifierLink":"https://www.uniprot.org/uniprotkb/P32867/entry","name":"SSO1","description":"Protein SSO1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-35465","identifier":"Q12255","identifierLink":"https://www.uniprot.org/uniprotkb/Q12255/entry","name":"NYV1","description":"Vacuolar v-SNARE NYV1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21136","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5541","complexName":"MutHLS methyl-directed mismatch repair complex","organismName":"Escherichia coli (strain K12); 83333","description":"Mismatch repair complex, involved in the recognition and repair of base-base and small insertion/deletion mismatches that appear as a consequence of DNA polymerase errors during replication or homologous recombination. Strand recognition necessary for removal of DNA biosynthetic errors from the daughter strand is based on the transient absence of d(GATC) methylation in newly synthesized DNA (hemimethylation). Repair is initiated by the binding of mutS to a mismatch or to a small insertion-deletion loop. Assembly of the rotation-coupled diffusion-mediated MutHLS complex leads to activation of the mutH endonuclease which can cleave either side of the mismatch and increases mutH interactions with the mismatched DNA by at least 1000-fold, dramatically enhancing its GATC incision activity.","predictedComplex":false,"interactors":[{"ac":"EBI-545170","identifier":"P06722","identifierLink":"https://www.uniprot.org/uniprotkb/P06722/entry","name":"mutH","description":"DNA mismatch repair protein MutH","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-554913","identifier":"P23367","identifierLink":"https://www.uniprot.org/uniprotkb/P23367/entry","name":"mutL","description":"DNA mismatch repair protein MutL","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-554920","identifier":"P23909","identifierLink":"https://www.uniprot.org/uniprotkb/P23909/entry","name":"mutS","description":"DNA mismatch repair protein MutS","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11361","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5542","complexName":"MutL-UvrD DNA helicase complex","organismName":"Escherichia coli (strain K12); 83333","description":"DNA helicase complex, involved in the recognition and repair of base-base and small insertion/deletion mismatches that appear as a consequence of DNA polymerase errors during replication or homologous recombination. Strand recognition necessary for removal of DNA biosynthetic errors from the daughter strand is based on the transient absence of d(GATC) methylation in the newly synthesized DNA strand (hemimethylation). Repair is initiated by the binding of mutS to a mismatch or to a small insertion-deletion loop. Assembly of the rotation-coupled diffusion-mediated MutHLS complex (CPX-5541) leads to activation of the mutH endonuclease which can cleave either side of the mismatch. The MutL-UvrD complex forms near an mutH strand scission tethering it to the mismatched DNA where it randomly unwinds and rezips the DNA that is alternately bound and released by ssb (P0AGE0).  When MutL-UvrD unwinding reaches an adjacent  mutH GATC incision site, the intervening fragment is released creating an  SSB bound gap.","predictedComplex":false,"interactors":[{"ac":"EBI-554913","identifier":"P23367","identifierLink":"https://www.uniprot.org/uniprotkb/P23367/entry","name":"mutL","description":"DNA mismatch repair protein MutL","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-559573","identifier":"P03018","identifierLink":"https://www.uniprot.org/uniprotkb/P03018/entry","name":"uvrD","description":"DNA helicase II","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11070","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5544","complexName":"DNA polymerase V mutasome complex","organismName":"Escherichia coli (strain K12); 83333","description":"Low fidelity DNA polymerase required for mutagenic SOS DNA repair, replicating DNA across the lesions. Y-family DNA polymerases, such as umuC, have more open active sites and thus can more easily accommodate bulky DNA lesions and lack the 3'-5' exonucleolytic proofreading activity typical of high-fidelity DNA polymerases.","predictedComplex":false,"interactors":[{"ac":"EBI-1108845","identifier":"CHEBI:15422","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15422","name":"atp","description":"ATP","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1119849","identifier":"P04152","identifierLink":"https://www.uniprot.org/uniprotkb/P04152/entry","name":"umuC","description":"Protein UmuC","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25426537","identifier":"P0AG11-PRO_0000027305","identifierLink":"https://www.uniprot.org/uniprotkb/P0AG11-PRO_0000027305/entry","name":"umuD","description":"Protein UmuD'","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-370331","identifier":"P0A7G6","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7G6/entry","name":"recA","description":"Protein RecA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR45900","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5561","complexName":"NAD-dependent dihydropyrimidine dehydrogenase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Enzyme of the reductive pyrimidine catabolic pathway. Catalyzes the NADPH-dependent reduction of uracil and thymine to 5,6-dihydro derivatives, enabling uracil and thymine to be used as nitrogen and carbon sources for growth.","predictedComplex":false,"interactors":[{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-550312","identifier":"P76440","identifierLink":"https://www.uniprot.org/uniprotkb/P76440/entry","name":"preT","description":"NAD-dependent dihydropyrimidine dehydrogenase subunit PreT","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-907005","identifier":"P25889","identifierLink":"https://www.uniprot.org/uniprotkb/P25889/entry","name":"preA","description":"NAD-dependent dihydropyrimidine dehydrogenase subunit PreA","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5581","complexName":"Nitrate reductase Z complex","organismName":"Escherichia coli (strain K12); 83333","description":"Constitutively expressed nitrate reductase complex, which constitutes only 2% of total nitrate reductase activity when Nitrate reductase A (CPX-1974) is fully induced. Involved in electron transport during anaerobic respiration: electrons are passed from the formate dehydrogenase-N (Fdh-N) complex (CPX-1975) to the nitrate reductase complex via a quinone-quinol redox reaction. Within Nitrate reductase Z, the distal heme molecule of NarV receives electrons from quinol (hydroquinone), passes them on to the proximal heme which passes it down a Fe-S cluster chain to the molybdopterin cofactor Mo-bisMGD where  nitrate is reduced to nitrite.","predictedComplex":false,"interactors":[{"ac":"EBI-11297461","identifier":"CHEBI:21137","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:21137","name":"tri-mu-sulfido-mu3-sulfido-triiron","description":"tri-mu-sulfido-mu3-sulfido-triiron","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-11426020","identifier":"CHEBI:60539","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60539","name":"mo(=o)-bis(molybdopterin guanine dinucleotide)(4-)","description":"Mo(=O)-bis(molybdopterin guanine dinucleotide)(4-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-25428568","identifier":"P0AF32","identifierLink":"https://www.uniprot.org/uniprotkb/P0AF32/entry","name":"narV","description":"Respiratory nitrate reductase 2 gamma chain","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30598","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-547262","identifier":"P19319","identifierLink":"https://www.uniprot.org/uniprotkb/P19319/entry","name":"narZ","description":"Respiratory nitrate reductase 2 alpha chain","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-555059","identifier":"P19318","identifierLink":"https://www.uniprot.org/uniprotkb/P19318/entry","name":"narY","description":"Respiratory nitrate reductase 2 beta chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43518","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-5601","complexName":"Alternative pathway C3 convertase complex C3bBb","organismName":"Homo sapiens; 9606","description":"A serine-type endopeptidase complex of the alternative pathway of complement activation of the innate immune system. Cleaves Complement C3 precurser (P01024) into anaphylatoxin C3A (P01024-PRO_0000005910) and nascent core-convertase component C3b (CPX-973). Occurs in the fluid-phase and binds host and pathogen cells. \r\n\r\nC3bBb convertase is unstable. In fluid-phase or when bound to the host cell it is readily inactivated by Factor H (P08603), CR1 (P17927) or DAF (P08174, only on host cells) thus preventing autoimmune activation. \r\n\r\nLack of protection, due to familial mutations in the complement genes or the presence of autoantibodies against regulators has been linked to atypical hemolytic uremic syndrome (aHUS) and C3 glomerulopathies (C3G) in kidneys and age-related macular degeneration (AMD) in eyes. Conditions of chronic and acute inflammations, as in rheumatoid arthritis, strokes, and heart attacks, become aggravated by complement activation against the disturbed tissue.","predictedComplex":false,"interactors":[{"ac":"EBI-12735745","identifier":"CPX-973","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-973","name":"Complement C3b complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-21988629","identifier":"P00751-PRO_0000027547","identifierLink":"https://www.uniprot.org/uniprotkb/P00751-PRO_0000027547/entry","name":"CFB","description":"Complement factor B Bb","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-5602","complexName":"Alternative pathway pathogen cell-bound C3 convertase complex C3bBbP","organismName":"Homo sapiens; 9606","description":"A serine-type endopeptidase complex of the alternative pathway of complement activation of the innate immune system. Cleaves Complement C3 precurser (P01024) into anaphylatoxin C3A (P01024-PRO_0000005910) and nascent convertase core-component C3b (CPX-973). Only occurs bound to pathogen cells and binds to target cells via its reactive thioester moiety. \r\n\r\nProperdin-binding stablises C3bBb convertase (CPX-5601) and prevents its inactivation by Factor H (P08603). \r\n\r\nLack of protection, due to familial mutations in the complement genes or the presence of autoantibodies against regulators has been linked to atypical hemolytic uremic syndrome (aHUS) and C3 glomerulopathies (C3G) in kidneys and age-related macular degeneration (AMD) in eyes. Conditions of chronic and acute inflammations, as in rheumatoid arthritis, strokes, and heart attacks, become aggravated by complement activation against the disturbed tissue.","predictedComplex":false,"interactors":[{"ac":"EBI-25436732","identifier":"CPX-5601","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-5601","name":"Alternative pathway C3 convertase complex C3bBb","description":null,"stochiometry":"minValue: 1, maxValue: 5","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-9038570","identifier":"P27918","identifierLink":"https://www.uniprot.org/uniprotkb/P27918/entry","name":"CFP","description":"Properdin","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22906","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5604","complexName":"Alternative pathway solid-phase C5 convertase complex C3bBbC3b","organismName":"Homo sapiens; 9606","description":"A serine-type endopeptidase complex of the alternative pathway of complement activation of the innate immune system. Cleaves Complement C5 precurser (P01031) into anaphylatoxin C5a (P01031-PRO_0000005988) and Complement C5b (P01031-PRO_0000005985, P01031-PRO_0000005989). Binds host and pathogen cells via its reactive thioester moiety. \r\n\r\nC3bBbC3b convertase is more stable than C3bBb convertase (CPX-5601). When bound to the host cell it is readily inactivated by Factor H (P08603), CR1 (P17927) or DAF (P08174) thus preventing autoimmune activation. \r\n\r\nCombines with C5b, C6 (P13671), C7 (P10643), C8A (P07357), C8B (P07358) & C8G (P07360) and C9 (P02748) to form the Membrane Attack Complex (CPX-6159). \r\n\r\nLack of protection, due to familial mutations in the complement genes or the presence of autoantibodies against regulators has been linked to atypical hemolytic uremic syndrome (aHUS) and C3 glomerulopathies (C3G) in kidneys and age-related macular degeneration (AMD) in eyes. Conditions of chronic and acute inflammations, as in rheumatoid arthritis, strokes, and heart attacks, become aggravated by complement activation against the disturbed tissue.","predictedComplex":false,"interactors":[{"ac":"EBI-12735745","identifier":"CPX-973","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-973","name":"Complement C3b complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25436732","identifier":"CPX-5601","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-5601","name":"Alternative pathway C3 convertase complex C3bBb","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-5605","complexName":"Alternative pathway pathogen cell-bound C5 convertase complex C3bBbC3bP","organismName":"Homo sapiens; 9606","description":"A serine-type endopeptidase complex of the alternative pathway of complement activation of the innate immune system. Cleaves Complement C5 precurser (P01031) into anaphylatoxin C5a (P01031-PRO_0000005988) and Complement C5b (P01031-PRO_0000005985, P01031-PRO_0000005989). Only occurs bound to pathogen cells and binds to target cells via its reactive thioester moiety. \r\n\r\nProperdin-binding stablises C3bBbC3b convertase (CPX-5604) and prevents its inactivation by Factor H (P08603). \r\n\r\nFollowing properdin dissociation the complex combines with C5b, C6 (P13671), C7 (P10643), C8A (P07357), C8B (P07358) & C8G (P07360) and C9 (P02748) to form the Membrane Attack Complex (CPX-6159). \r\n\r\nLack of protection, due to familial mutations in the complement genes or the presence of autoantibodies against regulators has been linked to atypical hemolytic uremic syndrome (aHUS) and C3 glomerulopathies (C3G) in kidneys and age-related macular degeneration (AMD) in eyes. Conditions of chronic and acute inflammations, as in rheumatoid arthritis, strokes, and heart attacks, become aggravated by complement activation against the disturbed tissue.","predictedComplex":false,"interactors":[{"ac":"EBI-12735745","identifier":"CPX-973","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-973","name":"Complement C3b complex","description":null,"stochiometry":"minValue: 1, maxValue: 5","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25436732","identifier":"CPX-5601","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-5601","name":"Alternative pathway C3 convertase complex C3bBb","description":null,"stochiometry":"minValue: 1, maxValue: 5","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-9038570","identifier":"P27918","identifierLink":"https://www.uniprot.org/uniprotkb/P27918/entry","name":"CFP","description":"Properdin","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22906","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5606","complexName":"GEL multi-spanning membrane protein insertion complex","organismName":"Homo sapiens; 9606","description":"Mediates insertion of transmembrane regions of multi-spanning membrane proteins into the endoplasmic reticulum (ER) membrane. TMCO1 appears to form a luminel funnel into the central membrane cavity. Acts as part of an ER translocon that functions co-translationally with SEC61 channel-forming translocon complex (CPX-8073) during biogenesis of multi-pass membrane proteins, along with the PAT intramembrane chaperone complex (CPX-7020) and the BOS complex (CPX-8021/CPX-8022/CPX-8023).","predictedComplex":false,"interactors":[{"ac":"EBI-1050079","identifier":"Q9BUV8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BUV8/entry","name":"RAB5IF","description":"GEL complex subunit OPTI","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12906","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1051217","identifier":"Q9UM00","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UM00/entry","name":"TMCO1","description":"Calcium load-activated calcium channel","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20917","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5623","complexName":"NAD(P) transhydrogenase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Conformationally driven transhydrogenase proton pump, which links the reversible reduction of NADP+ by NADH to the translocation of protons across the cytoplasmic membrane. The transfer of a proton from the periplasm to the cytosol is linked to the transfer of a hydride ion equivalent from NADH to NADP+. High levels of NADPH are required for detoxification, via the glutathione peroxidase pathway, and anabolic purposes.","predictedComplex":false,"interactors":[{"ac":"EBI-25464377","identifier":"P0AB67","identifierLink":"https://www.uniprot.org/uniprotkb/P0AB67/entry","name":"pntB","description":"NAD(P) transhydrogenase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR44758","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-559555","identifier":"P07001","identifierLink":"https://www.uniprot.org/uniprotkb/P07001/entry","name":"pntA","description":"NAD(P) transhydrogenase subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10160","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5624","complexName":"Ornithine transcarbamoylase complex, argIII variant","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the first reaction in the urea cycle, in which l-ornithine is carbamoylated via transfer of the carbamoyl group from carbamoyl phosphate (CP) to form citrulline. Required for arginine biosynthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-1132864","identifier":"P04391","identifierLink":"https://www.uniprot.org/uniprotkb/P04391/entry","name":"argI","description":"Ornithine carbamoyltransferase subunit I","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR45753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 3, maxValue: 3","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-5625","complexName":"Ornithine transcarbamoylase complex, argFII variant","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the first reaction in the urea cycle, in which l-ornithine is carbamoylated via  transfer of the carbamoyl group from carbamoyl phosphate (CP) to form citrulline. Required for arginine biosynthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-1115215","identifier":"P06960","identifierLink":"https://www.uniprot.org/uniprotkb/P06960/entry","name":"argF","description":"Ornithine carbamoyltransferase subunit F","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR45753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1132864","identifier":"P04391","identifierLink":"https://www.uniprot.org/uniprotkb/P04391/entry","name":"argI","description":"Ornithine carbamoyltransferase subunit I","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR45753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 3, maxValue: 3","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-5626","complexName":"Ornithine transcarbamoylase complex, argFFI variant","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the first reaction in the urea cycle, in which l-ornithine is carbamoylated via  transfer of the carbamoyl group from carbamoyl phosphate (CP) to form citrulline. Required for arginine biosynthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-1115215","identifier":"P06960","identifierLink":"https://www.uniprot.org/uniprotkb/P06960/entry","name":"argF","description":"Ornithine carbamoyltransferase subunit F","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR45753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1132864","identifier":"P04391","identifierLink":"https://www.uniprot.org/uniprotkb/P04391/entry","name":"argI","description":"Ornithine carbamoyltransferase subunit I","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR45753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 3, maxValue: 3","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-5627","complexName":"Ornithine transcarbamoylase complex, argFFF variant","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the first reaction in the urea cycle, in which l-ornithine is carbamoylated via  transfer of the carbamoyl group from carbamoyl phosphate (CP) to form citrulline. Required for arginine biosynthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-1115215","identifier":"P06960","identifierLink":"https://www.uniprot.org/uniprotkb/P06960/entry","name":"argF","description":"Ornithine carbamoyltransferase subunit F","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR45753","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 3, maxValue: 3","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-5628","complexName":"Type I restriction-modification EcoKI complex","organismName":"Escherichia coli (strain K12); 83333","description":"Defense mechanisms against  foreign DNA introduced by an infectious agent (such as a bacteriophage). Comprises of two enzymatic activities: a restriction endonuclease (REase) and a methyltransferase (MTase). The REase recognizes and cleaves foreign DNA sequences at specific sites, cleaving endonucleolytically at phosphodiester bonds to generate 5′ or 3′ overhangs or blunt ends while the MTase activity ensures discrimination between self and non-self DNA, by transferring methyl groups to the same specific DNA sequence within the host's genome. The complex binds to a bipartite, asymmetric DNA sequence, 5'-AACN6GTGC-3', the MTase transfers the methyl group from S-adenosyl methionine to the C-5 carbon or the N4 amino group of cytosine or to the N6 amino group of adenine on newly replicated, hemimethylated host DNA and switches to an endonuclease activity on unmethylated foreign DNA, cleaving from approximately 100 base pairs to tens of thousands of base pairs away from the target. The latter reaction requires massive ATP hydrolysis to drive translocation of up to 50 kb of DNA at rates of up to 1 kb per second. The DNA is then cleaved at a random sequence remote from the original specificity sequence, with the generation of variable length single-strand overhangs Type-I DNA restriction-modification (R/M) systems are important agents in limiting the transmission of mobile genetic elements responsible for spreading bacterial resistance to antibiotics.","predictedComplex":false,"interactors":[{"ac":"EBI-1135164","identifier":"P05719","identifierLink":"https://www.uniprot.org/uniprotkb/P05719/entry","name":"hsdS","description":"Type I restriction enzyme EcoKI specificity subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43140","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-878500","identifier":"P08956","identifierLink":"https://www.uniprot.org/uniprotkb/P08956/entry","name":"hsdR","description":"Type I restriction enzyme EcoKI endonuclease subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR47396","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-878571","identifier":"P08957","identifierLink":"https://www.uniprot.org/uniprotkb/P08957/entry","name":"hsdM","description":"Type I restriction enzyme EcoKI methylase subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42933","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5629","complexName":"Sulfite reductase [NADPH] complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the 6-electron reduction of sulfite to sulfide, a key step in the biosynthesis of cysteine.","predictedComplex":false,"interactors":[{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-25465224","identifier":"CHEBI:60052","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60052","name":"siroheme(8-)","description":"siroheme(8-)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-544431","identifier":"P17846","identifierLink":"https://www.uniprot.org/uniprotkb/P17846/entry","name":"cysI","description":"Sulfite reductase [NADPH] hemoprotein beta-component","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11493","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544440","identifier":"P38038","identifierLink":"https://www.uniprot.org/uniprotkb/P38038/entry","name":"cysJ","description":"Sulfite reductase [NADPH] flavoprotein alpha-component","stochiometry":"minValue: 8, maxValue: 8","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR19384","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9663515","identifier":"CHEBI:58210","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58210","name":"fmn(3-)","description":"FMN(3-)","stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-5633","complexName":"AMPK complex, alpha1-beta1-gamma1 variant","organismName":"Homo sapiens; 9606","description":"Energy sensor serine/threonine kinase that plays a key role in regulating cellular energy metabolism. Energy stress manifests as a drop in the ratio of adenosine triphosphate (ATP) to AMP/ADP, which activates AMPK's kinase activity, allowing it to upregulate ATP-generating catabolic pathways and to reduce energy-consuming catabolic pathways and cellular programs: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators.","predictedComplex":false,"interactors":[{"ac":"EBI-1181405","identifier":"Q13131","identifierLink":"https://www.uniprot.org/uniprotkb/Q13131/entry","name":"PRKAA1","description":"5'-AMP-activated protein kinase catalytic subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1181439","identifier":"P54619","identifierLink":"https://www.uniprot.org/uniprotkb/P54619/entry","name":"PRKAG1","description":"5'-AMP-activated protein kinase subunit gamma-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-719769","identifier":"Q9Y478","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y478/entry","name":"PRKAB1","description":"5'-AMP-activated protein kinase subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5634","complexName":"Eukaryotic translation initiation factor 4F, EIF4A2 and EIF4G1 variant","organismName":"Homo sapiens; 9606","description":"Eukaryotic translation initiation factor 4F (eIF4F) consists of three subunits, eIF4A, eIF4E, and eIF4G. Cap-dependent translation initiation commences with the binding of the cap structure (m7GTP) found at the 5 prime end of mRNA to eIF4E subunit. The eIF4F complex then loads mRNAs onto the 40S ribosomal subunit together with eIF3.\r\nSubunit eIF4A is an ATP-dependent RNA helicase involved in cap recognition and is required for mRNA binding to ribosome. eIF4G subunit serves as a scaffold for eIF4A and eIF4E subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-73440","identifier":"P06730","identifierLink":"https://www.uniprot.org/uniprotkb/P06730/entry","name":"EIF4E","description":"Eukaryotic translation initiation factor 4E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-73473","identifier":"Q14240","identifierLink":"https://www.uniprot.org/uniprotkb/Q14240/entry","name":"EIF4A2","description":"Eukaryotic initiation factor 4A-II","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-73711","identifier":"Q04637","identifierLink":"https://www.uniprot.org/uniprotkb/Q04637/entry","name":"EIF4G1","description":"Eukaryotic translation initiation factor 4 gamma 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23253","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5635","complexName":"Eukaryotic translation initiation factor 4F, EIF4A1 and EIF4G3 variant","organismName":"Homo sapiens; 9606","description":"Eukaryotic translation initiation factor 4F (eIF4F) consists of three subunits, eIF4A, eIF4E, and eIF4G. Cap-dependent translation initiation commences with the binding of the cap structure (m7GTP) found at the 5 prime end of mRNA to eIF4E subunit. The eIF4F complex then loads mRNAs onto the 40S ribosomal subunit together with eIF3.\r\nSubunit eIF4A is an ATP-dependent RNA helicase involved in cap recognition and is required for mRNA binding to ribosome. eIF4G subunit serves as a scaffold for eIF4A and eIF4E subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-464766","identifier":"O43432","identifierLink":"https://www.uniprot.org/uniprotkb/O43432/entry","name":"EIF4G3","description":"Eukaryotic translation initiation factor 4 gamma 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23253","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-73440","identifier":"P06730","identifierLink":"https://www.uniprot.org/uniprotkb/P06730/entry","name":"EIF4E","description":"Eukaryotic translation initiation factor 4E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-73449","identifier":"P60842","identifierLink":"https://www.uniprot.org/uniprotkb/P60842/entry","name":"EIF4A1","description":"Eukaryotic initiation factor 4A-I","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5636","complexName":"Eukaryotic translation initiation factor 4F, EIF4A2 and EIF4G3 variant","organismName":"Homo sapiens; 9606","description":"Eukaryotic translation initiation factor 4F (eIF4F) consists of three subunits, eIF4A, eIF4E, and eIF4G. Cap-dependent translation initiation commences with the binding of the cap structure (m7GTP) found at the 5 prime end of mRNA to eIF4E subunit. The eIF4F complex then loads mRNAs onto the 40S ribosomal subunit together with eIF3.\r\nSubunit eIF4A is an ATP-dependent RNA helicase involved in cap recognition and is required for mRNA binding to ribosome. eIF4G subunit serves as a scaffold for eIF4A and eIF4E subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-464766","identifier":"O43432","identifierLink":"https://www.uniprot.org/uniprotkb/O43432/entry","name":"EIF4G3","description":"Eukaryotic translation initiation factor 4 gamma 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23253","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-73440","identifier":"P06730","identifierLink":"https://www.uniprot.org/uniprotkb/P06730/entry","name":"EIF4E","description":"Eukaryotic translation initiation factor 4E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-73473","identifier":"Q14240","identifierLink":"https://www.uniprot.org/uniprotkb/Q14240/entry","name":"EIF4A2","description":"Eukaryotic initiation factor 4A-II","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5642","complexName":"Kinetochore SKA complex","organismName":"Homo sapiens; 9606","description":"A microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation.","predictedComplex":false,"interactors":[{"ac":"EBI-1773976","identifier":"Q8IX90","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IX90/entry","name":"SKA3","description":"Spindle and kinetochore-associated protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48118","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1773994","identifier":"Q8WVK7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WVK7/entry","name":"SKA2","description":"Spindle and kinetochore-associated protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32017","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-741854","identifier":"Q96BD8","identifierLink":"https://www.uniprot.org/uniprotkb/Q96BD8/entry","name":"SKA1","description":"SKA complex subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28573","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5643","complexName":"Kinetochore MIS12 complex","organismName":"Homo sapiens; 9606","description":"Required for normal chromosome alignment and segregation, kinetochore formation during mitosis, proper kinetochore microtubule attachments and for the spindle assembly checkpoint. The complex plays a role in establishing a bipolar spindle-kinetochore interaction by joining kinetochore subunits contacting DNA to those contacting microtubules.\r\n\r\nKNL1 (CPX-5644), MIS12 and NDC80 (CPX-550) form the KMN protein network.","predictedComplex":false,"interactors":[{"ac":"EBI-1001144","identifier":"Q9H410","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H410/entry","name":"DSN1","description":"Kinetochore-associated protein DSN1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14778","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1001205","identifier":"Q9H081","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H081/entry","name":"MIS12","description":"Protein MIS12 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2554690","identifier":"Q96IY1","identifierLink":"https://www.uniprot.org/uniprotkb/Q96IY1/entry","name":"NSL1","description":"Kinetochore-associated protein NSL1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31749","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-713832","identifier":"Q6P1K2","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P1K2/entry","name":"PMF1","description":"Polyamine-modulated factor 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15459","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5644","complexName":"Kinetochore KNL1 complex","organismName":"Homo sapiens; 9606","description":"Required for normal chromosome alignment and segregation and for kinetochore formation during mitosis and for proper kinetochore microtubule attachments. Binds, at its outer end, to kinetochore microtubule and, at its inner end, to the MIS12 complex (CPX-5643).\r\n\r\nKNL1, MIS12 and NCD80 (CPX-550) form the KMN protein network.","predictedComplex":false,"interactors":[{"ac":"EBI-1001132","identifier":"O95229","identifierLink":"https://www.uniprot.org/uniprotkb/O95229/entry","name":"ZWINT","description":"Outer kinetochore KNL1 complex subunit ZWINT","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31504","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1001161","identifier":"Q8NG31","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NG31/entry","name":"KNL1","description":"Outer kinetochore KNL1 complex subunit KNL1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16520","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5645","complexName":"KMN complex","organismName":"Homo sapiens; 9606","description":"Part of the protein architecture within kinetochores that links centromeric DNA to the plus ends of spindle microtubules.","predictedComplex":false,"interactors":[{"ac":"EBI-1209326","identifier":"CPX-550","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-550","name":"Ndc80 complex","description":"Ndc80 complex","stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25468341","identifier":"CPX-5643","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-5643","name":"Kinetochore MIS12 complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25468806","identifier":"CPX-5644","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-5644","name":"Kinetochore KNL1 complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-5646","complexName":"Kinetochore CCAN complex","organismName":"Homo sapiens; 9606","description":"Interacts with duplex DNA and facilitates accurate chromosome segregation.. Plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. Binds to CENPA (P49450)-associated nucleosomes providing a platform for assembly of the outer layer of kinetochore, the KMN complex (CPX-5645).","predictedComplex":false,"interactors":[{"ac":"EBI-1003700","identifier":"Q9H3R5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H3R5/entry","name":"CENPH","description":"Centromere protein H","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48122","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10250303","identifier":"Q6IPU0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6IPU0/entry","name":"CENPP","description":"Centromere protein P","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28577","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11051095","identifier":"Q9NSP4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NSP4/entry","name":"CENPM","description":"Centromere protein M","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR34436","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11085153","identifier":"Q92674","identifierLink":"https://www.uniprot.org/uniprotkb/Q92674/entry","name":"CENPI","description":"Centromere protein I","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48208","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2340053","identifier":"Q96H22","identifierLink":"https://www.uniprot.org/uniprotkb/Q96H22/entry","name":"CENPN","description":"Centromere protein N","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46790","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2350265","identifier":"Q7L2Z9","identifierLink":"https://www.uniprot.org/uniprotkb/Q7L2Z9/entry","name":"CENPQ","description":"Centromere protein Q","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31345","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2515234","identifier":"Q71F23","identifierLink":"https://www.uniprot.org/uniprotkb/Q71F23/entry","name":"CENPU","description":"Centromere protein U","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-295799","identifier":"Q03188","identifierLink":"https://www.uniprot.org/uniprotkb/Q03188/entry","name":"CENPC","description":"Centromere protein C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5529625","identifier":"Q5EE01","identifierLink":"https://www.uniprot.org/uniprotkb/Q5EE01/entry","name":"CENPW","description":"Centromere protein W","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR34832","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5529649","identifier":"Q8N2Z9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N2Z9/entry","name":"CENPS","description":"Centromere protein S","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22980","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5529694","identifier":"A8MT69","identifierLink":"https://www.uniprot.org/uniprotkb/A8MT69/entry","name":"CENPX","description":"Centromere protein X","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28680","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6871750","identifier":"Q9BS16","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BS16/entry","name":"CENPK","description":"Centromere protein K","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14401","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712105","identifier":"Q13352","identifierLink":"https://www.uniprot.org/uniprotkb/Q13352/entry","name":"ITGB3BP","description":"Centromere protein R","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15581","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-719918","identifier":"Q96BT3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96BT3/entry","name":"CENPT","description":"Centromere protein T","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46904","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-745954","identifier":"Q9BU64","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BU64/entry","name":"CENPO","description":"Centromere protein O","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14582","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8467109","identifier":"Q8N0S6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N0S6/entry","name":"CENPL","description":"Centromere protein L","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5647","complexName":"CENP-A nucleosome complex","organismName":"Homo sapiens; 9606","description":"Replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. 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Mostly found in hair.","predictedComplex":false,"interactors":[{"ac":"EBI-1054946","identifier":"O76013","identifierLink":"https://www.uniprot.org/uniprotkb/O76013/entry","name":"KRT36","description":"Keratin, type I cuticular Ha6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9996498","identifier":"O43790","identifierLink":"https://www.uniprot.org/uniprotkb/O43790/entry","name":"KRT86","description":"Keratin, type II cuticular Hb6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45616","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5664","complexName":"Keratin-80- Keratin-82 dimer complex","organismName":"Homo sapiens; 9606","description":"Part of the intermediate filaments of the cytoskeleton. Mostly found in hair.","predictedComplex":false,"interactors":[{"ac":"EBI-1045341","identifier":"Q9NSB4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NSB4/entry","name":"KRT82","description":"Keratin, type II cuticular Hb2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45616","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3046635","identifier":"Q6KB66","identifierLink":"https://www.uniprot.org/uniprotkb/Q6KB66/entry","name":"KRT80","description":"Keratin, type II cytoskeletal 80","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45616","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5665","complexName":"Keratin-25 - Keratin-71 dimer complex","organismName":"Homo sapiens; 9606","description":"Part of the intermediate filaments of the cytoskeleton. Mostly found in hair.","predictedComplex":false,"interactors":[{"ac":"EBI-11980019","identifier":"Q7Z3Z0","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z3Z0/entry","name":"KRT25","description":"Keratin, type I cytoskeletal 25","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2952676","identifier":"Q3SY84","identifierLink":"https://www.uniprot.org/uniprotkb/Q3SY84/entry","name":"KRT71","description":"Keratin, type II cytoskeletal 71","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45616","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5666","complexName":"CCAAT-binding factor complex, nfya-1 variant","organismName":"Caenorhabditis elegans; 6239","description":"Transcription factor complex, which binds to the 5'-CCAAT-3' box motif found in the promoters of its target genes to regulate their expression. 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May regulate egl-5 expression in association with the Polycomb Repressive Complex 2 (CPX-368).","predictedComplex":false,"interactors":[{"ac":"EBI-318121","identifier":"G5EEG1","identifierLink":"https://www.uniprot.org/uniprotkb/G5EEG1/entry","name":"nfya-1","description":"Nuclear transcription factor Y subunit nfya-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12632","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-325152","identifier":"O17286","identifierLink":"https://www.uniprot.org/uniprotkb/O17286/entry","name":"nfyb-1","description":"Nuclear transcription factor Y subunit nfyb-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11064","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-367886","identifier":"O17072","identifierLink":"https://www.uniprot.org/uniprotkb/O17072/entry","name":"nfyc-1","description":"Nuclear transcription factor Y subunit nfyc-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10252","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5667","complexName":"CCAAT-binding factor complex, nfya-2 variant","organismName":"Caenorhabditis elegans; 6239","description":"Transcription factor complex, which binds to the 5'-CCAAT-3' box motif found in the promoters of its target genes to regulate their expression. 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Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability.","predictedComplex":false,"interactors":[{"ac":"EBI-1199859","identifier":"P0C0S5","identifierLink":"https://www.uniprot.org/uniprotkb/P0C0S5/entry","name":"H2AZ1","description":"Histone H2A.Z","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23430","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302023","identifier":"P62805","identifierLink":"https://www.uniprot.org/uniprotkb/P62805/entry","name":"H4C16","description":"Histone H4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10484","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6150252","identifier":"P06899","identifierLink":"https://www.uniprot.org/uniprotkb/P06899/entry","name":"H2BC11","description":"Histone H2B type 1-J","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23428","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-79722","identifier":"P68431","identifierLink":"https://www.uniprot.org/uniprotkb/P68431/entry","name":"H3C1","description":"Histone H3.1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11426","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9636457","identifier":"CHEBI:4705","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:4705","name":"double-stranded dna","description":"double-stranded DNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-5671","complexName":"Nucleosome, variant H3.1-H2A.V-H2B.1","organismName":"Homo sapiens; 9606","description":"Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability.","predictedComplex":false,"interactors":[{"ac":"EBI-2954755","identifier":"Q71UI9","identifierLink":"https://www.uniprot.org/uniprotkb/Q71UI9/entry","name":"H2AZ2","description":"Histone H2A.V","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23430","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302023","identifier":"P62805","identifierLink":"https://www.uniprot.org/uniprotkb/P62805/entry","name":"H4C16","description":"Histone H4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10484","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6150252","identifier":"P06899","identifierLink":"https://www.uniprot.org/uniprotkb/P06899/entry","name":"H2BC11","description":"Histone H2B type 1-J","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23428","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-79722","identifier":"P68431","identifierLink":"https://www.uniprot.org/uniprotkb/P68431/entry","name":"H3C1","description":"Histone H3.1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11426","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9636457","identifier":"CHEBI:4705","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:4705","name":"double-stranded dna","description":"double-stranded DNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-5674","complexName":"Transcription elongation complex","organismName":"Escherichia coli (strain K12); 83333","description":"RNA polymerase (RNAP)-containing complex that suppresses transcription termination and accelerates the rate of transcription elongation and folding of ribosomal RNA. During elongation, the sigma factor is replaced by nupA and nupG binding to RNAP and enhances RNAP pausing at specific sites. nusA also binds to rRNA just downstream to the single stranded BOXA motif. nusB appears to enhance nusE binding to BOXA RNA and the RNA polymerase complex. NusG increases the RNA chain elongation rate.","predictedComplex":false,"interactors":[{"ac":"EBI-369628","identifier":"P0AFG0","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFG0/entry","name":"nusG","description":"Transcription termination/antitermination protein NusG","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30265","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-370560","identifier":"P0A800","identifierLink":"https://www.uniprot.org/uniprotkb/P0A800/entry","name":"rpoZ","description":"DNA-directed RNA polymerase subunit omega","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-543604","identifier":"P0A8T7","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8T7/entry","name":"rpoC","description":"DNA-directed RNA polymerase subunit beta'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR19376","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544602","identifier":"P0A7R5","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7R5/entry","name":"rpsJ","description":"Small ribosomal subunit protein uS10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11700","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544985","identifier":"P0A7Z4","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7Z4/entry","name":"rpoA","description":"DNA-directed RNA polymerase subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32108","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-544996","identifier":"P0A8V2","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8V2/entry","name":"rpoB","description":"DNA-directed RNA polymerase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR20856","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-551571","identifier":"P0AFF6","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFF6/entry","name":"nusA","description":"Transcription termination/antitermination protein NusA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR22648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-555387","identifier":"P0A780","identifierLink":"https://www.uniprot.org/uniprotkb/P0A780/entry","name":"nusB","description":"Transcription antitermination protein NusB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11078","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-5675","complexName":"Classical and lectin pathway C3 convertase complex C4b2a-A","organismName":"Homo sapiens; 9606","description":"A serine-type endopeptidase complex of the lectin and classical pathway of complement activation of the innate immune system. Cleaves Complement C3 precurser (P01024) into anaphylatoxin C3A (P01024-PRO_0000005910) and nascent convertase core-component C3b (CPX-973). Components are cleaved by the C1s component of Complement C1 complex (CPX-1920) of the classical pathway or lectins of the lectin pathway. Binds to pathogen cells via its reactive thioester moiety. \r\n\r\nCan also act as C5 convertase by cleaving Complement C5 precurser (P01031) into anaphylatoxin C5A (P01031-PRO_0000005988) and C5b (P01031-PRO_0000005985, P01031-PRO_0000005989) but with low efficiency. \r\n\r\nActs as an opsonin and interacts with glycoproteins and carbohydrates on pathogenic or apoptotic target cell surfaces through its reactive thioester moiety. Opsonization of target cells leads to enhanced phagocytosis, lysis of target cells via membrane attack complex (CPX-6159) assembly, clearance of antibody-antigen complexes and up-regulation of the adaptive response.","predictedComplex":false,"interactors":[{"ac":"EBI-25474387","identifier":"P0C0L4-PRO_0000005972","identifierLink":"https://www.uniprot.org/uniprotkb/P0C0L4-PRO_0000005972/entry","name":"C4A","description":"Complement C4 gamma chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25474394","identifier":"P06681-PRO_0000027612","identifierLink":"https://www.uniprot.org/uniprotkb/P06681-PRO_0000027612/entry","name":"C2","description":"Complement C2a fragment","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25474399","identifier":"P0C0L4-PRO_0000005970","identifierLink":"https://www.uniprot.org/uniprotkb/P0C0L4-PRO_0000005970/entry","name":"C4A","description":"Complement C4b-A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-25474406","identifier":"P0C0L4-PRO_0000005966","identifierLink":"https://www.uniprot.org/uniprotkb/P0C0L4-PRO_0000005966/entry","name":"C4A","description":"Complement C4 beta chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-5681","complexName":"Enoyl CoA hydratase/isomerase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes consecutive steps along the phenylacetate degradation pathway: the unusual rearrangement of the 2-oxepin-2(3H)-ylideneacetyl-CoA (oxepin-CoA) to the alpha,beta-unsaturated thioester 2,3-dehydroadipyl-CoA and the  reversible conversion of  2,3-dehydroadipyl-CoA into 3-hydroxyadipyl-CoA. The PA utilization pathway is the main mechanism for degradation of a variety of organic compounds.","predictedComplex":false,"interactors":[{"ac":"EBI-1115747","identifier":"P76082","identifierLink":"https://www.uniprot.org/uniprotkb/P76082/entry","name":"paaF","description":"2,3-dehydroadipyl-CoA hydratase","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11941","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1118484","identifier":"P77467","identifierLink":"https://www.uniprot.org/uniprotkb/P77467/entry","name":"paaG","description":"1,2-epoxyphenylacetyl-CoA isomerase","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11941","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5682","complexName":"SARS-CoV-2 cleaved Spike protein complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","description":"Spike protein complex of the SARS-CoV-2 coronavirus that binds to human receptor ACE2 (Q9BYF1). May also bind CLEC4M/DC-SIGNR (Q9H2X3) (by homology from SARS-CoV-S (CPX-5694)). Cell entry via binding of Spike to the ACE2 receptor (CPX-5683) relies on two proteolytic cleavage events facilitated by host proteases, such as furin (P09958) and TMPRSS2 (O15393): the first cleavage occurs at the S1/S2 site, the second at the S2' site. Cleavage at the S1/S2 site can occur prior to exit from an infected cell or once bound to ACE2 on the surface of a new host cell. Cleavage at the S2' site occurs only on the surface of the new host cell. While furin is active in the Golgi and on the plasma membrane and can cleave Spike at both cleavage sites, TMPRSS2 only facilitates S2' cleavage on the plasma membrane. \r\n\r\nWhile cleaved Spike greatly enhances viral entry into the host cell, it is not strictly required for infection and not all Spike complexes on the viral surface are cleaved (CPX-7042). Alternatively, virions can enter the cell via the endosomal pathway and the use of an alternative protease, e.g. cathepsin L (P07711). Some variants of Spike carry mutations in the furin cleavage site that increases the proportion of cleaved Spike complexes which is linked to a higher infectivity of these variants.","predictedComplex":false,"interactors":[{"ac":"EBI-25490323","identifier":"P0DTC2-PRO_0000449647","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTC2-PRO_0000449647/entry","name":"S","description":"Spike protein S1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]},{"ac":"EBI-25490326","identifier":"P0DTC2-PRO_0000449648","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTC2-PRO_0000449648/entry","name":"S","description":"Spike protein S2","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]}]},{"complexAC":"CPX-5683","complexName":"SARS-CoV-2 Spike - human ACE2 receptor complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","description":"Binding of SARS-CoV-2 coronavirus Spike protein to human receptor ACE2 facilitates virus entry into host cell.","predictedComplex":false,"interactors":[{"ac":"EBI-25490330","identifier":"CPX-5682","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-5682","name":"SARS-CoV-2 cleaved Spike protein complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]},{"ac":"EBI-7730807","identifier":"Q9BYF1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BYF1/entry","name":"ACE2","description":"Angiotensin-converting enzyme 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10514","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5684","complexName":"SARS-CoV-2 Spike - human ACE2-SLC6A19 complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","description":"Internalised SARS-CoV-2 coronavirus Spike - human receptor ACE2 complex binds amino acid transporter SLC6A19 (B0AT1). SLC6A19 may play a regulatory role for the enteric infections of some coronaviruses.","predictedComplex":false,"interactors":[{"ac":"EBI-25475705","identifier":"Q695T7","identifierLink":"https://www.uniprot.org/uniprotkb/Q695T7/entry","name":"SLC6A19","description":"Sodium-dependent neutral amino acid transporter B(0)AT1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11616","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25490330","identifier":"CPX-5682","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-5682","name":"SARS-CoV-2 cleaved Spike protein complex","description":null,"stochiometry":"minValue: 2, maxValue: 2","interactorType":"stable complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]},{"ac":"EBI-7730807","identifier":"Q9BYF1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BYF1/entry","name":"ACE2","description":"Angiotensin-converting enzyme 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10514","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5685","complexName":"SARS-CoV-2 main protease complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","description":"The 3C-like protease of the SARS-CoV-2 coronavirus required for processing the polyproteins that are translated from the viral RNA. Cleaves at 11 cleavage sites on the large polyprotein 1ab (P0DTD1); the recognition sequence at most sites is [ILMVF]-Q-|-[SGACN].","predictedComplex":false,"interactors":[{"ac":"EBI-25475864","identifier":"P0DTD1-PRO_0000449623","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTD1-PRO_0000449623/entry","name":"rep","description":"3C-like proteinase nsp5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]}]},{"complexAC":"CPX-5686","complexName":"SARS-CoV-2 nucleocapsid complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","description":"Forms the helical ribonucleocapsid (RNP) of the SARS-CoV coronavirus. Packages the positive strand viral genome RNA and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M (P0DTC5). Recognises and binds to a packaging signal, a cis-regulatory element encoded within the viral RNA. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. \r\n\r\nForms viral-like particles (VLPs) together with proteins M, E  (P0DTC4) and S (P0DTC2) without the requirement of genomic RNA. \r\n\r\nInhibits type I interferon (IFN-beta) activation and downstream innate immune responses.","predictedComplex":false,"interactors":[{"ac":"EBI-25475856","identifier":"P0DTC9","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTC9/entry","name":"N","description":"Nucleoprotein","stochiometry":null,"interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]}]},{"complexAC":"CPX-5687","complexName":"SARS-CoV-2 NSP9 complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","description":"RNA binding complex of the SARS-CoV-2 coronavirus. It has been speculated that nsp9 dimers bind to single-stranded nascent and template strands as they emerge from the channel of the nsp7-nsp8 primase complex (CPX-5690) at a time when stable secondary structures have not yet formed, protecting ssRNAs from ribonucleolytic cleavage.","predictedComplex":false,"interactors":[{"ac":"EBI-25475877","identifier":"P0DTD1-PRO_0000449627","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTD1-PRO_0000449627/entry","name":"rep","description":"Viral protein genome-linked nsp9","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]}]},{"complexAC":"CPX-5688","complexName":"SARS-CoV-2 NSP10-NSP16 2'-O-methyltransferase complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","description":"2'-O-methyltransferase complex of the SARS-CoV-2 coronavirus which mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs. using S-adenosyl-L-methionine (SAM, CHEBI:15414) as the methyl donor. The cap structure is essential for efficient splicing, nuclear export, translation and mRNA stability.","predictedComplex":false,"interactors":[{"ac":"EBI-25475880","identifier":"P0DTD1-PRO_0000449628","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTD1-PRO_0000449628/entry","name":"rep","description":"Non-structural protein 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]},{"ac":"EBI-25492395","identifier":"P0DTD1-PRO_0000449633","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTD1-PRO_0000449633/entry","name":"rep","description":"2'-O-methyltransferase nsp16","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]}]},{"complexAC":"CPX-5689","complexName":"SARS-CoV-2 NSP15 complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","description":"The SARS-CoV-2 coronavirus uridylate-specific endoribonuclease complex which cleaves RNA of uridylates through the formation of a 2′-3′ cyclic phosphodiester and 5'-hydroxyl termini, acting on both, single-and double stranded RNA.","predictedComplex":false,"interactors":[{"ac":"EBI-25475891","identifier":"P0DTD1-PRO_0000449632","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTD1-PRO_0000449632/entry","name":"rep","description":"Uridylate-specific endoribonuclease nsp15","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]}]},{"complexAC":"CPX-5691","complexName":"SARS-CoV-2 NSP3-NSP4-NSP6 complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","description":"Complex of the SARS-CoV-2 coronavirus involved in replication. Potentially acts by inducing rearrangement of the host membranes to form double-membrane vesicles which may form a framework for viral genome replication by localizing and concentrating the necessary factors and possibly providing protection from host cell defenses. \r\n\r\nThe multi-spanning transmembrane domains in nsp3, nsp4 and nsp6 may serve as a scaffold for the assembly of the membrane-associated replication/transcription complex (RTC), a large multisubunit assembly that is comprised of more than a dozen proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-25475862","identifier":"P0DTD1-PRO_0000449622","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTD1-PRO_0000449622/entry","name":"rep","description":"Non-structural protein 4","stochiometry":null,"interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]},{"ac":"EBI-25475868","identifier":"P0DTD1-PRO_0000449624","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTD1-PRO_0000449624/entry","name":"rep","description":"Non-structural protein 6","stochiometry":null,"interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]},{"ac":"EBI-25492388","identifier":"P0DTD1-PRO_0000449621","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTD1-PRO_0000449621/entry","name":"rep","description":"Papain-like protease nsp3","stochiometry":null,"interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]}]},{"complexAC":"CPX-5694","complexName":"SARS-CoV cleaved Spike protein complex","organismName":"Severe acute respiratory syndrome coronavirus; 694009","description":"Spike protein complex of the SARS-CoV coronavirus that binds to human receptor ACE2 (Q9BYF1) and CLEC4M/DC-SIGNR (Q9H2X3). Cell entry via binding of Spike to the ACE2 receptor (CPX-5695) relies on two proteolytic cleavage events facilitated by host proteases, such as furin (P09958) and TMPRSS2 (O15393): the first cleavage occurs at the S1/S2 site, the second at the S2' site. Cleavage at the S1/S2 site can occur prior to exit from an infected cell or once bound to ACE2 on the surface of a new host cell. Cleavage at the S2' site occurs only on the surface of the new host cell. While furin is active in the Golgi and on the plasma membrane and can cleave Spike at both cleavage sites, TMPRSS2 only facilitates S2' cleavage on the plasma membrane. \r\n\r\nWhile cleaved Spike greatly enhances viral entry into the host cell, it is not strictly required for infection and not all Spike complexes on the viral surface are cleaved. Contrary to the activity of Spike in related SARS-CoV-2 (CPX-5682), owing to a different furin cleavage site, cleavage and activation of SARS-CoV Spike by furin and TMPRSS2 is less efficient. It is therefore thought that SARS-CoV virions may rely more heavily on the less efficient cell entry process via endosomes and the use of an alternative protease, e.g. cathepsin L (P07711).","predictedComplex":false,"interactors":[{"ac":"EBI-25474961","identifier":"P59594-PRO_0000037210","identifierLink":"https://www.uniprot.org/uniprotkb/P59594-PRO_0000037210/entry","name":"S","description":"Spike protein S2","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus; 694009","xrefs":[]},{"ac":"EBI-25475261","identifier":"P59594-PRO_0000037209","identifierLink":"https://www.uniprot.org/uniprotkb/P59594-PRO_0000037209/entry","name":"S","description":"Spike protein S1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus; 694009","xrefs":[]}]},{"complexAC":"CPX-5695","complexName":"SARS-CoV Spike - human ACE2 receptor complex","organismName":"Severe acute respiratory syndrome coronavirus; 694009","description":"Binding of SARS-CoV coronavirus Spike protein to human receptor ACE2 facilitates virus entry into host cell.","predictedComplex":false,"interactors":[{"ac":"EBI-25492456","identifier":"CPX-5694","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-5694","name":"SARS-CoV cleaved Spike protein complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Severe acute respiratory syndrome coronavirus; 694009","xrefs":[]},{"ac":"EBI-7730807","identifier":"Q9BYF1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BYF1/entry","name":"ACE2","description":"Angiotensin-converting enzyme 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10514","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5696","complexName":"SARS-CoV Spike - human CLEC4M lectin complex","organismName":"Severe acute respiratory syndrome coronavirus; 694009","description":"Binding of SARS-CoV coronavirus Spike protein to human lectin CLEC4M expressed on innate immune cells and subsequent internalisation may lead to virus clearance or, on the contrary, result in spread of the virus to susceptible cells, or even other hosts.","predictedComplex":false,"interactors":[{"ac":"EBI-1391211","identifier":"Q9H2X3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H2X3/entry","name":"CLEC4M","description":"C-type lectin domain family 4 member M","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25492456","identifier":"CPX-5694","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-5694","name":"SARS-CoV cleaved Spike protein complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Severe acute respiratory syndrome coronavirus; 694009","xrefs":[]}]},{"complexAC":"CPX-5698","complexName":"AMPK complex, alpha1-beta1-gamma1 variant","organismName":"Mus musculus; 10090","description":"Energy sensor serine/threonine kinase that plays a key role in regulating cellular energy metabolism. Energy stress manifests as a drop in the ratio of adenosine triphosphate (ATP) to AMP/ADP, which activates AMPK's kinase activity, allowing it to upregulate ATP-generating catabolic pathways and to reduce energy-consuming catabolic pathways and cellular programs: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators.","predictedComplex":false,"interactors":[{"ac":"EBI-2366248","identifier":"Q9R078","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R078/entry","name":"Prkab1","description":"5'-AMP-activated protein kinase subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7282395","identifier":"Q5EG47","identifierLink":"https://www.uniprot.org/uniprotkb/Q5EG47/entry","name":"Prkaa1","description":"5'-AMP-activated protein kinase catalytic subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7927886","identifier":"O54950","identifierLink":"https://www.uniprot.org/uniprotkb/O54950/entry","name":"Prkag1","description":"5'-AMP-activated protein kinase subunit gamma-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5699","complexName":"Cytoplasmic dynein complex, variant 1","organismName":"Mus musculus; 10090","description":"Cytoplasmic motor for the intracellular retrograde motility of vesicles and organelles along microtubules.","predictedComplex":false,"interactors":[{"ac":"EBI-25495024","identifier":"Q6PDL0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDL0/entry","name":"Dync1li2","description":"Cytoplasmic dynein 1 light intermediate chain 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12688","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-349121","identifier":"P63168","identifierLink":"https://www.uniprot.org/uniprotkb/P63168/entry","name":"Dynll1","description":"Dynein light chain 1, cytoplasmic","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642797","identifier":"P51807","identifierLink":"https://www.uniprot.org/uniprotkb/P51807/entry","name":"Dynlt1","description":"Dynein light chain Tctex-type 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-645061","identifier":"Q9JHU4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JHU4/entry","name":"Dync1h1","description":"Cytoplasmic dynein 1 heavy chain 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-776055","identifier":"O88487","identifierLink":"https://www.uniprot.org/uniprotkb/O88487/entry","name":"Dync1i2","description":"Cytoplasmic dynein 1 intermediate chain 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8320234","identifier":"P62627","identifierLink":"https://www.uniprot.org/uniprotkb/P62627/entry","name":"Dynlrb1","description":"Dynein light chain roadblock-type 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5700","complexName":"Kinetochore SKA complex","organismName":"Mus musculus; 10090","description":"A microtubule-binding subcomplex of the outer kinetochore that is essential for proper chromosome segregation.","predictedComplex":false,"interactors":[{"ac":"EBI-10972845","identifier":"Q9CPV1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CPV1/entry","name":"Ska1","description":"SKA complex subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR28573","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25495084","identifier":"Q8C263","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C263/entry","name":"Ska3","description":"SKA complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR48118","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9987825","identifier":"Q9CR46","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CR46/entry","name":"Ska2","description":"SKA complex subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR32017","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5701","complexName":"Kinetochore MIS12 complex","organismName":"Mus musculus; 10090","description":"Required for normal chromosome alignment and segregation, kinetochore formation during mitosis, proper kinetochore microtubule attachments and for the spindle assembly checkpoint. The complex plays a role in establishing a bipolar spindle-kinetochore interaction by joining kinetochore subunits contacting DNA to those contacting microtubules\r\n\r\nKNL1 (CPX-5702), MIS12 and NDC80 (CPX-551) form the KMN protein network.","predictedComplex":false,"interactors":[{"ac":"EBI-25495179","identifier":"Q8K305","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K305/entry","name":"Nsl1","description":"Kinetochore-associated protein NSL1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR31749","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2552696","identifier":"Q9CYC5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CYC5/entry","name":"Dsn1","description":"Kinetochore-associated protein DSN1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14778","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2553800","identifier":"Q9CY25","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CY25/entry","name":"Mis12","description":"Protein MIS12 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8572549","identifier":"Q9CPV5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CPV5/entry","name":"Pmf1","description":"Polyamine-modulated factor 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15459","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5702","complexName":"Kinetochore KNL1 complex","organismName":"Mus musculus; 10090","description":"Required for normal chromosome alignment and segregation and for kinetochore formation during mitosis and for proper kinetochore microtubule attachments. Binds, at its outer end, to kinetochore microtubule and, at its inner end, to the MIS12 complex (CPX-5701).\r\n\r\nKNL1, MIS12 and NCD80 (CPX-551) form the KMN protein network.","predictedComplex":false,"interactors":[{"ac":"EBI-2551595","identifier":"Q9CQU5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQU5/entry","name":"Zwint","description":"Outer kinetochore KNL1 complex subunit ZWINT","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR31504","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2552633","identifier":"Q66JQ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q66JQ7/entry","name":"Knl1","description":"Outer kinetochore KNL1 complex subunit KNL1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-5703","complexName":"KMN complex","organismName":"Mus musculus; 10090","description":"Part of the protein architecture within kinetochores that links centromeric DNA to the plus ends of spindle microtubules.","predictedComplex":false,"interactors":[{"ac":"EBI-1209357","identifier":"CPX-551","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-551","name":"Ndc80 complex","description":"Ndc80 complex","stochiometry":null,"interactorType":"stable complex","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-25495108","identifier":"CPX-5701","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-5701","name":"Kinetochore MIS12 complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-25495142","identifier":"CPX-5702","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-5702","name":"Kinetochore KNL1 complex","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-5704","complexName":"Kinetochore CCAN complex","organismName":"Mus musculus; 10090","description":"Interacts with duplex DNA and facilitates accurate chromosome segregation. Plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. It may be involved in incorporation of newly synthesized Cenpa (O35216) into centromeres to form CENP-A nucleosomes (CPX-5705). Required for chromosome congression and efficient alignment of the chromosomes on a metaphase plate.","predictedComplex":false,"interactors":[{"ac":"EBI-11085146","identifier":"Q9QYM8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9QYM8/entry","name":"Cenph","description":"Centromere protein H","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR48122","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1186252","identifier":"P49452","identifierLink":"https://www.uniprot.org/uniprotkb/P49452/entry","name":"Cenpc","description":"Centromere protein C","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25495357","identifier":"Q9CQ82","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQ82/entry","name":"Itgb3bp","description":"Centromere protein R","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15581","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25495387","identifier":"Q9D084","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D084/entry","name":"Cenps","description":"Centromere protein S","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22980","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25495426","identifier":"Q3TJM4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TJM4/entry","name":"Cenpt","description":"Centromere protein T","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46904","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25495462","identifier":"Q8C4M7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C4M7/entry","name":"Cenpu","description":"Centromere protein U","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR32222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25495488","identifier":"Q3URR0","identifierLink":"https://www.uniprot.org/uniprotkb/Q3URR0/entry","name":"Cenpw","description":"Centromere protein W","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR34832","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25495514","identifier":"Q8C4X1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C4X1/entry","name":"Cenpx","description":"Centromere protein X","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR28680","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25495551","identifier":"Q3U3S3","identifierLink":"https://www.uniprot.org/uniprotkb/Q3U3S3/entry","name":"Cenpl","description":"Centromere protein L","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR31740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8369541","identifier":"Q8K1K4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K1K4/entry","name":"Cenpi","description":"Centromere protein I","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR48208","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8572186","identifier":"Q9CQA0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQA0/entry","name":"Cenpm","description":"Centromere protein M","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR34436","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8572352","identifier":"Q9CPQ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CPQ5/entry","name":"Cenpq","description":"Centromere protein Q","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR31345","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8572410","identifier":"Q9ESN5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ESN5/entry","name":"Cenpk","description":"Centromere protein K","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14401","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8572472","identifier":"Q8K015","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K015/entry","name":"Cenpo","description":"Centromere protein O","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14582","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8573253","identifier":"Q9CZW2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CZW2/entry","name":"Cenpn","description":"Centromere protein N","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46790","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8573270","identifier":"Q9CZ92","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CZ92/entry","name":"Cenpp","description":"Centromere protein P","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR28577","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5705","complexName":"CENP-A nucleosome complex","organismName":"Mus musculus; 10090","description":"Replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. Required for recruitment and assembly of kinetochore proteins, and as a consequence required for progress through mitosis, chromosome segregation and cytokinesis","predictedComplex":false,"interactors":[{"ac":"EBI-2527113","identifier":"C0HKE2","identifierLink":"https://www.uniprot.org/uniprotkb/C0HKE2/entry","name":"H2ac4","description":"Histone H2A type 1-B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23430","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25469870","identifier":"CHEBI:75909","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:75909","name":"double-stranded dna fragment","description":"double-stranded DNA fragment","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-299632","identifier":"P62806","identifierLink":"https://www.uniprot.org/uniprotkb/P62806/entry","name":"H4c11","description":"Histone H4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10484","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7144613","identifier":"P10853","identifierLink":"https://www.uniprot.org/uniprotkb/P10853/entry","name":"H2bc11","description":"Histone H2B type 1-F/J/L","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23428","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8572794","identifier":"O35216","identifierLink":"https://www.uniprot.org/uniprotkb/O35216/entry","name":"Cenpa","description":"Histone H3-like centromeric protein A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11426","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5706","complexName":"SARS-CoV main protease complex","organismName":"Severe acute respiratory syndrome coronavirus; 694009","description":"The 3C-like protease of the SARS-CoV coronavirus required for processing the polyproteins that are translated from the viral RNA. Cleaves at 11 cleavage sites on the large polyprotein 1ab (P0C6X7); the recognition sequence at most sites is [ILMVF]-Q-|-[SGACN].","predictedComplex":false,"interactors":[{"ac":"EBI-25487250","identifier":"P0C6X7-PRO_0000037312","identifierLink":"https://www.uniprot.org/uniprotkb/P0C6X7-PRO_0000037312/entry","name":"rep","description":"3C-like proteinase nsp5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus; 694009","xrefs":[]}]},{"complexAC":"CPX-5707","complexName":"SARS-CoV 3'-5' exoribonuclease proof-reading complex","organismName":"Severe acute respiratory syndrome coronavirus; 694009","description":"The SARS-CoV coronavirus 3'-5' exoribonuclease complex which strictly targets double-stranded RNA and can also selectively remove a mismatched ribonucleotide at the 3'-end of a dsRNA substrate. Formation of the NSP10-NSP14 complex strongly enhances the exonuclease activity of the bifunctional NSP14 and enhances the fidelity of RNA synthesis by correcting nucleotide incorporation errors made by the RNA-dependent RNA polymerase. May bind to, and act with the nsp7/nsp8/nsp12 polymerase complex (CPX-5717). Proof-reading exonuclease activity may explain why coronaviruses have the largest RNA genomes known to date. Complex formation does not appear to effect the C-terminal N7-methyltransferase activity of NSP14 involved in RNA cap modification.","predictedComplex":false,"interactors":[{"ac":"EBI-25487277","identifier":"P0C6X7-PRO_0000037317","identifierLink":"https://www.uniprot.org/uniprotkb/P0C6X7-PRO_0000037317/entry","name":"rep","description":"Non-structural protein 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus; 694009","xrefs":[]},{"ac":"EBI-25487328","identifier":"P0C6X7-PRO_0000037320","identifierLink":"https://www.uniprot.org/uniprotkb/P0C6X7-PRO_0000037320/entry","name":"rep","description":"Guanine-N7 methyltransferase nsp14","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus; 694009","xrefs":[]}]},{"complexAC":"CPX-5709","complexName":"SARS-CoV NSP10-NSP16 2'-O-methyltransferase complex","organismName":"Severe acute respiratory syndrome coronavirus; 694009","description":"2'-O-methyltransferase complex of the SARS-CoV coronavirus which mediates mRNA cap 2'-O-ribose methylation to the 5'-cap structure of viral mRNAs using S-adenosyl-L-methionine (SAM, CHEBI:15414) as the methyl donor. The cap structure is essential for efficient splicing, nuclear export, translation and mRNA stability.","predictedComplex":false,"interactors":[{"ac":"EBI-25487235","identifier":"P0C6X7-PRO_0000037322","identifierLink":"https://www.uniprot.org/uniprotkb/P0C6X7-PRO_0000037322/entry","name":"rep","description":"2'-O-methyltransferase nsp16","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus; 694009","xrefs":[]},{"ac":"EBI-25487277","identifier":"P0C6X7-PRO_0000037317","identifierLink":"https://www.uniprot.org/uniprotkb/P0C6X7-PRO_0000037317/entry","name":"rep","description":"Non-structural protein 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus; 694009","xrefs":[]}]},{"complexAC":"CPX-5711","complexName":"SARS-CoV NSP15 complex","organismName":"Severe acute respiratory syndrome coronavirus; 694009","description":"The SARS-CoV coronavirus uridylate-specific endoribonuclease complex which cleaves RNA of uridylates through the formation of a 2′-3′ cyclic phosphodiester and 5'-hydroxyl termini, acting on both, single-and double stranded RNA.","predictedComplex":false,"interactors":[{"ac":"EBI-25487301","identifier":"P0C6X7-PRO_0000037321","identifierLink":"https://www.uniprot.org/uniprotkb/P0C6X7-PRO_0000037321/entry","name":"rep","description":"Uridylate-specific endoribonuclease nsp15","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus; 694009","xrefs":[]}]},{"complexAC":"CPX-5712","complexName":"Nucleosome, variant H3.1-H2A.2-H2B.1","organismName":"Mus musculus; 10090","description":"Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability.","predictedComplex":false,"interactors":[{"ac":"EBI-2527113","identifier":"C0HKE2","identifierLink":"https://www.uniprot.org/uniprotkb/C0HKE2/entry","name":"H2ac4","description":"Histone H2A type 1-B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23430","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-299632","identifier":"P62806","identifierLink":"https://www.uniprot.org/uniprotkb/P62806/entry","name":"H4c11","description":"Histone H4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10484","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7144613","identifier":"P10853","identifierLink":"https://www.uniprot.org/uniprotkb/P10853/entry","name":"H2bc11","description":"Histone H2B type 1-F/J/L","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23428","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-79743","identifier":"P68433","identifierLink":"https://www.uniprot.org/uniprotkb/P68433/entry","name":"H3c1","description":"Histone H3.1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11426","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9636457","identifier":"CHEBI:4705","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:4705","name":"double-stranded dna","description":"double-stranded DNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-5713","complexName":"Nucleosome, variant H3.2-H2A.2-H2B.1","organismName":"Mus musculus; 10090","description":"Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability.","predictedComplex":false,"interactors":[{"ac":"EBI-2527113","identifier":"C0HKE2","identifierLink":"https://www.uniprot.org/uniprotkb/C0HKE2/entry","name":"H2ac4","description":"Histone H2A type 1-B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23430","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2658213","identifier":"P84228","identifierLink":"https://www.uniprot.org/uniprotkb/P84228/entry","name":"H3c13","description":"Histone H3.2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11426","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-299632","identifier":"P62806","identifierLink":"https://www.uniprot.org/uniprotkb/P62806/entry","name":"H4c11","description":"Histone H4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10484","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7144613","identifier":"P10853","identifierLink":"https://www.uniprot.org/uniprotkb/P10853/entry","name":"H2bc11","description":"Histone H2B type 1-F/J/L","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23428","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9636457","identifier":"CHEBI:4705","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:4705","name":"double-stranded dna","description":"double-stranded DNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-5715","complexName":"Nucleosome, variant H3.1-H2A.Z-H2B.1","organismName":"Mus musculus; 10090","description":"Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability.","predictedComplex":false,"interactors":[{"ac":"EBI-299632","identifier":"P62806","identifierLink":"https://www.uniprot.org/uniprotkb/P62806/entry","name":"H4c11","description":"Histone H4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10484","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642131","identifier":"P0C0S6","identifierLink":"https://www.uniprot.org/uniprotkb/P0C0S6/entry","name":"H2az1","description":"Histone H2A.Z","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23430","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7144613","identifier":"P10853","identifierLink":"https://www.uniprot.org/uniprotkb/P10853/entry","name":"H2bc11","description":"Histone H2B type 1-F/J/L","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23428","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-79743","identifier":"P68433","identifierLink":"https://www.uniprot.org/uniprotkb/P68433/entry","name":"H3c1","description":"Histone H3.1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11426","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9636457","identifier":"CHEBI:4705","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:4705","name":"double-stranded dna","description":"double-stranded DNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-5716","complexName":"Nucleosome, variant H3.1-H2A.V-H2B.1","organismName":"Mus musculus; 10090","description":"Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability.","predictedComplex":false,"interactors":[{"ac":"EBI-299632","identifier":"P62806","identifierLink":"https://www.uniprot.org/uniprotkb/P62806/entry","name":"H4c11","description":"Histone H4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10484","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7144613","identifier":"P10853","identifierLink":"https://www.uniprot.org/uniprotkb/P10853/entry","name":"H2bc11","description":"Histone H2B type 1-F/J/L","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23428","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-79743","identifier":"P68433","identifierLink":"https://www.uniprot.org/uniprotkb/P68433/entry","name":"H3c1","description":"Histone H3.1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11426","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9636457","identifier":"CHEBI:4705","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:4705","name":"double-stranded dna","description":"double-stranded DNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9986437","identifier":"Q3THW5","identifierLink":"https://www.uniprot.org/uniprotkb/Q3THW5/entry","name":"H2az2","description":"Histone H2A.V","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23430","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5717","complexName":"SARS-CoV polymerase complex","organismName":"Severe acute respiratory syndrome coronavirus; 694009","description":"RNA-directed 5'-3' RNA polymerase of the SARS-CoV coronavirus which consists of the main polymerase protein NSP12 and a stoichiometric variant of the primase complex (CPX-5710). Extends partially double-stranded RNA templates and is probably also required for transcription initiation, though the mechanism for this has yet to be determined. Complex formation enhances dsRNA binding of the individual protomers.","predictedComplex":false,"interactors":[{"ac":"EBI-25487672","identifier":"P0C6X7-PRO_0000037314","identifierLink":"https://www.uniprot.org/uniprotkb/P0C6X7-PRO_0000037314/entry","name":"rep","description":"Non-structural protein 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus; 694009","xrefs":[]},{"ac":"EBI-25487684","identifier":"P0C6X7-PRO_0000037318","identifierLink":"https://www.uniprot.org/uniprotkb/P0C6X7-PRO_0000037318/entry","name":"rep","description":"RNA-directed RNA polymerase nsp12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus; 694009","xrefs":[]},{"ac":"EBI-25487941","identifier":"P0C6X7-PRO_0000037315","identifierLink":"https://www.uniprot.org/uniprotkb/P0C6X7-PRO_0000037315/entry","name":"rep","description":"Non-structural protein 8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus; 694009","xrefs":[]}]},{"complexAC":"CPX-5718","complexName":"Elongasome complex","organismName":"Escherichia coli (strain K12); 83333","description":"Mediates the process of cell elongation and the maintenance of rod-shaped cell morphology by orchestrating the synthesis and insertion of peptidoglycan into the cylindrical part of the cell wall.","predictedComplex":false,"interactors":[{"ac":"EBI-1124032","identifier":"P0AD65","identifierLink":"https://www.uniprot.org/uniprotkb/P0AD65/entry","name":"mrdA","description":"Peptidoglycan D,D-transpeptidase MrdA","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30627","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1126191","identifier":"P02918","identifierLink":"https://www.uniprot.org/uniprotkb/P02918/entry","name":"mrcA","description":"Penicillin-binding protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32282","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1129185","identifier":"P27434","identifierLink":"https://www.uniprot.org/uniprotkb/P27434/entry","name":"rodZ","description":"Cytoskeleton protein RodZ","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34475","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25757009","identifier":"P0ABH4","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABH4/entry","name":"mreD","description":"Rod shape-determining protein MreD","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR37484","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371008","identifier":"P0A9X4","identifierLink":"https://www.uniprot.org/uniprotkb/P0A9X4/entry","name":"mreB","description":"Cell shape-determining protein MreB","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42749","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-553515","identifier":"P16926","identifierLink":"https://www.uniprot.org/uniprotkb/P16926/entry","name":"mreC","description":"Cell shape-determining protein MreC","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34138","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-554827","identifier":"P0ABG7","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABG7/entry","name":"mrdB","description":"Peptidoglycan glycosyltransferase MrdB","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30474","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5719","complexName":"SARS-CoV NSP9 complex","organismName":"Severe acute respiratory syndrome coronavirus; 694009","description":"RNA binding complex of the SARS-CoV coronavirus. It has been speculated that nsp9 dimers bind to single-stranded nascent and template strands as they emerge from the channel of the nsp7-nsp8 primase complex (CPX-5710) at a time when stable secondary structures have not yet formed, protecting ssRNAs from ribonucleolytic cleavage.","predictedComplex":false,"interactors":[{"ac":"EBI-25475825","identifier":"P0C6X7-PRO_0000037316","identifierLink":"https://www.uniprot.org/uniprotkb/P0C6X7-PRO_0000037316/entry","name":"rep","description":"Viral protein genome-linked nsp9","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus; 694009","xrefs":[]}]},{"complexAC":"CPX-5720","complexName":"SARS-CoV nucleocapsid complex","organismName":"Severe acute respiratory syndrome coronavirus; 694009","description":"Forms the helical ribonucleocapsid (RNP) of the SARS-CoV coronavirus. Packages the positive strand viral genome RNA and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M (P59596). Recognises and binds to a packaging signal, a cis-regulatory element encoded within the viral RNA. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication. \r\n\r\nForms viral-like particles (VLPs) together with proteins M, E  (P59637) and S (P59594) without the requirement of genomic RNA. \r\n\r\nInhibits type I interferon (IFN-beta) activation and downstream innate immune responses.","predictedComplex":false,"interactors":[{"ac":"EBI-7602718","identifier":"P59595","identifierLink":"https://www.uniprot.org/uniprotkb/P59595/entry","name":"N","description":"Nucleoprotein","stochiometry":null,"interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus; 694009","xrefs":[]}]},{"complexAC":"CPX-5721","complexName":"SARS-CoV NSP3-NSP4-NSP6 complex","organismName":"Severe acute respiratory syndrome coronavirus; 694009","description":"Complex of the SARS-CoV coronavirus involved in replication. Potentially acts by inducing rearrangement of the host membranes to form double-membrane vesicles which may form a framework for viral genome replication by localizing and concentrating the necessary factors and possibly providing protection from host cell defenses. \r\n\r\nThe multi-spanning transmembrane domains in nsp3, nsp4 and nsp6 may serve as a scaffold for the assembly of the membrane-associated replication/transcription complex (RTC), a large multisubunit assembly that is comprised of more than a dozen proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-25474079","identifier":"P0C6X7-PRO_0000037311","identifierLink":"https://www.uniprot.org/uniprotkb/P0C6X7-PRO_0000037311/entry","name":"rep","description":"Papain-like protease nsp3","stochiometry":null,"interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus; 694009","xrefs":[]},{"ac":"EBI-25487192","identifier":"P0C6X7-PRO_0000037313","identifierLink":"https://www.uniprot.org/uniprotkb/P0C6X7-PRO_0000037313/entry","name":"rep","description":"Non-structural protein 6","stochiometry":null,"interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus; 694009","xrefs":[]},{"ac":"EBI-25488721","identifier":"P0C6X7-PRO_0000283841","identifierLink":"https://www.uniprot.org/uniprotkb/P0C6X7-PRO_0000283841/entry","name":"rep","description":"Non-structural protein 4","stochiometry":null,"interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus; 694009","xrefs":[]}]},{"complexAC":"CPX-5741","complexName":"Prohibitin complex","organismName":"Homo sapiens; 9606","description":"Chaperone which is essential for mitochondrial biogenesis and degradation, and for the mitochondrial stress response. Inhibits m-AAA and OMA1 proteases (Q96E52) and is recruited to cardiolipin-enriched mitochondrial membranes by STOML2 protein (Q9UJZ1), resulting in a reciprocal protein stabilization. The stabilization of the PHB complex affects the maturation of cardiolipin that, in turn, together with the PHB complex, promotes the stabilization of the dynamin-related GTPase OPA1 (O60313) and the formation of a respiratory chain supercomplex. The PHB complex also ensures a correct biogenesis of ATP synthase.","predictedComplex":false,"interactors":[{"ac":"EBI-354213","identifier":"P35232","identifierLink":"https://www.uniprot.org/uniprotkb/P35232/entry","name":"PHB1","description":"Prohibitin 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358348","identifier":"Q99623","identifierLink":"https://www.uniprot.org/uniprotkb/Q99623/entry","name":"PHB2","description":"Prohibitin-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5692","complexName":"SARS-CoV-2 3'-5' exoribonuclease proof-reading complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","description":"The SARS-CoV-2 coronavirus 3'-5' exoribonuclease complex which strictly targets double-stranded RNA and can selectively remove a mismatched ribonucleotide at the 3'-end of a dsRNA substrate. Formation of the NSP10-NSP14 complex strongly enhances the exonuclease activity of the bifunctional NSP14 and enhances the fidelity of RNA synthesis by correcting nucleotide incorporation errors made by the RNA-dependent RNA polymerase. May bind to, and act with the nsp7/nsp8/nsp12 polymerase complex (CPX-5742). Proof-reading exonuclease activity may explain why coronaviruses have the largest RNA genomes known to date. Complex formation does not appear to effect the C-terminal N7-methyltransferase activity of NSP14 involved in RNA cap modification.","predictedComplex":false,"interactors":[{"ac":"EBI-25475880","identifier":"P0DTD1-PRO_0000449628","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTD1-PRO_0000449628/entry","name":"rep","description":"Non-structural protein 10","stochiometry":null,"interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]},{"ac":"EBI-25475920","identifier":"P0DTD1-PRO_0000449631","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTD1-PRO_0000449631/entry","name":"rep","description":"Guanine-N7 methyltransferase nsp14","stochiometry":null,"interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]}]},{"complexAC":"CPX-5742","complexName":"SARS-CoV-2 polymerase complex","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","description":"RNA-directed 5'-3' RNA polymerase of the SARS-CoV-2 coronavirus which consists of the main polymerase protein NSP12 and a stoichiometric variant of the primase complex (CPX-5690). Extends partially double-stranded RNA templates and is probably also required for transcription initiation, though the mechanism for this has yet to be determined. Complex formation enhances dsRNA binding of the individual protomers.","predictedComplex":false,"interactors":[{"ac":"EBI-25475871","identifier":"P0DTD1-PRO_0000449625","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTD1-PRO_0000449625/entry","name":"rep","description":"Non-structural protein 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]},{"ac":"EBI-25475874","identifier":"P0DTD1-PRO_0000449626","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTD1-PRO_0000449626/entry","name":"rep","description":"Non-structural protein 8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]},{"ac":"EBI-25475885","identifier":"P0DTD1-PRO_0000449629","identifierLink":"https://www.uniprot.org/uniprotkb/P0DTD1-PRO_0000449629/entry","name":"rep","description":"RNA-directed RNA polymerase nsp12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Severe acute respiratory syndrome coronavirus 2; 2697049","xrefs":[]}]},{"complexAC":"CPX-5743","complexName":"Prohibitin complex","organismName":"Mus musculus; 10090","description":"Chaperone which is essential for mitochondrial biogenesis and degradation, and for the mitochondrial stress response. Inhibits m-AAA and OMA1 proteases (Q9D8H7) and is recruited to cardiolipin-enriched mitochondrial membranes by STOML2 protein (Q99JB2), resulting in a reciprocal protein stabilization. The stabilization of the PHB complex affects the maturation of cardiolipin (CHEBI:28494) that, in turn, together with the PHB complex, promotes the stabilization of the dynamin-related GTPase OPA1 (P58281) and the formation of a respiratory chain supercomplex. The PHB complex also ensures a correct biogenesis of ATP synthase.","predictedComplex":false,"interactors":[{"ac":"EBI-298507","identifier":"P67778","identifierLink":"https://www.uniprot.org/uniprotkb/P67778/entry","name":"Phb1","description":"Prohibitin 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-445002","identifier":"O35129","identifierLink":"https://www.uniprot.org/uniprotkb/O35129/entry","name":"Phb2","description":"Prohibitin-2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5744","complexName":"Nascent polypeptide-associated complex","organismName":"Caenorhabditis elegans; 6239","description":"Protein chaperone that reversibly binds to cytoplasmic ribosomes. Prevents inappropriate targeting of non-secretory polypeptides to the endoplasmic reticulum (ER) by binding to nascent polypeptide chains as they emerge from the ribosome and blocking their interaction with the signal recognition particle (SRP), which normally targets nascent secretory peptides to the ER. May play a role in modulating the unfolded protein response in response to heat stress.","predictedComplex":false,"interactors":[{"ac":"EBI-326530","identifier":"Q18885","identifierLink":"https://www.uniprot.org/uniprotkb/Q18885/entry","name":"icd-1","description":"Transcription factor BTF3 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-326549","identifier":"Q86S66","identifierLink":"https://www.uniprot.org/uniprotkb/Q86S66/entry","name":"icd-2","description":"Nascent polypeptide-associated complex subunit alpha","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR21713","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5745","complexName":"pspAF transcription regulation complex","organismName":"Escherichia coli (strain K12); 83333","description":"Transcription regulator, formation of which in the absence of membrane stress inhibits the ATPase activity of the enhancer binding and activator protein pspF. ATPase activity of pspF is required to induce an open complex formation of the DNA‐bound RNA polymerase at its target promoters. The pspAF complex retains only a basal ATPase activity. Membrane stresses, such as the mislocalisation of proteins to the inner membrane, appear to lead to the recruitment of pspA to the pspBC complex (CPX-5892), enabling at least a partial release of pspA from pspF. This allows transcription of the Psp membrane-stabilizing system through binding of pspF to the sigma factor rpoN (P24255).","predictedComplex":false,"interactors":[{"ac":"EBI-1123431","identifier":"P37344","identifierLink":"https://www.uniprot.org/uniprotkb/P37344/entry","name":"pspF","description":"Psp operon transcriptional activator","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32071","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1123459","identifier":"P0AFM6","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFM6/entry","name":"pspA","description":"Phage shock protein A","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR31088","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5747","complexName":"entAE 2,3-dihydroxybenzoate-AMP ligase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Required for a step in the synthesis of enterobactin (CHEBI:28855), a catecholate-type siderophore. Complex formation optimises the  activation of the carboxylate group of 2,3-dihydroxy-benzoate (CHEBI:36654) by entE, via a reversible ATP-dependent pyrophosphate exchange reactions to yield the acyladenylate intermediate 2,3-dihydroxybenzoyl-AMP.","predictedComplex":false,"interactors":[{"ac":"EBI-1118936","identifier":"P15047","identifierLink":"https://www.uniprot.org/uniprotkb/P15047/entry","name":"entA","description":"2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR24321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-550322","identifier":"P10378","identifierLink":"https://www.uniprot.org/uniprotkb/P10378/entry","name":"entE","description":"Enterobactin synthase component E","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5748","complexName":"entBE aryl carrier complex","organismName":"Escherichia coli (strain K12); 83333","description":"Required for a step in the synthesis of enterobactin (CHEBI:28855), a catecholate-type siderophore. entE-2,3-dihydroxy-benzoate (DHB, CHEBI:36654) -AMP binds to dimeric phosphopantetheinylated entB, resulting in the transfer of DHB to the phosphopantetheine group on Ser-245 of entB, resulting in the production of acyl-entB; this is followed by release of AMP from entE and dissociation of entE from the complex","predictedComplex":false,"interactors":[{"ac":"EBI-25570580","identifier":"CHEBI:47942","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:47942","name":"pantetheine 4'-phosphate(2-)","description":"pantetheine 4'-phosphate(2-)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-25570857","identifier":"CHEBI:57417","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57417","name":"2,3-dihydroxybenzoyl 5'-adenylate(1-)","description":"2,3-dihydroxybenzoyl 5'-adenylate(1-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-547993","identifier":"P0ADI4","identifierLink":"https://www.uniprot.org/uniprotkb/P0ADI4/entry","name":"entB","description":"Enterobactin synthase component B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43540","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-550322","identifier":"P10378","identifierLink":"https://www.uniprot.org/uniprotkb/P10378/entry","name":"entE","description":"Enterobactin synthase component E","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-5762","complexName":"rcsAB DNA-binding transcription factor complex","organismName":"Escherichia coli (strain K12); 83333","description":"Transcription factor complex activated by phosphorylation on Asp-56 of rcsB by the Rcs phosphorelay system. Required for expression of the colanic acid capsular polysaccharide operon, binding to the RcsAB box centered at 105 nucleotides upstream of the transcription start site. Also activates the yjb operon involved in exopolysaccharide synthesis, auto-regulates rcsA expression and negatively regulates the flhDC flagellar master regulator.","predictedComplex":false,"interactors":[{"ac":"EBI-369670","identifier":"P0DMC7","identifierLink":"https://www.uniprot.org/uniprotkb/P0DMC7/entry","name":"rcsB","description":"Transcriptional regulatory protein RcsB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43214","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-556695","identifier":"P0DMC9","identifierLink":"https://www.uniprot.org/uniprotkb/P0DMC9/entry","name":"rcsA","description":"Transcriptional regulatory protein RcsA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]}]},{"complexAC":"CPX-5763","complexName":"bglJ-rcsB DNA-binding transcription factor complex","organismName":"Escherichia coli (strain K12); 83333","description":"Transcription factor complex regulated independently of rcsB phosphorylation status. Activates the expression of the cryptic bgl operon, required for beta-glucoside degradation, by relieving repression by H-NS (P0ACF8).","predictedComplex":false,"interactors":[{"ac":"EBI-369670","identifier":"P0DMC7","identifierLink":"https://www.uniprot.org/uniprotkb/P0DMC7/entry","name":"rcsB","description":"Transcriptional regulatory protein RcsB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43214","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-551429","identifier":"P39404","identifierLink":"https://www.uniprot.org/uniprotkb/P39404/entry","name":"bglJ","description":"Transcriptional activator protein BglJ","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43214","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5764","complexName":"matA-rcsB DNA-binding transcription factor complex","organismName":"Escherichia coli (strain K12); 83333","description":"Transcription factor complex regulated independently of rcsB phosphorylation status. Probable role in regulating cell motility.","predictedComplex":false,"interactors":[{"ac":"EBI-369670","identifier":"P0DMC7","identifierLink":"https://www.uniprot.org/uniprotkb/P0DMC7/entry","name":"rcsB","description":"Transcriptional regulatory protein RcsB","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43214","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9152884","identifier":"P71301","identifierLink":"https://www.uniprot.org/uniprotkb/P71301/entry","name":"ecpR","description":"HTH-type transcriptional regulator EcpR","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]}]},{"complexAC":"CPX-5765","complexName":"rcsB DNA-binding transcription factor homodimer","organismName":"Escherichia coli (strain K12); 83333","description":"Transcription factor complex activated by phosphorylation on Asp-56 of rcsB by the Rcs phosphorelay system. Regulates the expression of rprA, which encoding a small RNA that  positively regulates translation of the general stress sigma factor, RpoS (P13445).","predictedComplex":false,"interactors":[{"ac":"EBI-369670","identifier":"P0DMC7","identifierLink":"https://www.uniprot.org/uniprotkb/P0DMC7/entry","name":"rcsB","description":"Transcriptional regulatory protein RcsB","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43214","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5766","complexName":"MERS-CoV cleaved Spike protein complex","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","description":"Spike protein complex of the MERS coronavirus that binds to human receptor DPP4 (P27487). Cell entry via binding of Spike to the DPP4 receptor (CPX-5768) relies on two proteolytic cleavage events facilitated by host proteases, such as furin (P09958) and TMPRSS2 (O15393): the first cleavage occurs at the S1/S2 site, the second at the S2' site. Cleavage at the S1/S2 site can occur prior to exit from an infected cell or once bound to DPP4 on the surface of a new host cell. Cleavage at the S2' site occurs only on the surface of the new host cell. While furin is active in the Golgi and on the plasma membrane and can cleave Spike at both cleavage sites, TMPRSS2 only facilitates S2' cleavage on the plasma membrane. \r\n\r\nWhile cleaved Spike greatly enhances viral entry into the host cell, it is not strictly required for infection and not all Spike complexes on the viral surface are cleaved. Alternatively, virions can enter the cell via the endosomal pathway and the use of an alternative protease, e.g. cathepsin L (P07711). Some variants of Spike carry mutations in the furin cleavage site that increases the proportion of cleaved Spike complexes which is linked to a higher infectivity of these variants.","predictedComplex":false,"interactors":[{"ac":"EBI-25591620","identifier":"K9N5Q8-PRO_0000422466","identifierLink":"https://www.uniprot.org/uniprotkb/K9N5Q8-PRO_0000422466/entry","name":"S","description":"Spike protein S1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","xrefs":[]},{"ac":"EBI-25591626","identifier":"K9N5Q8-PRO_0000422467","identifierLink":"https://www.uniprot.org/uniprotkb/K9N5Q8-PRO_0000422467/entry","name":"S","description":"Spike protein S2","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","xrefs":[]}]},{"complexAC":"CPX-5767","complexName":"MERS-CoV cleaved Spike protein complex","organismName":"Human betacoronavirus 2c EMC/2012; 1235996","description":"Spike protein complex of the MERS coronavirus that binds to human receptor DPP4 (P27487). Cell entry via binding of Spike to the DPP4 receptor (CPX-5768) relies on two proteolytic cleavage events facilitated by host proteases, such as furin (P09958) and TMPRSS2 (O15393): the first cleavage occurs at the S1/S2 site, the second at the S2' site. Cleavage at the S1/S2 site can occur prior to exit from an infected cell or once bound to DPP4 on the surface of a new host cell. Cleavage at the S2' site occurs only on the surface of the new host cell. While furin is active in the Golgi and on the plasma membrane and can cleave Spike at both cleavage sites, TMPRSS2 only facilitates S2' cleavage on the plasma membrane. \r\n\r\nWhile cleaved Spike greatly enhances viral entry into the host cell, it is not strictly required for infection and not all Spike complexes on the viral surface are cleaved. Alternatively, virions can enter the cell via the endosomal pathway and the use of an alternative protease, e.g. cathepsin L (P07711). Some variants of Spike carry mutations in the furin cleavage site that increases the proportion of cleaved Spike complexes which is linked to a higher infectivity of these variants.","predictedComplex":false,"interactors":[{"ac":"EBI-16040613","identifier":"K0BRG7","identifierLink":"https://www.uniprot.org/uniprotkb/K0BRG7/entry","name":"S","description":"Spike glycoprotein","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Human betacoronavirus 2c EMC/2012; 1235996","xrefs":[]},{"ac":"EBI-25591687","identifier":"K0BRG7-PRO_5023435957","identifierLink":"https://www.uniprot.org/uniprotkb/K0BRG7-PRO_5023435957/entry","name":"S","description":"Spike protein S2","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Human betacoronavirus 2c EMC/2012; 1235996","xrefs":[]}]},{"complexAC":"CPX-5768","complexName":"MERS-CoV Spike - human DPP4 receptor complex","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","description":"Binding of MERS coronavirus Spike protein to human receptor DPP2 facilitates virus entry into host cell.","predictedComplex":false,"interactors":[{"ac":"EBI-25591583","identifier":"CPX-5766","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-5766","name":"MERS-CoV cleaved Spike protein complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012); 1263720","xrefs":[]},{"ac":"EBI-2871277","identifier":"P27487","identifierLink":"https://www.uniprot.org/uniprotkb/P27487/entry","name":"DPP4","description":"Dipeptidyl peptidase 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11731","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5769","complexName":"MERS-CoV Spike - human DPP4 receptor complex","organismName":"Human betacoronavirus 2c EMC/2012; 1235996","description":"Binding of MERS coronavirus Spike protein to human receptor DPP4 facilitates virus entry into host cell.","predictedComplex":false,"interactors":[{"ac":"EBI-25591664","identifier":"CPX-5767","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-5767","name":"MERS-CoV cleaved Spike protein complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Human betacoronavirus 2c EMC/2012; 1235996","xrefs":[]},{"ac":"EBI-2871277","identifier":"P27487","identifierLink":"https://www.uniprot.org/uniprotkb/P27487/entry","name":"DPP4","description":"Dipeptidyl peptidase 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11731","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1937","complexName":"Carbamoyl phosphate synthetase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Plays a key role in both pyrimidine and arginine biosynthesis by catalyzing the production of carbamoyl phosphate from one molecule of bicarbonate, two molecules of MgATP, and one molecule of glutamine. Consists of two polypeptide chains referred to as the small and large subunits, which contain a total of three separate active sites that are connected by an intramolecular tunnel. The small subunit harbors one of these active sites and is responsible for the hydrolysis of glutamine to glutamate and ammonia. The large subunit binds the two required molecules of MgATP and is involved in assembling the final product. Compounds such as L-ornithine, UMP, and IMP allosterically regulate the enzyme.","predictedComplex":false,"interactors":[{"ac":"EBI-546107","identifier":"P0A6F1","identifierLink":"https://www.uniprot.org/uniprotkb/P0A6F1/entry","name":"carA","description":"Carbamoyl phosphate synthase small chain","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11405","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-546118","identifier":"P00968","identifierLink":"https://www.uniprot.org/uniprotkb/P00968/entry","name":"carB","description":"Carbamoyl phosphate synthase large chain","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11405","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3206","complexName":"Acetyl-CoA carboxylase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Biotin-dependent, multifunctional enzyme that catalyzes the first committed step in fatty acid synthesis.The overall reaction is the biotin-dependent carboxylation of acetyl-CoA to form malonyl-CoA. The first half-reaction catalyzed by biotin carboxylase, is an ATP-dependent carboxylation of biotin, which is covalently attached to biotin carboxyl carrier protein. The second half-reaction, catalyzed by carboxyl transferase, transfers the activated carboxyl group from carboxy-biotin to acetyl-CoA to form malonyl-CoA.","predictedComplex":false,"interactors":[{"ac":"EBI-542031","identifier":"P0ABD5","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABD5/entry","name":"accA","description":"Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42853","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-542064","identifier":"P0A9Q5","identifierLink":"https://www.uniprot.org/uniprotkb/P0A9Q5/entry","name":"accD","description":"Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42995","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-542308","identifier":"P24182","identifierLink":"https://www.uniprot.org/uniprotkb/P24182/entry","name":"accC","description":"Biotin carboxylase","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR48095","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-542320","identifier":"P0ABD8","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABD8/entry","name":"accB","description":"Biotin carboxyl carrier protein of acetyl-CoA carboxylase","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9690049","identifier":"CHEBI:15956","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15956","name":"biotin","description":"biotin","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1939","complexName":"TRAPP II complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Tethering complexes which provide the initial recognition event that links a particular vesicle with its target membrane. Participates in intra-Golgi and endosome-Golgi transport. Binds to a component of the COPI coat. BET3, BET5, TRS23, and TRS31 create a catalytic site for promoting GDP/GTP exchange in YPT1.","predictedComplex":false,"interactors":[{"ac":"EBI-19461","identifier":"Q03660","identifierLink":"https://www.uniprot.org/uniprotkb/Q03660/entry","name":"TRS130","description":"Trafficking protein particle complex II-specific subunit 130","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13251","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19468","identifier":"P38334","identifierLink":"https://www.uniprot.org/uniprotkb/P38334/entry","name":"TRS20","description":"Trafficking protein particle complex subunit 20","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12403","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19474","identifier":"Q03784","identifierLink":"https://www.uniprot.org/uniprotkb/Q03784/entry","name":"TRS23","description":"Trafficking protein particle complex subunit 23","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23249","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19480","identifier":"Q99394","identifierLink":"https://www.uniprot.org/uniprotkb/Q99394/entry","name":"TRS33","description":"Trafficking protein particle complex subunit 33","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12817","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22370","identifier":"P32613","identifierLink":"https://www.uniprot.org/uniprotkb/P32613/entry","name":"TCA17","description":"TRAPP-associated protein TCA17","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12403","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32112","identifier":"Q04183","identifierLink":"https://www.uniprot.org/uniprotkb/Q04183/entry","name":"TRS120","description":"Trafficking protein particle complex II-specific subunit 120","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21512","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3567","identifier":"P36149","identifierLink":"https://www.uniprot.org/uniprotkb/P36149/entry","name":"BET3","description":"Trafficking protein particle complex subunit BET3","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3580","identifier":"Q03630","identifierLink":"https://www.uniprot.org/uniprotkb/Q03630/entry","name":"BET5","description":"Trafficking protein particle complex subunit BET5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23249","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-38770","identifier":"Q03337","identifierLink":"https://www.uniprot.org/uniprotkb/Q03337/entry","name":"TRS31","description":"Trafficking protein particle complex subunit 31","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR20902","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9900","identifier":"P32893","identifierLink":"https://www.uniprot.org/uniprotkb/P32893/entry","name":"TRS65","description":"Trafficking protein particle complex II-specific subunit 65","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28159","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1940","complexName":"TRAPPI protein complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Tethering complexes which provide the initial recognition event that links a particular vesicle with its target membrane. Participates in ER-Golgi transport and is a guanine nucleotide exchange factor for the Rab protein YPT1 (P01123). BET3 binds the SEC23 (P15303) subunit of the coat protein II (COPII) coat. BET3, BET5, TRS23, and TRS31 create a catalytic site for promoting GDP/GTP exchange in YPT1.","predictedComplex":false,"interactors":[{"ac":"EBI-19468","identifier":"P38334","identifierLink":"https://www.uniprot.org/uniprotkb/P38334/entry","name":"TRS20","description":"Trafficking protein particle complex subunit 20","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12403","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19474","identifier":"Q03784","identifierLink":"https://www.uniprot.org/uniprotkb/Q03784/entry","name":"TRS23","description":"Trafficking protein particle complex subunit 23","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23249","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19480","identifier":"Q99394","identifierLink":"https://www.uniprot.org/uniprotkb/Q99394/entry","name":"TRS33","description":"Trafficking protein particle complex subunit 33","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12817","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3567","identifier":"P36149","identifierLink":"https://www.uniprot.org/uniprotkb/P36149/entry","name":"BET3","description":"Trafficking protein particle complex subunit BET3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3580","identifier":"Q03630","identifierLink":"https://www.uniprot.org/uniprotkb/Q03630/entry","name":"BET5","description":"Trafficking protein particle complex subunit BET5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23249","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-38770","identifier":"Q03337","identifierLink":"https://www.uniprot.org/uniprotkb/Q03337/entry","name":"TRS31","description":"Trafficking protein particle complex subunit 31","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR20902","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1943","complexName":"dnaA oligomeric complex","organismName":"Escherichia coli (strain K12); 83333","description":"A dnaA homo-oligomer consisting of some 20 dnaA molecules binds specific DNA regions (dnaA boxes, R sites, I sites and tau sites) at the replication origin oriC. The dnaA box has a 9bp consensus structure 5'-TTATC[CA]A[CA]A-3'. ATP-dnaA binds to low affinity boxes and oligomerizes to form a helical filament on oriC. Aided by diaA (P66817) and HU (CPX-1958/CPX-1959) and catalysed through ATP hydrolysis, dnaA undergoes a major conformational change and unwinds double-stranded DNA at specific 13mer sites. DNA wrapping around the dnaA filament causes torsional strain in the AT-rich DNA unwinding element (DUE), contributing to DNA melting. The dnaA filament then extends beyond the dnaA boxes with the AAA+ domain interacting with DnaA-trio.This sequesters and stretches one strand of the DUE ,facilitating DNA melting and bubble formation before recruiting the dnaB-dnaC complex (CPX-1934) and associated proteins to initiate DNA replication.","predictedComplex":false,"interactors":[{"ac":"EBI-548951","identifier":"P03004","identifierLink":"https://www.uniprot.org/uniprotkb/P03004/entry","name":"dnaA","description":"Chromosomal replication initiator protein DnaA","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1944","complexName":"DnaA-L2 DNA replication initiation inhibitory complex","organismName":"Escherichia coli (strain K12); 83333","description":"Contributes to the regulation of replication initiation preventing multiple replication origins during one replication cycle: L2 interacts with the N-terminal domain of DnaA destabilizing dnaA oligomers at the replication origin (oriC) and thus inhibits DNA-dependent duplex unwinding element unwinding.","predictedComplex":false,"interactors":[{"ac":"EBI-543515","identifier":"P60422","identifierLink":"https://www.uniprot.org/uniprotkb/P60422/entry","name":"rplB","description":"Large ribosomal subunit protein uL2","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR13691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-548951","identifier":"P03004","identifierLink":"https://www.uniprot.org/uniprotkb/P03004/entry","name":"dnaA","description":"Chromosomal replication initiator protein DnaA","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1954","complexName":"hda-beta clamp complex","organismName":"Escherichia coli (strain K12); 83333","description":"Functions to regulate the level of hda made available for the regulatory inactivation of dnaA (RIDA), which is is one of the major control mechanisms of DNA replication licensing.","predictedComplex":false,"interactors":[{"ac":"EBI-542385","identifier":"P0A988","identifierLink":"https://www.uniprot.org/uniprotkb/P0A988/entry","name":"dnaN","description":"Beta sliding clamp","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30478","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-545453","identifier":"P69931","identifierLink":"https://www.uniprot.org/uniprotkb/P69931/entry","name":"hda","description":"DnaA regulatory inactivator Hda","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1949","complexName":"Elongator holoenzyme complex","organismName":"Homo sapiens; 9606","description":"N-acetyltransferase which acts to form modified wobble uridines in tRNA, such as 5-methoxycarbonylmethyl-uridine (mcm5U), 5-methoxycarbonylmethyl-2-thio-uridine (mcm5s2U), and 5-carbamoylmethyl-uridine (ncm5U). These sites  influence the recognition rate and affinity between incoming tRNAs and codons in the A site of the translating ribosome, stablizing transient pausing events thus supporting proper domain folding of the nascent polypeptide chains during  the elongation phase of the ribosome‐mediated translation process.","predictedComplex":false,"interactors":[{"ac":"EBI-2680411","identifier":"Q6IA86","identifierLink":"https://www.uniprot.org/uniprotkb/Q6IA86/entry","name":"ELP2","description":"Elongator complex protein 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44111","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2932659","identifier":"Q0PNE2","identifierLink":"https://www.uniprot.org/uniprotkb/Q0PNE2/entry","name":"ELP6","description":"Elongator complex protein 6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16184","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347559","identifier":"O95163","identifierLink":"https://www.uniprot.org/uniprotkb/O95163/entry","name":"ELP1","description":"Elongator complex protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12747","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355217","identifier":"Q9H9T3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H9T3/entry","name":"ELP3","description":"Elongator complex protein 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11135","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3951755","identifier":"Q96EB1","identifierLink":"https://www.uniprot.org/uniprotkb/Q96EB1/entry","name":"ELP4","description":"Elongator complex protein 4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12896","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-946189","identifier":"Q8TE02","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TE02/entry","name":"ELP5","description":"Elongator complex protein 5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15641","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1947","complexName":"Methionyl glutamyl tRNA synthetase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the aminoacylation of tRNAs by their cognate amino acid. Arc1p makes contact with MetRS and GluRS through its amino-terminal domain, while its carboxy-terminal contains a tRNA-binding domain. As a result of the formation of this complex, cognate tRNAs are bound with high affinity and aminoacylation efficiency is increased.","predictedComplex":false,"interactors":[{"ac":"EBI-18665","identifier":"P46655","identifierLink":"https://www.uniprot.org/uniprotkb/P46655/entry","name":"GUS1","description":"Glutamate--tRNA ligase, cytoplasmic","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18762","identifier":"P00958","identifierLink":"https://www.uniprot.org/uniprotkb/P00958/entry","name":"MES1","description":"Methionine--tRNA ligase, cytoplasmic","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45765","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6555942","identifier":"CHEBI:29173","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29173","name":"trnamet","description":"tRNA(Met)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"transfer rna","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-6555944","identifier":"CHEBI:29175","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29175","name":"trnaglu","description":"CHEBI:29175","stochiometry":"minValue: 1, maxValue: 1","interactorType":"transfer rna","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-7224","identifier":"P46672","identifierLink":"https://www.uniprot.org/uniprotkb/P46672/entry","name":"ARC1","description":"tRNA-aminoacylation cofactor ARC1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11586","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1948","complexName":"dnaA-dps DNA replication initiation inhibitory complex","organismName":"Escherichia coli (strain K12); 83333","description":"Complex formation reduces replication initiation on oriC under oxidative stress conditions, preventing DNA opening by dnaA thus allowing DNA repair to proceed prior to new rounds of replication. The incomplete blockage of replication initiation is thought to produce genetic variation in the bacterial population inhibits replication","predictedComplex":false,"interactors":[{"ac":"EBI-548951","identifier":"P03004","identifierLink":"https://www.uniprot.org/uniprotkb/P03004/entry","name":"dnaA","description":"Chromosomal replication initiator protein DnaA","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549640","identifier":"P0ABT2","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABT2/entry","name":"dps","description":"DNA protection during starvation protein","stochiometry":"minValue: 12, maxValue: 12","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1950","complexName":"dnaA-dnaB-dnaC loader complex","organismName":"Escherichia coli (strain K12); 83333","description":"The dnaB helicase is associated with a inhibitory/loader protein, dnaC, an AAA+ ATPase which, together with dnaA, chaperones two dnaB hexamers onto single-stranded DNA strands during initiation of replication. dnaA loads one dnaB-dnaC complex (CPX-1934)  on the top strand near the left border of oriC and a second dnaB-dnaC complex on the lower strand next to dnaA box R1.","predictedComplex":false,"interactors":[{"ac":"EBI-548951","identifier":"P03004","identifierLink":"https://www.uniprot.org/uniprotkb/P03004/entry","name":"dnaA","description":"Chromosomal replication initiator protein DnaA","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-548978","identifier":"P0ACB0","identifierLink":"https://www.uniprot.org/uniprotkb/P0ACB0/entry","name":"dnaB","description":"Replicative DNA helicase DnaB","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30153","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549012","identifier":"P0AEF0","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEF0/entry","name":"dnaC","description":"Replicative helicase loader DnaC","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1951","complexName":"Replication restart pre-primosome complex, priAB variant","organismName":"Escherichia coli (strain K12); 83333","description":"Required for the restart of replication at sites of premature termination of DNA replication which leaves collapsed/abandoned replication forks that would otherwise create double-strand DNA breaks (DSBs) on the next round of replication. Serves to reload the replicative helicase dnaB on sites far removed from the origin of replication in a DNA structure-dependent manner.The PriA-PriB variant appears to be the dominant restart mechanism in E.coli, with priA binding single-stranded, double-stranded and forked DNA with high affinity. PriB appears to be important for restart following DNA recombination. On binding, priA undergoes a conformational change, exposing the priB binding site. The priA:priB:DNA ternary interaction stabilizes priA on the DNA and enhances its helicase activity, facilitating unwinding of the nascent lagging strand if one is present. dnaT is recruited to the priA:priB:DNA ternary complex which leads to release of ssDNA by priB. The dnaB-dnaC complex (CPX-1934) is recruited to the primosome, possibly through direct contacts with dnaT and the dnaB is loaded from dnaB-dnaC onto ssDNA on the lagging strand template.","predictedComplex":false,"interactors":[{"ac":"EBI-1125223","identifier":"P07013","identifierLink":"https://www.uniprot.org/uniprotkb/P07013/entry","name":"priB","description":"Replication restart protein PriB","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-548978","identifier":"P0ACB0","identifierLink":"https://www.uniprot.org/uniprotkb/P0ACB0/entry","name":"dnaB","description":"Replicative DNA helicase DnaB","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30153","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549012","identifier":"P0AEF0","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEF0/entry","name":"dnaC","description":"Replicative helicase loader DnaC","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549621","identifier":"P0A8J2","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8J2/entry","name":"dnaT","description":"Replication restart protein DnaT","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-552050","identifier":"P17888","identifierLink":"https://www.uniprot.org/uniprotkb/P17888/entry","name":"priA","description":"Replication restart protein PriA","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30580","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1952","complexName":"Replication restart pre-primosome complex, priAC variant","organismName":"Escherichia coli (strain K12); 83333","description":"Required for the restart of replication at sites of premature termination of DNA replication which leaves collapsed/abandoned replication forks that would otherwise create double-strand DNA breaks (DSBs) on the next round of replication. Serves to reload the replicative helicase dnaB on sites far removed from the origin of replication in a DNA structure-dependent manner. priA binds single-stranded, double-stranded and forked DNA with high affinity. priC binds ssDNA, preferentially associating with replication forks that include at least 7 nucleotide gaps between the nascent leading strand and replication fork. The dnaB-dnaC complex (CPX-1934) is recruited to the primosome, possibly through direct contacts with dnaT and the dnaB is loaded from dnaB-dnaC onto ssDNA on the lagging strand template.","predictedComplex":false,"interactors":[{"ac":"EBI-1117383","identifier":"P23862","identifierLink":"https://www.uniprot.org/uniprotkb/P23862/entry","name":"priC","description":"Replication restart protein PriC","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-548978","identifier":"P0ACB0","identifierLink":"https://www.uniprot.org/uniprotkb/P0ACB0/entry","name":"dnaB","description":"Replicative DNA helicase DnaB","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30153","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549012","identifier":"P0AEF0","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEF0/entry","name":"dnaC","description":"Replicative helicase loader DnaC","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549621","identifier":"P0A8J2","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8J2/entry","name":"dnaT","description":"Replication restart protein DnaT","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-552050","identifier":"P17888","identifierLink":"https://www.uniprot.org/uniprotkb/P17888/entry","name":"priA","description":"Replication restart protein PriA","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30580","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1953","complexName":"Replication restart pre-primosome complex priC-rep variant","organismName":"Escherichia coli (strain K12); 83333","description":"Required for the restart of replication at sites of premature termination of DNA replication which leaves collapsed/abandoned replication forks that would otherwise create double-strand DNA breaks (DSBs) on the next round of replication. Serves to reload the replicative helicase dnaB on sites far removed from the origin of replication in a DNA structure-dependent manner. On replication forks lacking nascent leading and lagging strands priC is sufficient to load DnaB from the DnaB-DnaC complex in the absence of any other restart proteins but appears to require the rep helicase to create single-stranded DNA on the lagging strand for restart pathway progression or to remove nascent lagging strand DNA to enable priC-mediated loading of dnaB.","predictedComplex":false,"interactors":[{"ac":"EBI-1117383","identifier":"P23862","identifierLink":"https://www.uniprot.org/uniprotkb/P23862/entry","name":"priC","description":"Replication restart protein PriC","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-548978","identifier":"P0ACB0","identifierLink":"https://www.uniprot.org/uniprotkb/P0ACB0/entry","name":"dnaB","description":"Replicative DNA helicase DnaB","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30153","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-549012","identifier":"P0AEF0","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEF0/entry","name":"dnaC","description":"Replicative helicase loader DnaC","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6558011","identifier":"P09980","identifierLink":"https://www.uniprot.org/uniprotkb/P09980/entry","name":"rep","description":"ATP-dependent DNA helicase Rep","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11070","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1955","complexName":"SeqA-DNA complex","organismName":"Escherichia coli (strain K12); 83333","description":"Believed to be involved in negative supercoiling of the DNA forming nucleoid compaction. SeqA forms filaments on methylated and hemimethylated DNA but has a higher avidity for hemimethylated GATC sites. Hemimethylated DNA is created during complementary strand synthesis before Dam protein fully methylates the new stand. Binding of SeqA to hemimethylated DNA sequesters the chromosomal replication origin, oriC, preventing re-methylation of DNA by Dam and in turn stopping premature re-initiation of replication during one replication cycle. Depletion of the SeqA pool towards the end of the replication cycle allows Dam protein to displace SeqA from the hemimethylated DNA, allowing it to fully methylate the DNA and initiate a new cycle of DNA replication.\r\nThe SeqA-DNA complex travels with the replication folk sequentially binding to the majority of hemimethylated GATC sites of the newly-synthesized dsDNA.\r\nSeqA can form multimers consisting of dimers, tetramers octamers and higher order filaments but it is believed that the main form in vivo are filaments.","predictedComplex":false,"interactors":[{"ac":"EBI-552553","identifier":"P0AFY8","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFY8/entry","name":"seqA","description":"Negative modulator of initiation of replication","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-6672067","identifier":null,"identifierLink":null,"name":"hemimeth_dna_random","description":"random-generated hemimethylated dsDNA","stochiometry":null,"interactorType":"double stranded deoxyribonucleic acid","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1956","complexName":"CCAAT-binding factor complex","organismName":"Homo sapiens; 9606","description":"Transcription factor which binds to the CCAAT box, which occurs in 30% of eukaryotic promoters and appears to be crucial for promoter activity. May also play a role in histone methylation and some acetylation through recruitment of relevant enzymes to active promoters.","predictedComplex":false,"interactors":[{"ac":"EBI-389728","identifier":"P25208","identifierLink":"https://www.uniprot.org/uniprotkb/P25208/entry","name":"NFYB","description":"Nuclear transcription factor Y subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11064","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-389739","identifier":"P23511","identifierLink":"https://www.uniprot.org/uniprotkb/P23511/entry","name":"NFYA","description":"Nuclear transcription factor Y subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12632","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-389755","identifier":"Q13952","identifierLink":"https://www.uniprot.org/uniprotkb/Q13952/entry","name":"NFYC","description":"Nuclear transcription factor Y subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10252","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1957","complexName":"Integration host factor complex","organismName":"Escherichia coli (strain K12); 83333","description":"Nucleoid-associated, sequence-specific DNA-binding complex that functions in genetic recombination as well as in transcriptional and translational control. Binding of IHF to  the IHF-binding site of DNA (5'-(A/T)ATCAAnnnnTT(A/G)-3') causes a sharp (120-180 degree) bend in the double helix, thereby bringing towdnaA bding regions of the DNA, R1 (moderate-affinity) and R5 (low-affinity)  in proximity ofeach other, and allows for the formation of the rightward filament responsible for duplex opening at the duplex unwinding element of the replication origin (oriC) by dnaA as a first step in DNA replication.","predictedComplex":false,"interactors":[{"ac":"EBI-551753","identifier":"P0A6X7","identifierLink":"https://www.uniprot.org/uniprotkb/P0A6X7/entry","name":"ihfA","description":"Integration host factor subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33175","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-551813","identifier":"P0A6Y1","identifierLink":"https://www.uniprot.org/uniprotkb/P0A6Y1/entry","name":"ihfB","description":"Integration host factor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33175","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1958","complexName":"HU complex, variant hupAB","organismName":"Escherichia coli (strain K12); 83333","description":"Non-sequence specific DNA binding protein complex that is capable of wrapping DNA forming nucleosome-like structures. May play a role in replication initiation, transcription, DNA repair and protect DNA against UV or gamma radiation. Binds with high affinity to structurally distorted, kinked or distorted DNA and double-stranded DNA containing a single-stranded break but also has a key architectural roles in DNA nucleoid compaction and in constraining negative supercoils in DNA via largely sequence-independent DNA binding. Introduces flexible bends (10-180 degrees) into DNA. HU also causes stiffening of DNA at high concentrations. Also binds to dnaA during replication initiation as does the alpha homodimer (CPX-1959).\r\n\r\nThe alpha/beta heterodimer is predominantly present during the transition phase, end of exponential phase and stationary phase.","predictedComplex":false,"interactors":[{"ac":"EBI-370411","identifier":"P0ACF4","identifierLink":"https://www.uniprot.org/uniprotkb/P0ACF4/entry","name":"hupB","description":"DNA-binding protein HU-beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33175","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-547648","identifier":"P0ACF0","identifierLink":"https://www.uniprot.org/uniprotkb/P0ACF0/entry","name":"hupA","description":"DNA-binding protein HU-alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33175","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1959","complexName":"HU complex, variant hupA","organismName":"Escherichia coli (strain K12); 83333","description":"Non-sequence specific DNA binding protein complex that is capable of wrapping DNA forming nucleosome-like structures. May play a role in replication initiation, transcription, DNA repair and may protect DNA against UV- or gamma-radiation. Binds strongly bent, kinked or distorted DNA, such as that found in damaged DNA with high affinity, but also has a key architectural roles in DNA nucleoid compaction and in constraining negative supercoils in DNA via largely sequence-independent DNA binding. HU also causes stiffening of DNA at high concentrations. Also binds to dnaA during replication initiation as does the alpha homodimer (CPX-1959). Also binds to DnaA during replication initiation as does the heterodimer (CPX-1958).\r\n\r\nThe alpha homodimer is predominantly present in the early log phase.\r\n\r\nDNA-binding is both, topology- or structural-dependent and sequence-specific.","predictedComplex":false,"interactors":[{"ac":"EBI-547648","identifier":"P0ACF0","identifierLink":"https://www.uniprot.org/uniprotkb/P0ACF0/entry","name":"hupA","description":"DNA-binding protein HU-alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33175","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1960","complexName":"HU complex variant 2","organismName":"Escherichia coli (strain K12); 83333","description":"Histone-like DNA-binding complex. Preferentially binds cruciform DNA in comparison to the alpha/beta heterodimer (CPX-1958) or alpha homodimer (CPX-1959) that bind to several forms of bent, kinked or damaged DNA.\r\n\r\nThe precise role for the beta homodimer is unknown as knock-out mutants produce no measurable phenotype.","predictedComplex":false,"interactors":[{"ac":"EBI-370411","identifier":"P0ACF4","identifierLink":"https://www.uniprot.org/uniprotkb/P0ACF4/entry","name":"hupB","description":"DNA-binding protein HU-beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33175","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1961","complexName":"DnaA-HU complex, variant hupAB","organismName":"Escherichia coli (strain K12); 83333","description":"HU dimers (alpha-beta dimers as well as alpha homodimers [CPX-1959]) are essential proteins during the DnaA-dependent initiation of replication. They facilitate DnaA oligomerization and proper timing of initiation of replication, potentially by suppressing dnaA binding to DNA at a low affinity binding site, I3.","predictedComplex":false,"interactors":[{"ac":"EBI-370411","identifier":"P0ACF4","identifierLink":"https://www.uniprot.org/uniprotkb/P0ACF4/entry","name":"hupB","description":"DNA-binding protein HU-beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33175","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-547648","identifier":"P0ACF0","identifierLink":"https://www.uniprot.org/uniprotkb/P0ACF0/entry","name":"hupA","description":"DNA-binding protein HU-alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33175","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-548951","identifier":"P03004","identifierLink":"https://www.uniprot.org/uniprotkb/P03004/entry","name":"dnaA","description":"Chromosomal replication initiator protein DnaA","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1962","complexName":"DnaA-HU complex, variant hupA","organismName":"Escherichia coli (strain K12); 83333","description":"HU dimers (alpha homodimers as well as alpha-beta dimers [CPX-1958]) are essential proteins during the DnaA-dependent initiation of replication. They facilitate DnaA oligomerization and proper timing of initiation of replication, potentially by suppressing dnaA binding to DNA at a low affinity binding site, I3.","predictedComplex":false,"interactors":[{"ac":"EBI-547648","identifier":"P0ACF0","identifierLink":"https://www.uniprot.org/uniprotkb/P0ACF0/entry","name":"hupA","description":"DNA-binding protein HU-alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33175","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-548951","identifier":"P03004","identifierLink":"https://www.uniprot.org/uniprotkb/P03004/entry","name":"dnaA","description":"Chromosomal replication initiator protein DnaA","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1963","complexName":"dnaA-diaA complex","organismName":"Escherichia coli (strain K12); 83333","description":"A diaA tetramer binds to up 4 molecules of dnaA and stimulates dnaA assembly at the dnaA-oligomerization region of the chromosomal origin, oriC. This drastically increases the affinity of the linked dnaA molecules for DNA. diaA also has a negative effect on the initiation of DNA replication by inhibiting. dnaA from binding to the DnaB-DnaC complex (CPX-1934).","predictedComplex":false,"interactors":[{"ac":"EBI-1108845","identifier":"CHEBI:15422","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15422","name":"atp","description":"ATP","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1125806","identifier":"P66817","identifierLink":"https://www.uniprot.org/uniprotkb/P66817/entry","name":"diaA","description":"DnaA initiator-associating protein DiaA","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30390","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-548951","identifier":"P03004","identifierLink":"https://www.uniprot.org/uniprotkb/P03004/entry","name":"dnaA","description":"Chromosomal replication initiator protein DnaA","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1965","complexName":"H-NS complex, dimeric","organismName":"Escherichia coli (strain K12); 83333","description":"Involved in bacterial nucleoid condensation and regulation of global gene expression by directly binding to promoter regions, regulation is generally negative although examples of positive regulation are known. Repression of transcription is mediated by cooperative spreading along the DNA (DNA stiffening) and by creating looped structures through formation of DNA-protein-DNA bridges. Recognises both structural and sequence-specific motifs in double-stranded DNA and binds preferably to bent DNA. \r\nWhilst dimerization is essential for its transcriptional repressor activity it may be the tetrameric form is more commonly found in vivo.\r\nTetramerization is environmentally dependent and decreases under low ionic strength or temperature conditions. This environmental-dependency of the H-NS tetramer may allow for gene regulation under extreme conditions.","predictedComplex":false,"interactors":[{"ac":"EBI-544934","identifier":"P0ACF8","identifierLink":"https://www.uniprot.org/uniprotkb/P0ACF8/entry","name":"hns","description":"DNA-binding protein H-NS","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR38097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1966","complexName":"H-NS complex, tetrameric","organismName":"Escherichia coli (strain K12); 83333","description":"Involved in bacterial nucleoid condensation and regulation of global gene expression by directly binding to promoter regions, regulation is generally negative although examples of positive regulation are known. Repression of transcription is mediated by cooperative spreading along the DNA (DNA stiffening) and by creating looped structures through formation of DNA-protein-DNA bridges. Recognises both structural and sequence-specific motifs in double-stranded DNA and binds preferably to bent DNA. \r\nWhilst dimerization is essential for its transcriptional repressor activity it may be the tetrameric form is more commonly found in vivo.\r\nTetramerization is environmentally dependent and decreases under low ionic strength or temperature conditions. This environmental-dependency of the H-NS tetramer may allow for gene regulation under extreme conditions.the H-NS tetramer may allow for gene regulation under extreme conditions.","predictedComplex":false,"interactors":[{"ac":"EBI-544934","identifier":"P0ACF8","identifierLink":"https://www.uniprot.org/uniprotkb/P0ACF8/entry","name":"hns","description":"DNA-binding protein H-NS","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR38097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1979","complexName":"H-NS-Hha transcription factor complex","organismName":"Escherichia coli (strain K12); 83333","description":"Functions as transcription factor that negatively regulates a range of genes, in particular those acquired by horizontal transfer.","predictedComplex":false,"interactors":[{"ac":"EBI-1122578","identifier":"P0ACE3","identifierLink":"https://www.uniprot.org/uniprotkb/P0ACE3/entry","name":"hha","description":"Hemolysin expression-modulating protein Hha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-544934","identifier":"P0ACF8","identifierLink":"https://www.uniprot.org/uniprotkb/P0ACF8/entry","name":"hns","description":"DNA-binding protein H-NS","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR38097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1980","complexName":"H-NS-Cnu transcription factor complex","organismName":"Escherichia coli (strain K12); 83333","description":"Functions as a transcription factor that negatively regulates a range of bacterial genes. May modulate filamentous growth by antagonizing the binding of dicA (P06966) to a putative operator sequence on its own gene promoter.","predictedComplex":false,"interactors":[{"ac":"EBI-544934","identifier":"P0ACF8","identifierLink":"https://www.uniprot.org/uniprotkb/P0ACF8/entry","name":"hns","description":"DNA-binding protein H-NS","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR38097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-551907","identifier":"P64467","identifierLink":"https://www.uniprot.org/uniprotkb/P64467/entry","name":"cnu","description":"OriC-binding nucleoid-associated protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]}]},{"complexAC":"CPX-1967","complexName":"Plasma membrane fumarate reductase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the terminal step of anaerobic respiration. Electrons are donated to membrane-bound subunits FrdC and FrdD by 2 quinol (hydroquinone) molecules and transferred to a flavin adenine nucleotide (FAD, covalently-bound to subunit FrdA) through three distinct Fe-S clusters (within subunit FrdB). Ultimately, the electrons are used to reduce FAD-bound fumarate to succinate.\r\n\r\nElectrons can also be transported in the opposite direction where they are donated by succinate and ultimately reduce quinone to quinol.\r\n\r\nMember of the Complex II family. The functionally inverse complex found in aerobic respiration is the SQR complex (CPX-1931).","predictedComplex":false,"interactors":[{"ac":"EBI-1032954","identifier":"P0A8Q3","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8Q3/entry","name":"frdD","description":"Fumarate reductase subunit D","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-1225105","identifier":"CHEBI:16238","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16238","name":"fad","description":"FAD - Flavin adenine dinucleotide","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-550480","identifier":"P00363","identifierLink":"https://www.uniprot.org/uniprotkb/P00363/entry","name":"frdA","description":"Fumarate reductase flavoprotein subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11632","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-556074","identifier":"P0A8Q0","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8Q0/entry","name":"frdC","description":"Fumarate reductase subunit C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-6880484","identifier":"CHEBI:33725","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:33725","name":"fe4-s4","description":"tetra-μ3-sulfido-tetrairon","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-6880488","identifier":"CHEBI:47402","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:47402","name":"fe3-s4","description":"tri-μ-sulfido-μ3-sulfido-triiron","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-6880987","identifier":"CHEBI:33739","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:33739","name":"fe2-s2","description":"di-μ-sulfido-diiron(0)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-6894755","identifier":"CHEBI:17594","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:17594","name":"hydroquinone","description":"hydroquinone","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-906724","identifier":"P0AC47","identifierLink":"https://www.uniprot.org/uniprotkb/P0AC47/entry","name":"frdB","description":"Fumarate reductase iron-sulfur subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43551","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1969","complexName":"Cyclin C-CDK8 complex","organismName":"Homo sapiens; 9606","description":"Cyclin-dependent protein kinase complex. Forms part of the Mediator complex and also the CDK module sub-complex but also exists as a heterodimer which is involved in transcription and regulation of  transcription initiation from RNA polymerase II promoter. Decreases Notch acetylation and transcriptional activity.","predictedComplex":false,"interactors":[{"ac":"EBI-394377","identifier":"P49336","identifierLink":"https://www.uniprot.org/uniprotkb/P49336/entry","name":"CDK8","description":"Cyclin-dependent kinase 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395261","identifier":"P24863","identifierLink":"https://www.uniprot.org/uniprotkb/P24863/entry","name":"CCNC","description":"Cyclin-C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1971","complexName":"E2F1-DP1 transcription factor complex","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds DNA through the E2 recognition site, 5'-TTTC[CG]CGC-3', typically associated with the promoters of genes active in S phase. Activates genes that stimulate DNA synthesis and cell cycle advancement.","predictedComplex":false,"interactors":[{"ac":"EBI-448924","identifier":"Q01094","identifierLink":"https://www.uniprot.org/uniprotkb/Q01094/entry","name":"E2F1","description":"Transcription factor E2F1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12081","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749713","identifier":"Q14186","identifierLink":"https://www.uniprot.org/uniprotkb/Q14186/entry","name":"TFDP1","description":"Transcription factor Dp-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12548","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1972","complexName":"E2F2-DP1 transcription factor complex","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds DNA  through the E2 recognition site, 5'-TTTC[CG]CGC-3', typically associated with active promoters in S phase, activating genes that stimulate DNA synthesis and cell cycle advancement.","predictedComplex":false,"interactors":[{"ac":"EBI-718476","identifier":"Q14209","identifierLink":"https://www.uniprot.org/uniprotkb/Q14209/entry","name":"E2F2","description":"Transcription factor E2F2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12081","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749713","identifier":"Q14186","identifierLink":"https://www.uniprot.org/uniprotkb/Q14186/entry","name":"TFDP1","description":"Transcription factor Dp-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12548","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1973","complexName":"E2F3-DP1 transcription factor complex","organismName":"Homo sapiens; 9606","description":"Transcription factor which binds DNA  through the E2 recognition site, 5'-TTTC[CG]CGC-3'. Typically associated with active promoters in S phase, activating genes that stimulate DNA synthesis and cell cycle advancement.","predictedComplex":false,"interactors":[{"ac":"EBI-749713","identifier":"Q14186","identifierLink":"https://www.uniprot.org/uniprotkb/Q14186/entry","name":"TFDP1","description":"Transcription factor Dp-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12548","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-765551","identifier":"O00716","identifierLink":"https://www.uniprot.org/uniprotkb/O00716/entry","name":"E2F3","description":"Transcription factor E2F3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12081","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1975","complexName":"Formate dehydrogenase N complex","organismName":"Escherichia coli (strain K12); 83333","description":"Formate:quinone oxidoreductase involved in electron transport during anaerobic respiration, induced anaerobically in the presence of nitrate. Uses formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor.","predictedComplex":false,"interactors":[{"ac":"EBI-1130815","identifier":"P0AEK7","identifierLink":"https://www.uniprot.org/uniprotkb/P0AEK7/entry","name":"fdnI","description":"Formate dehydrogenase, nitrate-inducible, cytochrome b556(Fdn) subunit","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30074","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11426020","identifier":"CHEBI:60539","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60539","name":"mo(=o)-bis(molybdopterin guanine dinucleotide)(4-)","description":"Mo(=O)-bis(molybdopterin guanine dinucleotide)(4-)","stochiometry":"minValue: 3, maxValue: 3","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-25760299","identifier":"CHEBI:16374","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16374","name":"menaquinone","description":"menaquinone","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-550115","identifier":"P24183","identifierLink":"https://www.uniprot.org/uniprotkb/P24183/entry","name":"fdnG","description":"Formate dehydrogenase, nitrate-inducible, major subunit","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43598","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-551976","identifier":"P0AAJ3","identifierLink":"https://www.uniprot.org/uniprotkb/P0AAJ3/entry","name":"fdnH","description":"Formate dehydrogenase, nitrate-inducible, iron-sulfur subunit","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43545","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 6, maxValue: 6","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-6880484","identifier":"CHEBI:33725","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:33725","name":"fe4-s4","description":"tetra-μ3-sulfido-tetrairon","stochiometry":"minValue: 15, maxValue: 15","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1976","complexName":"Glutamate dehydrogenase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyses the reversible oxidative deamination of L-glutamate to alpha-ketoglutarate via oxidative deamination using NADH+ as the cofactor. Links amino acid metabolism to the tricarboxylic acid (TCA) cycle.","predictedComplex":false,"interactors":[{"ac":"EBI-1115290","identifier":"P00370","identifierLink":"https://www.uniprot.org/uniprotkb/P00370/entry","name":"gdhA","description":"NADP-specific glutamate dehydrogenase","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43571","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6554966","identifier":"CHEBI:18009","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18009","name":"nadp+","description":"2'-O-phosphonoadenosine 5'-{3-[1-(3-carbamoylpyridinio)-1,4-anhydro-D-ribitol-5-yl] dihydrogen diphosphate}","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1977","complexName":"Vascular endothelial growth factor A complex","organismName":"Homo sapiens; 9606","description":"Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Can promote tumor vascularization. Ligand to vascular endothelial growth factor receptor (VGFR-1) complex. Has heparin-binding properties.","predictedComplex":false,"interactors":[{"ac":"EBI-1026643","identifier":"P15692","identifierLink":"https://www.uniprot.org/uniprotkb/P15692/entry","name":"VEGFA","description":"Vascular endothelial growth factor A, long form","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12025","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3160","complexName":"Vascular endothelial growth factor A complex","organismName":"Mus musculus; 10090","description":"Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Can promote tumor vascularization. Ligand to vascular endothelial growth factor receptor (VGFR-1) complex. Has heparin-binding properties.","predictedComplex":false,"interactors":[{"ac":"EBI-444774","identifier":"Q00731","identifierLink":"https://www.uniprot.org/uniprotkb/Q00731/entry","name":"Vegfa","description":"Vascular endothelial growth factor A, long form","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12025","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2156","complexName":"Chaperonin-containing T-complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Group II Heat Shock Protein 60 chaperonins which catalyses the cytoplasmic ATP-dependent folding of newly synthesized proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-1108845","identifier":"CHEBI:15422","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15422","name":"atp","description":"ATP","stochiometry":"minValue: 16, maxValue: 16","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-19045","identifier":"P12612","identifierLink":"https://www.uniprot.org/uniprotkb/P12612/entry","name":"TCP1","description":"T-complex protein 1 subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19049","identifier":"P39076","identifierLink":"https://www.uniprot.org/uniprotkb/P39076/entry","name":"CCT2","description":"T-complex protein 1 subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19054","identifier":"P39078","identifierLink":"https://www.uniprot.org/uniprotkb/P39078/entry","name":"CCT4","description":"T-complex protein 1 subunit delta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19059","identifier":"P40413","identifierLink":"https://www.uniprot.org/uniprotkb/P40413/entry","name":"CCT5","description":"T-complex protein 1 subunit epsilon","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19063","identifier":"P39077","identifierLink":"https://www.uniprot.org/uniprotkb/P39077/entry","name":"CCT3","description":"T-complex protein 1 subunit gamma","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19067","identifier":"P42943","identifierLink":"https://www.uniprot.org/uniprotkb/P42943/entry","name":"CCT7","description":"T-complex protein 1 subunit eta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19072","identifier":"P47079","identifierLink":"https://www.uniprot.org/uniprotkb/P47079/entry","name":"CCT8","description":"T-complex protein 1 subunit theta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19077","identifier":"P39079","identifierLink":"https://www.uniprot.org/uniprotkb/P39079/entry","name":"CCT6","description":"T-complex protein 1 subunit zeta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2146","complexName":"SYP1 endocytic adapter complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Acts as a component of the machinery that drives clathrin-mediated endocytosis in budding yeast. Plays a role in the distribution of endocytic sites. Recruits Ede1 (P34216) which is important for endocytic site formation. Negatively regulates the WAS-Arp2/3 complex that helps choreograph the precise timing of actin assembly during endocytosis. Also functions in polarized cell growth.","predictedComplex":false,"interactors":[{"ac":"EBI-21900","identifier":"P25623","identifierLink":"https://www.uniprot.org/uniprotkb/P25623/entry","name":"SYP1","description":"Suppressor of yeast profilin deletion","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23065","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2105","complexName":"Cobalamin ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity cobalamin (vitamin B12) transporter. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-1033420","identifier":"P06611","identifierLink":"https://www.uniprot.org/uniprotkb/P06611/entry","name":"btuD","description":"Vitamin B12 import ATP-binding protein BtuD","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42734","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1033427","identifier":"P06609","identifierLink":"https://www.uniprot.org/uniprotkb/P06609/entry","name":"btuC","description":"Vitamin B12 import system permease protein BtuC","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30472","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1118724","identifier":"P37028","identifierLink":"https://www.uniprot.org/uniprotkb/P37028/entry","name":"btuF","description":"Vitamin B12-binding protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42860","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2106","complexName":"BtuCD complex","organismName":"Escherichia coli (strain K12); 83333","description":"Core subunit of the cobalamin transport complex containing the transmembrane homodimer BtuC and the cytoplasmic ATPase homodimer BtuD.\r\nRequires the binding of cobalamin (vitamin B12)-bound subunit BtuF to bind to the periplasmic site of the transmembrane subunit in order to transport cobalamin through the periplasmic membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-1033420","identifier":"P06611","identifierLink":"https://www.uniprot.org/uniprotkb/P06611/entry","name":"btuD","description":"Vitamin B12 import ATP-binding protein BtuD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42734","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1033427","identifier":"P06609","identifierLink":"https://www.uniprot.org/uniprotkb/P06609/entry","name":"btuC","description":"Vitamin B12 import system permease protein BtuC","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30472","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3087","complexName":"Shu complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Role in the early stages of the homologous recombination DNA damage repair process. Recruits the Rad55-Rad57 complex (CPX-3139) and the homologous recombination machinery to the sites of single-stranded DNA gaps left by replication-blocking lesions to complete error-free DNA-damage tolerance.","predictedComplex":false,"interactors":[{"ac":"EBI-22154","identifier":"P38957","identifierLink":"https://www.uniprot.org/uniprotkb/P38957/entry","name":"SHU2","description":"Suppressor of hydroxyurea sensitivity protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-24305","identifier":"P38751","identifierLink":"https://www.uniprot.org/uniprotkb/P38751/entry","name":"SHU1","description":"Suppressor of HU sensitivity involved in recombination protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-25229","identifier":"P40465","identifierLink":"https://www.uniprot.org/uniprotkb/P40465/entry","name":"CSM2","description":"Chromosome segregation in meiosis protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-37340","identifier":"Q12318","identifierLink":"https://www.uniprot.org/uniprotkb/Q12318/entry","name":"PSY3","description":"Platinum sensitivity protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-2148","complexName":"Phosphatidylinositol transporter complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Phosphatidylinositol transfer homodimer a lipid droplet-associated protein that inhibits lipid mobilization from these particles. May assist in shuttling sterols or their intermediates, between membranes or, alternatively, between sterol biosynthetic enzymes or complexes. Required for the resistance of yeast cells to azole antifungals.","predictedComplex":false,"interactors":[{"ac":"EBI-29195","identifier":"P53860","identifierLink":"https://www.uniprot.org/uniprotkb/P53860/entry","name":"PDR16","description":"Phosphatidylinositol transfer protein PDR16","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2947","complexName":"YgjK glucosidase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Glucoside hydrolase that cleaves the alpha-1,3-glucosidic linkage in nigerose. Has very low activity towards maltooligosaccharides, soluble starch, nigerotriose, kojibiose and trehalose.","predictedComplex":false,"interactors":[{"ac":"EBI-1121018","identifier":"P42592","identifierLink":"https://www.uniprot.org/uniprotkb/P42592/entry","name":"ygjK","description":"Glucosidase YgjK","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR23403","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2102","complexName":"Cytochrome bo3 ubiquinol oxidase complex","organismName":"Escherichia coli (strain K12); 83333","description":"A  heme-copper oxidase integral to the bacterial electron transport chain. Electrons are donated by the oxidation of ubiquinol to ubiquinone, transferred to a slow-spinning heme b and subsequently accepted by a binuclear centre consisting of a heme o3 and a copper ion. In the process, the ubiquinol oxidase functions as a proton pump creating a transmembrane electrochemical gradient as 4 hydrogen ions are pumped through the membrane into the periplasmic space while 1/2 O2 molecule is oxidized to water. The electron transport happens exclusively in subunit I (cyoB). \r\n\r\nUbiquinol oxidase is the final electron acceptor in the bacterial respiratory chain and thought to possess one of the most important functions in the cellular system due to its anti-oxidant properties.","predictedComplex":false,"interactors":[{"ac":"EBI-1116940","identifier":"P0ABJ1","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABJ1/entry","name":"cyoA","description":"Cytochrome bo(3) ubiquinol oxidase subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR22888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1225103","identifier":"CHEBI:26355","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:26355","name":"heme b","description":"Heme b","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-26564956","identifier":"CHEBI:132124","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:132124","name":"1,4-benzoquinones","description":"1,4-benzoquinones","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2932021","identifier":"P0ABI8","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABI8/entry","name":"cyoB","description":"Cytochrome bo(3) ubiquinol oxidase subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10422","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8697823","identifier":"P0ABJ3","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABJ3/entry","name":"cyoC","description":"Cytochrome bo(3) ubiquinol oxidase subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11403","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8697850","identifier":"P0ABJ6","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABJ6/entry","name":"cyoD","description":"Cytochrome bo(3) ubiquinol oxidase subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR36835","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8697993","identifier":"CHEBI:28694","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:28694","name":"copper atom","description":"copper atom","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-8698010","identifier":"CHEBI:24480","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:24480","name":"heme o","description":"heme o","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2104","complexName":"HslUV protease complex","organismName":"Escherichia coli (strain K12); 83333","description":"A proteasome-like degradation complex with two functional subunits: the hslU hexamer forms the ATPase subunit which has chaperone activity and the hslV duodecamer forms the protease subunit. \r\n\r\nThe binding of ATP and its subsequent hydrolysis by hslU are essential for unfolding of protein substrates subsequently hydrolyzed by hslV. hslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to hslV for hydrolysis.\r\n\r\nATP hydrolysis causes a conformational change in the hslU subunit 'closing' the central pore and 'un-docking' the ATPase unit from the protease by way of flicking the hslU C-terminus from the hslV-hslV interface into the hslU-hslU interface.\r\n\r\nThe complex has been shown to be involved in the specific degradation of heat shock induced transcription factors such as rpoH and sulA. In addition, small hydrophobic peptides are also hydrolyzed by hslV. hslV has weak protease activity even in the absence of hslU, but this activity is induced more than 100-fold in the presence of hslU. Owing to the size of the central pore of both subunits hslUV is not believed to degrade folded proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-369317","identifier":"P0A6H5","identifierLink":"https://www.uniprot.org/uniprotkb/P0A6H5/entry","name":"hslU","description":"ATP-dependent protease ATPase subunit HslU","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR48102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-552265","identifier":"P0A7B8","identifierLink":"https://www.uniprot.org/uniprotkb/P0A7B8/entry","name":"hslV","description":"ATP-dependent protease subunit HslV","stochiometry":"minValue: 12, maxValue: 12","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR32194","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2112","complexName":"Telosome complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A protective cap that inhibits telomerase, counteracts SIR-mediated transcriptional silencing, and prevents inadvertent recognition of telomeres as DNA double-strand breaks. Rif1 and Rif2 have separable and independent Rap1-binding epitopes, allowing Rap1 recruitment and binding over large distances (42-110 A).","predictedComplex":false,"interactors":[{"ac":"EBI-14821","identifier":"P11938","identifierLink":"https://www.uniprot.org/uniprotkb/P11938/entry","name":"RAP1","description":"DNA-binding protein RAP1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR16466","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15199","identifier":"Q06208","identifierLink":"https://www.uniprot.org/uniprotkb/Q06208/entry","name":"RIF2","description":"Protein RIF2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-2083307","identifier":"P29539","identifierLink":"https://www.uniprot.org/uniprotkb/P29539/entry","name":"RIF1","description":"Telomere length regulator protein RIF1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22928","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8769060","identifier":null,"identifierLink":null,"name":"telomeric_dna","description":"Telomeric DNA","stochiometry":null,"interactorType":"double stranded deoxyribonucleic acid","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-2113","complexName":"GroEL-GroES complex","organismName":"Escherichia coli (strain K12); 83333","description":"Member of the chaperonin class of molecular chaperones required for the ATP-driven assisted folding of many proteins. Direct contact between substrate proteins and the C-terminal tails of the GroEL subunits helps prevent premature substrate protein escape during encapsulation. Encapsulation seals the GroEL cavity and results in the release of the substrate protein into an enlarged GroEL-GroES chamber. Protein folding is initiated by a conformational shift within the GroEL-GroES complex. Hydrolysis of ATP and binding of a new substrate protein to the opposite cavity sends an allosteric signal causing GroES and the encapsulated protein to be released into the cytosol.","predictedComplex":false,"interactors":[{"ac":"EBI-369169","identifier":"P0A6F9","identifierLink":"https://www.uniprot.org/uniprotkb/P0A6F9/entry","name":"groES","description":"Co-chaperonin GroES","stochiometry":"minValue: 7, maxValue: 7","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10772","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-543750","identifier":"P0A6F5","identifierLink":"https://www.uniprot.org/uniprotkb/P0A6F5/entry","name":"groEL","description":"Chaperonin GroEL","stochiometry":"minValue: 14, maxValue: 14","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR45633","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2115","complexName":"modE transcription regulation complex","organismName":"Escherichia coli (strain K12); 83333","description":"Transcriptional regulator involved in various aspects of molybdenum metabolism by both limiting molybdate uptake by repressing the molybdate transporter operon modABCD, and enhancing the transcription of molybdenum-dependent and of molybdenum cofactor biosynthesis enzymes. It is activated by the binding of 2 molecules of molybdate to the dimerization interface. Upon binding of molybdate, the conformation of the dimer changes probably enhancing the DNA affinity of the complex. It recognizes an 8-base inverted repeat 5'-TAACGTTA-3' flanked by two CAT boxes upstream of the modABCD operon. \r\n\r\nModE also interacts with tungstate.","predictedComplex":false,"interactors":[{"ac":"EBI-8774375","identifier":"P0A9G8","identifierLink":"https://www.uniprot.org/uniprotkb/P0A9G8/entry","name":"modE","description":"DNA-binding transcriptional dual regulator ModE","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30432","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8774409","identifier":"CHEBI:36264","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:36264","name":"molybdate","description":"molybdate","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2116","complexName":"MsbA transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"Member of the ATP-binding cassette (ABC) transporter proteins that facilitates the export of lipid A and lipopolysaccheride (LPS) across the plasma membrane, flipping LPS synthesized in the cytoplasmic leaflet of the inner membrane to the periplasmic leaflet  Couples substrate transport to a transmembrane electrochemical proton gradient in addition to hydrolysis of ATP at the nicleotide-binding domains.\r\n\r\nThe MabA dimer is also capable of transporting a wide spectrum of drugs through the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-556367","identifier":"P60752","identifierLink":"https://www.uniprot.org/uniprotkb/P60752/entry","name":"msbA","description":"ATP-dependent lipid A-core flippase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR24221","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2117","complexName":"Alkanesulfonate monooxygenase complex","organismName":"Escherichia coli (strain K12); 83333","description":"An alkanesulfonate monooxygenase that catalyses the conversion of alkanesulfonates into aldehydes and sulfite under conditions of sulfate or cysteine starvation. This process absolutely requires the presences of oxygen and FMNH2, the latter is provided by the flavin oxidoreductase SsuE (CPX-2118).","predictedComplex":false,"interactors":[{"ac":"EBI-561637","identifier":"P80645","identifierLink":"https://www.uniprot.org/uniprotkb/P80645/entry","name":"ssuD","description":"Alkanesulfonate monooxygenase","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR42847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2118","complexName":"FMN reductase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Flavin oxidoreductase subunit that reduces flavin mononucleotid (FMN) to FMNH2 in a NAD(P)H-dependent manner. It provides FMNH2 to the alkanesulfonate monooxygenase subunit ssuD (CPX-2117) which catalyses the conversion of alkanesulfonates into aldehydes and sulfite under conditions of sulfur or cysteine starvation.","predictedComplex":false,"interactors":[{"ac":"EBI-1121047","identifier":"P80644","identifierLink":"https://www.uniprot.org/uniprotkb/P80644/entry","name":"ssuE","description":"FMN reductase (NADPH)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43408","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2120","complexName":"Taurine dioxygenase complex, tetrameric","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the conversion of taurine and alpha ketoglutarate to sulfite, aminoacetaldehyde and succinate under sulfur or cysteine starvation conditions. Expression is repressed by the presence of sulfate or cysteine.","predictedComplex":false,"interactors":[{"ac":"EBI-1116170","identifier":"P37610","identifierLink":"https://www.uniprot.org/uniprotkb/P37610/entry","name":"tauD","description":"Alpha-ketoglutarate-dependent taurine dioxygenase","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30468","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2929936","identifier":"CHEBI:29033","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29033","name":"iron2plus","description":"iron(2+)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-3190","complexName":"Taurine dioxygenase complex, dimeric","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyzes the conversion of taurine and alpha ketoglutarate to sulfite, aminoacetaldehyde and succinate under sulfur or cysteine starvation conditions. Expression is repressed by the presence of sulfate or cysteine.","predictedComplex":false,"interactors":[{"ac":"EBI-1116170","identifier":"P37610","identifierLink":"https://www.uniprot.org/uniprotkb/P37610/entry","name":"tauD","description":"Alpha-ketoglutarate-dependent taurine dioxygenase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30468","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2929936","identifier":"CHEBI:29033","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29033","name":"iron2plus","description":"iron(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2121","complexName":"EmrE multidrug transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"Transmembrane homodimer that transports positively charged hydrophobic xenobiotics across the plasma membrane into the periplasmic space, coupling efflux to the inward movement of protons across the cell membrane  thereby conferring resistance to a wide range of toxic compounds (e.g. methyl viologen, ethidium bromide and acriflavine).","predictedComplex":false,"interactors":[{"ac":"EBI-8789431","identifier":"P23895","identifierLink":"https://www.uniprot.org/uniprotkb/P23895/entry","name":"emrE","description":"Multidrug transporter EmrE","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30561","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2122","complexName":"Swr1 chromatin remodelling complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"ATP-dependent chromatin-remodeling complex. SWR1 replaces the canonical H2A/H2B dimer at nucleosomes flanking histone-depleted regions, such as promoters, with a variant histone H2A.Z/H2B dimer. H2A.Z has been shown to affect the stability of its host nucleosome, higher-order chromatin folding, and recruitment of transcriptional factors.","predictedComplex":false,"interactors":[{"ac":"EBI-20613","identifier":"P31376","identifierLink":"https://www.uniprot.org/uniprotkb/P31376/entry","name":"SWC3","description":"SWR1-complex protein 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28108","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21031","identifier":"P38326","identifierLink":"https://www.uniprot.org/uniprotkb/P38326/entry","name":"SWC5","description":"SWR1-complex protein 5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR48407","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2169","identifier":"P60010","identifierLink":"https://www.uniprot.org/uniprotkb/P60010/entry","name":"ACT1","description":"Actin","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22102","identifier":"Q05471","identifierLink":"https://www.uniprot.org/uniprotkb/Q05471/entry","name":"SWR1","description":"Helicase SWR1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45685","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23061","identifier":"P53201","identifierLink":"https://www.uniprot.org/uniprotkb/P53201/entry","name":"SWC4","description":"SWR1-complex protein 4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12855","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27814","identifier":"Q03433","identifierLink":"https://www.uniprot.org/uniprotkb/Q03433/entry","name":"VPS71","description":"Vacuolar protein sorting-associated protein 71","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28841","identifier":"P53930","identifierLink":"https://www.uniprot.org/uniprotkb/P53930/entry","name":"YAF9","description":"Protein AF-9 homolog","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23195","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2939","identifier":"P80428","identifierLink":"https://www.uniprot.org/uniprotkb/P80428/entry","name":"ARP4","description":"Actin-related protein 4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2957","identifier":"Q12509","identifierLink":"https://www.uniprot.org/uniprotkb/Q12509/entry","name":"ARP6","description":"Actin-like protein ARP6","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30712","identifier":"Q03940","identifierLink":"https://www.uniprot.org/uniprotkb/Q03940/entry","name":"RVB1","description":"RuvB-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31814","identifier":"Q12464","identifierLink":"https://www.uniprot.org/uniprotkb/Q12464/entry","name":"RVB2","description":"RuvB-like protein 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32671","identifier":"Q06707","identifierLink":"https://www.uniprot.org/uniprotkb/Q06707/entry","name":"SWC7","description":"SWR1-complex protein 7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-3493","identifier":"P35817","identifierLink":"https://www.uniprot.org/uniprotkb/P35817/entry","name":"BDF1","description":"Bromodomain-containing factor 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22880","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-38035","identifier":"Q03388","identifierLink":"https://www.uniprot.org/uniprotkb/Q03388/entry","name":"VPS72","description":"Vacuolar protein sorting-associated protein 72","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13275","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2123","complexName":"sufBCD complex","organismName":"Escherichia coli (strain K12); 83333","description":"Scaffold complex that assembles an Fe-S cluster. The sufB protomer of the sufBCD complex accepts the atomic sulfur from the sulfur transfer protein SufE (CPX-2125) and incorporates it into an [4Fe-4S] cluster. sufBCD further transfers the Fe-S cluster to the carrier protein sufA (CPX-2142). \r\n\r\nsufBCD is a component of the sufABCDSE operon, which is activated and required under specific conditions such as oxidative stress and iron limitation.\r\n\r\nThe sufBCD complex is a putative ATP-binding cassette (ABC) complex, inferred by its structural similarity with  ABC transporters. sufC has been shown to be an ATPase whose activity is enhanced by the presence of sufB and sufD (PMID:20857974). Under aerobic conditions FADH2 is oxidised to FAD and dissociates from sufBCD.","predictedComplex":false,"interactors":[{"ac":"EBI-561601","identifier":"P77499","identifierLink":"https://www.uniprot.org/uniprotkb/P77499/entry","name":"sufC","description":"Probable ATP-dependent transporter SufC","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43204","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-562751","identifier":"P77689","identifierLink":"https://www.uniprot.org/uniprotkb/P77689/entry","name":"sufD","description":"Iron-sulfur cluster assembly protein SufD","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43575","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-562758","identifier":"P77522","identifierLink":"https://www.uniprot.org/uniprotkb/P77522/entry","name":"sufB","description":"Iron-sulfur cluster assembly protein SufB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30508","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2129","complexName":"CST complex","organismName":"Homo sapiens; 9606","description":"Binds to ssDNA without sequence specificity. May play a role in telomere metabolism, protecting telomeres from DNA degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-2562799","identifier":"Q86WV5","identifierLink":"https://www.uniprot.org/uniprotkb/Q86WV5/entry","name":"TEN1","description":"CST complex subunit TEN1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR33905","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2562802","identifier":"Q2NKJ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q2NKJ3/entry","name":"CTC1","description":"CST complex subunit CTC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14865","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-746930","identifier":"Q9H668","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H668/entry","name":"STN1","description":"CST complex subunit STN1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13989","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2130","complexName":"CST complex","organismName":"Mus musculus; 10090","description":"Binds to ssDNA without sequence specificity. May play a role in telomere metabolism, protecting telomeres from DNA degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-2553883","identifier":"Q8K2X3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K2X3/entry","name":"Stn1","description":"CST complex subunit STN1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13989","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6258382","identifier":"Q5SUQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q5SUQ9/entry","name":"Ctc1","description":"CST complex subunit CTC1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14865","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6258509","identifier":"Q9D7K2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D7K2/entry","name":"Ten1","description":"CST complex subunit TEN1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR33905","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2124","complexName":"sufS cysteine desulfurase complex","organismName":"Escherichia coli (strain K12); 83333","description":"An L-cysteine desulfurase which cleaves the C-S bond in cysteine to yield alanine and persulfide, an enzyme-bound S-sulfanylcysteine species. The desulfurase activity is coupled via a ping-pong mechanism to a second transpersulfuration step where the persulfide species is transferred from the active-site cysteine residue to acceptor sufE homodimer (CPX-2125). \r\n\r\nsufS is activated and required under specific conditions such as oxidative stress and iron limitation. It plays a role in iron-sulfur cluster formation on SufBCD (CPX-2123).\r\n\r\nsufS is part of the sufABCDSE operon and its cysteine desulfurization activity is enhanced by the SufE dimer and SufBCD complex.\r\n\r\nIn vitro it also acts as a potent selenocysteine lyase, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo.","predictedComplex":false,"interactors":[{"ac":"EBI-1124981","identifier":"P77444","identifierLink":"https://www.uniprot.org/uniprotkb/P77444/entry","name":"sufS","description":"Cysteine desulfurase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43586","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8852014","identifier":"CHEBI:597326","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:597326","name":"pyridoxal 5'-phosphate(2-)","description":"pyridoxal 5'-phosphate(2-)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2125","complexName":"SufE complex","organismName":"Escherichia coli (strain K12); 83333","description":"Sulfur transfer homodimer that accepts the atomic sulfur resulting from the L-cysteine desulfurase activity of SufS (CPX-2124) and further transfers it to the SufBCD scaffold protein complex (CPX-2123). \r\n\r\nIt is a component of the sufABCDSE operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. It plays a role in the iron-sulfur cluster formation on SufBCD.","predictedComplex":false,"interactors":[{"ac":"EBI-1124973","identifier":"P76194","identifierLink":"https://www.uniprot.org/uniprotkb/P76194/entry","name":"sufE","description":"Cysteine desulfuration protein SufE","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43597","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2126","complexName":"Glycine/Proline betaine ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity glycine betaine and proline betaine transporter. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily. Responsible for the regulation of cell volume by translocating solutes across the plasma membrane. The proVWX operon is activated under osmotic stress conditions and the complex itself is regulated by osmotic stress, presumably via an increase in the internal salt concentration .","predictedComplex":false,"interactors":[{"ac":"EBI-1129961","identifier":"P0AFM2","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFM2/entry","name":"proX","description":"Glycine betaine/proline betaine-binding periplasmic protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-546797","identifier":"P14175","identifierLink":"https://www.uniprot.org/uniprotkb/P14175/entry","name":"proV","description":"Glycine betaine/proline betaine transport system ATP-binding protein ProV","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43869","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8794761","identifier":"P14176","identifierLink":"https://www.uniprot.org/uniprotkb/P14176/entry","name":"proW","description":"Glycine betaine/proline betaine transport system permease protein ProW","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR47737","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2127","complexName":"STING complex","organismName":"Homo sapiens; 9606","description":"Central player in the innate immune response to nucleic acids, particularly cytosolic double-stranded DNA from bacteria and viruses and mitochondrial damage. cyclic GMP-AMP (cGAMP) synthase acts as a cytosolic DNA sensor and, in response to nucleic acid binding, synthesizes one specific isomer of cGAMP, an endogenous second messenger that activates the type I IFN pathway. Binding of this isomer (CHEBI:75947) to STING activates a cascade of events whereby STING recruits and activates I-kappa-B kinase and TANK-binding kinase which, following their phosphorylation, activate nuclear transcription factor kappa-B and interferon regulatory factor 3, respectively. These activated proteins translocate to the nucleus to induce transcription of the genes encoding type I IFN and cytokines for promoting intercellular host immune defence.\r\n\r\nImplicated in a growing number of non-canonical roles independent of MITA functions in a variety of processes including antiviral activity, senescence, autophagy, metabolism, lysosomal biogenesis, and the development of neurological disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-2800345","identifier":"Q86WV6","identifierLink":"https://www.uniprot.org/uniprotkb/Q86WV6/entry","name":"STING1","description":"Stimulator of interferon genes protein","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR34339","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8801022","identifier":"CHEBI:75947","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:75947","name":"cg(2'5')_pa(3'5')p","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2128","complexName":"Sting complex","organismName":"Mus musculus; 10090","description":"Central player in the innate immune response to nucleic acids, particularly cytosolic dsDNA from bacteria and viruses and mitochondrial damage. cyclic GMP-AMP (cGAMP) synthase acts as a cytosolic DNA sensor and, in response to nucleic acid binding, synthesizes one specific isomer of cGAMP, an endogenous second messenger that activates the type I IFN pathway. Binding of this isomer (CHEBI:75947) to STING activates a cascade of events whereby STING recruits and activates I-kappa-B kinase  and TANK-binding kinase  which, following their phosphorylation, activate nuclear transcription factor kappa-B and interferon regulatory factor 3, respectively. These activated proteins translocate to the nucleus to induce transcription of the genes encoding type I IFN and cytokines for promoting intercellular host immune defence.","predictedComplex":false,"interactors":[{"ac":"EBI-3862093","identifier":"Q3TBT3","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TBT3/entry","name":"Sting1","description":"Stimulator of interferon genes protein","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR34339","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8801022","identifier":"CHEBI:75947","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:75947","name":"cg(2'5')_pa(3'5')p","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2142","complexName":"sufA complex","organismName":"Escherichia coli (strain K12); 83333","description":"An Fe-S cluster carrier homodimer that accepts the Fe-S cluster from the SufBCD scaffold protein complex (CPX-2123 [complex], EBI-8805910 [transfer interaction]) and transfers it to the target apo-protein. The Fe-S cluster has a [2Fe-2S] conformation when associated with SufA which can transfer its Fe-S cluster to both [2Fe-2S] and [4Fe-4S] apoproteins.\r\n\r\nIt is a component of the sufABCDSE operon, which is activated and required under specific conditions such as oxidative stress and iron limitation.","predictedComplex":false,"interactors":[{"ac":"EBI-1125011","identifier":"P77667","identifierLink":"https://www.uniprot.org/uniprotkb/P77667/entry","name":"sufA","description":"Iron-sulfur cluster assembly protein SufA","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10072","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2131","complexName":"alpha-D-mannose 1,6-phosphomutase","organismName":"Homo sapiens; 9606","description":"Catalyzes the conversion of d-mannose 6-phosphate to alpha-d-mannose 1-phosphate. Required for GDP-mannose and dolichol-phosphate-mannose biosynthesis.\r\nMutations in this protein may cause the congenital disease congential disorder of glycosylation type 1a (CDG-1a)","predictedComplex":false,"interactors":[{"ac":"EBI-746784","identifier":"Q92871","identifierLink":"https://www.uniprot.org/uniprotkb/Q92871/entry","name":"PMM1","description":"Phosphomannomutase 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10466","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2132","complexName":"IscA complex","organismName":"Escherichia coli (strain K12); 83333","description":"Transfers [2Fe2S] clusters to apo-protein forms of other iron-sulfur proteins. It may also function as a [2Fe2S] scaffold protein for the formation of [2Fe2S] clusters.","predictedComplex":false,"interactors":[{"ac":"EBI-11472102","identifier":"CHEBI:24875","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:24875","name":"iron cation","description":"iron cation","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-767026","identifier":"P0AAC8","identifierLink":"https://www.uniprot.org/uniprotkb/P0AAC8/entry","name":"iscA","description":"Iron-binding protein IscA","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10072","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2133","complexName":"Spermidine N(1)-acetyltransferase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Regulates polyamine concentration in the cell. Transfers an acetyl group from acetyl-coenzyme A to an N-terminal amino group of intracellular spermidine forming N(1)- and N(8)-acetylspermidine.This transformis spermidine into a less toxic form that can be easily exported from or kept within the cell.","predictedComplex":false,"interactors":[{"ac":"EBI-1115796","identifier":"P0A951","identifierLink":"https://www.uniprot.org/uniprotkb/P0A951/entry","name":"speG","description":"Spermidine N(1)-acetyltransferase","stochiometry":"minValue: 12, maxValue: 12","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43415","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2134","complexName":"ThiF-ThiS complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyses the initial steps of thiamine (vitamin B1) pyrophosphate synthesis. thiF catalyzes the adenylation of the carboxy terminus of thiS and the subsequent displacement of AMP catalyzed by thiI (P77718)-persulfide to give a thiS−thiI acyl disulfide. Disulfide interchange, involving thiF Cys-184, then generates the thiS−thiF acyl disulfide, the sulfur donor for thiazole formation.","predictedComplex":false,"interactors":[{"ac":"EBI-1127777","identifier":"P30138","identifierLink":"https://www.uniprot.org/uniprotkb/P30138/entry","name":"thiF","description":"Sulfur carrier protein ThiS adenylyltransferase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8850092","identifier":"O32583","identifierLink":"https://www.uniprot.org/uniprotkb/O32583/entry","name":"thiS","description":"Sulfur carrier protein ThiS","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34472","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2135","complexName":"thiG-thiH thiazole phosphate synthase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Role in thiamine biosynthesis, catalysing the synthesis of the thiazole phosphate moiety of thiamine. thiG-thiH is found downstream of the activities of iscS, the thiS-thiF complex (CPX-2134) and thiI and requires the activity of 1-deoxy-D-xylulose 5-phosphate (CHEBI:57792). The thiH subunit binds a 4Fe-4S cluster that is coordinated by 3 cysteines (Cys-X-X-X-Cys-X-X-Cys) and an exchangeable S-adenosyl-L-methionine molecule. Sulfur is donated by the thiS-thiF complex.","predictedComplex":false,"interactors":[{"ac":"EBI-1125553","identifier":"P30140","identifierLink":"https://www.uniprot.org/uniprotkb/P30140/entry","name":"thiH","description":"2-iminoacetate synthase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43583","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-547059","identifier":"P30139","identifierLink":"https://www.uniprot.org/uniprotkb/P30139/entry","name":"thiG","description":"Thiazole synthase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2136","complexName":"L-cysteine desulfurase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyses L-cysteine or selenocysteine to L-alanine and either atomic sulfur, as sulfane or (per)sulfide (under reducing conditions) group, or selenium, respectively. The desulfurase activity of IscS is activated by interaction of partner proteins to form a persulfide adduct of Cys-328. By changing binding partners, IscS selects the sulfur flow through various sulfur trafficking pathways in the cell\r\n\r\nProvides the sulfur moiety for a variety of pathways such as iron-sulfur cluster formation, e.g. on apo-protein IscU (P0ACD4), for transpersulfidation reactions, e.g. thiol-group formation on Cys-456-ThiF (P30138) during thiamine pyrophospate biosynthesis and for biosynthesis pathways of nicotinic acids, biotin or molybdopterin (via MoeB-MoaD complex, CPX-1968). It is a master enzyme responsible for biosynthesis of all thio-containing RNA modifications (e.g. via ThiL (CPX-2140), TusA-TusBCD-TusE cascade (CPX-2139), IscU (CPX-2141)). It delivers selenium in the pathway for the biosynthesis of selenophosphate.","predictedComplex":false,"interactors":[{"ac":"EBI-550055","identifier":"P0A6B7","identifierLink":"https://www.uniprot.org/uniprotkb/P0A6B7/entry","name":"iscS","description":"Cysteine desulfurase IscS","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11601","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8852014","identifier":"CHEBI:597326","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:597326","name":"pyridoxal 5'-phosphate(2-)","description":"pyridoxal 5'-phosphate(2-)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2137","complexName":"csdA L-cysteine desulfurase complex","organismName":"Escherichia coli (strain K12); 83333","description":"An L-cysteine desulfurase and L-selenocysteine lyase that catalyses the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine, and transiently retains the released sulfur atom on a cysteine residue, in the form of a persulfide. It transfers the sulfur to (a) csdE that increases the cysteine desulfurase activity of csdA (csdA-csdE complex CPX-2138) or to (b) tcdA/csdL where it appears to support the function of TcdA in the generation of cyclic threonylcarbamoyladenosine at position 37 (ct6A37) in tRNAs that read codons beginning with adenine (in vitro). csdA also desulfinates L-cysteine sulfinate, which is the best substrate of the enzyme. \r\n\r\ncsdA functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate and participates in Fe/S biogenesis (by recruiting the sufBCD-sufE proteins).","predictedComplex":false,"interactors":[{"ac":"EBI-545660","identifier":"Q46925","identifierLink":"https://www.uniprot.org/uniprotkb/Q46925/entry","name":"csdA","description":"Cysteine desulfurase CsdA","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43586","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8852014","identifier":"CHEBI:597326","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:597326","name":"pyridoxal 5'-phosphate(2-)","description":"pyridoxal 5'-phosphate(2-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2138","complexName":"cdsA-cdsE complex","organismName":"Escherichia coli (strain K12); 83333","description":"Acts as a L-cysteine desulfurase and sufurtransferase. csdA desulfurases L-cysteine to produce L-alanine atomic sulfur (in the form of a persulfide). It transfers the sulfur to csdE which increases the cysteine desulfurase activity of csdA. csdE accepts the sulfur on Cys-61.\r\n\r\nWhile the csdE dimer can be isolated in vitro it is uncertain whether it also exists on its own in vivo.","predictedComplex":false,"interactors":[{"ac":"EBI-1130454","identifier":"P0AGF2","identifierLink":"https://www.uniprot.org/uniprotkb/P0AGF2/entry","name":"csdE","description":"Sulfur acceptor protein CsdE","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43597","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-545660","identifier":"Q46925","identifierLink":"https://www.uniprot.org/uniprotkb/Q46925/entry","name":"csdA","description":"Cysteine desulfurase CsdA","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43586","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8852014","identifier":"CHEBI:597326","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:597326","name":"pyridoxal 5'-phosphate(2-)","description":"pyridoxal 5'-phosphate(2-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2139","complexName":"iscS-tusA cysteine desulfurase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Cysteine desulfurase involved in the sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm5s2U) at tRNA wobble positions. tusA  stimulates iscS activity while iscS transfers sulfur to tusA in a transpersulfidation reaction. In turn, tusA transfers the sulfur to tusD in the TusA-tusBCD-tusE-mnmA pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-550055","identifier":"P0A6B7","identifierLink":"https://www.uniprot.org/uniprotkb/P0A6B7/entry","name":"iscS","description":"Cysteine desulfurase IscS","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11601","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-561780","identifier":"P0A890","identifierLink":"https://www.uniprot.org/uniprotkb/P0A890/entry","name":"tusA","description":"Sulfur carrier protein TusA","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33279","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8852014","identifier":"CHEBI:597326","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:597326","name":"pyridoxal 5'-phosphate(2-)","description":"pyridoxal 5'-phosphate(2-)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2141","complexName":"iscS-iscU iron-sulfur cluster assembly complex","organismName":"Escherichia coli (strain K12); 83333","description":"Involved in the sulfur transfer during iron-sulfur cluster assembly. iscU forms a scaffold for sequential cluster assembly of first one [2Fe-2S]2+ cluster is observed that  first first to a form containing two [2Fe-2S]2+ clusters and finally to a form that contains one [4Fe-4S]2+ cluster. \r\n\r\niscA transfers sulfur to iscU while the latter is in the D-state, a partly disordered state that contains an ordered domain that stabilizes two cis peptidyl-prolyl peptide bonds. After Fe-S cluster formation on IscU, IscU converts to the S-state, which has a lower affinity for IscS and minimizes product inhibition.","predictedComplex":false,"interactors":[{"ac":"EBI-550055","identifier":"P0A6B7","identifierLink":"https://www.uniprot.org/uniprotkb/P0A6B7/entry","name":"iscS","description":"Cysteine desulfurase IscS","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11601","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-561646","identifier":"P0ACD4","identifierLink":"https://www.uniprot.org/uniprotkb/P0ACD4/entry","name":"iscU","description":"Iron-sulfur cluster assembly scaffold protein IscU","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8852014","identifier":"CHEBI:597326","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:597326","name":"pyridoxal 5'-phosphate(2-)","description":"pyridoxal 5'-phosphate(2-)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2144","complexName":"TusBCDE complex","organismName":"Escherichia coli (strain K12); 83333","description":"Involved in the sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm5s2U) at tRNA wobble positions. It transfers sulfur (most likely in persulfide form) from TusA (P0A890) to the TusE-MnmA complex (CPX-2145) via Cys78-TusD and Cys108-TusE.\r\n\r\nAlthough TusBCD complex has been crystallised it has not yet been shown experimentally that it exists in vivo without subunit TusE attached.","predictedComplex":false,"interactors":[{"ac":"EBI-1121167","identifier":"P0AB18","identifierLink":"https://www.uniprot.org/uniprotkb/P0AB18/entry","name":"tusE","description":"Sulfurtransferase TusE","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR37010","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-546671","identifier":"P45531","identifierLink":"https://www.uniprot.org/uniprotkb/P45531/entry","name":"tusC","description":"Protein TusC","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR38780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8871385","identifier":"P45530","identifierLink":"https://www.uniprot.org/uniprotkb/P45530/entry","name":"tusB","description":"Protein TusB","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR37526","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8871402","identifier":"P45532","identifierLink":"https://www.uniprot.org/uniprotkb/P45532/entry","name":"tusD","description":"Sulfurtransferase TusD","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34874","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2145","complexName":"tRNA-specific 2-thiouridylase tusE-mnmA complex","organismName":"Escherichia coli (strain K12); 83333","description":"mnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln), leading to the formation of s2U34, the first step of tRNA-mnm5s2U34 synthesis. Sulfur is provided by iscS, via a sulfur-relay system. The tusE subunit transfers sulfur (most likely bound to Cys-108 as persulfide) from the TusBCDE complex (CPX-2144) to the tRNA.","predictedComplex":false,"interactors":[{"ac":"EBI-1121167","identifier":"P0AB18","identifierLink":"https://www.uniprot.org/uniprotkb/P0AB18/entry","name":"tusE","description":"Sulfurtransferase TusE","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR37010","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1122413","identifier":"P25745","identifierLink":"https://www.uniprot.org/uniprotkb/P25745/entry","name":"mnmA","description":"tRNA-specific 2-thiouridylase MnmA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11933","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6556605","identifier":"CHEBI:17843","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:17843","name":"trna","description":"transfer RNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"transfer rna","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2149","complexName":"Thioredoxin reductase complex","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyses the reversible reduction and reoxidation of NADP+ and thioredoxin to NADPH and thioredoxin disulfide. In this process, the dithiol-disulfide residues in the active site of TrxR and the flavin adenine dinucleotide (FAD) cofactor are also reduced and reoxidised. Reduced thioredoxin is a reductant for ribonucleotide reductase and an activator of T7 DNA polymerase.","predictedComplex":false,"interactors":[{"ac":"EBI-1029826","identifier":"P0A9P4","identifierLink":"https://www.uniprot.org/uniprotkb/P0A9P4/entry","name":"trxB","description":"Thioredoxin reductase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR48105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1225105","identifier":"CHEBI:16238","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16238","name":"fad","description":"FAD - Flavin adenine dinucleotide","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2150","complexName":"sn-glycerol-3-phosphate ABC transporter complex","organismName":"Escherichia coli (strain K12); 83333","description":"High affinity  glycerol-3-phosphate (G3P) and glycerol-3-phosphocholine (GPC)  transporter. Member of the ATP-binding cassette (ABC) superfamily of transporters, prokaryote-type (PK-type) subfamily. sn-glycerol-3-phosphate, a degradation  product of phospholipids, is utilized as a source  of  carbon and phosphate under starvation conditions.","predictedComplex":false,"interactors":[{"ac":"EBI-1132852","identifier":"P10907","identifierLink":"https://www.uniprot.org/uniprotkb/P10907/entry","name":"ugpC","description":"sn-glycerol-3-phosphate import ATP-binding protein UgpC","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43875","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-546637","identifier":"P0AG80","identifierLink":"https://www.uniprot.org/uniprotkb/P0AG80/entry","name":"ugpB","description":"sn-glycerol-3-phosphate-binding periplasmic protein UgpB","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43649","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8875114","identifier":"P10906","identifierLink":"https://www.uniprot.org/uniprotkb/P10906/entry","name":"ugpE","description":"sn-glycerol-3-phosphate transport system permease protein UgpE","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43744","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8875129","identifier":"P10905","identifierLink":"https://www.uniprot.org/uniprotkb/P10905/entry","name":"ugpA","description":"sn-glycerol-3-phosphate transport system permease protein UgpA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43227","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2151","complexName":"UvrAB DNA damage sensor complex","organismName":"Escherichia coli (strain K12); 83333","description":"Part of the UvrABC repair system that catalyzes the recognition and processing of DNA lesions. It scans the DNA for abnormalities. Upon binding of the UvrAB complex to a putative damaged site, the DNA wraps around one of the uvrB subunits.  uvrB then probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate and the UvrB-DNA preincision complex (CPX-2152) is formed. This complex is subsequently bound by uvrC (P0A8G0) and one of the uvrB monomers is released (CPX-2153). If no lesion is found, the DNA wraps around the other uvrB subunit that will check the other stand for damage. ATP hydrolysis may initiate dissociation of uvrB from the DNA, possibly because no lesion is found.\r\n\r\nThe recruitment process of the uvrAB complex to the DNA remains unknown. A uvrA dimer exists in vitro but it is uncertain if it also exists in vivo as uvrA is sequestered to the DNA by Mfd (CPX-2155).","predictedComplex":false,"interactors":[{"ac":"EBI-552091","identifier":"P0A698","identifierLink":"https://www.uniprot.org/uniprotkb/P0A698/entry","name":"uvrA","description":"UvrABC system protein A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43152","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-552176","identifier":"P0A8F8","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8F8/entry","name":"uvrB","description":"UvrABC system protein B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR24029","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2152","complexName":"UvrB pre-incision complex","organismName":"Escherichia coli (strain K12); 83333","description":"Helicase that couples ATP binding and hydrolysis with domain motion to implement 5'->3' ssDNA translocase activity. The UvrB DNA pre‐incision complex is part of the UvrABC repair system that catalyzes the recognition and processing of DNA lesions. Upon binding of the UvrAB complex (CPX-2151) to a putative damaged site, the DNA wraps around one of the uvrB subunits. If a lesion is found the uvrA subunits dissociate and the UvrB-DNA preincision complex is formed. This complex is subsequently bound by uvrC (P0A8G0) and one of the UvrB monomers is released (CPX-2153). If no lesion is found, the DNA wraps around the other uvrB subunit that will check the other stand for damage.","predictedComplex":false,"interactors":[{"ac":"EBI-552176","identifier":"P0A8F8","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8F8/entry","name":"uvrB","description":"UvrABC system protein B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR24029","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2153","complexName":"UvrBC excinuclease repair complex","organismName":"Escherichia coli (strain K12); 83333","description":"The UvrBC excinuclease repair complex is part of the UvrABC repair system that catalyzes the recognition and processing of DNA lesions. It scans the DNA for abnormalities. Upon binding of the UvrAB complex (CPX-2151) to a putative damaged site, the DNA wraps around one of the uvrB subunits. uvrB probes one DNA strand for the presence of a lesion. If a lesion is found the uvrA subunits dissociate and the uvrB-DNA preincision complex (CPX-2152) is formed. This complex is subsequently bound by uvrC and one of the uvrB monomers is released. uvrC is a  dual endonuclease making incisions on either side of the lesion. The first incision is damage-dependent and is made at the 4th or 5th phosphodiester bond 3' to the lesion by the N-terminal domain of uvrC, while the second, damage-independent incision is made at the 8th phosphodiester bond 5' to the lesion by another endonuclease domain located towards the C-terminus","predictedComplex":false,"interactors":[{"ac":"EBI-552176","identifier":"P0A8F8","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8F8/entry","name":"uvrB","description":"UvrABC system protein B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR24029","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-559448","identifier":"P0A8G0","identifierLink":"https://www.uniprot.org/uniprotkb/P0A8G0/entry","name":"uvrC","description":"UvrABC system protein C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30562","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2155","complexName":"TRCF-UvrA complex","organismName":"Escherichia coli (strain K12); 83333","description":"An SF2 ATPase that orchestrates a preferential pathway for nucleotide excision repair (NER) called transcription-coupled repair (TCR) by specific recognition of the transcription and NER assemblies. mfd recruits the UvrABC repair system (CPX-2151, CPX-2152, CPX-2153) to the unmasked lesion by binding to uvrA, a subunit of the UvrAB complex (CPX-2151). uvrA binding to mdf and uvrB are probably mutually exclusive owing to the conserved interface on uvrA. Formation of the TRCF-UvrA complex initiates a cascade of events resulting in lesion excision and gap filling.","predictedComplex":false,"interactors":[{"ac":"EBI-552091","identifier":"P0A698","identifierLink":"https://www.uniprot.org/uniprotkb/P0A698/entry","name":"uvrA","description":"UvrABC system protein A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43152","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-554211","identifier":"P30958","identifierLink":"https://www.uniprot.org/uniprotkb/P30958/entry","name":"mfd","description":"Transcription-repair-coupling factor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR14025","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2154","complexName":"Guanosine monophosphate reductase 2","organismName":"Homo sapiens; 9606","description":"Plays an important role in the conversion of nucleoside and nucleotide derivatives of guanine (G) to adenine (A) nucleotides, and the maintenance of the intracellular balance between G and A nucleotides. As one of the purine salvage enzymes, GMPR catalyzes the irreversible reductive deamination of GMP to IMP (GMP + 2 H+ + NADPH => IMP + NADP+ + NH4+) and participates in the re-utilization of free intracellular bases and purine nucleosides.","predictedComplex":false,"interactors":[{"ac":"EBI-2806548","identifier":"Q9P2T1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P2T1/entry","name":"GMPR2","description":"GMP reductase 2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43170","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2157","complexName":"Protein geranylgeranyl transferase type I complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the transfer of a 20-carbon lipid, the geranyl-geranyl moiety, from geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X (CaaX box). The Zn2+ is required for peptide, but not for isoprenoid, substrate binding.\r\n\r\nThe hydrophobic geranyl-geranyl moiety aids membrane attachment of the target proteins which include many essential signal transduction proteins, including members of the Ras superfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-602336","identifier":"P49354","identifierLink":"https://www.uniprot.org/uniprotkb/P49354/entry","name":"FNTA","description":"Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8456634","identifier":"P53609","identifierLink":"https://www.uniprot.org/uniprotkb/P53609/entry","name":"PGGT1B","description":"Geranylgeranyl transferase type-1 subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11774","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2949","complexName":"Protein geranylgeranyl transferase type I complex","organismName":"Mus musculus; 10090","description":"Catalyzes the transfer of a 20-carbon lipid, the geranyl-geranyl moiety, from geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X (CaaX box). The Zn2+ is required for peptide, but not for isoprenoid, substrate binding.\r\n\r\nThe hydrophobic geranyl-geranyl moiety aids membrane attachment of the target proteins which include many essential signal transduction proteins, including members of the Ras superfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-9008925","identifier":"Q61239","identifierLink":"https://www.uniprot.org/uniprotkb/Q61239/entry","name":"Fnta","description":"Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9207286","identifier":"Q8BUY9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BUY9/entry","name":"Pggt1b","description":"Geranylgeranyl transferase type-1 subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11774","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2158","complexName":"Hemoglobin HbA complex","organismName":"Homo sapiens; 9606","description":"Adult hemoglobin A (HbA) is expressed in erythrocytes in the bone marrow. Binds oxygen in the lungs and transports it to the various peripheral tissues. Transports CO2 from cells back to the lungs. It appears in late pregnancy and becomes the dominant hemoglobin type in adults, replacing fetal hemoglobin (CPX-2932 & CPX-2933).","predictedComplex":false,"interactors":[{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-714680","identifier":"P69905","identifierLink":"https://www.uniprot.org/uniprotkb/P69905/entry","name":"HBA1","description":"Hemoglobin subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-715554","identifier":"P68871","identifierLink":"https://www.uniprot.org/uniprotkb/P68871/entry","name":"HBB","description":"Hemoglobin subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2922","complexName":"Hemoglobin HbA complex, variant HBB1","organismName":"Mus musculus; 10090","description":"Adult hemoglobin A (HbA) is expressed in erythrocytes in the bone marrow. Binds oxygen in the lungs and transports it to the various peripheral tissues. Transports CO2 from cells back to the lungs. It replaces embryonic haemoglobin zeta-epsilon (CPX-2939) during late pregnancy.","predictedComplex":false,"interactors":[{"ac":"EBI-494191","identifier":"P01942","identifierLink":"https://www.uniprot.org/uniprotkb/P01942/entry","name":"Hba","description":"Hemoglobin subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-494201","identifier":"P02088","identifierLink":"https://www.uniprot.org/uniprotkb/P02088/entry","name":"Hbb-b1","description":"Hemoglobin subunit beta-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2924","complexName":"Hemoglobin HbA complex, variant HBB2","organismName":"Mus musculus; 10090","description":"Adult hemoglobin A (HbA) is expressed in erythrocytes in the bone marrow. Binds oxygen in the lungs and transports it to the various peripheral tissues. Transports CO2 from cells back to the lungs. It replaces embryonic haemoglobin zeta-epsilon (CPX-2939) during late pregnancy.","predictedComplex":false,"interactors":[{"ac":"EBI-494191","identifier":"P01942","identifierLink":"https://www.uniprot.org/uniprotkb/P01942/entry","name":"Hba","description":"Hemoglobin subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-494213","identifier":"P02089","identifierLink":"https://www.uniprot.org/uniprotkb/P02089/entry","name":"Hbb-b2","description":"Hemoglobin subunit beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2925","complexName":"Hemoglobin HbA complex, variant HBB1","organismName":"Rattus norvegicus; 10116","description":"Adult hemoglobin A (HbA) is located within erythrocytes and is involved in oxygen transport from the lung to the various peripheral tissues.","predictedComplex":false,"interactors":[{"ac":"EBI-1209456","identifier":"P01946","identifierLink":"https://www.uniprot.org/uniprotkb/P01946/entry","name":"Hba1","description":"Hemoglobin subunit alpha-1/2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2255993","identifier":"P02091","identifierLink":"https://www.uniprot.org/uniprotkb/P02091/entry","name":"Hbb","description":"Hemoglobin subunit beta-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2926","complexName":"Hemoglobin HbA complex, variant HBB2","organismName":"Rattus norvegicus; 10116","description":"Adult hemoglobin A (HbA) is located within erythrocytes and is involved in oxygen transport from the lung to the various peripheral tissues.","predictedComplex":false,"interactors":[{"ac":"EBI-1209456","identifier":"P01946","identifierLink":"https://www.uniprot.org/uniprotkb/P01946/entry","name":"Hba1","description":"Hemoglobin subunit alpha-1/2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6122082","identifier":"P11517","identifierLink":"https://www.uniprot.org/uniprotkb/P11517/entry","name":"hbb2","description":"Hemoglobin subunit beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2936","complexName":"Hemoglobin HbH complex","organismName":"Homo sapiens; 9606","description":"Hemoglobin H (HbH) is formed when mutations in the gene expressing hemoglobin alpha chain results in a lack of available alpha hemoglobin. The excess beta chains form homotetrameric hemoglobin H that severely reduces oxygen binding and transport.","predictedComplex":false,"interactors":[{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-715554","identifier":"P68871","identifierLink":"https://www.uniprot.org/uniprotkb/P68871/entry","name":"HBB","description":"Hemoglobin subunit beta","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2159","complexName":"GABA-A receptor, alpha1-beta2-gamma2","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets. The alpha1-beta2-gamma2 conformation is thought to be the most common GABA-A receptor found in the brain. Also found in liver, smooth airways muscle and immune cells. Mediates the sedative, anterograde amnestic and in part anticonvulsant actions of diazepam. Isoform 1 and isoform 2 of GABRB2 show reduced expression in schizophrenic brain. Isoform 3 shows increased expression in schizophrenic and bipolar disorder brains while isoform 4 shows reduced expression.","predictedComplex":false,"interactors":[{"ac":"EBI-6258308","identifier":"P14867","identifierLink":"https://www.uniprot.org/uniprotkb/P14867/entry","name":"GABRA1","description":"Gamma-aminobutyric acid receptor subunit alpha-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6949072","identifier":"P47870","identifierLink":"https://www.uniprot.org/uniprotkb/P47870/entry","name":"GABRB2","description":"Gamma-aminobutyric acid receptor subunit beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008430","identifier":"P18507","identifierLink":"https://www.uniprot.org/uniprotkb/P18507/entry","name":"GABRG2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2979","complexName":"GABA-A receptor, alpha1-beta2-gamma2","organismName":"Mus musculus; 10090","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets. The alpha1-beta2-gamma2 conformation is thought to be the most common GABA-A receptor found in the brain. Also found in liver, smooth airways muscle and immune cells.","predictedComplex":false,"interactors":[{"ac":"EBI-770691","identifier":"P62812","identifierLink":"https://www.uniprot.org/uniprotkb/P62812/entry","name":"Gabra1","description":"Gamma-aminobutyric acid receptor subunit alpha-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9215146","identifier":"P22723","identifierLink":"https://www.uniprot.org/uniprotkb/P22723/entry","name":"Gabrg2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9215199","identifier":"P63137","identifierLink":"https://www.uniprot.org/uniprotkb/P63137/entry","name":"Gabrb2","description":"Gamma-aminobutyric acid receptor subunit beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2160","complexName":"Hydrogen:potassium-exchanging ATPase complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the hydrolysis of ATP coupled with the exchange of H+ (outwards) and K+ (inwards) ions across the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-3904463","identifier":"P51164","identifierLink":"https://www.uniprot.org/uniprotkb/P51164/entry","name":"ATP4B","description":"Potassium-transporting ATPase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11523","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6916197","identifier":"P20648","identifierLink":"https://www.uniprot.org/uniprotkb/P20648/entry","name":"ATP4A","description":"Potassium-transporting ATPase alpha chain 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9514326","identifier":"CHEBI:39128","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:39128","name":"magnesium ion","description":"magnesium ion","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2161","complexName":"SUMO activating enzyme complex, SAE1-UBA2","organismName":"Homo sapiens; 9606","description":"An E1 ligase for SUMO1 (P63165-pro_0000035939), SUMO2 (P61956-pro_0000035949), SUMO3 (P55854-pro_0000035957), and probably SUMO4 (Q6eeV6-pro_0000042710). It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2. SUMOylation of UBA2 on three Lys residues on the bipartite nuclear localization sequence (NLS) and two Lys residues outside of but adjacent to the NLS catalyzed by Ubc9 is required for nuclear retention on the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-718569","identifier":"Q9UBT2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UBT2/entry","name":"UBA2","description":"SUMO-activating enzyme subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743154","identifier":"Q9UBE0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UBE0/entry","name":"SAE1","description":"SUMO-activating enzyme subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3041","complexName":"SUMO activating enzyme complex, SAE1-UBA2","organismName":"Mus musculus; 10090","description":"An E1 ligase for SUMO1 (P63166-pro_0000035941), SUMO2 (P61957-pro_0000035951) and SUMO3 (Q9Z172-pro_0000035959). It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2. SUMOylation of UBA2 on three Lys residues on the bipartite nuclear localization sequence (NLS) and two Lys residues outside of but adjacent to the NLS catalyzed by Ubc9 is required for nuclear retention of the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-8320065","identifier":"Q9R1T2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R1T2/entry","name":"Sae1","description":"SUMO-activating enzyme subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-908714","identifier":"Q9Z1F9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z1F9/entry","name":"Uba2","description":"SUMO-activating enzyme subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3075","complexName":"Hydrogen:potassium-exchanging ATPase complex","organismName":"Mus musculus; 10090","description":"Catalyzes the hydrolysis of ATP coupled with the exchange of H+ (outwards) and K+ (inwards) ions across the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-7780224","identifier":"Q64436","identifierLink":"https://www.uniprot.org/uniprotkb/Q64436/entry","name":"Atp4a","description":"Potassium-transporting ATPase alpha chain 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR43294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9514326","identifier":"CHEBI:39128","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:39128","name":"magnesium ion","description":"magnesium ion","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9514455","identifier":"P50992","identifierLink":"https://www.uniprot.org/uniprotkb/P50992/entry","name":"Atp4b","description":"Potassium-transporting ATPase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11523","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2162","complexName":"Protein farnesyltransferase complex","organismName":"Bos taurus; 9913","description":"Catalyzes the transfer of a 15-carbon lipid, the farnesyl moiety, from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X (CaaX box).\r\n\r\nThe hydrophobic farnesyl moiety aids membrane attachment of the target proteins which include many essential signal transduction proteins, including members of the Ras superfamily. Farnesylation is essential both for normal functioning of these proteins, and for the transforming activity of oncogenic mutants.","predictedComplex":false,"interactors":[{"ac":"EBI-9008459","identifier":"P29702","identifierLink":"https://www.uniprot.org/uniprotkb/P29702/entry","name":"FNTA","description":"Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR11129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008468","identifier":"P49355","identifierLink":"https://www.uniprot.org/uniprotkb/P49355/entry","name":"FNTB","description":"Protein farnesyltransferase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR11774","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3077","complexName":"Integrin alpha4-beta7 complex","organismName":"Mus musculus; 10090","description":"Adhesion molecule that mediates lymphocyte transendothelial migration and homing to gut-associated lymphoid tissue (GALT). Mediates rolling as well as firm adhesion through signals from within the cell. Primary ligand is mucosal adhesion molecule-1 (MAdCAM-1, Q13477), an addressin with two immunoglobulin superfamily (IgSF) domains and a mucin-like stalk. Also binds VCAM-1 (P19320) and fibronectin (P02751).","predictedComplex":false,"interactors":[{"ac":"EBI-9516968","identifier":"Q00651","identifierLink":"https://www.uniprot.org/uniprotkb/Q00651/entry","name":"Itga4","description":"Integrin alpha-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9517003","identifier":"P26011","identifierLink":"https://www.uniprot.org/uniprotkb/P26011/entry","name":"Itgb7","description":"Integrin beta-7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2164","complexName":"GABA-A receptor, alpha6-beta3-gamma2","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptor assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.The alpha6-beta3-gamma2 receptor is relatively diazepam-insensitive but able to bind imidazobenzodiazepines and flumazenil.","predictedComplex":false,"interactors":[{"ac":"EBI-6258252","identifier":"P28472","identifierLink":"https://www.uniprot.org/uniprotkb/P28472/entry","name":"GABRB3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008430","identifier":"P18507","identifierLink":"https://www.uniprot.org/uniprotkb/P18507/entry","name":"GABRG2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008507","identifier":"Q16445","identifierLink":"https://www.uniprot.org/uniprotkb/Q16445/entry","name":"GABRA6","description":"Gamma-aminobutyric acid receptor subunit alpha-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1428","complexName":"CAX1 homodimer","organismName":"Arabidopsis thaliana; 3702","description":"Cation antiporter complex that facilitates influx of cations, mainly Ca(2+) ions, into the cell and proton out of the cell. Required for normal growth and ion homeostasis. Loss of CAX1 results in a significant alteration in flowering time and disruption in Ca(2)/H(+) antiport activity. The cax1 mutant displays reduced vacuolar Ca(2+)-ATPase activity and increased expression of CAX3 (Q93Z81) and CAX4 (Q945S5).","predictedComplex":false,"interactors":[{"ac":"EBI-2292388","identifier":"Q39253","identifierLink":"https://www.uniprot.org/uniprotkb/Q39253/entry","name":"CAX1","description":"Vacuolar cation/proton exchanger 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR31503","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1429","complexName":"SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-SKP1B","organismName":"Arabidopsis thaliana; 3702","description":"SCF(COI1) is a member of the SCF (Skp1-Cullin-F-box) E3 ubiquitin ligase family, which catalyse the last step of ubiquitination cascade, promoting transfer of ubiquitin from an E2 enzyme to form a covalent bond with a substrate lysine. It perceives jasmonate signal and degrades Jasmonate ZIM Domain (JAZ) proteins, which repress the transcription factor MYC2 (Q39204) that binds to cis-acting elements of jasmonate response genes.","predictedComplex":false,"interactors":[{"ac":"EBI-16686500","identifier":"CHEBI:24937","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:24937","name":"jasmonates","description":"jasmonates","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-401159","identifier":"O04197","identifierLink":"https://www.uniprot.org/uniprotkb/O04197/entry","name":"COI1","description":"Coronatine-insensitive protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR16134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-532404","identifier":"Q940X7","identifierLink":"https://www.uniprot.org/uniprotkb/Q940X7/entry","name":"RBX1A","description":"RING-box protein 1a","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-532411","identifier":"Q94AH6","identifierLink":"https://www.uniprot.org/uniprotkb/Q94AH6/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-604076","identifier":"Q9FHW7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9FHW7/entry","name":"SKP1B","description":"SKP1-like protein 1B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 3, maxValue: 3","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1430","complexName":"SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK3","organismName":"Arabidopsis thaliana; 3702","description":"SCF(COI1) is a member of the SCF (Skp1-Cullin-F-box) E3 ubiquitin ligase family, which catalyse the last step of ubiquitination cascade, promoting transfer of ubiquitin from an E2 enzyme to form a covalent bond with a substrate lysine. 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It perceives auxin signal and degrades Aux/IAA transcription repressors.","predictedComplex":false,"interactors":[{"ac":"EBI-1251377","identifier":"CHEBI:17401","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:17401","name":"myo-inositol hexakisphosphate","description":"myo-inositol hexakisphosphate","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-307183","identifier":"Q570C0","identifierLink":"https://www.uniprot.org/uniprotkb/Q570C0/entry","name":"TIR1","description":"Protein TRANSPORT INHIBITOR RESPONSE 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR16134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-401215","identifier":"Q9M1X5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9M1X5/entry","name":"ASK13","description":"SKP1-like protein 13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-532404","identifier":"Q940X7","identifierLink":"https://www.uniprot.org/uniprotkb/Q940X7/entry","name":"RBX1A","description":"RING-box protein 1a","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-532411","identifier":"Q94AH6","identifierLink":"https://www.uniprot.org/uniprotkb/Q94AH6/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 3, maxValue: 3","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1527","complexName":"SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK14","organismName":"Arabidopsis thaliana; 3702","description":"SCF-TIR1 is a member of the SCF (Skp1-Cullin-F-box) E3 ubiquitin ligase family, which catalyse the last step of ubiquitination cascade, promoting transfer of ubiquitin from an E2 enzyme to form a covalent bond with a substrate lysine. 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RB1 dissociates from the complex following hyperphosphorylation by cyclin-dependent kinases.","predictedComplex":false,"interactors":[{"ac":"EBI-491274","identifier":"P06400","identifierLink":"https://www.uniprot.org/uniprotkb/P06400/entry","name":"RB1","description":"Retinoblastoma-associated protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-718476","identifier":"Q14209","identifierLink":"https://www.uniprot.org/uniprotkb/Q14209/entry","name":"E2F2","description":"Transcription factor E2F2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12081","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749713","identifier":"Q14186","identifierLink":"https://www.uniprot.org/uniprotkb/Q14186/entry","name":"TFDP1","description":"Transcription factor Dp-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12548","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-176","complexName":"E2F2-DP1 transcription factor complex","organismName":"Mus musculus; 10090","description":"Transcription factor which binds DNA  through the E2 recognition site, 5'-TTTC[CG]CGC-3', typically associated with active promoters in S phase, activating genes that stimulate DNA synthesis and cell cycle advancement.","predictedComplex":false,"interactors":[{"ac":"EBI-1216575","identifier":"Q08639","identifierLink":"https://www.uniprot.org/uniprotkb/Q08639/entry","name":"Tfdp1","description":"Transcription factor Dp-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12548","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8407856","identifier":"P56931","identifierLink":"https://www.uniprot.org/uniprotkb/P56931/entry","name":"E2f2","description":"Transcription factor E2F2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12081","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-177","complexName":"RB1-E2F2-DP1 transcription repressor complex","organismName":"Mus musculus; 10090","description":"Formation of this complex, by binding to Rb1 to the E2F2-DP1 transcription factor complex (CPX-176), negatively regulates the G1-S transition by blocking the transactivation domain of E2F1. Rb1 dissociates from the complex following hyperphosphorylation by cyclin-dependent kinases.","predictedComplex":false,"interactors":[{"ac":"EBI-1216575","identifier":"Q08639","identifierLink":"https://www.uniprot.org/uniprotkb/Q08639/entry","name":"Tfdp1","description":"Transcription factor Dp-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12548","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8407856","identifier":"P56931","identifierLink":"https://www.uniprot.org/uniprotkb/P56931/entry","name":"E2f2","description":"Transcription factor E2F2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12081","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-971782","identifier":"P13405","identifierLink":"https://www.uniprot.org/uniprotkb/P13405/entry","name":"Rb1","description":"Retinoblastoma-associated protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-178","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha2-beta2","organismName":"Rattus norvegicus; 10116","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. Mainly found in optic lobe. Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10916775","identifier":"P12390-PRO_0000000381","identifierLink":"https://www.uniprot.org/uniprotkb/P12390-PRO_0000000381/entry","name":"Chrnb2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-10950443","identifier":"P12389-PRO_0000000343","identifierLink":"https://www.uniprot.org/uniprotkb/P12389-PRO_0000000343/entry","name":"Chrna2","description":"Neuronal acetylcholine receptor subunit alpha-2","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-179","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha2-beta2","organismName":"Gallus gallus; 9031","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. Mainly found in optic lobe. Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10916933","identifier":"P09484-PRO_0000000382","identifierLink":"https://www.uniprot.org/uniprotkb/P09484-PRO_0000000382/entry","name":"CHRNB2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]},{"ac":"EBI-10950449","identifier":"P09480-PRO_0000000344","identifierLink":"https://www.uniprot.org/uniprotkb/P09480-PRO_0000000344/entry","name":"CHRNA2","description":"Neuronal acetylcholine receptor subunit alpha-2","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]}]},{"complexAC":"CPX-180","complexName":"HipBA toxin-antitoxin complex","organismName":"Escherichia coli (strain K12); 83333","description":"Type II toxin-antitoxin (TA) system formed by the toxin (hipA), and the antitoxin (hipB). TA systems act as effectors of dormancy and persistence, with the toxin causing growth arrest by interfering with a vital cellular process, such as  transcription, translation or DNA replication,  and the cognate antitoxin neutralizing the toxin activity during normal growth conditions. The protein kinase HipA acts as a persistence factor, inducing multi-drug tolerance by triggering growth arrest. HipA activity is inhibited upon binding to HipB through sequestration to the nucleoid and binding to DNA. Under conditions of stress the antitoxins are selectively degraded by cellular proteases such as Lon (P0A9M0) and ClpXP (CPX-3176), leaving the toxins to exert their effectsl which result in growth arrest and cell dormancy. Both the antitoxin and, in most cases, the TA complex bind the TA promoter to repress transcription, with TA complexes repressing transcription more efficiently than the antitoxins alone by increasing the co-operativity of antitoxin binding to operators. Complex formation prevents the protein kinase HipA acting as a persistence factor, inducing multi-drug tolerance by triggering growth arrest.","predictedComplex":false,"interactors":[{"ac":"EBI-1129654","identifier":"P23873","identifierLink":"https://www.uniprot.org/uniprotkb/P23873/entry","name":"hipB","description":"Antitoxin HipB","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-560590","identifier":"P23874","identifierLink":"https://www.uniprot.org/uniprotkb/P23874/entry","name":"hipA","description":"Serine/threonine-protein kinase toxin HipA","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR37419","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-181","complexName":"Inward rectifying potassium channel complex, Kir6.2-SUR2A","organismName":"Rattus norvegicus; 10116","description":"Weak inwards rectifying plasma membrane channel complex that facilitated the influx of potassium ions in an ATP- and MgADP-dependent manner and results in membrane hyperpolarisation and shortened action potentials. Activated by binding of MgADP or MgATP to the nucleotide binding domains (NBD) of the ABCC9/SUR2A subunit as well as extracellular K+ binding to the KCNJ11/Kir6.2 subunit. If MgATP binds it must first get hydrolised by the ATP hydrolysis activity of the NBD which also generates PtdIns(4,5)P2 from phosphatidylinositol. Channel activation possibly driven by conformational changes resulting from MgADP binding to SUR subunits and reducing ATP affinity to Kir6.2. Inhibited by intracellular ATP or ADP, Mg2+ and polyamines that bind to the Kir6.2 subunits. ATP/ADP probably changes the conformation of Kir6.2 while Mg2+ and polyamines physically block the flow of K+ through the channel pore. Also inhibited by exogenous sulfonylureas by binding to intracellular loops (possibly by displacing MgADP from NBDs). \r\n\r\nAs ATP is a weak inhibitor Kir6.2 channels can open spontaneously and are classified as constitutively active ion channels. In the absence of ATP (but presence of MgATP), cardiac channels exhibit spontaneous bursts of rapid openings and closings (fast kinetics), which are separated by long closed intervals (slow kinetics). Conversely, ATP destabilizes channel open state and stabilizes its closed states by increasing the speed of gating. \r\n\r\nFound predominantly in cardiac smooth muscle, skeletal muscle smooth muscle, neurons and ovaries. Gating of the atrial K+ channel is mechanosensitive, and mechanical pressure applied to a cardiac cell leads to an increase in their activity.","predictedComplex":false,"interactors":[{"ac":"EBI-10948929","identifier":"Q63563-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q63563-1/entry","name":"Abcc9","description":"ATP-binding cassette sub-family C member 9","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-9560239","identifier":"P70673","identifierLink":"https://www.uniprot.org/uniprotkb/P70673/entry","name":"Kcnj11","description":"ATP-sensitive inward rectifier potassium channel 11","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-182","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha2-beta4","organismName":"Mus musculus; 10090","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10950438","identifier":"Q91X60-PRO_0000000341","identifierLink":"https://www.uniprot.org/uniprotkb/Q91X60-PRO_0000000341/entry","name":"Chrna2","description":"Neuronal acetylcholine receptor subunit alpha-2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-10950470","identifier":"Q8R493-PRO_0000000390","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R493-PRO_0000000390/entry","name":"Chrnb4","description":"Neuronal acetylcholine receptor subunit beta-4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-183","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha2-beta4","organismName":"Rattus norvegicus; 10116","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10950443","identifier":"P12389-PRO_0000000343","identifierLink":"https://www.uniprot.org/uniprotkb/P12389-PRO_0000000343/entry","name":"Chrna2","description":"Neuronal acetylcholine receptor subunit alpha-2","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-10950464","identifier":"P12392-PRO_0000000391","identifierLink":"https://www.uniprot.org/uniprotkb/P12392-PRO_0000000391/entry","name":"Chrnb4","description":"Neuronal acetylcholine receptor subunit beta-4","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-184","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha2-beta4","organismName":"Gallus gallus; 9031","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10950449","identifier":"P09480-PRO_0000000344","identifierLink":"https://www.uniprot.org/uniprotkb/P09480-PRO_0000000344/entry","name":"CHRNA2","description":"Neuronal acetylcholine receptor subunit alpha-2","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]},{"ac":"EBI-10950459","identifier":"P26153-PRO_0000000392","identifierLink":"https://www.uniprot.org/uniprotkb/P26153-PRO_0000000392/entry","name":"CHRNB4","description":"Neuronal acetylcholine receptor subunit beta-4","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]}]},{"complexAC":"CPX-185","complexName":"Inward rectifying potassium channel complex, Kir6.2-SUR2B","organismName":"Rattus norvegicus; 10116","description":"Weak inwards rectifying plasma membrane channel complex that facilitated the influx of potassium ions in an ATP- and MgADP-dependent manner and results in membrane hyperpolarisation and shortened action potentials. Activated by binding of MgADP or MgATP to the nucleotide binding domains (NBD) of the ABCC9/SUR2B subunit as well as extracellular K+ binding to the KCNJ11/Kir6.2 subunit. If MgATP binds it must first get hydrolised by the ATP hydrolysis activity of the NBD which also generates PtdIns(4,5)P2 from phosphatidylinositol. Channel activation possibly driven by conformational changes resulting from MgADP binding to SUR subunits and reducing ATP affinity to Kir6.2. Inhibited by intracellular ATP or ADP, Mg2+ and polyamines that bind to the Kir6.2 subunits. ATP/ADP probably changes the conformation of Kir6.2 while Mg2+ and polyamines physically block the flow of K+ through the channel pore. Also inhibited by exogenous sulfonylureas by binding to intracellular loops (possibly by displacing MgADP from NBDs). \r\n\r\nAs ATP is a weak inhibitor Kir6.2 channels can open spontaneously and are classified as constitutively active ion channels. In the absence of ATP (but presence of MgATP), cardiac channels exhibit spontaneous bursts of rapid openings and closings (fast kinetics), which are separated by long closed intervals (slow kinetics). Conversely, ATP destabilizes channel open state and stabilizes its closed states by increasing the speed of gating. \r\n\r\nFound predominantly in cardiac and vascular smooth muscle and neurons. Gating of the atrial K+ channel is mechanosensitive, and mechanical pressure applied to a cardiac cell leads to an increase in their activity.","predictedComplex":false,"interactors":[{"ac":"EBI-8282518","identifier":"Q63563-2","identifierLink":"https://www.uniprot.org/uniprotkb/Q63563-2/entry","name":"Abcc9","description":"ATP-binding cassette sub-family C member 9","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-9560239","identifier":"P70673","identifierLink":"https://www.uniprot.org/uniprotkb/P70673/entry","name":"Kcnj11","description":"ATP-sensitive inward rectifier potassium channel 11","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-186","complexName":"Inward rectifying potassium channel complex, Kir6.2-SUR1","organismName":"Rattus norvegicus; 10116","description":"Weak inwards rectifying plasma membrane channel complex that facilitated the influx of potassium ions in an ATP- and MgADP-dependent manner and results in membrane hyperpolarisation and shortened action potentials. Activated by binding of MgADP or MgATP to the nucleotide binding domains (NBD) of the ABCC8/SUR1 subunit as well as extracellular K+ binding to the KCNJ11/Kir6.2 subunit. If MgATP binds it must first get hydrolised by the ATP hydrolysis activity of the NBD which also generates PtdIns(4,5)P2 from phosphatidylinositol. Channel activation possibly driven by conformational changes resulting from MgADP binding to SUR subunits and reducing ATP affinity to Kir6.2. Inhibited by intracellular ATP or ADP, Mg2+ and polyamines that bind to the Kir6.2 subunits. ATP/ADP probably changes the conformation of Kir6.2 while Mg2+ and polyamines physically block the flow of K+ through the channel pore. \r\n\r\nAs ATP is a weak inhibitor Kir6.2 channels can open spontaneously and are classified as constitutively active ion channels. In the absence of ATP (but presence of MgATP), cardiac and pancreatic channels exhibit spontaneous bursts of rapid openings and closings (fast kinetics), which are separated by long closed intervals (slow kinetics). Conversely, ATP destabilizes channel open state and stabilizes its closed states by increasing the speed of gating. \r\n\r\nFound predominantly in pancreatic beta-cells where glucose metabolism leads to an increase in intracellular ATP and a concomitant fall in MgADP causing closure of K+ channels, membrane depolarization and opening of voltage-gated calcium channels which ultimately triggers insulin release.","predictedComplex":false,"interactors":[{"ac":"EBI-10949943","identifier":"Q09429","identifierLink":"https://www.uniprot.org/uniprotkb/Q09429/entry","name":"Abcc8","description":"ATP-binding cassette sub-family C member 8","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR24223","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9560239","identifier":"P70673","identifierLink":"https://www.uniprot.org/uniprotkb/P70673/entry","name":"Kcnj11","description":"ATP-sensitive inward rectifier potassium channel 11","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-187","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta2","organismName":"Homo sapiens; 9606","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived, predominantly post-synaptic (PMID:8461135) synaptic transmission of neurotransmitters. alpha5 subunit increases burst duration and rate of desensitization compared to alpha3-beta2 variant. Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10899404","identifier":"P17787-PRO_0000000379","identifierLink":"https://www.uniprot.org/uniprotkb/P17787-PRO_0000000379/entry","name":"CHRNB2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-10950432","identifier":"P32297-PRO_0000000346","identifierLink":"https://www.uniprot.org/uniprotkb/P32297-PRO_0000000346/entry","name":"CHRNA3","description":"Neuronal acetylcholine receptor subunit alpha-3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-10950578","identifier":"P30532-PRO_0000000356","identifierLink":"https://www.uniprot.org/uniprotkb/P30532-PRO_0000000356/entry","name":"CHRNA5","description":"Neuronal acetylcholine receptor subunit alpha-5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-188","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta2","organismName":"Mus musculus; 10090","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived, predominantly post-synaptic (PMID:8461135) synaptic transmission of neurotransmitters. alpha5 subunit increases burst duration and rate of desensitization compared to alpha3-beta2 variant. Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10916261","identifier":"Q9ERK7-PRO_0000000380","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ERK7-PRO_0000000380/entry","name":"Chrnb2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-10951871","identifier":"Q8R4G9-PRO_0000000347","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R4G9-PRO_0000000347/entry","name":"Chrna3","description":"Neuronal acetylcholine receptor subunit alpha-3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-10951910","identifier":"Q2MKA5-PRO_0000304938","identifierLink":"https://www.uniprot.org/uniprotkb/Q2MKA5-PRO_0000304938/entry","name":"Chrna5","description":"Neuronal acetylcholine receptor subunit alpha-5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-189","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha3-beta2","organismName":"Mus musculus; 10090","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. Mainly found in autonomic ganglia. Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10916261","identifier":"Q9ERK7-PRO_0000000380","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ERK7-PRO_0000000380/entry","name":"Chrnb2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-10951871","identifier":"Q8R4G9-PRO_0000000347","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R4G9-PRO_0000000347/entry","name":"Chrna3","description":"Neuronal acetylcholine receptor subunit alpha-3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-190","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta2","organismName":"Rattus norvegicus; 10116","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived, predominantly post-synaptic (PMID:8461135) synaptic transmission of neurotransmitters. alpha5 subunit increases burst duration and rate of desensitization compared to alpha3-beta2 variant. Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10916775","identifier":"P12390-PRO_0000000381","identifierLink":"https://www.uniprot.org/uniprotkb/P12390-PRO_0000000381/entry","name":"Chrnb2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-10951993","identifier":"P04757-PRO_0000000348","identifierLink":"https://www.uniprot.org/uniprotkb/P04757-PRO_0000000348/entry","name":"Chrna3","description":"Neuronal acetylcholine receptor subunit alpha-3","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-10952162","identifier":"P20420-PRO_0000000358","identifierLink":"https://www.uniprot.org/uniprotkb/P20420-PRO_0000000358/entry","name":"Chrna5","description":"Neuronal acetylcholine receptor subunit alpha-5","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-191","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha3-beta2","organismName":"Rattus norvegicus; 10116","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. Mainly found in autonomic ganglia. Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10916775","identifier":"P12390-PRO_0000000381","identifierLink":"https://www.uniprot.org/uniprotkb/P12390-PRO_0000000381/entry","name":"Chrnb2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-10951993","identifier":"P04757-PRO_0000000348","identifierLink":"https://www.uniprot.org/uniprotkb/P04757-PRO_0000000348/entry","name":"Chrna3","description":"Neuronal acetylcholine receptor subunit alpha-3","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-192","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta2","organismName":"Gallus gallus; 9031","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived, predominantly post-synaptic (PMID:8461135) synaptic transmission of neurotransmitters. alpha5 subunit increases burst duration and rate of desensitization compared to alpha3-beta2 variant. Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10916933","identifier":"P09484-PRO_0000000382","identifierLink":"https://www.uniprot.org/uniprotkb/P09484-PRO_0000000382/entry","name":"CHRNB2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]},{"ac":"EBI-10952170","identifier":"P09481-PRO_0000000349","identifierLink":"https://www.uniprot.org/uniprotkb/P09481-PRO_0000000349/entry","name":"CHRNA3","description":"Neuronal acetylcholine receptor subunit alpha-3","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]},{"ac":"EBI-10952185","identifier":"P26152-PRO_0000000359","identifierLink":"https://www.uniprot.org/uniprotkb/P26152-PRO_0000000359/entry","name":"CHRNA5","description":"Neuronal acetylcholine receptor subunit alpha-5","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]}]},{"complexAC":"CPX-193","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha3-beta2","organismName":"Gallus gallus; 9031","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived, predominantly post-synaptic (PMID:8461135) synaptic transmission of neurotransmitters. alpha5 subunit increases burst duration and rate of desensitization compared to alpha3-beta2 variant. Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10916933","identifier":"P09484-PRO_0000000382","identifierLink":"https://www.uniprot.org/uniprotkb/P09484-PRO_0000000382/entry","name":"CHRNB2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]},{"ac":"EBI-10952170","identifier":"P09481-PRO_0000000349","identifierLink":"https://www.uniprot.org/uniprotkb/P09481-PRO_0000000349/entry","name":"CHRNA3","description":"Neuronal acetylcholine receptor subunit alpha-3","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]}]},{"complexAC":"CPX-194","complexName":"Inward rectifying potassium channel complex, Kir6.2-SUR1","organismName":"Mus musculus; 10090","description":"Weak inwards rectifying plasma membrane channel complex that facilitated the influx of potassium ions in an ATP- and MgADP-dependent manner and results in membrane hyperpolarisation and shortened action potentials. Activated by binding of MgADP or MgATP to the nucleotide binding domains (NBD) of the ABCC8/SUR1 subunit as well as extracellular K+ binding to the KCNJ11/Kir6.2 subunit. If MgATP binds it must first get hydrolised by the ATP hydrolysis activity of the NBD which also generates PtdIns(4,5)P2 from phosphatidylinositol. Channel activation possibly driven by conformational changes resulting from MgADP binding to SUR subunits and reducing ATP affinity to Kir6.2. Inhibited by intracellular ATP or ADP, Mg2+ and polyamines that bind to the Kir6.2 subunits. ATP/ADP probably changes the conformation of Kir6.2 while Mg2+ and polyamines physically block the flow of K+ through the channel pore. \r\n\r\nAs ATP is a weak inhibitor Kir6.2 channels can open spontaneously and are classified as constitutively active ion channels. In the absence of ATP (but presence of MgATP), cardiac and pancreatic channels exhibit spontaneous bursts of rapid openings and closings (fast kinetics), which are separated by long closed intervals (slow kinetics). Conversely, ATP destabilizes channel open state and stabilizes its closed states by increasing the speed of gating. \r\n\r\nFound predominantly in pancreatic beta-cells where glucose metabolism leads to an increase in intracellular ATP and a concomitant fall in MgADP causing closure of K+ channels, membrane depolarization and opening of voltage-gated calcium channels which ultimately triggers insulin release.","predictedComplex":false,"interactors":[{"ac":"EBI-10953778","identifier":"B2RUS7","identifierLink":"https://www.uniprot.org/uniprotkb/B2RUS7/entry","name":"Abcc8","description":"ATP-binding cassette sub-family C member 8","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24223","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8603527","identifier":"Q61743","identifierLink":"https://www.uniprot.org/uniprotkb/Q61743/entry","name":"Kcnj11","description":"ATP-sensitive inward rectifier potassium channel 11","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-195","complexName":"Inward rectifying potassium channel complex, Kir6.2-SUR1","organismName":"Homo sapiens; 9606","description":"Weak inwards rectifying plasma membrane channel complex that facilitated the influx of potassium ions in an ATP- and MgADP-dependent manner and results in membrane hyperpolarisation and shortened action potentials. Activated by binding of MgADP or MgATP to the nucleotide binding domains (NBD) of the ABCC8/SUR1 subunit as well as extracellular K+ binding to the KCNJ11/Kir6.2 subunit. If MgATP binds it must first get hydrolised by the ATP hydrolysis activity of the NBD which also generates PtdIns(4,5)P2 from phosphatidylinositol. Channel activation possibly driven by conformational changes resulting from MgADP binding to SUR subunits and reducing ATP affinity to Kir6.2. Inhibited by intracellular ATP or ADP, Mg2+ and polyamines that bind to the Kir6.2 subunits. ATP/ADP probably changes the conformation of Kir6.2 while Mg2+ and polyamines physically block the flow of K+ through the channel pore. Also inhibited by exogenous sulfonylureas by binding to intracellular loops (possibly by displacing MgADP from NBDs) and used to treat diabetic disorders. \r\n\r\nAs ATP is a weak inhibitor Kir6.2 channels can open spontaneously and are classified as constitutively active ion channels. In the absence of ATP (but presence of MgATP), cardiac and pancreatic channels exhibit spontaneous bursts of rapid openings and closings (fast kinetics), which are separated by long closed intervals (slow kinetics). Conversely, ATP destabilizes channel open state and stabilizes its closed states by increasing the speed of gating. \r\n\r\nFound predominantly in pancreatic beta-cells where glucose metabolism leads to an increase in intracellular ATP and a concomitant fall in MgADP causing closure of K+ channels, membrane depolarization and opening of voltage-gated calcium channels which ultimately triggers insulin release.","predictedComplex":false,"interactors":[{"ac":"EBI-2866553","identifier":"Q14654","identifierLink":"https://www.uniprot.org/uniprotkb/Q14654/entry","name":"KCNJ11","description":"ATP-sensitive inward rectifier potassium channel 11","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008940","identifier":"Q09428","identifierLink":"https://www.uniprot.org/uniprotkb/Q09428/entry","name":"ABCC8","description":"ATP-binding cassette sub-family C member 8","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24223","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-196","complexName":"Inward rectifying potassium channel complex, Kir6.2-SUR2A","organismName":"Mus musculus; 10090","description":"Weak inwards rectifying plasma membrane channel complex that facilitated the influx of potassium ions in an ATP- and MgADP-dependent manner and results in membrane hyperpolarisation and shortened action potentials. Activated by binding of MgADP or MgATP to the nucleotide binding domains (NBD) of the ABCC9/SUR2A subunit as well as extracellular K+ binding to the KCNJ11/Kir6.2 subunit. If MgATP binds it must first get hydrolised by the ATP hydrolysis activity of the NBD which also generates PtdIns(4,5)P2 from phosphatidylinositol. Channel activation possibly driven by conformational changes resulting from MgADP binding to SUR subunits and reducing ATP affinity to Kir6.2. Inhibited by intracellular ATP or ADP, Mg2+ and polyamines that bind to the Kir6.2 subunits. ATP/ADP probably changes the conformation of Kir6.2 while Mg2+ and polyamines physically block the flow of K+ through the channel pore. Also inhibited by exogenous sulfonylureas by binding to intracellular loops (possibly by displacing MgADP from NBDs). \r\n\r\nAs ATP is a weak inhibitor Kir6.2 channels can open spontaneously and are classified as constitutively active ion channels. In the absence of ATP (but presence of MgATP), cardiac channels exhibit spontaneous bursts of rapid openings and closings (fast kinetics), which are separated by long closed intervals (slow kinetics). Conversely, ATP destabilizes channel open state and stabilizes its closed states by increasing the speed of gating. \r\n\r\nFound predominantly in cardiac smooth muscle, skeletal muscle smooth muscle, neurons and ovaries. Gating of the atrial K+ channel is mechanosensitive, and mechanical pressure applied to a cardiac cell leads to an increase in their activity.","predictedComplex":false,"interactors":[{"ac":"EBI-10954734","identifier":"P70170-1","identifierLink":"https://www.uniprot.org/uniprotkb/P70170-1/entry","name":"Abcc9","description":"ATP-binding cassette sub-family C member 9","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-8603527","identifier":"Q61743","identifierLink":"https://www.uniprot.org/uniprotkb/Q61743/entry","name":"Kcnj11","description":"ATP-sensitive inward rectifier potassium channel 11","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-197","complexName":"Inward rectifying potassium channel complex, Kir6.2-SUR2A","organismName":"Homo sapiens; 9606","description":"Weak inwards rectifying plasma membrane channel complex that facilitated the influx of potassium ions in an ATP- and MgADP-dependent manner and results in membrane hyperpolarisation and shortened action potentials. Activated by binding of MgADP or MgATP to the nucleotide binding domains (NBD) of the ABCC9/SUR2A subunit as well as extracellular K+ binding to the KCNJ11/Kir6.2 subunit. If MgATP binds it must first get hydrolised by the ATP hydrolysis activity of the NBD which also generates PtdIns(4,5)P2 from phosphatidylinositol. Channel activation possibly driven by conformational changes resulting from MgADP binding to SUR subunits and reducing ATP affinity to Kir6.2. Inhibited by intracellular ATP or ADP, Mg2+ and polyamines that bind to the Kir6.2 subunits. ATP/ADP probably changes the conformation of Kir6.2 while Mg2+ and polyamines physically block the flow of K+ through the channel pore. Also inhibited by exogenous sulfonylureas by binding to intracellular loops (possibly by displacing MgADP from NBDs). \r\n\r\nAs ATP is a weak inhibitor Kir6.2 channels can open spontaneously and are classified as constitutively active ion channels. In the absence of ATP (but presence of MgATP), cardiac channels exhibit spontaneous bursts of rapid openings and closings (fast kinetics), which are separated by long closed intervals (slow kinetics). Conversely, ATP destabilizes channel open state and stabilizes its closed states by increasing the speed of gating. \r\n\r\nFound predominantly in cardiac smooth muscle, skeletal muscle smooth muscle, neurons and ovaries. Gating of the atrial K+ channel is mechanosensitive, and mechanical pressure applied to a cardiac cell leads to an increase in their activity.","predictedComplex":false,"interactors":[{"ac":"EBI-10954780","identifier":"O60706-1","identifierLink":"https://www.uniprot.org/uniprotkb/O60706-1/entry","name":"ABCC9","description":"ATP-binding cassette sub-family C member 9","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2866553","identifier":"Q14654","identifierLink":"https://www.uniprot.org/uniprotkb/Q14654/entry","name":"KCNJ11","description":"ATP-sensitive inward rectifier potassium channel 11","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-198","complexName":"Inward rectifying potassium channel complex, Kir6.2-SUR2B","organismName":"Mus musculus; 10090","description":"Weak inwards rectifying plasma membrane channel complex that facilitated the influx of potassium ions in an ATP- and MgADP-dependent manner and results in membrane hyperpolarisation and shortened action potentials. Activated by binding of MgADP or MgATP to the nucleotide binding domains (NBD) of the ABCC9/SUR2B subunit as well as extracellular K+ binding to the KCNJ11/Kir6.2 subunit. If MgATP binds it must first get hydrolised by the ATP hydrolysis activity of the NBD which also generates PtdIns(4,5)P2 from phosphatidylinositol. Channel activation possibly driven by conformational changes resulting from MgADP binding to SUR subunits and reducing ATP affinity to Kir6.2. Inhibited by intracellular ATP or ADP, Mg2+ and polyamines that bind to the Kir6.2 subunits. ATP/ADP probably changes the conformation of Kir6.2 while Mg2+ and polyamines physically block the flow of K+ through the channel pore. Also inhibited by exogenous sulfonylureas by binding to intracellular loops (possibly by displacing MgADP from NBDs). \r\n\r\nAs ATP is a weak inhibitor Kir6.2 channels can open spontaneously and are classified as constitutively active ion channels. In the absence of ATP (but presence of MgATP), cardiac channels exhibit spontaneous bursts of rapid openings and closings (fast kinetics), which are separated by long closed intervals (slow kinetics). Conversely, ATP destabilizes channel open state and stabilizes its closed states by increasing the speed of gating. \r\n\r\nFound predominantly in cardiac and vascular smooth muscle and neurons. Gating of the atrial K+ channel is mechanosensitive, and mechanical pressure applied to a cardiac cell leads to an increase in their activity.","predictedComplex":false,"interactors":[{"ac":"EBI-10954842","identifier":"P70170-2","identifierLink":"https://www.uniprot.org/uniprotkb/P70170-2/entry","name":"Abcc9","description":"ATP-binding cassette sub-family C member 9","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-8603527","identifier":"Q61743","identifierLink":"https://www.uniprot.org/uniprotkb/Q61743/entry","name":"Kcnj11","description":"ATP-sensitive inward rectifier potassium channel 11","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-199","complexName":"Inward rectifying potassium channel complex, Kir6.2-SUR2B","organismName":"Homo sapiens; 9606","description":"Weak inwards rectifying plasma membrane channel complex that facilitated the influx of potassium ions in an ATP- and MgADP-dependent manner and results in membrane hyperpolarisation and shortened action potentials. Activated by binding of MgADP or MgATP to the nucleotide binding domains (NBD) of the ABCC9/SUR2A subunit as well as extracellular K+ binding to the KCNJ11/Kir6.2 subunit. If MgATP binds it must first get hydrolised by the ATP hydrolysis activity of the NBD which also generates PtdIns(4,5)P2 from phosphatidylinositol. Channel activation possibly driven by conformational changes resulting from MgADP binding to SUR subunits and reducing ATP affinity to Kir6.2. Inhibited by intracellular ATP or ADP, Mg2+ and polyamines that bind to the Kir6.2 subunits. ATP/ADP probably changes the conformation of Kir6.2 while Mg2+ and polyamines physically block the flow of K+ through the channel pore. Also inhibited by exogenous sulfonylureas by binding to intracellular loops (possibly by displacing MgADP from NBDs). \r\n\r\nAs ATP is a weak inhibitor Kir6.2 channels can open spontaneously and are classified as constitutively active ion channels. In the absence of ATP (but presence of MgATP), cardiac channels exhibit spontaneous bursts of rapid openings and closings (fast kinetics), which are separated by long closed intervals (slow kinetics). Conversely, ATP destabilizes channel open state and stabilizes its closed states by increasing the speed of gating. \r\n\r\nFound predominantly in cardiac smooth muscle, skeletal muscle smooth muscle, neurons and ovaries. Gating of the atrial K+ channel is mechanosensitive, and mechanical pressure applied to a cardiac cell leads to an increase in their activity.","predictedComplex":false,"interactors":[{"ac":"EBI-10954896","identifier":"O60706-2","identifierLink":"https://www.uniprot.org/uniprotkb/O60706-2/entry","name":"ABCC9","description":"ATP-binding cassette sub-family C member 9","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2866553","identifier":"Q14654","identifierLink":"https://www.uniprot.org/uniprotkb/Q14654/entry","name":"KCNJ11","description":"ATP-sensitive inward rectifier potassium channel 11","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-200","complexName":"ATG12-ATG5-ATG16L1 complex","organismName":"Homo sapiens; 9606","description":"Essential for autophagy during nutrient deprivation, a catabolic process that sequesters undesired cellular material into autophagosomes for delivery to lysosomes for degradation. Required for the elongation of isolation membranes (phagophores).\r\n\r\nActs as an E3-like enzyme to recruit the E2-like protein ATG3, conjugated to LC3-I, to the endoplasmic reticulum-derived  omegasome. ATG3 binds to and is activated by ATG12, facilitating conjugation of the LC3 to phosphatidylethanolamine, thus converting LC3-I to LC3-II. Therefore, the site of ATG12–ATG5-ATG16L1 complex recruitment determines the site of LC3-II formation. The LC3 family is required for phagophore expansion, closure, and cargo recruitment.","predictedComplex":false,"interactors":[{"ac":"EBI-1047414","identifier":"Q9H1Y0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H1Y0/entry","name":"ATG5","description":"Autophagy protein 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-535909","identifier":"Q676U5","identifierLink":"https://www.uniprot.org/uniprotkb/Q676U5/entry","name":"ATG16L1","description":"Autophagy-related protein 16-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19878","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-746742","identifier":"O94817","identifierLink":"https://www.uniprot.org/uniprotkb/O94817/entry","name":"ATG12","description":"Ubiquitin-like protein ATG12","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13385","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-201","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta2-beta3","organismName":"Gallus gallus; 9031","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10916933","identifier":"P09484-PRO_0000000382","identifierLink":"https://www.uniprot.org/uniprotkb/P09484-PRO_0000000382/entry","name":"CHRNB2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]},{"ac":"EBI-10952170","identifier":"P09481-PRO_0000000349","identifierLink":"https://www.uniprot.org/uniprotkb/P09481-PRO_0000000349/entry","name":"CHRNA3","description":"Neuronal acetylcholine receptor subunit alpha-3","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]},{"ac":"EBI-10955714","identifier":"P49581-PRO_0000000364","identifierLink":"https://www.uniprot.org/uniprotkb/P49581-PRO_0000000364/entry","name":"CHRNA6","description":"Neuronal acetylcholine receptor subunit alpha-6","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]},{"ac":"EBI-10955733","identifier":"P43679-PRO_0000000387","identifierLink":"https://www.uniprot.org/uniprotkb/P43679-PRO_0000000387/entry","name":"CHRNB3","description":"Neuronal acetylcholine receptor subunit beta-3","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]}]},{"complexAC":"CPX-202","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta2-beta3","organismName":"Mus musculus; 10090","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10916261","identifier":"Q9ERK7-PRO_0000000380","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ERK7-PRO_0000000380/entry","name":"Chrnb2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-10951871","identifier":"Q8R4G9-PRO_0000000347","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R4G9-PRO_0000000347/entry","name":"Chrna3","description":"Neuronal acetylcholine receptor subunit alpha-3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-10955799","identifier":"Q9R0W9-PRO_0000000361","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R0W9-PRO_0000000361/entry","name":"Chrna6","description":"Neuronal acetylcholine receptor subunit alpha-6","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-10955834","identifier":"Q8BMN3-PRO_0000000384","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BMN3-PRO_0000000384/entry","name":"Chrnb3","description":"Neuronal acetylcholine receptor subunit beta-3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-203","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta2-beta3","organismName":"Rattus norvegicus; 10116","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10916775","identifier":"P12390-PRO_0000000381","identifierLink":"https://www.uniprot.org/uniprotkb/P12390-PRO_0000000381/entry","name":"Chrnb2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-10951993","identifier":"P04757-PRO_0000000348","identifierLink":"https://www.uniprot.org/uniprotkb/P04757-PRO_0000000348/entry","name":"Chrna3","description":"Neuronal acetylcholine receptor subunit alpha-3","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-10955898","identifier":"P43143-PRO_0000000363","identifierLink":"https://www.uniprot.org/uniprotkb/P43143-PRO_0000000363/entry","name":"Chrna6","description":"Neuronal acetylcholine receptor subunit alpha-6","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-10955942","identifier":"P12391-PRO_0000000386","identifierLink":"https://www.uniprot.org/uniprotkb/P12391-PRO_0000000386/entry","name":"Chrnb3","description":"Neuronal acetylcholine receptor subunit beta-3","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-204","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha3-beta4","organismName":"Mus musculus; 10090","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. Found in the central nervous systems brain (cerebellum, habenula, pineal gland, trigeminal nerve, vagus nerve), the peripheral nervous system (autonomic ganglia, ciliary ganglia) and non-neural tissues (adrenal medulla).\r\nUpregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10950470","identifier":"Q8R493-PRO_0000000390","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R493-PRO_0000000390/entry","name":"Chrnb4","description":"Neuronal acetylcholine receptor subunit beta-4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-10951871","identifier":"Q8R4G9-PRO_0000000347","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R4G9-PRO_0000000347/entry","name":"Chrna3","description":"Neuronal acetylcholine receptor subunit alpha-3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-205","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha3-beta4","organismName":"Rattus norvegicus; 10116","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. Found in the central nervous systems brain (cerebellum, habenula, pineal gland, trigeminal nerve, vagus nerve), the peripheral nervous system (autonomic ganglia, ciliary ganglia) and non-neural tissues (adrenal medulla).\r\nUpregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10950464","identifier":"P12392-PRO_0000000391","identifierLink":"https://www.uniprot.org/uniprotkb/P12392-PRO_0000000391/entry","name":"Chrnb4","description":"Neuronal acetylcholine receptor subunit beta-4","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-10951993","identifier":"P04757-PRO_0000000348","identifierLink":"https://www.uniprot.org/uniprotkb/P04757-PRO_0000000348/entry","name":"Chrna3","description":"Neuronal acetylcholine receptor subunit alpha-3","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-206","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha3-beta4","organismName":"Gallus gallus; 9031","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. Found in the central nervous systems brain (cerebellum, habenula, pineal gland, trigeminal nerve, vagus nerve), the peripheral nervous system (autonomic ganglia, ciliary ganglia) and non-neural tissues (adrenal medulla).\r\nUpregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10950459","identifier":"P26153-PRO_0000000392","identifierLink":"https://www.uniprot.org/uniprotkb/P26153-PRO_0000000392/entry","name":"CHRNB4","description":"Neuronal acetylcholine receptor subunit beta-4","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]},{"ac":"EBI-10952170","identifier":"P09481-PRO_0000000349","identifierLink":"https://www.uniprot.org/uniprotkb/P09481-PRO_0000000349/entry","name":"CHRNA3","description":"Neuronal acetylcholine receptor subunit alpha-3","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]}]},{"complexAC":"CPX-207","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta4","organismName":"Gallus gallus; 9031","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived, predominantly post-synaptic (PMID:8461135) transmission of neurotransmitters. alpha5 subunit increases burst duration and rate of desensitization compared to alpha3-beta2 variant. Mainly found in autonomic or ciliary ganglia (and chick retina). Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10950459","identifier":"P26153-PRO_0000000392","identifierLink":"https://www.uniprot.org/uniprotkb/P26153-PRO_0000000392/entry","name":"CHRNB4","description":"Neuronal acetylcholine receptor subunit beta-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]},{"ac":"EBI-10952170","identifier":"P09481-PRO_0000000349","identifierLink":"https://www.uniprot.org/uniprotkb/P09481-PRO_0000000349/entry","name":"CHRNA3","description":"Neuronal acetylcholine receptor subunit alpha-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]},{"ac":"EBI-10952185","identifier":"P26152-PRO_0000000359","identifierLink":"https://www.uniprot.org/uniprotkb/P26152-PRO_0000000359/entry","name":"CHRNA5","description":"Neuronal acetylcholine receptor subunit alpha-5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]}]},{"complexAC":"CPX-208","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta4","organismName":"Rattus norvegicus; 10116","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived, predominantly post-synaptic (PMID:8461135) transmission of neurotransmitters. alpha5 subunit increases burst duration and rate of desensitization compared to alpha3-beta2 variant. Mainly found in autonomic or ciliary ganglia (and chick retina). Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10950464","identifier":"P12392-PRO_0000000391","identifierLink":"https://www.uniprot.org/uniprotkb/P12392-PRO_0000000391/entry","name":"Chrnb4","description":"Neuronal acetylcholine receptor subunit beta-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-10951993","identifier":"P04757-PRO_0000000348","identifierLink":"https://www.uniprot.org/uniprotkb/P04757-PRO_0000000348/entry","name":"Chrna3","description":"Neuronal acetylcholine receptor subunit alpha-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-10952162","identifier":"P20420-PRO_0000000358","identifierLink":"https://www.uniprot.org/uniprotkb/P20420-PRO_0000000358/entry","name":"Chrna5","description":"Neuronal acetylcholine receptor subunit alpha-5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-209","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta4","organismName":"Mus musculus; 10090","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived, predominantly post-synaptic (PMID:8461135) transmission of neurotransmitters. alpha5 subunit increases burst duration and rate of desensitization compared to alpha3-beta2 variant. Mainly found in autonomic or ciliary ganglia (and chick retina). Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10950470","identifier":"Q8R493-PRO_0000000390","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R493-PRO_0000000390/entry","name":"Chrnb4","description":"Neuronal acetylcholine receptor subunit beta-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-10951871","identifier":"Q8R4G9-PRO_0000000347","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R4G9-PRO_0000000347/entry","name":"Chrna3","description":"Neuronal acetylcholine receptor subunit alpha-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-10951910","identifier":"Q2MKA5-PRO_0000304938","identifierLink":"https://www.uniprot.org/uniprotkb/Q2MKA5-PRO_0000304938/entry","name":"Chrna5","description":"Neuronal acetylcholine receptor subunit alpha-5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-210","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha5-beta4","organismName":"Homo sapiens; 9606","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived, predominantly post-synaptic (PMID:8461135) transmission of neurotransmitters. alpha5 subunit increases burst duration and rate of desensitization compared to alpha3-beta2 variant. Mainly found in autonomic or ciliary ganglia (and chick retina). Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10950432","identifier":"P32297-PRO_0000000346","identifierLink":"https://www.uniprot.org/uniprotkb/P32297-PRO_0000000346/entry","name":"CHRNA3","description":"Neuronal acetylcholine receptor subunit alpha-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-10950454","identifier":"P30926-PRO_0000000389","identifierLink":"https://www.uniprot.org/uniprotkb/P30926-PRO_0000000389/entry","name":"CHRNB4","description":"Neuronal acetylcholine receptor subunit beta-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-10950578","identifier":"P30532-PRO_0000000356","identifierLink":"https://www.uniprot.org/uniprotkb/P30532-PRO_0000000356/entry","name":"CHRNA5","description":"Neuronal acetylcholine receptor subunit alpha-5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-211","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta4","organismName":"Rattus norvegicus; 10116","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. (Mainly found in chick retina). Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10950464","identifier":"P12392-PRO_0000000391","identifierLink":"https://www.uniprot.org/uniprotkb/P12392-PRO_0000000391/entry","name":"Chrnb4","description":"Neuronal acetylcholine receptor subunit beta-4","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-10951993","identifier":"P04757-PRO_0000000348","identifierLink":"https://www.uniprot.org/uniprotkb/P04757-PRO_0000000348/entry","name":"Chrna3","description":"Neuronal acetylcholine receptor subunit alpha-3","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-10955898","identifier":"P43143-PRO_0000000363","identifierLink":"https://www.uniprot.org/uniprotkb/P43143-PRO_0000000363/entry","name":"Chrna6","description":"Neuronal acetylcholine receptor subunit alpha-6","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-212","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta4","organismName":"Mus musculus; 10090","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. (Mainly found in chick retina). Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10950470","identifier":"Q8R493-PRO_0000000390","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R493-PRO_0000000390/entry","name":"Chrnb4","description":"Neuronal acetylcholine receptor subunit beta-4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-10951871","identifier":"Q8R4G9-PRO_0000000347","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R4G9-PRO_0000000347/entry","name":"Chrna3","description":"Neuronal acetylcholine receptor subunit alpha-3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-10955799","identifier":"Q9R0W9-PRO_0000000361","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R0W9-PRO_0000000361/entry","name":"Chrna6","description":"Neuronal acetylcholine receptor subunit alpha-6","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-213","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta4","organismName":"Homo sapiens; 9606","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. (Mainly found in chick retina). Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10950432","identifier":"P32297-PRO_0000000346","identifierLink":"https://www.uniprot.org/uniprotkb/P32297-PRO_0000000346/entry","name":"CHRNA3","description":"Neuronal acetylcholine receptor subunit alpha-3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-10950454","identifier":"P30926-PRO_0000000389","identifierLink":"https://www.uniprot.org/uniprotkb/P30926-PRO_0000000389/entry","name":"CHRNB4","description":"Neuronal acetylcholine receptor subunit beta-4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-10955383","identifier":"Q15825-PRO_0000000360","identifierLink":"https://www.uniprot.org/uniprotkb/Q15825-PRO_0000000360/entry","name":"CHRNA6","description":"Neuronal acetylcholine receptor subunit alpha-6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-214","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha3-alpha6-beta4","organismName":"Gallus gallus; 9031","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. (Mainly found in chick retina). Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10950459","identifier":"P26153-PRO_0000000392","identifierLink":"https://www.uniprot.org/uniprotkb/P26153-PRO_0000000392/entry","name":"CHRNB4","description":"Neuronal acetylcholine receptor subunit beta-4","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]},{"ac":"EBI-10952170","identifier":"P09481-PRO_0000000349","identifierLink":"https://www.uniprot.org/uniprotkb/P09481-PRO_0000000349/entry","name":"CHRNA3","description":"Neuronal acetylcholine receptor subunit alpha-3","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]},{"ac":"EBI-10955714","identifier":"P49581-PRO_0000000364","identifierLink":"https://www.uniprot.org/uniprotkb/P49581-PRO_0000000364/entry","name":"CHRNA6","description":"Neuronal acetylcholine receptor subunit alpha-6","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]}]},{"complexAC":"CPX-215","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha4-alpha5-beta2","organismName":"Rattus norvegicus; 10116","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived, predominantly post-synaptic (PMID:8461135) transmission of neurotransmitters. Mainly found in Central Nervous System. Has limited nicotine sensitivity compared to alpha4-beta2 receptor and is insensitive to pro-inflammatory cytokines, such as TNF-alpha or IL-1beta.","predictedComplex":false,"interactors":[{"ac":"EBI-10916765","identifier":"P09483-PRO_0000000354","identifierLink":"https://www.uniprot.org/uniprotkb/P09483-PRO_0000000354/entry","name":"Chrna4","description":"Neuronal acetylcholine receptor subunit alpha-4","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-10916775","identifier":"P12390-PRO_0000000381","identifierLink":"https://www.uniprot.org/uniprotkb/P12390-PRO_0000000381/entry","name":"Chrnb2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-10952162","identifier":"P20420-PRO_0000000358","identifierLink":"https://www.uniprot.org/uniprotkb/P20420-PRO_0000000358/entry","name":"Chrna5","description":"Neuronal acetylcholine receptor subunit alpha-5","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-216","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha4-alpha5-beta2","organismName":"Mus musculus; 10090","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived, predominantly post-synaptic (PMID:8461135) transmission of neurotransmitters. Mainly found in Central Nervous System. Has limited nicotine sensitivity compared to alpha4-beta2 receptor and is insensitive to pro-inflammatory cytokines, such as TNF-alpha or IL-1beta.","predictedComplex":false,"interactors":[{"ac":"EBI-10916254","identifier":"O70174-PRO_0000000352","identifierLink":"https://www.uniprot.org/uniprotkb/O70174-PRO_0000000352/entry","name":"Chrna4","description":"Neuronal acetylcholine receptor subunit alpha-4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-10916261","identifier":"Q9ERK7-PRO_0000000380","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ERK7-PRO_0000000380/entry","name":"Chrnb2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-10951910","identifier":"Q2MKA5-PRO_0000304938","identifierLink":"https://www.uniprot.org/uniprotkb/Q2MKA5-PRO_0000304938/entry","name":"Chrna5","description":"Neuronal acetylcholine receptor subunit alpha-5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-217","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha4-alpha5-beta2","organismName":"Gallus gallus; 9031","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived, predominantly post-synaptic (PMID:8461135) transmission of neurotransmitters. Mainly found in Central Nervous System. Has limited nicotine sensitivity compared to alpha4-beta2 receptor and is insensitive to pro-inflammatory cytokines, such as TNF-alpha or IL-1beta.","predictedComplex":false,"interactors":[{"ac":"EBI-10916921","identifier":"P09482-PRO_0000000355","identifierLink":"https://www.uniprot.org/uniprotkb/P09482-PRO_0000000355/entry","name":"CHRNA4","description":"Neuronal acetylcholine receptor subunit alpha-4","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]},{"ac":"EBI-10916933","identifier":"P09484-PRO_0000000382","identifierLink":"https://www.uniprot.org/uniprotkb/P09484-PRO_0000000382/entry","name":"CHRNB2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]},{"ac":"EBI-10952185","identifier":"P26152-PRO_0000000359","identifierLink":"https://www.uniprot.org/uniprotkb/P26152-PRO_0000000359/entry","name":"CHRNA5","description":"Neuronal acetylcholine receptor subunit alpha-5","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]}]},{"complexAC":"CPX-218","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha4-alpha5-beta2","organismName":"Homo sapiens; 9606","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived, predominantly post-synaptic (PMID:8461135) transmission of neurotransmitters. Mainly found in Central Nervous System. Has limited nicotine sensitivity compared to alpha4-beta2 receptor and is insensitive to pro-inflammatory cytokines, such as TNF-alpha or IL-1beta.","predictedComplex":false,"interactors":[{"ac":"EBI-10899398","identifier":"P43681-PRO_0000000351","identifierLink":"https://www.uniprot.org/uniprotkb/P43681-PRO_0000000351/entry","name":"CHRNA4","description":"Neuronal acetylcholine receptor subunit alpha-4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-10899404","identifier":"P17787-PRO_0000000379","identifierLink":"https://www.uniprot.org/uniprotkb/P17787-PRO_0000000379/entry","name":"CHRNB2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-10950578","identifier":"P30532-PRO_0000000356","identifierLink":"https://www.uniprot.org/uniprotkb/P30532-PRO_0000000356/entry","name":"CHRNA5","description":"Neuronal acetylcholine receptor subunit alpha-5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-219","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha4-beta4","organismName":"Rattus norvegicus; 10116","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10916765","identifier":"P09483-PRO_0000000354","identifierLink":"https://www.uniprot.org/uniprotkb/P09483-PRO_0000000354/entry","name":"Chrna4","description":"Neuronal acetylcholine receptor subunit alpha-4","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-10950464","identifier":"P12392-PRO_0000000391","identifierLink":"https://www.uniprot.org/uniprotkb/P12392-PRO_0000000391/entry","name":"Chrnb4","description":"Neuronal acetylcholine receptor subunit beta-4","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-220","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha4-beta4","organismName":"Mus musculus; 10090","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10916254","identifier":"O70174-PRO_0000000352","identifierLink":"https://www.uniprot.org/uniprotkb/O70174-PRO_0000000352/entry","name":"Chrna4","description":"Neuronal acetylcholine receptor subunit alpha-4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-10950470","identifier":"Q8R493-PRO_0000000390","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R493-PRO_0000000390/entry","name":"Chrnb4","description":"Neuronal acetylcholine receptor subunit beta-4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-221","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha4-beta4","organismName":"Gallus gallus; 9031","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters. Upregulated by pro-inflammatory cytokines, like TNF-alpha.","predictedComplex":false,"interactors":[{"ac":"EBI-10916921","identifier":"P09482-PRO_0000000355","identifierLink":"https://www.uniprot.org/uniprotkb/P09482-PRO_0000000355/entry","name":"CHRNA4","description":"Neuronal acetylcholine receptor subunit alpha-4","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]},{"ac":"EBI-10950459","identifier":"P26153-PRO_0000000392","identifierLink":"https://www.uniprot.org/uniprotkb/P26153-PRO_0000000392/entry","name":"CHRNB4","description":"Neuronal acetylcholine receptor subunit beta-4","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]}]},{"complexAC":"CPX-222","complexName":"Positive transcription elongation factor B, CDK9-cyclinT1 complex","organismName":"Homo sapiens; 9606","description":"A serine kinase complex that phosphorylates elongation pausing factors such as DSIF (CPX-891) and NELF (CPX-6267) and Ser-2 and Ser-5 of RNA polymerase II (RNA Pol II), thus positively regulating productive mRNA elongation through the gene body after promoter-proximal pausing of RNA Pol II. Involved in cotranscriptional histone modification, mRNA processing and mRNA export. Potential target of anticancer drugs. \r\n\r\nBinds to the transactivation domain of the HIV-1, HIV-2 and SIV nuclear transcriptional activator, Tat, thereby increasing Tat's affinity for the transactivating response RNA element (TAR RNA) leading to RNA Pol II activation and transcription of viral genes.","predictedComplex":false,"interactors":[{"ac":"EBI-1383449","identifier":"P50750","identifierLink":"https://www.uniprot.org/uniprotkb/P50750/entry","name":"CDK9","description":"Cyclin-dependent kinase 9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2479671","identifier":"O60563","identifierLink":"https://www.uniprot.org/uniprotkb/O60563/entry","name":"CCNT1","description":"Cyclin-T1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-223","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha9-alpha10","organismName":"Mus musculus; 10090","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous antagonists such as alpha-bungarotoxin. Unlike classic nicotinic acetylcholine receptors, nicotine blocks acetylcholine-evoked currents in alpha9-alpha10 receptors giving these receptors a pharmacological profile unknown for any other nicotinic or muscarinic cholinergic receptor subtype. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Upregulated by pro-inflammatory cytokines, for example TNF-alpha. Mediates fast, short-lived synaptic transmission of neurotransmitters and is more active than the alpha9 homopentamer (CPX-227). Mainly found in peripheral nervous system and non-neuronal cells, especially in the auditory system (mechanosensory hair, inner-ear tissue, the cochlea) but also in tonsils, immortalized B-cells, cultured T-cells and PBMCs, keratinocytes and in the pituitary gland. In the auditory system the subunits assemble to form the receptor that mediates synaptic transmission between efferent olivocochlear cholinergic fibers which descend from the brainstem and hair cells of the cochlea.","predictedComplex":false,"interactors":[{"ac":"EBI-11165036","identifier":"B2RX82","identifierLink":"https://www.uniprot.org/uniprotkb/B2RX82/entry","name":"Chrna10","description":"Neuronal acetylcholine receptor subunit alpha-10","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11165066","identifier":"G3X8Z7","identifierLink":"https://www.uniprot.org/uniprotkb/G3X8Z7/entry","name":"Chrna9","description":"Neuronal acetylcholine receptor subunit alpha-9","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-224","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha9-alpha10","organismName":"Rattus norvegicus; 10116","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous antagonists such as alpha-bungarotoxin. Unlike classic nicotinic acetylcholine receptors, nicotine blocks acetylcholine-evoked currents in alpha9-alpha10 receptors giving these receptors a pharmacological profile unknown for any other nicotinic or muscarinic cholinergic receptor subtype. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Upregulated by pro-inflammatory cytokines, for example TNF-alpha. Mediates fast, short-lived synaptic transmission of neurotransmitters and is more active than the alpha9 homopentamer (CPX-228). Mainly found in peripheral nervous system and non-neuronal cells, especially in the auditory system (mechanosensory hair, inner-ear tissue, the cochlea) but also in tonsils, immortalized B-cells, cultured T-cells and PBMCs, keratinocytes and in the pituitary gland. In the auditory system the subunits assemble to form the receptor that mediates synaptic transmission between efferent olivocochlear cholinergic fibers which descend from the brainstem and hair cells of the cochlea.","predictedComplex":false,"interactors":[{"ac":"EBI-11165157","identifier":"P43144-PRO_0000000372","identifierLink":"https://www.uniprot.org/uniprotkb/P43144-PRO_0000000372/entry","name":"Chrna9","description":"Neuronal acetylcholine receptor subunit alpha-9","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-11165189","identifier":"Q9JLB5-PRO_0000000377","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JLB5-PRO_0000000377/entry","name":"Chrna10","description":"Neuronal acetylcholine receptor subunit alpha-10","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-225","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha9-alpha10","organismName":"Gallus gallus; 9031","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous antagonists such as alpha-bungarotoxin. Unlike classic nicotinic acetylcholine receptors, nicotine blocks acetylcholine-evoked currents in alpha9-alpha10 receptors giving these receptors a pharmacological profile unknown for any other nicotinic or muscarinic cholinergic receptor subtype. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Upregulated by pro-inflammatory cytokines, for example TNF-alpha. Mediates fast, short-lived synaptic transmission of neurotransmitters and is more active than the alpha9 homopentamer (CPX-229). Mainly found in peripheral nervous system and non-neuronal cells, especially in the auditory system (mechanosensory hair, inner-ear tissue, the cochlea) but also in tonsils, immortalized B-cells, cultured T-cells and PBMCs, keratinocytes and in the pituitary gland. In the auditory system the subunits assemble to form the receptor that mediates synaptic transmission between efferent olivocochlear cholinergic fibers which descend from the brainstem and hair cells of the cochlea.","predictedComplex":false,"interactors":[{"ac":"EBI-11165416","identifier":"Q9PTS8-PRO_0000000373","identifierLink":"https://www.uniprot.org/uniprotkb/Q9PTS8-PRO_0000000373/entry","name":"CHRNA9","description":"Neuronal acetylcholine receptor subunit alpha-9","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]},{"ac":"EBI-11165438","identifier":"Q9I8C7-PRO_0000000378","identifierLink":"https://www.uniprot.org/uniprotkb/Q9I8C7-PRO_0000000378/entry","name":"CHRNA10","description":"Neuronal acetylcholine receptor subunit alpha-10","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]}]},{"complexAC":"CPX-226","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha9","organismName":"Homo sapiens; 9606","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous antagonists like alpha-bungarotoxin. Contrary to classic nicotinic acetylcholine receptors nicotine blocks acetylcholine-evoked currents in alpha9 receptors giving these receptors a pharmacological profile unknown for any other nicotinic or muscarinic cholinergic receptor subtype. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Upregulated by pro-inflammatory cytokines, like TNF-alpha. Mediates fast, short-lived synaptic transmission of neurotransmitters and is less active than the alpha9-alpha10 heteropentamer (CPX-2171). Mainly found in peripheral nervous system and non-neuronal cells, esp. in the auditory system (mechanosensory hair, inner-ear tissue, the cochlea) but also in tonsils, immortalized B-cells, cultured T-cells and PBMCs, keratinocytes and in the pituitary gland. In the auditory system assembles, possibly with the alpha10 subunit, to form the receptor that mediates synaptic transmission between efferent olivocochlear cholinergic fibers which descend from the brainstem and hair cells of the cochlea.","predictedComplex":false,"interactors":[{"ac":"EBI-11164927","identifier":"Q9UGM1-PRO_0000000371","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UGM1-PRO_0000000371/entry","name":"CHRNA9","description":"Neuronal acetylcholine receptor subunit alpha-9","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-227","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha9","organismName":"Mus musculus; 10090","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous antagonists like alpha-bungarotoxin. Contrary to classic nicotinic acetylcholine receptors nicotine blocks acetylcholine-evoked currents in alpha9 receptors giving these receptors a pharmacological profile unknown for any other nicotinic or muscarinic cholinergic receptor subtype. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Upregulated by pro-inflammatory cytokines, like TNF-alpha. Mediates fast, short-lived synaptic transmission of neurotransmitters and is less active than the alpha9-alpha10 heteropentamer (CPX-223). Mainly found in peripheral nervous system and non-neuronal cells, esp. in the auditory system (mechanosensory hair, inner-ear tissue, the cochlea) but also in tonsils, immortalized B-cells, cultured T-cells and PBMCs, keratinocytes and in the pituitary gland. In the auditory system assembles, possibly with the alpha10 subunit, to form the receptor that mediates synaptic transmission between efferent olivocochlear cholinergic fibers which descend from the brainstem and hair cells of the cochlea.","predictedComplex":false,"interactors":[{"ac":"EBI-11165066","identifier":"G3X8Z7","identifierLink":"https://www.uniprot.org/uniprotkb/G3X8Z7/entry","name":"Chrna9","description":"Neuronal acetylcholine receptor subunit alpha-9","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-228","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha9","organismName":"Rattus norvegicus; 10116","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous antagonists like alpha-bungarotoxin. Contrary to classic nicotinic acetylcholine receptors nicotine blocks acetylcholine-evoked currents in alpha9 receptors giving these receptors a pharmacological profile unknown for any other nicotinic or muscarinic cholinergic receptor subtype. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Upregulated by pro-inflammatory cytokines, like TNF-alpha. Mediates fast, short-lived synaptic transmission of neurotransmitters and is less active than the alpha9-alpha10 heteropentamer (CPX-224). Mainly found in peripheral nervous system and non-neuronal cells, esp. in the auditory system (mechanosensory hair, inner-ear tissue, the cochlea) but also in tonsils, immortalized B-cells, cultured T-cells and PBMCs, keratinocytes and in the pituitary gland. In the auditory system assembles, possibly with the alpha10 subunit, to form the receptor that mediates synaptic transmission between efferent olivocochlear cholinergic fibers which descend from the brainstem and hair cells of the cochlea.","predictedComplex":false,"interactors":[{"ac":"EBI-11165157","identifier":"P43144-PRO_0000000372","identifierLink":"https://www.uniprot.org/uniprotkb/P43144-PRO_0000000372/entry","name":"Chrna9","description":"Neuronal acetylcholine receptor subunit alpha-9","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-229","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha9","organismName":"Gallus gallus; 9031","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous antagonists like alpha-bungarotoxin. Contrary to classic nicotinic acetylcholine receptors nicotine blocks acetylcholine-evoked currents in alpha9 receptors giving these receptors a pharmacological profile unknown for any other nicotinic or muscarinic cholinergic receptor subtype. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Upregulated by pro-inflammatory cytokines, like TNF-alpha. Mediates fast, short-lived synaptic transmission of neurotransmitters and is less active than the alpha9-alpha10 heteropentamer (CPX-225). Mainly found in peripheral nervous system and non-neuronal cells, esp. in the auditory system (mechanosensory hair, inner-ear tissue, the cochlea) but also in tonsils, immortalized B-cells, cultured T-cells and PBMCs, keratinocytes and in the pituitary gland. In the auditory system assembles, possibly with the alpha10 subunit, to form the receptor that mediates synaptic transmission between efferent olivocochlear cholinergic fibers which descend from the brainstem and hair cells of the cochlea.","predictedComplex":false,"interactors":[{"ac":"EBI-11165416","identifier":"Q9PTS8-PRO_0000000373","identifierLink":"https://www.uniprot.org/uniprotkb/Q9PTS8-PRO_0000000373/entry","name":"CHRNA9","description":"Neuronal acetylcholine receptor subunit alpha-9","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]}]},{"complexAC":"CPX-230","complexName":"Positive transcription elongation factor B, CDK9-cyclinT1 complex","organismName":"Mus musculus; 10090","description":"A serine kinase complex that phosphorylates elongation pausing factors (e.g. DSIF - DRB sensitivity-inducing factor and NELF - negative elongation factor) and Ser-2 and Ser-5 of RNA polymerase II (RNA Pol II) heptapeptide repeat, thus positively regulating productive mRNA elongation through the gene body after promoter-proximal pausing of RNA Pol II. Involved in cotranscriptional histone modification, mRNA processing and mRNA export.","predictedComplex":false,"interactors":[{"ac":"EBI-2654963","identifier":"Q99J95","identifierLink":"https://www.uniprot.org/uniprotkb/Q99J95/entry","name":"Cdk9","description":"Cyclin-dependent kinase 9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2655009","identifier":"Q9QWV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9QWV9/entry","name":"Ccnt1","description":"Cyclin-T1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-231","complexName":"Snf1 protein kinase complex variant GAL83","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Energy sensor protein kinase complex, activated by glucose depletion. Regulates cellular energy metabolism by activating energy-producing pathways and inhibiting energy-consuming processes via derepression of glucose-repressed genes. Required for the diauxic shift, in which genes required for mitochondrial oxidative metabolism (normally repressed by glucose) are switched on; growth then resumes at a lower rate.  Role in filamentous invasive growth, on glucose depletion, in haploid cells. Regulates haploid invasive growth in response to glucose depletion by affecting adherence by antagonizing NRG1- and NRG2-mediated repression of the FLO11 flocculin and adhesin gene. \r\nThe activity of this complex is modulated by reversible phosphorylation of SNF1 Thr-210 which increases in response to glucose starvation and correlates with large increases in cellular ADP-to-ATP and AMP-to-ATP ratios. Binding of ADP, but not AMP, to the complex protects against dephosphorylation of Thr-210, suggesting that ADP, rather than AMP, may be the critical activating signal. When glucose levels are high, the complex is cytoplasmic. Upon glucose depletion, Gal83-containing SNF1 locates to the nucleus.","predictedComplex":false,"interactors":[{"ac":"EBI-17516","identifier":"P06782","identifierLink":"https://www.uniprot.org/uniprotkb/P06782/entry","name":"SNF1","description":"Carbon catabolite-derepressing protein kinase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17537","identifier":"P12904","identifierLink":"https://www.uniprot.org/uniprotkb/P12904/entry","name":"SNF4","description":"5'-AMP-activated protein kinase subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7244","identifier":"Q04739","identifierLink":"https://www.uniprot.org/uniprotkb/Q04739/entry","name":"GAL83","description":"SNF1 protein kinase subunit beta-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-232","complexName":"Snf1 protein kinase complex variant SIP1","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Energy sensor protein kinase complex, activated by glucose depletion. Regulates cellular energy metabolism by activating energy-producing pathways and inhibiting energy-consuming processes via derepression of glucose-repressed genes. Required for the diauxic shift, in which genes required for mitochondrial oxidative metabolism (normally repressed by glucose) are switched on; growth then resumes at a lower rate. \r\nThe activity of this complex is modulated by reversible phosphorylation of SNF1 Thr-210 which increases in response to glucose starvation and correlates with large increases in cellular ADP-to-ATP and AMP-to-ATP ratios. Binding of ADP, but not AMP, to the complex protects against dephosphorylation of Thr-210, suggesting that ADP, rather than AMP, may be the critical activating signal. When glucose levels are high, the complex is cytoplasmic. Upon glucose depletion, SIP1-containing SNF1 locates to the vacuolar membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-17179","identifier":"P32578","identifierLink":"https://www.uniprot.org/uniprotkb/P32578/entry","name":"SIP1","description":"SNF1 protein kinase subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17516","identifier":"P06782","identifierLink":"https://www.uniprot.org/uniprotkb/P06782/entry","name":"SNF1","description":"Carbon catabolite-derepressing protein kinase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17537","identifier":"P12904","identifierLink":"https://www.uniprot.org/uniprotkb/P12904/entry","name":"SNF4","description":"5'-AMP-activated protein kinase subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-233","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha7","organismName":"Rattus norvegicus; 10116","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous agonists such as nicotine and alpha-bungarotoxin. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived, mainly presynaptic, transmission of neurotransmitters. Found in the Central Nervous System (fore- and midbrain, cerebellum, hippocampus, hypothalamus) and autonomic ganglia (e.g. ciliary ganglia) and retina. Also located non-synaptically. Suppresses inflammatory responses and is up-regulated by pro-inflammatory cytokines, such as TNF-alpha. Promotes endothelial proliferation.","predictedComplex":false,"interactors":[{"ac":"EBI-11166365","identifier":"Q05941-PRO_0000000369","identifierLink":"https://www.uniprot.org/uniprotkb/Q05941-PRO_0000000369/entry","name":"Chrna7","description":"Neuronal acetylcholine receptor subunit alpha-7","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-234","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha7","organismName":"Mus musculus; 10090","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous agonists such as nicotine and alpha-bungarotoxin. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived, mainly presynaptic, transmission of neurotransmitters. Found in the Central Nervous System (fore- and midbrain, cerebellum, hippocampus, hypothalamus) and autonomic ganglia (e.g. ciliary ganglia) and retina. Also located non-synaptically. Suppresses inflammatory responses and is up-regulated by pro-inflammatory cytokines, such as TNF-alpha. Promotes endothelial proliferation.","predictedComplex":false,"interactors":[{"ac":"EBI-11166580","identifier":"P49582-PRO_0000000368","identifierLink":"https://www.uniprot.org/uniprotkb/P49582-PRO_0000000368/entry","name":"Chrna7","description":"Neuronal acetylcholine receptor subunit alpha-7","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-235","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha7","organismName":"Gallus gallus; 9031","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous agonists such as nicotine and alpha-bungarotoxin. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived, mainly presynaptic, transmission of neurotransmitters. Found in the Central Nervous System (fore- and midbrain, cerebellum, hippocampus, hypothalamus) and autonomic ganglia (e.g. ciliary ganglia) and retina. Also located non-synaptically. Suppresses inflammatory responses and is up-regulated by pro-inflammatory cytokines, such as TNF-alpha. Promotes endothelial proliferation.","predictedComplex":false,"interactors":[{"ac":"EBI-11166620","identifier":"P22770-PRO_0000000370","identifierLink":"https://www.uniprot.org/uniprotkb/P22770-PRO_0000000370/entry","name":"CHRNA7","description":"Neuronal acetylcholine receptor subunit alpha-7","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]}]},{"complexAC":"CPX-236","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha7","organismName":"Homo sapiens; 9606","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous agonists such as nicotine and alpha-bungarotoxin. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived, mainly presynaptic, transmission of neurotransmitters. Found in the Central Nervous System (fore- and midbrain, cerebellum, hippocampus, hypothalamus) and autonomic ganglia (e.g. ciliary ganglia) and retina. Also located non-synaptically. Suppresses inflammatory responses and is up-regulated by pro-inflammatory cytokines, such as TNF-alpha. Promotes endothelial proliferation. \r\nCHRFAM7A (Q494W8), is a CHRNA7-FAM7A fusion protein linked to inflammatory response that acts as a negative regulator for the expression of alpha7 pentamers.","predictedComplex":false,"interactors":[{"ac":"EBI-11166664","identifier":"P36544-PRO_0000000366","identifierLink":"https://www.uniprot.org/uniprotkb/P36544-PRO_0000000366/entry","name":"CHRNA7","description":"Neuronal acetylcholine receptor subunit alpha-7","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-237","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha7-beta2","organismName":"Rattus norvegicus; 10116","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous agonists such as nicotine and alpha-bungarotoxin. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters but has lower activity than the alpha7 homopentamer. Found in the forebrain, hippocampus and cerebellum. Up-regulated by pro-inflammatory cytokines, such as TNF-alpha. Activity highly sensitive to beta-amyloid(1-42) peptides.","predictedComplex":false,"interactors":[{"ac":"EBI-10916775","identifier":"P12390-PRO_0000000381","identifierLink":"https://www.uniprot.org/uniprotkb/P12390-PRO_0000000381/entry","name":"Chrnb2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-11166365","identifier":"Q05941-PRO_0000000369","identifierLink":"https://www.uniprot.org/uniprotkb/Q05941-PRO_0000000369/entry","name":"Chrna7","description":"Neuronal acetylcholine receptor subunit alpha-7","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-238","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha7-beta2","organismName":"Mus musculus; 10090","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous agonists such as nicotine and alpha-bungarotoxin. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters but has lower activity than the alpha7 homopentamer. Found in the forebrain, hippocampus and cerebellum. Upregulated by pro-inflammatory cytokines, like TNF-alpha. Activity highly sensitive to beta-amyloid(1-42) peptides.","predictedComplex":false,"interactors":[{"ac":"EBI-10916261","identifier":"Q9ERK7-PRO_0000000380","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ERK7-PRO_0000000380/entry","name":"Chrnb2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-11166580","identifier":"P49582-PRO_0000000368","identifierLink":"https://www.uniprot.org/uniprotkb/P49582-PRO_0000000368/entry","name":"Chrna7","description":"Neuronal acetylcholine receptor subunit alpha-7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-239","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha7-beta2","organismName":"Gallus gallus; 9031","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous agonists such as nicotine and alpha-bungarotoxin. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters but has lower activity than the alpha7 homopentamer. Found in the forebrain, hippocampus and cerebellum. Upregulated by pro-inflammatory cytokines, like TNF-alpha. Activity highly sensitive to beta-amyloid(1-42) peptides.","predictedComplex":false,"interactors":[{"ac":"EBI-10916933","identifier":"P09484-PRO_0000000382","identifierLink":"https://www.uniprot.org/uniprotkb/P09484-PRO_0000000382/entry","name":"CHRNB2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]},{"ac":"EBI-11166620","identifier":"P22770-PRO_0000000370","identifierLink":"https://www.uniprot.org/uniprotkb/P22770-PRO_0000000370/entry","name":"CHRNA7","description":"Neuronal acetylcholine receptor subunit alpha-7","stochiometry":null,"interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]}]},{"complexAC":"CPX-240","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha7-beta2","organismName":"Homo sapiens; 9606","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous agonists such as nicotine and alpha-bungarotoxin. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters but has lower activity than the alpha7 homopentamer. Found in the forebrain, hippocampus and cerebellum. Up-regulated by pro-inflammatory cytokines, such as TNF-alpha. Activity highly sensitive to beta-amyloid(1-42) peptides.","predictedComplex":false,"interactors":[{"ac":"EBI-10899404","identifier":"P17787-PRO_0000000379","identifierLink":"https://www.uniprot.org/uniprotkb/P17787-PRO_0000000379/entry","name":"CHRNB2","description":"Neuronal acetylcholine receptor subunit beta-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-11166664","identifier":"P36544-PRO_0000000366","identifierLink":"https://www.uniprot.org/uniprotkb/P36544-PRO_0000000366/entry","name":"CHRNA7","description":"Neuronal acetylcholine receptor subunit alpha-7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-241","complexName":"Cyclin K-CDK12 complex","organismName":"Homo sapiens; 9606","description":"Cyclin-dependent protein kinase complex involved in regulation of different transcription phases. Phosphorylates the C-terminal domain (CTD) of RNA polymerase II (RNAP II). Preferentially phosphorylates 'Ser-5' in CTD repeats that are already phosphorylated at 'Ser-7', but can also phosphorylate 'Ser-2'. Target of various anti-cancer drugs.","predictedComplex":false,"interactors":[{"ac":"EBI-1055431","identifier":"Q9NYV4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NYV4/entry","name":"CDK12","description":"Cyclin-dependent kinase 12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-739806","identifier":"O75909","identifierLink":"https://www.uniprot.org/uniprotkb/O75909/entry","name":"CCNK","description":"Cyclin-K","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-242","complexName":"FAL1-SGD1 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"ATP-dependent RNA helicase complex required for efficient pre-rRNA processing at the A0, A1 and A2 sites necessary for early steps in maturation of the 18S rRNA of the small ribosomal subunit processome complex (CPX-1604).","predictedComplex":false,"interactors":[{"ac":"EBI-34377","identifier":"Q06132","identifierLink":"https://www.uniprot.org/uniprotkb/Q06132/entry","name":"SGD1","description":"Suppressor of glycerol defect protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR18034","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6776","identifier":"Q12099","identifierLink":"https://www.uniprot.org/uniprotkb/Q12099/entry","name":"FAL1","description":"ATP-dependent RNA helicase FAL1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47958","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-243","complexName":"Respiratory chain complex I","organismName":"Escherichia coli (strain K12); 83333","description":"Catalyses the first step of electron transport by the oxidation of NADH, thus providing two electrons for the reduction of ubiquinone. Electron transfer is coupled with the translocation of protons across the membrane, generating a proton motive force. Preferred NADH dehydrogenase under anaerobic conditions.","predictedComplex":false,"interactors":[{"ac":"EBI-11169646","identifier":"P0AFC3","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFC3/entry","name":"nuoA","description":"NADH-quinone oxidoreductase subunit A","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11058","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11169665","identifier":"P0AFE0","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFE0/entry","name":"nuoJ","description":"NADH-quinone oxidoreductase subunit J","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR33269","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11169682","identifier":"P33607","identifierLink":"https://www.uniprot.org/uniprotkb/P33607/entry","name":"nuoL","description":"NADH-quinone oxidoreductase subunit L","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 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83333","xrefs":[{"identifier":"PTHR10371","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11172266","identifier":"CHEBI:49601","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49601","name":"fe2s2 iron-sulfur cluster","description":"Fe2S2 iron-sulfur cluster","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1118880","identifier":"P31979","identifierLink":"https://www.uniprot.org/uniprotkb/P31979/entry","name":"nuoF","description":"NADH-quinone oxidoreductase subunit F","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1126139","identifier":"P0AFE4","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFE4/entry","name":"nuoK","description":"NADH-quinone oxidoreductase subunit K","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11434","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1131346","identifier":"P0AFD4","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFD4/entry","name":"nuoH","description":"NADH-quinone oxidoreductase subunit H","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11432","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-552399","identifier":"P33599","identifierLink":"https://www.uniprot.org/uniprotkb/P33599/entry","name":"nuoC","description":"NADH-quinone oxidoreductase subunit C/D","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11993","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-558181","identifier":"P0AFD6","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFD6/entry","name":"nuoI","description":"NADH-quinone oxidoreductase subunit I","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR10849","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-559737","identifier":"P33602","identifierLink":"https://www.uniprot.org/uniprotkb/P33602/entry","name":"nuoG","description":"NADH-quinone oxidoreductase subunit G","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9028779","identifier":"CHEBI:64607","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:64607","name":"fe4s4 iron-sulfur cluster","description":"Fe4S4 iron-sulfur cluster","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-906797","identifier":"P0AFC7","identifierLink":"https://www.uniprot.org/uniprotkb/P0AFC7/entry","name":"nuoB","description":"NADH-quinone oxidoreductase subunit B","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR11995","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663515","identifier":"CHEBI:58210","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58210","name":"fmn(3-)","description":"FMN(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-244","complexName":"Adrenomedullin receptor AM1 complex","organismName":"Rattus norvegicus; 10116","description":"A transmembrane, G-protein-coupled signalling receptor complex that serves as the adrenomedullin (AM) receptor to control neovascularization and the stabilization of vascular integrity. AM, a polypeptide, belongs to the calcitonin family of peptides. It is produced by vascular smooth muscle cells and endothelial cells and has strong hypotensive and vasodilation activity. RAMP2 is responsible for transporting CALCRL to the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-11171435","identifier":"Q9JHJ1-PRO_0000030174","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JHJ1-PRO_0000030174/entry","name":"Ramp2","description":"Receptor activity-modifying protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-9008658","identifier":"Q63118","identifierLink":"https://www.uniprot.org/uniprotkb/Q63118/entry","name":"Calcrl","description":"Calcitonin gene-related peptide type 1 receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR45620","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-245","complexName":"Adrenomedullin receptor AM2 complex","organismName":"Rattus norvegicus; 10116","description":"A transmembrane, G-protein-coupled signalling receptor complex that serves as the adrenomedullin (AM) receptor to control neovascularization and the stabilization of vascular integrity. AM, a polypeptide, belongs to the calcitonin family of peptides. It is produced by vascular smooth muscle cells and endothelial cells and has strong hypotensive and vasodilation activity. RAMP3 is responsible for transporting CALCRL to the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-11171471","identifier":"Q9JJ73-PRO_0000030178","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JJ73-PRO_0000030178/entry","name":"Ramp3","description":"Receptor activity-modifying protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-9008658","identifier":"Q63118","identifierLink":"https://www.uniprot.org/uniprotkb/Q63118/entry","name":"Calcrl","description":"Calcitonin gene-related peptide type 1 receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR45620","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-246","complexName":"Amylin receptor 1 complex","organismName":"Rattus norvegicus; 10116","description":"A transmembrane, G-protein-coupled signalling receptor complex that serves as receptor for amylin polypeptide (Amy). \r\n\r\nAmylin is produced in beta-islet cells of the pancreas. It is implicated in selective inhibition of insulin-stimulated glucose utilization and glycogen deposition in muscle, gastric emptying, gastric acid secretion, postprandial glucagon secretion and food intake and aids weight loss. \r\n\r\nCALCR only acts as amylin receptor when bound by RAMP proteins. In the absence of RAMP proteins, CALCR functions as calcitonin receptor. Unlike the calcitonin receptor-like receptors (CPX-248, CPX-244, CPX-245), the calcitonin receptor can migrate to the plasma membrane without guidance from RAMP proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-9008672","identifier":"Q9JJ74","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JJ74/entry","name":"Ramp1","description":"Receptor activity-modifying protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR14076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9009001","identifier":"P32214","identifierLink":"https://www.uniprot.org/uniprotkb/P32214/entry","name":"Calcr","description":"Calcitonin receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR45620","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-247","complexName":"Amylin receptor 2 complex","organismName":"Rattus norvegicus; 10116","description":"A transmembrane, G-protein-coupled signalling receptor complex that serves as receptor for amylin polypeptide (Amy). \r\n\r\nAmylin is produced in beta-islet cells of the pancreas. It is implicated in selective inhibition of insulin-stimulated glucose utilization and glycogen deposition in muscle, gastric emptying, gastric acid secretion, postprandial glucagon secretion and food intake and aids weight loss. \r\n\r\nCALCR only acts as amylin receptor when bound by RAMP proteins. In the absence of RAMP proteins, CALCR functions as calcitonin receptor. Unlike the calcitonin receptor-like receptors (CPX-248, CPX-244, CPX-245), the calcitonin receptor can migrate to the plasma membrane without guidance from RAMP proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-9008980","identifier":"Q9JHJ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JHJ1/entry","name":"Ramp2","description":"Receptor activity-modifying protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR14076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9009001","identifier":"P32214","identifierLink":"https://www.uniprot.org/uniprotkb/P32214/entry","name":"Calcr","description":"Calcitonin receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR45620","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-248","complexName":"CGRP receptor complex","organismName":"Rattus norvegicus; 10116","description":"A transmembrane, G-protein-coupled signalling receptor complex that serves as receptor for calcitonin gene-related peptides (CGRP). CGRPs are produced in both peripheral and central neurons and are one of the most potent peptide vasodilators known. They are expressed at trigeminal nerve endings that innervate cerebral blood vessels, and this localization, its vasodilatory effect, and other evidence suggest a direct role of CGRPs in migraine. RAMP1 is responsible for transporting CALCRL to the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-11171623","identifier":"Q9JJ74-PRO_0000030170","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JJ74-PRO_0000030170/entry","name":"Ramp1","description":"Receptor activity-modifying protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-9008658","identifier":"Q63118","identifierLink":"https://www.uniprot.org/uniprotkb/Q63118/entry","name":"Calcrl","description":"Calcitonin gene-related peptide type 1 receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR45620","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-249","complexName":"Amylin receptor 3 complex","organismName":"Rattus norvegicus; 10116","description":"A transmembrane, G-protein-coupled signalling receptor complex that serves as receptor for amylin polypeptide (Amy). \r\n\r\nAmylin is produced in beta-islet cells of the pancreas. It is implicated in selective inhibition of insulin-stimulated glucose utilization and glycogen deposition in muscle, gastric emptying, gastric acid secretion, postprandial glucagon secretion and food intake and aids weight loss. \r\n\r\nCALCR only acts as amylin receptor when bound by RAMP proteins. In the absence of RAMP proteins, CALCR functions as calcitonin receptor. Unlike the calcitonin receptor-like receptors (CPX-248, CPX-244, CPX-245), the calcitonin receptor can migrate to the plasma membrane without guidance from RAMP proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-9008666","identifier":"Q9JJ73","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JJ73/entry","name":"Ramp3","description":"Receptor activity-modifying protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR14076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9009001","identifier":"P32214","identifierLink":"https://www.uniprot.org/uniprotkb/P32214/entry","name":"Calcr","description":"Calcitonin receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR45620","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-250","complexName":"GABA-A receptor, alpha1-beta2-gamma2","organismName":"Rattus norvegicus; 10116","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.\r\n\r\nThe alpha1-beta2-gamma2 conformation is thought to be the most common GABA-A receptor found in the brain. Also found in liver, smooth airways muscle and immune cells. Mediates the sedative, anterograde amnestic and in part anticonvulsant actions of diazepam. Isoform 1 and isoform 2 of GABRB2 show reduced expression in schizophrenic brain. Isoform 3 shows increased expression in schizophrenic and bipolar disorder brains while isoform 4 shows reduced expression.","predictedComplex":false,"interactors":[{"ac":"EBI-6258047","identifier":"P63138","identifierLink":"https://www.uniprot.org/uniprotkb/P63138/entry","name":"Gabrb2","description":"Gamma-aminobutyric acid receptor subunit beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6258192","identifier":"P62813","identifierLink":"https://www.uniprot.org/uniprotkb/P62813/entry","name":"Gabra1","description":"Gamma-aminobutyric acid receptor subunit alpha-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8601559","identifier":"P18508","identifierLink":"https://www.uniprot.org/uniprotkb/P18508/entry","name":"Gabrg2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-251","complexName":"Cyclin K-CDK12 complex","organismName":"Mus musculus; 10090","description":"Cyclin-dependent protein kinase complex involved in regulation of different transcription phases. Phosphorylates the C-terminal domain (CTD) of RNA polymerase II (RNAP II). Preferentially phosphorylates 'Ser-5' in CTD repeats that are already phosphorylated at 'Ser-7', but can also phosphorylate 'Ser-2'.","predictedComplex":false,"interactors":[{"ac":"EBI-8357367","identifier":"O88874","identifierLink":"https://www.uniprot.org/uniprotkb/O88874/entry","name":"Ccnk","description":"Cyclin-K","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10026","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8387497","identifier":"Q14AX6","identifierLink":"https://www.uniprot.org/uniprotkb/Q14AX6/entry","name":"Cdk12","description":"Cyclin-dependent kinase 12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-252","complexName":"Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-gamma","organismName":"Mus musculus; 10090","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron and ultimately producing muscle contractions. Mediates fast, short-lived synaptic transmission of neurotransmitters at the foetal extrajunctional, non-innervated muscle but acts slower than the adult receptor.","predictedComplex":false,"interactors":[{"ac":"EBI-11172547","identifier":"P04756-PRO_0000000306","identifierLink":"https://www.uniprot.org/uniprotkb/P04756-PRO_0000000306/entry","name":"Chrna1","description":"Acetylcholine receptor subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-11172553","identifier":"P09690-PRO_0000000316","identifierLink":"https://www.uniprot.org/uniprotkb/P09690-PRO_0000000316/entry","name":"Chrnb1","description":"Acetylcholine receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-11172586","identifier":"P02716-PRO_0000000323","identifierLink":"https://www.uniprot.org/uniprotkb/P02716-PRO_0000000323/entry","name":"Chrnd","description":"Acetylcholine receptor subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-11172611","identifier":"P04760-PRO_0000000335","identifierLink":"https://www.uniprot.org/uniprotkb/P04760-PRO_0000000335/entry","name":"Chrng","description":"Acetylcholine receptor subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-253","complexName":"Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-gamma","organismName":"Rattus norvegicus; 10116","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron and ultimately producing muscle contractions. Mediates fast, short-lived synaptic transmission of neurotransmitters at the foetal extra-junctional, non-innervated muscle but acts slower than the adult receptor.","predictedComplex":false,"interactors":[{"ac":"EBI-11172711","identifier":"P25108-PRO_0000000307","identifierLink":"https://www.uniprot.org/uniprotkb/P25108-PRO_0000000307/entry","name":"Chrna1","description":"Acetylcholine receptor subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-11172750","identifier":"P25109-PRO_0000000317","identifierLink":"https://www.uniprot.org/uniprotkb/P25109-PRO_0000000317/entry","name":"Chrnb1","description":"Acetylcholine receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-11172786","identifier":"P25110-PRO_0000000324","identifierLink":"https://www.uniprot.org/uniprotkb/P25110-PRO_0000000324/entry","name":"Chrnd","description":"Acetylcholine receptor subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-11172813","identifier":"P18916-PRO_0000000336","identifierLink":"https://www.uniprot.org/uniprotkb/P18916-PRO_0000000336/entry","name":"Chrng","description":"Acetylcholine receptor subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-254","complexName":"Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-gamma","organismName":"Gallus gallus; 9031","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron and ultimately producing muscle contractions. Mediates fast, short-lived synaptic transmission of neurotransmitters at the foetal extra-junctional, non-innervated muscle but acts slower than the adult receptor.","predictedComplex":false,"interactors":[{"ac":"EBI-11172903","identifier":"P09479-PRO_0000000308","identifierLink":"https://www.uniprot.org/uniprotkb/P09479-PRO_0000000308/entry","name":"CHRNA1","description":"Acetylcholine receptor subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]},{"ac":"EBI-11172919","identifier":"P16005-PRO_0000000318","identifierLink":"https://www.uniprot.org/uniprotkb/P16005-PRO_0000000318/entry","name":"CHRNB1","description":"Acetylcholine receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]},{"ac":"EBI-11172939","identifier":"P02717-PRO_0000000325","identifierLink":"https://www.uniprot.org/uniprotkb/P02717-PRO_0000000325/entry","name":"CHRND","description":"Acetylcholine receptor subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]},{"ac":"EBI-11172959","identifier":"P02713-PRO_0000000337","identifierLink":"https://www.uniprot.org/uniprotkb/P02713-PRO_0000000337/entry","name":"CHRNG","description":"Acetylcholine receptor subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]}]},{"complexAC":"CPX-255","complexName":"Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-epsilon","organismName":"Homo sapiens; 9606","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron and ultimately producing muscle contractions. Mediates fast, short-lived synaptic transmission of neurotransmitters at the neuromuscular junction.","predictedComplex":false,"interactors":[{"ac":"EBI-11172448","identifier":"P02708-PRO_0000000305","identifierLink":"https://www.uniprot.org/uniprotkb/P02708-PRO_0000000305/entry","name":"CHRNA1","description":"Acetylcholine receptor subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-11172459","identifier":"P11230-PRO_0000000315","identifierLink":"https://www.uniprot.org/uniprotkb/P11230-PRO_0000000315/entry","name":"CHRNB1","description":"Acetylcholine receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-11173053","identifier":"Q04844-PRO_0000000329","identifierLink":"https://www.uniprot.org/uniprotkb/Q04844-PRO_0000000329/entry","name":"CHRNE","description":"Acetylcholine receptor subunit epsilon","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-9008829","identifier":"Q07001","identifierLink":"https://www.uniprot.org/uniprotkb/Q07001/entry","name":"CHRND","description":"Acetylcholine receptor subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-256","complexName":"YAP1-TEAD1 transcription factor complex","organismName":"Homo sapiens; 9606","description":"Transcription factor complex of enhancer factor TEF-1 (TEAD) and coactivator YAP1. Plays key role in Hippo signaling pathway involved in organ size control and tumor supression by restricting proliferation and promoting apoptosis. Connective tissue growth factor (CTGF) has been identified as a direct target gene. Associated also with Sveinsson's chorioretinal atrophy caused by TEAD mutation.","predictedComplex":false,"interactors":[{"ac":"EBI-1044059","identifier":"P46937","identifierLink":"https://www.uniprot.org/uniprotkb/P46937/entry","name":"YAP1","description":"Transcriptional coactivator YAP1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR17616","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-529156","identifier":"P28347","identifierLink":"https://www.uniprot.org/uniprotkb/P28347/entry","name":"TEAD1","description":"Transcriptional enhancer factor TEF-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11834","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-257","complexName":"Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-epsilon","organismName":"Mus musculus; 10090","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron and ultimately producing muscle contractions. Mediates fast, short-lived synaptic transmission of neurotransmitters at the neuromuscular junction.","predictedComplex":false,"interactors":[{"ac":"EBI-11172547","identifier":"P04756-PRO_0000000306","identifierLink":"https://www.uniprot.org/uniprotkb/P04756-PRO_0000000306/entry","name":"Chrna1","description":"Acetylcholine receptor subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-11172553","identifier":"P09690-PRO_0000000316","identifierLink":"https://www.uniprot.org/uniprotkb/P09690-PRO_0000000316/entry","name":"Chrnb1","description":"Acetylcholine receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-11172586","identifier":"P02716-PRO_0000000323","identifierLink":"https://www.uniprot.org/uniprotkb/P02716-PRO_0000000323/entry","name":"Chrnd","description":"Acetylcholine receptor subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-11173215","identifier":"P20782-PRO_0000000330","identifierLink":"https://www.uniprot.org/uniprotkb/P20782-PRO_0000000330/entry","name":"Chrne","description":"Acetylcholine receptor subunit epsilon","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-258","complexName":"Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-epsilon","organismName":"Rattus norvegicus; 10116","description":"A ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron and ultimately producing muscle contractions. Mediates fast, short-lived synaptic transmission of neurotransmitters at the neuromuscular junction.","predictedComplex":false,"interactors":[{"ac":"EBI-11172711","identifier":"P25108-PRO_0000000307","identifierLink":"https://www.uniprot.org/uniprotkb/P25108-PRO_0000000307/entry","name":"Chrna1","description":"Acetylcholine receptor subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-11172750","identifier":"P25109-PRO_0000000317","identifierLink":"https://www.uniprot.org/uniprotkb/P25109-PRO_0000000317/entry","name":"Chrnb1","description":"Acetylcholine receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-11172786","identifier":"P25110-PRO_0000000324","identifierLink":"https://www.uniprot.org/uniprotkb/P25110-PRO_0000000324/entry","name":"Chrnd","description":"Acetylcholine receptor subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-11173295","identifier":"P09660-PRO_0000000331","identifierLink":"https://www.uniprot.org/uniprotkb/P09660-PRO_0000000331/entry","name":"Chrne","description":"Acetylcholine receptor subunit epsilon","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-259","complexName":"Acetylcholine binding protein complex","organismName":"Lymnaea stagnalis; 6523","description":"A protein complex released from perisynaptic astrocytes (a type of glial cell) into the synaptic cleft where it binds acetylcoline released from cholinergic presynapses suppressing cholinergic synaptic transmission. Release of AchBP balances the level of cholinergic neurotransmission.","predictedComplex":false,"interactors":[{"ac":"EBI-11173387","identifier":"P58154-PRO_0000000406","identifierLink":"https://www.uniprot.org/uniprotkb/P58154-PRO_0000000406/entry","name":"p58154-pro","description":"Acetylcholine-binding protein","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Lymnaea stagnalis; 6523","xrefs":[]}]},{"complexAC":"CPX-260","complexName":"HCN1 channel complex","organismName":"Mus musculus; 10090","description":"Hyperpolarization-activated cyclic nucleotide-gated (HCN) ion channel that is dually activated by hyperpolarization and binding of cAMP to their cyclic nucleotide binding domain (CNBD) thereby releasing the tonic inhibition exerted by the cytoplasmic CNBD on the channel pore. Contrary to other HCN channels, HCN1 CNBD tetramerises at basal cAMP concentrations and therefore only exhibits a moderate response to cAMP binding. Located presynaptically. Exhibits weak selectivity for potassium over sodium ions and contributes to the native pacemaker currents in heart (If) and in neurons (Ih). \r\n\r\nContrary to other ion-gated channels, HCN channels do not require an accessory unit but depolarisation activity is affected by optional accessory proteins such as TRIP8b (Pex5l, Q8C437) or lipids such as phosphatidylinositol-4,5-biphosphate.","predictedComplex":false,"interactors":[{"ac":"EBI-8766347","identifier":"O88704","identifierLink":"https://www.uniprot.org/uniprotkb/O88704/entry","name":"Hcn1","description":"Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45689","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-983884","identifier":"CHEBI:17489","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:17489","name":"3',5'-cyclic amp","description":"3',5'-cyclic AMP","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-261","complexName":"HCN1 channel complex","organismName":"Homo sapiens; 9606","description":"Hyperpolarization-activated cyclic nucleotide-gated (HCN) ion channel that is dually activated by hyperpolarization and binding of cAMP to their cyclic nucleotide binding domain (CNBD) thereby releasing the tonic inhibition exerted by the cytoplasmic CNBD on the channel pore. Contrary to other HCN channels, HCN1 CNBD tetramerises at basal cAMP concentrations and therefore only exhibits a moderate response to cAMP binding. Located presynaptically. Exhibits weak selectivity for potassium over sodium ions and contributes to the native pacemaker currents in heart (If) and in neurons (Ih). \r\n\r\nContrary to other ion-gated channels, HCN channels do not require an accessory unit but depolarisation activity is affected by optional accessory proteins such as TRIP8b (PEX5L, Q8IYB4) or lipids such as phosphatidylinositol-4,5-biphosphate.","predictedComplex":false,"interactors":[{"ac":"EBI-11173743","identifier":"O60741","identifierLink":"https://www.uniprot.org/uniprotkb/O60741/entry","name":"HCN1","description":"Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45689","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-983884","identifier":"CHEBI:17489","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:17489","name":"3',5'-cyclic amp","description":"3',5'-cyclic AMP","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-262","complexName":"VCP-NSFL1C AAA ATPase complex","organismName":"Homo sapiens; 9606","description":"A type II AAA ATPase that is involved in the dislocation/extraction step of its substrate proteins from cellular structures or multiprotein complexes into the cytosol where they are largely degraded by the proteasome. Required for the monoubiquitylation of Golgi proteins during mitotic Golgi disassembly essential for postmitotic Golgi membrane fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-355164","identifier":"P55072","identifierLink":"https://www.uniprot.org/uniprotkb/P55072/entry","name":"VCP","description":"Transitional endoplasmic reticulum ATPase","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-721577","identifier":"Q9UNZ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UNZ2/entry","name":"NSFL1C","description":"NSFL1 cofactor p47","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-263","complexName":"Vcp-Nsfl1c AAA ATPase complex","organismName":"Rattus norvegicus; 10116","description":"Promotes membrane fusion of nucleus-, endoplasmic reticulum-, and Golgi apparatus-derived membranes.","predictedComplex":false,"interactors":[{"ac":"EBI-1993760","identifier":"O35987","identifierLink":"https://www.uniprot.org/uniprotkb/O35987/entry","name":"Nsfl1c","description":"NSFL1 cofactor p47","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR23333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-399011","identifier":"P46462","identifierLink":"https://www.uniprot.org/uniprotkb/P46462/entry","name":"Vcp","description":"Transitional endoplasmic reticulum ATPase","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-264","complexName":"Vcp-Nsfl1c AAA ATPase complex","organismName":"Mus musculus; 10090","description":"Promotes membrane fusion of nucleus-, endoplasmic reticulum-, and Golgi apparatus-derived membranes.","predictedComplex":false,"interactors":[{"ac":"EBI-7961368","identifier":"Q9CZ44","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CZ44/entry","name":"Nsfl1c","description":"NSFL1 cofactor p47","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-80597","identifier":"Q01853","identifierLink":"https://www.uniprot.org/uniprotkb/Q01853/entry","name":"Vcp","description":"Transitional endoplasmic reticulum ATPase","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-266","complexName":"Mitochondrial respiratory chain complex I","organismName":"Mus musculus; 10090","description":"Catalyses the first step of electron transport by the oxidation of NADH, thus providing two electrons for the reduction of ubiquinone. Electron transfer is coupled with the translocation of protons across the membrane, generating a proton motive force. Human has one additional member of the complex, NDUFB1 (O75438) but an orthologue of this cannot be found in rodents. An additional protein, NDUFA4L2 (Q4FZG9), may also be apart of the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-11172266","identifier":"CHEBI:49601","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49601","name":"fe2s2 iron-sulfur cluster","description":"Fe2S2 iron-sulfur cluster","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-11177405","identifier":"Q8BK30","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BK30/entry","name":"Ndufv3","description":"NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR17117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11177420","identifier":"O35683","identifierLink":"https://www.uniprot.org/uniprotkb/O35683/entry","name":"Ndufa1","description":"NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 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10090","xrefs":[{"identifier":"PTHR17097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11177488","identifier":"P03899","identifierLink":"https://www.uniprot.org/uniprotkb/P03899/entry","name":"mt-Nd3","description":"NADH-ubiquinone oxidoreductase chain 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11058","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11177603","identifier":"Q9CPU2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CPU2/entry","name":"Ndufb2","description":"NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15223","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11177619","identifier":"P03903","identifierLink":"https://www.uniprot.org/uniprotkb/P03903/entry","name":"Mtnd4l","description":"NADH-ubiquinone oxidoreductase chain 4L","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11434","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1225105","identifier":"CHEBI:16238","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16238","name":"fad","description":"FAD - Flavin adenine dinucleotide","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-15326276","identifier":"P0DN34","identifierLink":"https://www.uniprot.org/uniprotkb/P0DN34/entry","name":"Ndufb1","description":"NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2255517","identifier":"Q9CQ75","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQ75/entry","name":"Ndufa2","description":"NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12878","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2255646","identifier":"Q9CQC7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQC7/entry","name":"Ndufb4","description":"NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15469","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2934254","identifier":"Q9D8B4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D8B4/entry","name":"Ndufa11","description":"NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 11","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21382","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2934268","identifier":"P03888","identifierLink":"https://www.uniprot.org/uniprotkb/P03888/entry","name":"Mtnd1","description":"NADH-ubiquinone oxidoreductase chain 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11432","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2934287","identifier":"Q99LY9","identifierLink":"https://www.uniprot.org/uniprotkb/Q99LY9/entry","name":"Ndufs5","description":"NADH dehydrogenase [ubiquinone] iron-sulfur protein 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15224","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2934302","identifier":"P03921","identifierLink":"https://www.uniprot.org/uniprotkb/P03921/entry","name":"Mtnd5","description":"NADH-ubiquinone oxidoreductase chain 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR42829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2934319","identifier":"Q91YT0","identifierLink":"https://www.uniprot.org/uniprotkb/Q91YT0/entry","name":"Ndufv1","description":"NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2934342","identifier":"O09111","identifierLink":"https://www.uniprot.org/uniprotkb/O09111/entry","name":"Ndufb11","description":"NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 11, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13327","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2934359","identifier":"Q9CXZ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CXZ1/entry","name":"Ndufs4","description":"NADH dehydrogenase [ubiquinone] iron-sulfur protein 4, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12219","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2934375","identifier":"Q9CQZ6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQZ6/entry","name":"Ndufb3","description":"NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2934391","identifier":"Q9D6J5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D6J5/entry","name":"Ndufb8","description":"NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12840","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2934407","identifier":"Q8K3J1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K3J1/entry","name":"Ndufs8","description":"NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10849","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2934427","identifier":"Q3UIU2","identifierLink":"https://www.uniprot.org/uniprotkb/Q3UIU2/entry","name":"Ndufb6","description":"NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 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-2","xrefs":[]},{"ac":"EBI-9663515","identifier":"CHEBI:58210","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58210","name":"fmn(3-)","description":"FMN(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-267","complexName":"HCN3 channel complex","organismName":"Homo sapiens; 9606","description":"Hyperpolarization-activated cyclic nucleotide-gated (HCN) ion channel that is activated by membrane hyperpolarization but contrary to other HCN channels, HCN3 is not activated by cAMP (which may even act as a weak inhibitor for the HCN3 channel). Exhibits selectivity for potassium over sodium ions and contributes to the native pacemaker currents in heart (If) and in neurons (Ih). \r\n\r\nContrary to other ion-gated channels, HCN channels do not require an accessory unit but depolarisation activity is affected by optional accessory proteins such as TRIP8b (PEX5L, Q8IYB4) or lipids such as phosphatidylinositol-4,5-biphosphate.","predictedComplex":false,"interactors":[{"ac":"EBI-11178054","identifier":"Q9P1Z3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P1Z3/entry","name":"HCN3","description":"Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45689","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-268","complexName":"Cytochrome bd-I ubiquinol oxidase complex","organismName":"Escherichia coli (strain K12); 83333","description":"A protein complex integral to the bacterial electron transport chain. Electrons are donated by the oxidation of ubiquinol to ubiquinone and used to reduce molecular oxygen, generating a proton motive force using protons and electrons from opposite sides of the membrane to generate water.","predictedComplex":false,"interactors":[{"ac":"EBI-11178108","identifier":"CHEBI:62811","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:62811","name":"heme d cis-diol","description":"heme d cis-diol","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1213195","identifier":"P0ABK2","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABK2/entry","name":"cydB","description":"Cytochrome bd-I ubiquinol oxidase subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43141","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1225103","identifier":"CHEBI:26355","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:26355","name":"heme b","description":"Heme b","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-906928","identifier":"P0ABJ9","identifierLink":"https://www.uniprot.org/uniprotkb/P0ABJ9/entry","name":"cydA","description":"Cytochrome bd-I ubiquinol oxidase subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30365","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9258541","identifier":"P56100","identifierLink":"https://www.uniprot.org/uniprotkb/P56100/entry","name":"cydX","description":"Cytochrome bd-I ubiquinol oxidase subunit X","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]}]},{"complexAC":"CPX-269","complexName":"Cytochrome bd-II ubiquinol oxidase complex","organismName":"Escherichia coli (strain K12); 83333","description":"A protein complex integral to the bacterial electron transport chain. Electrons are donated by the oxidation of ubiquinol to ubiquinone and used to reduce molecular oxygen, generating a proton motive force using protons and electrons from opposite sides of the membrane to generate water. This complex appears to be expressed under micro-aerobic conditions or under conditions of phosphate starvation.","predictedComplex":false,"interactors":[{"ac":"EBI-11178289","identifier":"P26458","identifierLink":"https://www.uniprot.org/uniprotkb/P26458/entry","name":"appB","description":"Cytochrome bd-II ubiquinol oxidase subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR43141","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-906911","identifier":"P26459","identifierLink":"https://www.uniprot.org/uniprotkb/P26459/entry","name":"appC","description":"Cytochrome bd-II ubiquinol oxidase subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR30365","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-270","complexName":"HCN3 channel complex","organismName":"Mus musculus; 10090","description":"Hyperpolarization-activated cyclic nucleotide-gated (HCN) ion channel that is activated by membrane hyperpolarization but contrary to other HCN channels, HCN3 is not activated by cAMP (which may even act as a weak inhibitor for the HCN3 channel). Exhibits selectivity for potassium over sodium ions and contributes to the native pacemaker currents in heart (If) and in neurons (Ih). \r\n\r\nContrary to other ion-gated channels, HCN channels do not require an accessory unit but depolarisation activity is affected by optional accessory proteins such as TRIP8b (PEX5L, Q8C437) or lipids such as phosphatidylinositol-4,5-biphosphate.","predictedComplex":false,"interactors":[{"ac":"EBI-11294251","identifier":"O88705","identifierLink":"https://www.uniprot.org/uniprotkb/O88705/entry","name":"Hcn3","description":"Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45689","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-271","complexName":"5-hydroxytryptamine-3A/B receptor complex","organismName":"Homo sapiens; 9606","description":"Inward-rectifying, ligand-gated ion channel, which when activated by 5-hydroxytryptamine (5-HT, serotonin) causes fast neuronal depolarization and excitation or modulation of neurotransmitter release depending on their neuronal localisation (central and/or peripheral nervous system). A cation-specific, but otherwise relatively non-selective, ion channel with low conductance. Ca2+-permeability is related to subunit composition with 5HT3A homopentamers being more permeable than 5HT3A/B heteropentamers. \r\n\r\nFound pre- and post-synaptically but with different properties - pre-synaptic 5-HT3 receptors are predominantly calcium-permeant while post-synaptic receptors are permeant to Na+ and K+. Also Mg2+ permeant. Pre-synaptic depolarisations are generally slower than post-synaptic depolarisations. \r\n\r\n5-HT3 receptors increase the frequency of spontaneous excitatory post-synaptic currents (sEPSCs) or miniature EPSCs (mEPSCs). These may be related to 5-HT3-induced depolarisation of pre-synaptic membranes and subsequent activation of cholinergic or glutamatergic neurotransmissions or evoked excitatory post-synaptic currents (eEPSCs) or spontaneous inhibitory post-synaptic currents (sIPSCs) related to GABAergic neurotransmissions post-synaptic 5-HT3 receptor activation. \r\n\r\nDue to different residues in transmembrane domain M2 of the 5-HT3A and 5-HT3B subunits the 5-HT3A/B heteromeric receptors are more efficient conductors than 5-HT3A homomeric receptors and have increased agonist and antagonist affinity. Homomeric receptors recover faster from desensitisation but are probably less prevalent in vivo. \r\n\r\nHigh levels of expression are found in the vagal terminals of the dorsal vagal complex where it is involved in the vomiting reflex (especially post-operative and chemotherapy- and radiation-induced vomiting and nausea), in the amygdala and the hippocampi. 5-HT3 receptor antagonists therefore act as effective anti-emetic drugs. Lower levels of expression are found in the forebrain with higher relative expression in the striatum than the cortical regions. \r\n\r\nInvolved in processes associated with emotion, cognition, memory and pain perception. \r\n\r\nInvolved in ganglionic transmission in the myenteric plexus in the mucosal layer and expressed in the gastrointestinal (GI) tract where serotonin mediates control over a variety of physiological functions such as the contraction/relaxation of smooth muscle, and peristaltic and secretory reflexes, directly or indirectly through intrinsic primary afferent neurons. \r\n\r\nPlays an important role in the regulation of inflammation and immune responses in the peripheral nervous system. \r\n\r\nActivation of 5-HT3 receptors on visceral afferents in some irritable bowel syndrome (IBS) patients results in visceral hypersensitivity. \r\n\r\nChaperone proteins assist assembly, modifications and export from the ER followed by transport in vesicle-like structures along microtubules to the plasma membrane where they typically form clusters in F-actin-rich regions.","predictedComplex":false,"interactors":[{"ac":"EBI-9008726","identifier":"O95264","identifierLink":"https://www.uniprot.org/uniprotkb/O95264/entry","name":"HTR3B","description":"5-hydroxytryptamine receptor 3B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008743","identifier":"P46098","identifierLink":"https://www.uniprot.org/uniprotkb/P46098/entry","name":"HTR3A","description":"5-hydroxytryptamine receptor 3A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-272","complexName":"5-hydroxytryptamine-3A/D receptor complex","organismName":"Homo sapiens; 9606","description":"Inward-rectifying, ligand-gated ion channel, which when activated by 5-hydroxytryptamine (5-HT, serotonin) causes fast neuronal depolarization and excitation or modulation of neurotransmitter release depending on their neuronal localisation (central and/or peripheral nervous system). A cation-specific, but otherwise relatively non-selective, ion channel with low conductance. Ca2+-permeability is related to subunit composition with 5HT3A homopentamers being more permeable than 5HT3A/B heteropentamers. \r\n\r\nFound pre- and post-synaptically but with different properties - pre-synaptic 5-HT3 receptors are predominantly calcium-permeant while post-synaptic receptors are permeant to Na+ and K+. Also Mg2+ permeant. Pre-synaptic depolarisations are generally slower than post-synaptic depolarisations. \r\n\r\n5-HT3 receptors increase the frequency of spontaneous excitatory post-synaptic currents (sEPSCs) or miniature EPSCs (mEPSCs). These may be related to 5-HT3-induced depolarisation of pre-synaptic membranes and subsequent activation of cholinergic or glutamatergic neurotransmissions or evoked excitatory post-synaptic currents (eEPSCs) or spontaneous inhibitory post-synaptic currents (sIPSCs) related to GABAergic neurotransmissions post-synaptic 5-HT3 receptor activation. \r\n\r\n5-HT3 receptors are highly expressed in the vagal terminals of the dorsal vagal complex where it is involved in the vomiting reflex (especially post-operative and chemotherapy- and radiation-induced vomiting and nausea). 5-HT3 receptor antagonists therefore act as effective anti-emetic drugs. \r\n\r\n5-HT3D subunits are predominantly expressed in the gastrointestinal (GI) tract where serotonin mediates control over a variety of physiological functions such as the contraction/relaxation of smooth muscle, and peristaltic and secretory reflexes, directly or indirectly through intrinsic primary afferent neurons. \r\n\r\nPlays an important role in the regulation of inflammation and immune responses in the peripheral nervous system. \r\n\r\nActivation of 5-HT3 receptors on visceral afferents in some irritable bowel syndrome (IBS) patients results in visceral hypersensitivity. \r\n\r\nChaperone proteins assist assembly, modifications and export from the ER followed by transport in vesicle-like structures along microtubules to the plasma membrane where they typically form clusters in F-actin-rich regions.","predictedComplex":false,"interactors":[{"ac":"EBI-9008717","identifier":"Q70Z44","identifierLink":"https://www.uniprot.org/uniprotkb/Q70Z44/entry","name":"HTR3D","description":"5-hydroxytryptamine receptor 3D","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008743","identifier":"P46098","identifierLink":"https://www.uniprot.org/uniprotkb/P46098/entry","name":"HTR3A","description":"5-hydroxytryptamine receptor 3A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-273","complexName":"5-hydroxytryptamine-3A/E receptor complex","organismName":"Homo sapiens; 9606","description":"Inward-rectifying, ligand-gated ion channel, which when activated by 5-hydroxytryptamine (5-HT, serotonin) causes fast neuronal depolarization and excitation or modulation of neurotransmitter release depending on their neuronal localisation (central and/or peripheral nervous system). A cation-specific, but otherwise relatively non-selective, ion channel with low conductance. Ca2+-permeability is related to subunit composition with 5HT3A homopentamers being more permeable than 5HT3A/B heteropentamers. \r\n\r\nFound pre- and post-synaptically but with different properties - pre-synaptic 5-HT3 receptors are predominantly calcium-permeant while post-synaptic receptors are permeant to Na+ and K+. Also Mg2+ permeant. Pre-synaptic depolarisations are generally slower than post-synaptic depolarisations. \r\n\r\n5-HT3 receptors increase the frequency of spontaneous excitatory post-synaptic currents (sEPSCs) or miniature EPSCs (mEPSCs). These may be related to 5-HT3-induced depolarisation of pre-synaptic membranes and subsequent activation of cholinergic or glutamatergic neurotransmissions or evoked excitatory post-synaptic currents (eEPSCs) or spontaneous inhibitory post-synaptic currents (sIPSCs) related to GABAergic neurotransmissions post-synaptic 5-HT3 receptor activation. \r\n\r\n5-HT3E subunits are exclusively expressed in the gastrointestinal (GI) tract where serotonin mediates control over a variety of physiological functions such as the contraction/relaxation of smooth muscle, and peristaltic and secretory reflexes, directly or indirectly through intrinsic primary afferent neurons. \r\n\r\nPlays an important role in the regulation of inflammation and immune responses in the peripheral nervous system. \r\n\r\nActivation of 5-HT3 receptors on visceral afferents in some irritable bowel syndrome (IBS) patients results in visceral hypersensitivity. \r\n\r\nChaperone proteins assist assembly, modifications and export from the ER followed by transport in vesicle-like structures along microtubules to the plasma membrane where they typically form clusters in F-actin-rich regions.","predictedComplex":false,"interactors":[{"ac":"EBI-9008732","identifier":"A5X5Y0","identifierLink":"https://www.uniprot.org/uniprotkb/A5X5Y0/entry","name":"HTR3E","description":"5-hydroxytryptamine receptor 3E","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008743","identifier":"P46098","identifierLink":"https://www.uniprot.org/uniprotkb/P46098/entry","name":"HTR3A","description":"5-hydroxytryptamine receptor 3A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-274","complexName":"5-hydroxytryptamine-3A receptor complex","organismName":"Mus musculus; 10090","description":"Inward-rectifying, ligand-gated ion channel, which when activated by 5-hydroxytryptamine (5-HT, serotonin) causes fast neuronal depolarization and excitation or modulation of neurotransmitter release depending on their neuronal localisation (central and/or peripheral nervous system). A cation-specific, but otherwise relatively non-selective, ion channel with low conductance. Ca2+-permeability is related to subunit composition with 5HT3A homopentamers being more permeable than 5HT3A/B heteropentamers. \r\n\r\nFound pre- and post-synaptically but with different properties - pre-synaptic 5-HT3 receptors are predominantly calcium-permeant while post-synaptic receptors are permeant to Na+ and K+. Also Mg2+ permeant. Pre-synaptic depolarisations are generally slower than post-synaptic depolarisations. \r\n\r\n5-HT3 receptors increase the frequency of spontaneous excitatory post-synaptic currents (sEPSCs) or miniature EPSCs (mEPSCs). These may be related to 5-HT3-induced depolarisation of pre-synaptic membranes and subsequent activation of cholinergic or glutamatergic neurotransmissions or evoked excitatory post-synaptic currents (eEPSCs) or spontaneous inhibitory post-synaptic currents (sIPSCs) related to GABAergic neurotransmissions post-synaptic 5-HT3 receptor activation. \r\n\r\nDue to different residues in transmembrane domain M2 of the 5-HT3A and 5-HT3B subunits the 5-HT3A/B heteromeric receptors are more efficient conductors than 5-HT3A homomeric receptors and have increased agonist and antagonist affinity. Homomeric receptors recover faster from desensitisation but are probably less prevalent in vivo. \r\n\r\nHigh levels of expression are found in the vagal terminals of the dorsal vagal complex, in the amygdala and the hippocampi. Lower levels of expression are found in the forebrain with lower relative expression in the striatum than the cortical regions. \r\n\r\nInvolved in processes associated with emotion, cognition, memory and pain perception. \r\n\r\nInvolved in ganglionic transmission in the myenteric plexus in the mucosal layer and expressed in the gastrointestinal (GI) tract serotonin mediates control over a variety of physiological functions such as the contraction/relaxation of smooth muscle, and peristaltic and secretory reflexes, directly or indirectly through intrinsic primary afferent neurons. \r\n\r\nPlays an important role in the regulation of inflammation and immune responses in the peripheral nervous system. \r\n\r\nChaperone proteins assist assembly, modifications and export from the ER followed by transport in vesicle-like structures along microtubules to the plasma membrane where they typically form clusters in F-actin-rich regions.","predictedComplex":false,"interactors":[{"ac":"EBI-11295097","identifier":"P23979","identifierLink":"https://www.uniprot.org/uniprotkb/P23979/entry","name":"Htr3a","description":"5-hydroxytryptamine receptor 3A","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-275","complexName":"5-hydroxytryptamine-3A/B receptor complex","organismName":"Mus musculus; 10090","description":"Inward-rectifying, ligand-gated ion channel, which when activated by 5-hydroxytryptamine (5-HT, serotonin) causes fast neuronal depolarization and excitation or modulation of neurotransmitter release depending on their neuronal localisation (central and/or peripheral nervous system). A cation-specific, but otherwise relatively non-selective, ion channel with low conductance. Ca2+-permeability is related to subunit composition with 5HT3A homopentamers being more permeable than 5HT3A/B heteropentamers. \r\n\r\nFound pre- and post-synaptically but with different properties - pre-synaptic 5-HT3 receptors are predominantly calcium-permeant while post-synaptic receptors are permeant to Na+ and K+. Also Mg2+ permeant. Pre-synaptic depolarisations are generally slower than post-synaptic depolarisations. \r\n\r\n5-HT3 receptors increase the frequency of spontaneous excitatory post-synaptic currents (sEPSCs) or miniature EPSCs (mEPSCs). These may be related to 5-HT3-induced depolarisation of pre-synaptic membranes and subsequent activation of cholinergic or glutamatergic neurotransmissions or evoked excitatory post-synaptic currents (eEPSCs) or spontaneous inhibitory post-synaptic currents (sIPSCs) related to GABAergic neurotransmissions post-synaptic 5-HT3 receptor activation. \r\n\r\nDue to different residues in transmembrane domain M2 of the 5-HT3A and 5-HT3B subunits the 5-HT3A/B heteromeric receptors are more efficient conductors than 5-HT3A homomeric receptors and have increased agonist and antagonist affinity. Homomeric receptors recover faster from desensitisation but are probably less prevalent in vivo. \r\n\r\nHigh levels of expression are found in the vagal terminals of the dorsal vagal complex, in the amygdala and the hippocampi. Lower levels of expression are found in the forebrain with lower relative expression in the striatum than the cortical regions. \r\n\r\nInvolved in processes associated with emotion, cognition, memory and pain perception. \r\n\r\nInvolved in ganglionic transmission in the myenteric plexus in the mucosal layer and expressed in the gastrointestinal (GI) tract serotonin mediates control over a variety of physiological functions such as the contraction/relaxation of smooth muscle, and peristaltic and secretory reflexes, directly or indirectly through intrinsic primary afferent neurons. \r\n\r\nPlays an important role in the regulation of inflammation and immune responses in the peripheral nervous system. \r\n\r\nChaperone proteins assist assembly, modifications and export from the ER followed by transport in vesicle-like structures along microtubules to the plasma membrane where they typically form clusters in F-actin-rich regions.","predictedComplex":false,"interactors":[{"ac":"EBI-11295097","identifier":"P23979","identifierLink":"https://www.uniprot.org/uniprotkb/P23979/entry","name":"Htr3a","description":"5-hydroxytryptamine receptor 3A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11295219","identifier":"Q9JHJ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JHJ5/entry","name":"Htr3b","description":"5-hydroxytryptamine receptor 3B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1737","complexName":"Collagen type VII trimer","organismName":"Homo sapiens; 9606","description":"Synthesized by keratinocytes. The non-collagenous NC1 domain has been shown  to bind basement membrane type IV collagen. Forms anchoring fibrils which may contribute to epithelial basement membrane organization and adherence","predictedComplex":false,"interactors":[{"ac":"EBI-724237","identifier":"Q02388","identifierLink":"https://www.uniprot.org/uniprotkb/Q02388/entry","name":"COL7A1","description":"Collagen alpha-1(VII) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2966","complexName":"Collagen type VII trimer","organismName":"Mus musculus; 10090","description":"Synthesized by keratinocytes. The non-collagenous NC1 domain has been shown  to bind basement membrane type IV collagen. Forms anchoring fibrils which may contribute to epithelial basement membrane organization and adherence","predictedComplex":false,"interactors":[{"ac":"EBI-8313134","identifier":"Q63870","identifierLink":"https://www.uniprot.org/uniprotkb/Q63870/entry","name":"Col7a1","description":"Collagen alpha-1(VII) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1738","complexName":"Phenylalanyl-tRNA synthetase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyses the esterificaion of phenylalanine to its cognate tRNA with the concomitant hydrolysis of ATP. The activated amino acid is transferred to the 2-OH group of a phenylalanine-accepting tRNA.","predictedComplex":false,"interactors":[{"ac":"EBI-18678","identifier":"P15625","identifierLink":"https://www.uniprot.org/uniprotkb/P15625/entry","name":"FRS2","description":"Phenylalanine--tRNA ligase alpha subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11538","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18684","identifier":"P15624","identifierLink":"https://www.uniprot.org/uniprotkb/P15624/entry","name":"FRS1","description":"Phenylalanine--tRNA ligase beta subunit","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10947","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1739","complexName":"Mannosyl phosphorylinositol ceramide synthase SUR1-CSG2","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the addition of mannosyl to phosphorylinositol ceramide, and essential step in the synthesis of mannosylinositol phosphorylceramide. Function in the Golgi. Preferentially active against IPC-B and IPC-C in comparison with Mannosyl phosphorylinositol ceramide synthase CSH1-CSG2 (CPX-1740).","predictedComplex":false,"interactors":[{"ac":"EBI-18569","identifier":"P33300","identifierLink":"https://www.uniprot.org/uniprotkb/P33300/entry","name":"SUR1","description":"Mannosyl phosphorylinositol ceramide synthase SUR1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR32385","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2051140","identifier":"P35206","identifierLink":"https://www.uniprot.org/uniprotkb/P35206/entry","name":"CSG2","description":"Mannosyl phosphorylinositol ceramide synthase regulatory protein CSG2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1740","complexName":"Mannosyl phosphorylinositol ceramide synthase CSH1-CSG2","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the addition of mannosyl to phosphorylinositol ceramide, and essential step in the synthesis of mannosylinositol phosphorylceramide. Function in the Golgi. Less active against IPC-B and IPC-C in comparison with Mannosyl phosphorylinositol ceramide synthase SUR1-CSG2 (CPX-1739).","predictedComplex":false,"interactors":[{"ac":"EBI-2051140","identifier":"P35206","identifierLink":"https://www.uniprot.org/uniprotkb/P35206/entry","name":"CSG2","description":"Mannosyl phosphorylinositol ceramide synthase regulatory protein CSG2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-20861","identifier":"P38287","identifierLink":"https://www.uniprot.org/uniprotkb/P38287/entry","name":"CSH1","description":"Mannosyl phosphorylinositol ceramide synthase CSH1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR32385","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1741","complexName":"Endonuclease SceI","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Mitochondrial endonuclease which cleaves mitochondrial DNA during the process of mitochondrial fusion, when haploid cells are mated to form zygotic cells, to induce genetic recombination among the heterogeneous mitochondrial DNAs inherited from the parents.","predictedComplex":false,"interactors":[{"ac":"EBI-6490","identifier":"P12294","identifierLink":"https://www.uniprot.org/uniprotkb/P12294/entry","name":"ENS2","description":"Endonuclease SceI small subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae; 4932","xrefs":[]},{"ac":"EBI-8637","identifier":"P0CS90","identifierLink":"https://www.uniprot.org/uniprotkb/P0CS90/entry","name":"SSC1","description":"Import motor subunit, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1742","complexName":"tRNA-specific adenosine-34 deaminase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Deaminates adenosine-34 (wobble position) to inosine in double-stranded tRNA. When present at the wobble position, inosine can pair degenerately with uracil, cytosine, or adenosine, enabling a single tRNA to recognize up to three different codons.","predictedComplex":false,"interactors":[{"ac":"EBI-18939","identifier":"P47058","identifierLink":"https://www.uniprot.org/uniprotkb/P47058/entry","name":"TAD2","description":"tRNA-specific adenosine deaminase subunit TAD2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11079","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2094330","identifier":"Q9URQ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9URQ3/entry","name":"TAD3","description":"tRNA-specific adenosine deaminase subunit TAD3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11079","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1743","complexName":"Ribosome-associated complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Chaperone complex involved in regulation of accurate translation termination and in folding or maintaining nascent polypeptides in a folding-competent state. RAC stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones SSB1/SSB2 that bind to the nascent polypeptide chain.","predictedComplex":false,"interactors":[{"ac":"EBI-24570","identifier":"P38788","identifierLink":"https://www.uniprot.org/uniprotkb/P38788/entry","name":"SSZ1","description":"Ribosome-associated complex subunit SSZ1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29684","identifier":"P32527","identifierLink":"https://www.uniprot.org/uniprotkb/P32527/entry","name":"ZUO1","description":"Zuotin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43999","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1744","complexName":"Mitochondrial sorting and assembly machinery complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Involved in the membrane assembly of mitochondrial beta-barrel proteins, which are synthesized on cytosolic ribosomes and recognized initially by the import receptors of the translocase of the mitochondrial outer membrane (TOM complex CPX-474). They are then translocated across the outer membrane via the general-import pore of the TOM complex and relayed to the SAM complex.","predictedComplex":false,"interactors":[{"ac":"EBI-2347180","identifier":"P50110","identifierLink":"https://www.uniprot.org/uniprotkb/P50110/entry","name":"SAM37","description":"Sorting assembly machinery 37 kDa subunit","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12289","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-24602","identifier":"P14693","identifierLink":"https://www.uniprot.org/uniprotkb/P14693/entry","name":"SAM35","description":"Sorting assembly machinery 35 kDa subunit","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-28646","identifier":"P53969","identifierLink":"https://www.uniprot.org/uniprotkb/P53969/entry","name":"SAM50","description":"Sorting assembly machinery 50 kDa subunit","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12815","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1745","complexName":"Collagen type VIII trimer variant 1","organismName":"Homo sapiens; 9606","description":"Type VIII collagens are the major component of the basement membrane of the corneal endothelium (Descemet's membranes).","predictedComplex":false,"interactors":[{"ac":"EBI-2528190","identifier":"P25067","identifierLink":"https://www.uniprot.org/uniprotkb/P25067/entry","name":"COL8A2","description":"Collagen alpha-2(VIII) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-747133","identifier":"P27658","identifierLink":"https://www.uniprot.org/uniprotkb/P27658/entry","name":"COL8A1","description":"Collagen alpha-1(VIII) chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2967","complexName":"Collagen type VIII trimer variant I","organismName":"Mus musculus; 10090","description":"Type VIII collagens are the major component of the basement membrane of the corneal endothelium (Descemet's membranes).","predictedComplex":false,"interactors":[{"ac":"EBI-9213341","identifier":"Q00780","identifierLink":"https://www.uniprot.org/uniprotkb/Q00780/entry","name":"Col8a1","description":"Collagen alpha-1(VIII) chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9213364","identifier":"P25318","identifierLink":"https://www.uniprot.org/uniprotkb/P25318/entry","name":"Col8a2","description":"Collagen alpha-2(VIII) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1746","complexName":"Collagen type VIII trimer variant 2","organismName":"Homo sapiens; 9606","description":"Type VIII collagens are the major component of the basement membrane of the corneal endothelium (Descemet's membranes).","predictedComplex":false,"interactors":[{"ac":"EBI-747133","identifier":"P27658","identifierLink":"https://www.uniprot.org/uniprotkb/P27658/entry","name":"COL8A1","description":"Collagen alpha-1(VIII) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2968","complexName":"Collagen type VIII trimer variant 2","organismName":"Mus musculus; 10090","description":"Type VIII collagens are the major component of the basement membrane of the corneal endothelium (Descemet's membranes).","predictedComplex":false,"interactors":[{"ac":"EBI-9213341","identifier":"Q00780","identifierLink":"https://www.uniprot.org/uniprotkb/Q00780/entry","name":"Col8a1","description":"Collagen alpha-1(VIII) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1747","complexName":"Collagen type VIII trimer variant 3","organismName":"Homo sapiens; 9606","description":"Type VIII collagens are the major component of the basement membrane of the corneal endothelium (Descemet's membranes).","predictedComplex":false,"interactors":[{"ac":"EBI-2528190","identifier":"P25067","identifierLink":"https://www.uniprot.org/uniprotkb/P25067/entry","name":"COL8A2","description":"Collagen alpha-2(VIII) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2969","complexName":"Collagen type VIII trimer variant 3","organismName":"Mus musculus; 10090","description":"Type VIII collagens are the major component of the basement membrane of the corneal endothelium (Descemet's membranes).","predictedComplex":false,"interactors":[{"ac":"EBI-9213364","identifier":"P25318","identifierLink":"https://www.uniprot.org/uniprotkb/P25318/entry","name":"Col8a2","description":"Collagen alpha-2(VIII) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1748","complexName":"Collagen type IX trimer","organismName":"Homo sapiens; 9606","description":"Nonfibrillar collagen (FACIT) that associate to form a structure that links glycosaminoglycans to type II collagen fibrils. The molecules contain three functional regions. One region comprises one or two triple helical domains and serves for the interaction and adhesion of these molecules to the fibrils. A second region, comprising another triple helical domain, serves as a rigid arm that projects out of the fibril and a third region, which does not include triple helices and may serve for interaction with other matrix elements or with cells. The various triple helical domains are separated by short nontriple helical domains (NC domains). Type IX collagen is found in ECMs containing type II collagen as their main fibril-forming structure, such as hyaline cartilage  and the vitreous body of the eye.","predictedComplex":false,"interactors":[{"ac":"EBI-2528238","identifier":"P20849","identifierLink":"https://www.uniprot.org/uniprotkb/P20849/entry","name":"COL9A1","description":"Collagen alpha-1(IX) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2528281","identifier":"Q14050","identifierLink":"https://www.uniprot.org/uniprotkb/Q14050/entry","name":"COL9A3","description":"Collagen alpha-3(IX) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714971","identifier":"Q14055","identifierLink":"https://www.uniprot.org/uniprotkb/Q14055/entry","name":"COL9A2","description":"Collagen alpha-2(IX) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2970","complexName":"Collagen type IX trimer","organismName":"Mus musculus; 10090","description":"Nonfibrillar collagen (FACIT) that associate to form a structure that links glycosaminoglycans to type II collagen fibrils. The molecules contain three functional regions. One region comprises one or two triple helical domains and serves for the interaction and adhesion of these molecules to the fibrils. A second region, comprising another triple helical domain, serves as a rigid arm that projects out of the fibril and a third region, which does not include triple helices and may serve for interaction with other matrix elements or with cells. The various triple helical domains are separated by short nontriple helical domains (NC domains). Type IX collagen is found in ECMs containing type II collagen as their main fibril-forming structure, such as hyaline cartilage  and the vitreous body of the eye.","predictedComplex":false,"interactors":[{"ac":"EBI-9213436","identifier":"A2ACT7","identifierLink":"https://www.uniprot.org/uniprotkb/A2ACT7/entry","name":"Col9a3","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9213449","identifier":"Q05722","identifierLink":"https://www.uniprot.org/uniprotkb/Q05722/entry","name":"Col9a1","description":"Collagen alpha-1(IX) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9213466","identifier":"Q07643","identifierLink":"https://www.uniprot.org/uniprotkb/Q07643/entry","name":"Col9a2","description":"Collagen alpha-2(IX) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1749","complexName":"Collagen type X trimer","organismName":"Homo sapiens; 9606","description":"Major constituent of the pericellular matrix of hypertrophic chondrocytes within the cartilage growth plate, and the expression of collagen X during endochondral ossification is intimately linked to the onset of cartilage calcification and extracellular matrix remodeling. Collagen X interactions within the cartilage extracellular matrix may establish the correct microenvironment for matrix mineralization and subsequent bone development.","predictedComplex":false,"interactors":[{"ac":"EBI-2528309","identifier":"Q03692","identifierLink":"https://www.uniprot.org/uniprotkb/Q03692/entry","name":"COL10A1","description":"Collagen alpha-1(X) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2971","complexName":"Collagen type X trimer","organismName":"Mus musculus; 10090","description":"Major constituent of the pericellular matrix of hypertrophic chondrocytes within the cartilage growth plate, and the expression of collagen X during endochondral ossification is intimately linked to the onset of cartilage calcification and extracellular matrix remodeling. Collagen X interactions within the cartilage extracellular matrix may establish the correct microenvironment for matrix mineralization and subsequent bone development.","predictedComplex":false,"interactors":[{"ac":"EBI-9213489","identifier":"Q05306","identifierLink":"https://www.uniprot.org/uniprotkb/Q05306/entry","name":"Col10a1","description":"Collagen alpha-1(X) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1750","complexName":"Collagen type XI trimer variant 1","organismName":"Homo sapiens; 9606","description":"Forms the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite. Located within heterotypic fibrils and might actually constitute  the core of fibrils. May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils.","predictedComplex":false,"interactors":[{"ac":"EBI-2431412","identifier":"P02458","identifierLink":"https://www.uniprot.org/uniprotkb/P02458/entry","name":"COL2A1","description":"Collagen alpha-1(II) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2515504","identifier":"P13942","identifierLink":"https://www.uniprot.org/uniprotkb/P13942/entry","name":"COL11A2","description":"Collagen alpha-2(XI) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2528334","identifier":"P12107","identifierLink":"https://www.uniprot.org/uniprotkb/P12107/entry","name":"COL11A1","description":"Collagen alpha-1(XI) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2975","complexName":"Collagen type XI trimer variant 1","organismName":"Mus musculus; 10090","description":"Forms the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite. Located within heterotypic fibrils and might actually constitute  the core of fibrils. May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils.","predictedComplex":false,"interactors":[{"ac":"EBI-738477","identifier":"P28481","identifierLink":"https://www.uniprot.org/uniprotkb/P28481/entry","name":"Col2a1","description":"Collagen alpha-1(II) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9214972","identifier":"Q64739","identifierLink":"https://www.uniprot.org/uniprotkb/Q64739/entry","name":"Col11a2","description":"Collagen alpha-2(XI) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9214999","identifier":"Q61245","identifierLink":"https://www.uniprot.org/uniprotkb/Q61245/entry","name":"Col11a1","description":"Collagen alpha-1(XI) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3108","complexName":"Collagen type XI trimer variant 1","organismName":"Bos taurus; 9913","description":"Forms the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite. Located within heterotypic fibrils and might actually constitute  the core of fibrils. May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils.","predictedComplex":false,"interactors":[{"ac":"EBI-5281315","identifier":"P02459","identifierLink":"https://www.uniprot.org/uniprotkb/P02459/entry","name":"COL2A1","description":"Collagen alpha-1(II) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5281724","identifier":"Q28083","identifierLink":"https://www.uniprot.org/uniprotkb/Q28083/entry","name":"COL11A1","description":"Collagen alpha-1(XI) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[]},{"ac":"EBI-5281731","identifier":"Q32S24","identifierLink":"https://www.uniprot.org/uniprotkb/Q32S24/entry","name":"COL11A2","description":"Collagen alpha-2(XI) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Bos taurus; 9913","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1751","complexName":"Collagen type XI trimer variant 2","organismName":"Homo sapiens; 9606","description":"Form the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite. Located within heterotypic fibrils and might actually constitute  the core of fibrils. May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils.","predictedComplex":false,"interactors":[{"ac":"EBI-2464544","identifier":"P05997","identifierLink":"https://www.uniprot.org/uniprotkb/P05997/entry","name":"COL5A2","description":"Collagen alpha-2(V) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2528334","identifier":"P12107","identifierLink":"https://www.uniprot.org/uniprotkb/P12107/entry","name":"COL11A1","description":"Collagen alpha-1(XI) chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2976","complexName":"Collagen type XI trimer variant 2","organismName":"Mus musculus; 10090","description":"Form the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite. Located within heterotypic fibrils and might actually constitute  the core of fibrils. May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils.","predictedComplex":false,"interactors":[{"ac":"EBI-9213185","identifier":"Q3U962","identifierLink":"https://www.uniprot.org/uniprotkb/Q3U962/entry","name":"Col5a2","description":"Collagen alpha-2(V) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9214999","identifier":"Q61245","identifierLink":"https://www.uniprot.org/uniprotkb/Q61245/entry","name":"Col11a1","description":"Collagen alpha-1(XI) chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1752","complexName":"Collagen type XI trimer variant 3","organismName":"Homo sapiens; 9606","description":"Form the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite. Located within heterotypic fibrils and might actually constitute  the core of fibrils. May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils.","predictedComplex":false,"interactors":[{"ac":"EBI-2464511","identifier":"P20908","identifierLink":"https://www.uniprot.org/uniprotkb/P20908/entry","name":"COL5A1","description":"Collagen alpha-1(V) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2464544","identifier":"P05997","identifierLink":"https://www.uniprot.org/uniprotkb/P05997/entry","name":"COL5A2","description":"Collagen alpha-2(V) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2528334","identifier":"P12107","identifierLink":"https://www.uniprot.org/uniprotkb/P12107/entry","name":"COL11A1","description":"Collagen alpha-1(XI) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2977","complexName":"Collagen type XI trimer variant 3","organismName":"Mus musculus; 10090","description":"Form the fibrils of tendon, ligaments and bones, also present in skin. In bones the fibrils are mineralized with calcium hydroxyapatite. Located within heterotypic fibrils and might actually constitute  the core of fibrils. May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils.","predictedComplex":false,"interactors":[{"ac":"EBI-762024","identifier":"O88207","identifierLink":"https://www.uniprot.org/uniprotkb/O88207/entry","name":"Col5a1","description":"Collagen alpha-1(V) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9213185","identifier":"Q3U962","identifierLink":"https://www.uniprot.org/uniprotkb/Q3U962/entry","name":"Col5a2","description":"Collagen alpha-2(V) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9214999","identifier":"Q61245","identifierLink":"https://www.uniprot.org/uniprotkb/Q61245/entry","name":"Col11a1","description":"Collagen alpha-1(XI) chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1753","complexName":"Collagen type XII trimer","organismName":"Homo sapiens; 9606","description":"Triple-helices consisting of about 1000 amino acids per chain forming a coiled coil structure. Each polypeptide forms a left-handed helix in which every third residue, glycine, comes into the centre of the superhelix. This is a fibril-associated collagen with interrupted triple helices (FACIT) that associate to form a structure that  interacts with type I collagen-containing fibrils. The molecules contain three functional regions, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix.","predictedComplex":false,"interactors":[{"ac":"EBI-2528424","identifier":"Q99715","identifierLink":"https://www.uniprot.org/uniprotkb/Q99715/entry","name":"COL12A1","description":"Collagen alpha-1(XII) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2978","complexName":"Collagen type XII trimer","organismName":"Mus musculus; 10090","description":"Triple-helices consisting of about 1000 amino acids per chain forming a coiled coil structure. Each polypeptide forms a left-handed helix in which every third residue, glycine, comes into the centre of the superhelix. This is a fibril-associated collagen with interrupted triple helices (FACIT) that associate to form a structure that  interacts with type I collagen-containing fibrils. The molecules contain three functional regions, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix.","predictedComplex":false,"interactors":[{"ac":"EBI-8429639","identifier":"Q60847","identifierLink":"https://www.uniprot.org/uniprotkb/Q60847/entry","name":"Col12a1","description":"Collagen alpha-1(XII) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-3109","complexName":"Collagen type XII trimer","organismName":"Gallus gallus; 9031","description":"Triple-helices consisting of about 1000 amino acids per chain forming a coiled coil structure. Each polypeptide forms a left-handed helix in which every third residue, glycine, comes into the centre of the superhelix. 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The molecules contain three functional regions, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix.","predictedComplex":false,"interactors":[{"ac":"EBI-9630729","identifier":"P13944","identifierLink":"https://www.uniprot.org/uniprotkb/P13944/entry","name":"COL12A1","description":"Collagen alpha-1(XII) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1754","complexName":"Collagen type XIII trimer","organismName":"Homo sapiens; 9606","description":"Nonfibrillar collagen that has been detected at low levels in all connective tissue-producing cells so may serve a general function in connective tissues. Collagen XIII contains a transmembrane domain and the protein has been localized to the plasma membrane. 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It is probably associated with the surface of interstitial collagen fibrils via COL1. 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It is probably associated with the surface of interstitial collagen fibrils via COL1. The COL2 domain may then serve as a rigid arm which sticks out from the fibril and protrudes the large N-terminal globular domain into the extracellular space, where it might interact with other matrix molecules or cell surface receptors","predictedComplex":false,"interactors":[{"ac":"EBI-9630710","identifier":"P32018","identifierLink":"https://www.uniprot.org/uniprotkb/P32018/entry","name":"COL14A1","description":"Collagen alpha-1(XIV) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[{"identifier":"PTHR24020","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1756","complexName":"Collagen type XV trimer","organismName":"Homo sapiens; 9606","description":"Fibril-associated collagen with interrupted triple helices  (FACIT) that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle. Its strongest expression is localized to basement membrane zones so it may function to adhere basement membranes to underlying connective tissue stroma.","predictedComplex":false,"interactors":[{"ac":"EBI-2528658","identifier":"P39059","identifierLink":"https://www.uniprot.org/uniprotkb/P39059/entry","name":"COL15A1","description":"Collagen alpha-1(XV) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2993","complexName":"Collagen type XV trimer","organismName":"Mus musculus; 10090","description":"Fibril-associated collagen with interrupted triple helices  (FACIT) that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle. Its strongest expression is localized to basement membrane zones so it may function to adhere basement membranes to underlying connective tissue stroma.","predictedComplex":false,"interactors":[{"ac":"EBI-8350088","identifier":"O35206","identifierLink":"https://www.uniprot.org/uniprotkb/O35206/entry","name":"Col15a1","description":"Collagen alpha-1(XV) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1757","complexName":"Collagen type XVI trimer","organismName":"Homo sapiens; 9606","description":"Fibril-associated collagen with interrupted triple helices  (FACIT) found in association with fibril-forming collagens such as type I and II, and serve to maintain the integrity of the extracellular matrix. Involved in mediating cell attachment and inducing integrin-mediated cellular reactions, such as cell spreading and alterations in cell morphology.","predictedComplex":false,"interactors":[{"ac":"EBI-2528695","identifier":"Q07092","identifierLink":"https://www.uniprot.org/uniprotkb/Q07092/entry","name":"COL16A1","description":"Collagen alpha-1(XVI) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2994","complexName":"Collagen type XVI trimer","organismName":"Mus musculus; 10090","description":"Fibril-associated collagen with interrupted triple helices  (FACIT) found in association with fibril-forming collagens such as type I and II, and serve to maintain the integrity of the extracellular matrix. Involved in mediating cell attachment and inducing integrin-mediated cellular reactions, such as cell spreading and alterations in cell morphology.","predictedComplex":false,"interactors":[{"ac":"EBI-9246729","identifier":"Q8BLX7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BLX7/entry","name":"Col16a1","description":"Collagen alpha-1(XVI) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1758","complexName":"Collagen type XVII trimer","organismName":"Homo sapiens; 9606","description":"Nonfibrillar collagen that is a transmembrane protein. Collagen XVII is a structural component of hemidesmosomes, multiprotein complexes at the dermal-epidermal basement membrane zone that mediate adhesion of keratinocytes to the underlying membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-2528742","identifier":"Q9UMD9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UMD9/entry","name":"COL17A1","description":"Collagen alpha-1(XVII) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2995","complexName":"Collagen type XVII trimer","organismName":"Mus musculus; 10090","description":"Nonfibrillar  collagen that is a transmembrane protein. 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Activated Tgfbr1 phosphorylates Smad2 (Q62432) which dissociates from the receptor and activates the canonical SMAD-dependent TGF-beta signaling cascade.","predictedComplex":false,"interactors":[{"ac":"EBI-12558560","identifier":"P27090-PRO_0000033787","identifierLink":"https://www.uniprot.org/uniprotkb/P27090-PRO_0000033787/entry","name":"Tgfb2","description":"Transforming growth factor beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-2899332","identifier":"Q62312","identifierLink":"https://www.uniprot.org/uniprotkb/Q62312/entry","name":"Tgfbr2","description":"TGF-beta receptor type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2899393","identifier":"Q64729","identifierLink":"https://www.uniprot.org/uniprotkb/Q64729/entry","name":"Tgfbr1","description":"TGF-beta receptor type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-841","complexName":"WICH chromatin remodelling complex","organismName":"Mus musculus; 10090","description":"Chromatin remodeling complex required for maintaining chromatin structure by regulating the spacing of nuclesomes during replication. It is recruited to the replication foci through a direct interaction between the Baz1b subunit and the DNA clamp Pcna. It opens up chromatin after nucleosome assembly upstream of the replication fork and prevents aberrant heterochromatin formation shortly after DNA replication. The Baz1b subunit phosphorylates H2A.X Tyr-143 regulating the H2A.X DNA damage response.","predictedComplex":false,"interactors":[{"ac":"EBI-927547","identifier":"Q91ZW3","identifierLink":"https://www.uniprot.org/uniprotkb/Q91ZW3/entry","name":"Smarca5","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-927576","identifier":"Q9Z277","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z277/entry","name":"Baz1b","description":"Tyrosine-protein kinase BAZ1B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-845","complexName":"BRCA1-PALB2-BRCA2 homologous recombination DNA repair complex","organismName":"Homo sapiens; 9606","description":"Potentiates homologoues recombinational DNA repair (HR) by promoting assembly of RAD51 family of DNA repair proteins onto newly synthesized single-stranded DNA. Act downstream of Fanconi anemia proteins and complexes to repair DNA interstrand crosslinks. The MRN complex (CPX-4442) recruits ATM (Q13315) to the site of double-stranded DNA breaks, which then auto-activates and recruits BRCA1, facilitating a shift from non-homologous end-joining to HR. A newly generated single-strand of DNA is covered by replication protein A (RPA) complex (CPX-1878/CPX-1879). PALB2 is phosphorylated on Ser-59 by ATR (Q13535) and the BRCA1-PALB2-BRCA2 complex forms, promoting RPA removal and RAD51 loading. The resulting RAD51-ssDNA filament invades the intact sister chromatid and the strand is extended through the action of DNA polymerases.","predictedComplex":false,"interactors":[{"ac":"EBI-1222653","identifier":"Q86YC2","identifierLink":"https://www.uniprot.org/uniprotkb/Q86YC2/entry","name":"PALB2","description":"Partner and localizer of BRCA2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14662","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-349905","identifier":"P38398","identifierLink":"https://www.uniprot.org/uniprotkb/P38398/entry","name":"BRCA1","description":"Breast cancer type 1 susceptibility protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13763","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-79792","identifier":"P51587","identifierLink":"https://www.uniprot.org/uniprotkb/P51587/entry","name":"BRCA2","description":"Breast cancer type 2 susceptibility protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11289","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-846","complexName":"INO80 chromatin remodeling complex","organismName":"Homo sapiens; 9606","description":"ATP-dependent nucleosome remodeling complex which slides mononucleosomes to a central position on a DNA template while tightly organizing nucleosomes within arrays. Functions in maintaining genome stability and removes H2AZ from nucleosomes. May play a largely repressive role in gene transcription, blocking H3K79 methylation and restricting transcription to gene units in euchromatin and away from silent regions, such as heterochromatin. Activates the expression of pluripotency factors by facilitating the recruitment of Mediator and Pol II at their promoters. Required for fork maintenance and progression in stalled replication forks. It is recruited to DNA damage sites and the ACTR8 subunit is required for this recruitment.","predictedComplex":false,"interactors":[{"ac":"EBI-1051183","identifier":"Q9Y5K5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5K5/entry","name":"UCHL5","description":"Ubiquitin carboxyl-terminal hydrolase isozyme L5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10589","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1245626","identifier":"P0C1Z6","identifierLink":"https://www.uniprot.org/uniprotkb/P0C1Z6/entry","name":"TFPT","description":"TCF3 fusion partner","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR35084","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2511210","identifier":"Q6P4R8","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P4R8/entry","name":"NFRKB","description":"Nuclear factor related to kappa-B-binding protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13052","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348259","identifier":"Q96EZ8","identifierLink":"https://www.uniprot.org/uniprotkb/Q96EZ8/entry","name":"MCRS1","description":"Microspherule protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13233","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352939","identifier":"Q9Y230","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y230/entry","name":"RUVBL2","description":"RuvB-like 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353675","identifier":"Q9Y265","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y265/entry","name":"RUVBL1","description":"RuvB-like 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355018","identifier":"O96019","identifierLink":"https://www.uniprot.org/uniprotkb/O96019/entry","name":"ACTL6A","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-715611","identifier":"Q9C086","identifierLink":"https://www.uniprot.org/uniprotkb/Q9C086/entry","name":"INO80B","description":"INO80 complex subunit B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21561","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-722540","identifier":"Q6PI98","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PI98/entry","name":"INO80C","description":"INO80 complex subunit C","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31200","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-765538","identifier":"P25490","identifierLink":"https://www.uniprot.org/uniprotkb/P25490/entry","name":"YY1","description":"Transcriptional repressor protein YY1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14003","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-769345","identifier":"Q9ULG1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ULG1/entry","name":"INO80","description":"Chromatin-remodeling ATPase INO80","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45685","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-769401","identifier":"Q8NBZ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NBZ0/entry","name":"INO80E","description":"INO80 complex subunit E","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21812","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-769418","identifier":"Q9H9F9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H9F9/entry","name":"ACTR5","description":"Actin-related protein 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-769597","identifier":"Q9H981","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H981/entry","name":"ACTR8","description":"Actin-related protein 8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-769603","identifier":"Q53TQ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q53TQ3/entry","name":"INO80D","description":"INO80 complex subunit D","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16198","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-847","complexName":"TMEM219-Interleukin-13 decoy-receptor-ligand alpha 2 complex","organismName":"Homo sapiens; 9606","description":"Transmembrane receptor complex. IL13RA2 was initially considered solely as a decoy receptor which elicited IL13 antagonistic responses, because of its short cytoplasmic tail. However, the phosphorylation of a Tyr-369 allows for the recruitment of phosphatases and kinases enabling IL13-mediated IL13RA2 signalling to occur via STAT6 (P42226) independent pathways. This leads to the subsequent activation of the activator protein 1 (AP-1) complex composed of proteins from the FOS (P01100), JUN (P05412), ATF and JDP families as well as the extracellular signal-related kinase (ERK1/2) to promote tumour invasion, metastasis, and fibrosis through the production of TGFB1 (P01137). \r\n\r\nTMEM219 facilitates IL13 and IL13RA2 binding and enhances the role of IL13RA2 as mostly, a decoy receptor. IL13RA2 also forms a complex with Chitinase-3-like protein 1 (CHI3L1, P36222) and TMEM219 (CPX-9184). IL13RA2 N-glycosylation is a critical determinant of whether it binds CHI3L1 or IL13; IL13 binding to IL13RA2 is dependent on each of four sites of N-glycosylation in IL13RA2, with increased N-glycosylation resulting in increased IL13 binding and signalling.\r\n\r\nThe over-expression of IL13RA2 in the epidermal and dermal compartments in skin lesions of patients with atopic dermatitis suggests that it attenuates IL13 mediated inflammatory responses.","predictedComplex":false,"interactors":[{"ac":"EBI-1647828","identifier":"P35225","identifierLink":"https://www.uniprot.org/uniprotkb/P35225/entry","name":"IL13","description":"Interleukin-13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48486","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20264080","identifier":"Q86XT9","identifierLink":"https://www.uniprot.org/uniprotkb/Q86XT9/entry","name":"TMEM219","description":"Insulin-like growth factor-binding protein 3 receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16002","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4320063","identifier":"Q14627","identifierLink":"https://www.uniprot.org/uniprotkb/Q14627/entry","name":"IL13RA2","description":"Interleukin-13 receptor subunit alpha-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-848","complexName":"METTL1-WDR4 tRNA (guanine-N(7)-)-methyltransferase complex","organismName":"Homo sapiens; 9606","description":"7-Methyltransferase that modifies guanosine-46 in the variable loop of certain tRNAs that contain the 5'-RAGGU-3' motif. m7G46 makes triple-base interactions with cytosine-13 and guanosine-22. The tertiary interactions increase the thermal stability of the tRNAs and thus modulates steady-state tRNA levels.","predictedComplex":false,"interactors":[{"ac":"EBI-30813205","identifier":"CHEBI:59789","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:59789","name":"s-adenosyl-l-methionine zwitterion","description":"S-adenosyl-L-methionine zwitterion","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-750415","identifier":"Q9UBP6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UBP6/entry","name":"METTL1","description":"tRNA (guanine-N(7)-)-methyltransferase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23417","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-750427","identifier":"P57081","identifierLink":"https://www.uniprot.org/uniprotkb/P57081/entry","name":"WDR4","description":"tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit WDR4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16288","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-850","complexName":"AHNAK - Annexin A2 - S100-A10 complex","organismName":"Homo sapiens; 9606","description":"Calcium-dependent membrane-tethering complex that acts on ruptured membranes and aids general membrane organisation. Rapid influx of Ca2+ at the rupture site activates complex formation by Ca2+ binding to Annexin A2; repair activity may also require dysferlin (O75923).","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2555881","identifier":"Q09666","identifierLink":"https://www.uniprot.org/uniprotkb/Q09666/entry","name":"AHNAK","description":"Neuroblast differentiation-associated protein AHNAK","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23348","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352622","identifier":"P07355","identifierLink":"https://www.uniprot.org/uniprotkb/P07355/entry","name":"ANXA2","description":"Annexin A2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10502","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-717048","identifier":"P60903","identifierLink":"https://www.uniprot.org/uniprotkb/P60903/entry","name":"S100A10","description":"Protein S100-A10","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-851","complexName":"NR5A2-NR0B2 transcription regulation complex","organismName":"Homo sapiens; 9606","description":"Transcriptional repressor complex. Binding of NR0B2/SHP to form this complex inhibits transactivation of AR. NR0B2 is able to bind both the apo receptor and the receptor loaded with phospholipids,","predictedComplex":false,"interactors":[{"ac":"EBI-3910729","identifier":"Q15466","identifierLink":"https://www.uniprot.org/uniprotkb/Q15466/entry","name":"NR0B2","description":"Nuclear receptor subfamily 0 group B member 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24081","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-781320","identifier":"O00482","identifierLink":"https://www.uniprot.org/uniprotkb/O00482/entry","name":"NR5A2","description":"Nuclear receptor subfamily 5 group A member 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24086","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-853","complexName":"Annexin A2 - S100-A10 complex","organismName":"Homo sapiens; 9606","description":"Calcium-dependent membrane-tethering complex that acts on ruptured membranes and aids general membrane organisation. Annexin A2 binds to negatively charged phospholipids at rupture sites while the S100-A10 dimer binds one molecule of annexin A2 at each end forming a junctions between adjacent bilayers. Rapid influx of Ca2+ at the rupture site activates complex formation by Ca2+ binding to Annexin A2. Membrane tethering is further aided by additional proteins forming larger complexes, such as the AHNAK - Annexin A2 - S100-A10 complex (CPX-850) or the SMARCA3 - Annexin A2 - S100-A10 complex (CPX-856); repair activity may also require dysferlin (O75923). \r\n\r\nAlso plays a role in the organization of membrane-associated actin at sites of cholesterol-rich membrane domains. Found at sites of plasma membrane/secretory granule membrane contact and intergranule contact and therefore possibly involved in exocytotic processes and vesicles aggregation. Can indirectly affect a number of membrane transport events. Linked to Cl− channel regulation. As an extracellular complex, it regulates the stimulation of t-PA-dependent activation of plasminogen.","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-352622","identifier":"P07355","identifierLink":"https://www.uniprot.org/uniprotkb/P07355/entry","name":"ANXA2","description":"Annexin A2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10502","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-717048","identifier":"P60903","identifierLink":"https://www.uniprot.org/uniprotkb/P60903/entry","name":"S100A10","description":"Protein S100-A10","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-854","complexName":"AR-NR0B2 transcription regulation complex","organismName":"Homo sapiens; 9606","description":"Transcriptional repressor complex. The agonist-stabilized conformation of AR recruits regulatory proteins necessary to regulate transcriptional machinery and gene expression. Binding of NR0B2/SHP to form this complex inhibits transactivation of AR.","predictedComplex":false,"interactors":[{"ac":"EBI-3910729","identifier":"Q15466","identifierLink":"https://www.uniprot.org/uniprotkb/Q15466/entry","name":"NR0B2","description":"Nuclear receptor subfamily 0 group B member 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24081","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-608057","identifier":"P10275","identifierLink":"https://www.uniprot.org/uniprotkb/P10275/entry","name":"AR","description":"Androgen receptor","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-856","complexName":"SMARCA3 - Annexin A2 - S100-A10 complex","organismName":"Homo sapiens; 9606","description":"A transcription factor complex that mediates neurogenic and behavioral responses to selective antidepressant serotonin-reuptake inhibitors. The core tetramer of annexin A2 - S100A10 (CPX-853) anchors the complex to the inner nuclear membrane while HLTF/SMARCA3 binds to promoter sequences. HLTF's DNA binding affinity is enhanced by the interaction with annexin A2 and S100-A10.","predictedComplex":false,"interactors":[{"ac":"EBI-1045161","identifier":"Q14527","identifierLink":"https://www.uniprot.org/uniprotkb/Q14527/entry","name":"HLTF","description":"Helicase-like transcription factor","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45626","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352622","identifier":"P07355","identifierLink":"https://www.uniprot.org/uniprotkb/P07355/entry","name":"ANXA2","description":"Annexin A2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10502","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-717048","identifier":"P60903","identifierLink":"https://www.uniprot.org/uniprotkb/P60903/entry","name":"S100A10","description":"Protein S100-A10","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-858","complexName":"CHRAC chromatin remodeling complex","organismName":"Mus musculus; 10090","description":"ATP-dependent chromatin remodeling complex required for efficient DNA replication through highly condensed chromatin. It facilitates this process by mediating the sliding of nucleosomes from an end position to the center of a 248 base pair rDNA without causing major trans displacement of histones.","predictedComplex":false,"interactors":[{"ac":"EBI-8585664","identifier":"Q9JKP8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JKP8/entry","name":"Chrac1","description":"Chromatin accessibility complex protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10252","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-876752","identifier":"Q9JKP7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JKP7/entry","name":"Pole3","description":"DNA polymerase epsilon subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46172","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-927547","identifier":"Q91ZW3","identifierLink":"https://www.uniprot.org/uniprotkb/Q91ZW3/entry","name":"Smarca5","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-927567","identifier":"O88379","identifierLink":"https://www.uniprot.org/uniprotkb/O88379/entry","name":"Baz1a","description":"Bromodomain adjacent to zinc finger domain protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46510","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-859","complexName":"MSL histone acetyltransferase complex","organismName":"Mus musculus; 10090","description":"Responsible for genome-wide H4K16 acetylation. Important for ATM-dependent cell cycle checkpoint control as well as transcriptional activation of Hox genes in coordination with the H3K4 methyltransferase, MLL. May achieve dosage compensation, equalizing the expression levels of X-chromosomal genes between males and females, by stochastic inactivation of one of the female X chromosomes.","predictedComplex":false,"interactors":[{"ac":"EBI-11566163","identifier":"Q9WVG9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WVG9/entry","name":"Msl3","description":"MSL complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10880","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12561966","identifier":"Q69ZF8","identifierLink":"https://www.uniprot.org/uniprotkb/Q69ZF8/entry","name":"Msl2","description":"E3 ubiquitin-protein ligase MSL2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2552981","identifier":"Q9D1P2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D1P2/entry","name":"Kat8","description":"Histone acetyltransferase KAT8","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-647298","identifier":"Q6PDM1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDM1/entry","name":"Msl1","description":"Male-specific lethal 1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-860","complexName":"BAK1-Bcl-X complex","organismName":"Homo sapiens; 9606","description":"The apoptosis effector system is largely controlled by the balance of, and interactions between, proapoptotic and prosurvival, antiapoptotic  members of the Bcl-2 family of proteins.. Bcl-X acts as an apoptosis inhibitor and BAK as an activator, heterodimerization of these antagonists regulates cell survival. When not in a complex with a prosurvival protein, BAK  oligomerizes in the outer mitochondrial membrane to form pores and induce the release of cytochrome c and other signaling factors.","predictedComplex":false,"interactors":[{"ac":"EBI-287195","identifier":"Q07817-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q07817-1/entry","name":"BCL2L1","description":"Bcl-2-like protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-519866","identifier":"Q16611","identifierLink":"https://www.uniprot.org/uniprotkb/Q16611/entry","name":"BAK1","description":"Bcl-2 homologous antagonist/killer","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11256","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-864","complexName":"PPARgamma-NCOA1 activated nuclear receptor complex","organismName":"Mus musculus; 10090","description":"Member of the nuclear receptor family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. PPARgamma binds to fatty acids and their metabolites and serves as a key regulator of adipocyte differentation and glucose homeostasis. The effects of ligands on PPARgamma, Rxr, and other nuclear receptors are mediated through the ligand-binding domain (LBD). Upon ligand binding, the LBD undergoes a conformational change that results in the release of corepressors, the recruitment of coactivators such as Ncoa1, and the activation of transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-11171952","identifier":"P70365","identifierLink":"https://www.uniprot.org/uniprotkb/P70365/entry","name":"Ncoa1","description":"Nuclear receptor coactivator 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10684","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5260705","identifier":"P37238","identifierLink":"https://www.uniprot.org/uniprotkb/P37238/entry","name":"Pparg","description":"Peroxisome proliferator-activated receptor gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-865","complexName":"Electron transfer flavoprotein complex","organismName":"Mus musculus; 10090","description":"Functions as a specific electron acceptor for primary dehydrogenases involved in mitochondrial fatty acid and amino acid catabolism, transferring the electrons to terminal respiratory systems such as the electron transfer flavoprotein-ubiquinone oxidoreductase protein (Q921G7) which then transfers the electron to the ubiquinone pool in the inner mitochondrial membrane. Located on the matrix face of the inner mitochondrial membrane and docks onto the surface of partner proteins via a recognition peptide element located within an anchor domain.","predictedComplex":false,"interactors":[{"ac":"EBI-12508985","identifier":"CHEBI:456215","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:456215","name":"amp(2-)","description":"AMP(2-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1634288","identifier":"Q9DCW4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DCW4/entry","name":"Etfb","description":"Electron transfer flavoprotein subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8334254","identifier":"Q99LC5","identifierLink":"https://www.uniprot.org/uniprotkb/Q99LC5/entry","name":"Etfa","description":"Electron transfer flavoprotein subunit alpha, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR43153","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-867","complexName":"DBF4-dependent CDC7 kinase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Serine/threonine-protein kinase essential for the initiation of DNA replication. Associates with replication origins where it phosphorylates components of the prereplicative complex including the MCM helicase (CPX-2944). Has post-replicative functions in meiosis and is essential for double-strand break formation and kinetochore localization of monopolin.","predictedComplex":false,"interactors":[{"ac":"EBI-4451","identifier":"P06243","identifierLink":"https://www.uniprot.org/uniprotkb/P06243/entry","name":"CDC7","description":"Cell division control protein 7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11909","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5575","identifier":"P32325","identifierLink":"https://www.uniprot.org/uniprotkb/P32325/entry","name":"DBF4","description":"DDK kinase regulatory subunit DBF4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-868","complexName":"FET3-FTR1 high affinity iron permease complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"High affinity iron uptake complex present in the plasma membrane.  The complex forms in the endoplasmic reticulum and then traffics to the plasma membrane. Environmental ferric iron (Fe(III), Fe3+) is mobilized by reduction to ferrous ion (Fe(II), Fe2+) by surface metalloreductases such as FRE1 (P32791), followed by oxidation to Fe(III) by FET3. This FET3-bound Fe(III) is the substrate for permeation facilitated by FTR1.","predictedComplex":false,"interactors":[{"ac":"EBI-12592690","identifier":"CHEBI:23378","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:23378","name":"copper cation","description":"copper cation","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-6876","identifier":"P38993","identifierLink":"https://www.uniprot.org/uniprotkb/P38993/entry","name":"FET3","description":"Iron transport multicopper oxidase FET3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11709","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7138","identifier":"P40088","identifierLink":"https://www.uniprot.org/uniprotkb/P40088/entry","name":"FTR1","description":"Plasma membrane iron permease","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31632","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-869","complexName":"FET5-FTH1 high affinity iron exporter complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"High-affinity vacuolar exporter complex which transports ferrous iron ions (Fe(II), Fe2+) from the vacuole, the main storage component of intracellular free iron, into the cytoplasm in a low iron environment. The complex forms in the endoplasmic reticulum and then traffics to the vacuolar membrane. Plays a role in the switch from fermentative metabolism to respiratory metabolism.","predictedComplex":false,"interactors":[{"ac":"EBI-12592690","identifier":"CHEBI:23378","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:23378","name":"copper cation","description":"copper cation","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-20959","identifier":"P38310","identifierLink":"https://www.uniprot.org/uniprotkb/P38310/entry","name":"FTH1","description":"Iron transporter FTH1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31632","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6891","identifier":"P43561","identifierLink":"https://www.uniprot.org/uniprotkb/P43561/entry","name":"FET5","description":"Iron transport multicopper oxidase FET5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11709","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-871","complexName":"RXRbeta-VDR nuclear hormone receptor complex","organismName":"Homo sapiens; 9606","description":"Member of the nuclear receptor family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. The Vitamin D receptor (VDR) mediates the transcriptional effects of Vitamin D and plays a central role in calcium homeostasis. The 9-cis retinoic acid receptor (retinoid X receptor, RXR) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including the all-trans retinoic acid receptor (RAR). Receptors bind to hormone response elements (HREs) via their DNA-binding domains (DBD) and contain a C-terminal ligand-binding domain (LBD) that binds the hormone. Unliganded VDR can occupy its response elements as a homodimer. RXRB-VDR is a non-permissive receptor that cannot be activated by an RXR agonist but only by an agonist of the dominant partner receptor, VDR. Upon binding of ligand, VDR forms a heterodimer with RXRB through their LBDs and binds to Vitamin D response elements. The ligand for RXRB, 9-cis retinoic acid, has the opposite effect of destabilizing the heterodimeric-DNA complex.","predictedComplex":false,"interactors":[{"ac":"EBI-286357","identifier":"P11473","identifierLink":"https://www.uniprot.org/uniprotkb/P11473/entry","name":"VDR","description":"Vitamin D3 receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-748576","identifier":"P28702","identifierLink":"https://www.uniprot.org/uniprotkb/P28702/entry","name":"RXRB","description":"Retinoic acid receptor RXR-beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-872","complexName":"RXRbeta-VDR nuclear hormone receptor complex","organismName":"Mus musculus; 10090","description":"Member of the nuclear receptor family of ligand-regulated transcription factor complexes controlling the expression of numerous genes with a role in cellular differentiation, proliferation and apoptosis. The Vitamin D receptor (Vdr)  mediates the transcriptional effects of Vitamin D and plays a central role in calcium homeostasis. The 9-cis retinoic acid receptor (retinoid X receptor, RXR) is an important member of the nuclear receptor family because it forms heterodimers with many other receptors, including the all-trans retinoic acid receptor (RAR). Receptors bind to hormone response elements (HREs) via their DNA-binding domains (DBD) and contain a C-terminal ligand-binding domain (LBD) that binds the hormone. Unliganded Vdr can occupy its response elements as a homodimer. Rxrb-Vdr is a non-permissive receptor that cannot be activated by an RXR agonist but only by an agonist of the dominant partner receptor, Vdr. Upon binding of ligand, Vdr forms a heterodimer with Rxra through their LBDs and binds to Vitamin D response elements. The ligand for Rxrb, 9-cis retinoic acid, has the opposite effect of destabilizing the heterodimeric-DNA complex.","predictedComplex":false,"interactors":[{"ac":"EBI-346797","identifier":"P48281","identifierLink":"https://www.uniprot.org/uniprotkb/P48281/entry","name":"Vdr","description":"Vitamin D3 receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6392036","identifier":"P28704","identifierLink":"https://www.uniprot.org/uniprotkb/P28704/entry","name":"Rxrb","description":"Retinoic acid receptor RXR-beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24083","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-874","complexName":"GRASP65-GM130 Golgi stacking complex","organismName":"Homo sapiens; 9606","description":"Peripheral membrane complex that plays a key role in Golgi stacking.  Each Golgi stack is formed by five to eight tightly aligned flattened cisternae, GRASP65-GM130 forms mitotically regulated trans-oligomers that act  to hold adjacent Golgi cisternae into a stack, in particular the cis-Golgi network, which is close to the endoplasmic reticulum (ER) and receives the ER output.","predictedComplex":false,"interactors":[{"ac":"EBI-2561458","identifier":"Q9BQQ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BQQ3/entry","name":"GORASP1","description":"Golgi reassembly-stacking protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12893","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-618309","identifier":"Q08379","identifierLink":"https://www.uniprot.org/uniprotkb/Q08379/entry","name":"GOLGA2","description":"Golgin subfamily A member 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10881","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-875","complexName":"NSL histone acetyltransferase complex","organismName":"Mus musculus; 10090","description":"A histone acetyltransferase complex that catalyzes the acetylation of  histone H4 on lysines 5, 8, and 16 but not on lysine 12. The complex is recruited by phosphorylated  c-Jun to the promoter of its target genes where it then catalyzes  H4K16  acetylation  to  promote  gene transcription and causes the  release of the repressive NuRD complex from c-Jun target genes.  Coordination between the NSL complex and MLL/SET complexes promotes histone H3K4 dimethylation via an acetylation-dependent mechanism, further contributing to gene regulation. The NSL complex also plays an important role in the maintenance of pluripotency factors which indirectly ensure the proper expression of the X chromosome in embryonic stem cells.","predictedComplex":false,"interactors":[{"ac":"EBI-1247084","identifier":"P61965","identifierLink":"https://www.uniprot.org/uniprotkb/P61965/entry","name":"Wdr5","description":"WD repeat-containing protein 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12594388","identifier":"Q80TG1","identifierLink":"https://www.uniprot.org/uniprotkb/Q80TG1/entry","name":"Kansl1","description":"KAT8 regulatory NSL complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22443","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12594428","identifier":"Q99L90","identifierLink":"https://www.uniprot.org/uniprotkb/Q99L90/entry","name":"Mcrs1","description":"Microspherule protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13233","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2552981","identifier":"Q9D1P2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D1P2/entry","name":"Kat8","description":"Histone acetyltransferase KAT8","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3043883","identifier":"Q61191","identifierLink":"https://www.uniprot.org/uniprotkb/Q61191/entry","name":"Hcfc1","description":"Host cell factor 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46003","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5737962","identifier":"A2RSY1","identifierLink":"https://www.uniprot.org/uniprotkb/A2RSY1/entry","name":"Kansl3","description":"KAT8 regulatory NSL complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13136","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880283","identifier":"Q8BLG0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BLG0/entry","name":"Phf20","description":"PHD finger protein 20","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15856","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8357110","identifier":"Q8BQR4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BQR4/entry","name":"Kansl2","description":"KAT8 regulatory NSL complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13453","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-928496","identifier":"Q8CGY8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CGY8/entry","name":"Ogt","description":"UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR44366","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-876","complexName":"GID E3 ubiquitin ligase complex, RMND5A-RANBP9 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase complex that triggers polyubiquitylation and subsequent proteasomal degradation of selected substrates. The complex functions as a specific N-recognin of the Pro/N-degron pathway, binding substrates with N-terminal proline residues.","predictedComplex":false,"interactors":[{"ac":"EBI-1046864","identifier":"Q9H7D7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H7D7/entry","name":"WDR26","description":"WD repeat-containing protein 26","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22838","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1048053","identifier":"Q9UL63","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UL63/entry","name":"MKLN1","description":"Muskelin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15526","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1049469","identifier":"Q8IUR7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IUR7/entry","name":"ARMC8","description":"Armadillo repeat-containing protein 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15651","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1051077","identifier":"Q9NWU2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NWU2/entry","name":"GID8","description":"Glucose-induced degradation protein 8 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12864","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10984762","identifier":"Q7L5Y9","identifierLink":"https://www.uniprot.org/uniprotkb/Q7L5Y9/entry","name":"MAEA","description":"E3 ubiquitin-protein transferase MAEA","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12170","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11721624","identifier":"P62699","identifierLink":"https://www.uniprot.org/uniprotkb/P62699/entry","name":"YPEL5","description":"Protein yippee-like 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13848","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11918778","identifier":"Q8IVV7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IVV7/entry","name":"GID4","description":"Glucose-induced degradation protein 4 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15898","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2797992","identifier":"Q9H871","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H871/entry","name":"RMND5A","description":"E3 ubiquitin-protein transferase RMND5A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12170","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-636085","identifier":"Q96S59","identifierLink":"https://www.uniprot.org/uniprotkb/Q96S59/entry","name":"RANBP9","description":"Ran-binding protein 9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12864","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-878","complexName":"INO80 chromatin remodeling complex","organismName":"Mus musculus; 10090","description":"ATP-dependent nucleosome remodeling complex which slides mononucleosomes to a central position on a DNA template while tightly organizing nucleosomes within arrays. Functions in maintaining genome stability and removes H2AZ from nucleosomes. May play a largely repressive role in gene transcription, blocking H3K79 methylation and restricting transcription to gene units in euchromatin and away from silent regions, such as heterochromatin. Activates the expression of pluripotency factors by facilitating the recruitment of Mediator and Pol II at their promoters. Required for fork maintenance and progression in stalled replication forks. It is recruited to DNA damage sites and the Actr8 subunit is required for this recruitment.","predictedComplex":false,"interactors":[{"ac":"EBI-12594428","identifier":"Q99L90","identifierLink":"https://www.uniprot.org/uniprotkb/Q99L90/entry","name":"Mcrs1","description":"Microspherule protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13233","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12595073","identifier":"Q80US4","identifierLink":"https://www.uniprot.org/uniprotkb/Q80US4/entry","name":"Actr5","description":"Actin-related protein 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12595090","identifier":"Q8R2S9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R2S9/entry","name":"Actr8","description":"Actin-related protein 8","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12595115","identifier":"Q8BHA0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BHA0/entry","name":"Ino80c","description":"INO80 complex subunit C","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR31200","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12595135","identifier":"Q66JY2","identifierLink":"https://www.uniprot.org/uniprotkb/Q66JY2/entry","name":"Ino80d","description":"INO80 complex subunit D","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16198","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12595153","identifier":"A0A0U1RP99","identifierLink":"https://www.uniprot.org/uniprotkb/A0A0U1RP99/entry","name":"Ino80e","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-1634999","identifier":"P60122","identifierLink":"https://www.uniprot.org/uniprotkb/P60122/entry","name":"Ruvbl1","description":"RuvB-like 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2365444","identifier":"Q3U1J1","identifierLink":"https://www.uniprot.org/uniprotkb/Q3U1J1/entry","name":"Tfpt","description":"TCF3 fusion partner homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR35084","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2549911","identifier":"Q9WTM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WTM5/entry","name":"Ruvbl2","description":"RuvB-like 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942759","identifier":"Q9Z2N8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z2N8/entry","name":"Actl6a","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3043902","identifier":"Q6ZPV2","identifierLink":"https://www.uniprot.org/uniprotkb/Q6ZPV2/entry","name":"Ino80","description":"Chromatin-remodeling ATPase INO80","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45685","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3043931","identifier":"Q6PIJ4","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PIJ4/entry","name":"Nfrkb","description":"Nuclear factor related to kappa-B-binding protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13052","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-626705","identifier":"Q99PT3","identifierLink":"https://www.uniprot.org/uniprotkb/Q99PT3/entry","name":"Ino80b","description":"INO80 complex subunit B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21561","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6921536","identifier":"Q00899","identifierLink":"https://www.uniprot.org/uniprotkb/Q00899/entry","name":"Yy1","description":"Transcriptional repressor protein YY1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14003","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8820873","identifier":"Q9WUP7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WUP7/entry","name":"Uchl5","description":"Ubiquitin carboxyl-terminal hydrolase isozyme L5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10589","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-880","complexName":"MBD2/NuRD nucleosome remodeling and deacetylase complex","organismName":"Homo sapiens; 9606","description":"Corepressor complex that couples histone deacetylase and ATP-dependent chromatin remodeling activities. It regulates the higher-order structure of chromatin, making chromatin more compact by removing acetyl groups from nucleosomes, and has important roles in the regulation of gene expression and DNA damage repair.\r\nThe core of the complex is composed of six groups of proteins, each one with several paralogues (HDAC1/2, MTA1/2/3, RBBP4/7, GATAD2A/B, MBD2, and CHD3/4). Combinatorial assembly of these isoforms contributes to the targeting and function of the complex.\r\nIt is currently not known whether GATAD2A/GATAD2B, RBBP4/RBBP7, and MTA1/MTA2/MTA3 form heterodimers/trimers or mutually exclusive homodimers/trimers. The  CHD3/4 ATPase, utilizes energy derived from hydrolysis of ATP for DNA sliding and repositioning of nucleosomes. The second catalytic subunit, HDAC1/2 (histone deacetylase), deacetylates acetylated lysine residues of histone and non-histone proteins. This dual enzymatic activity is proposed to be important for the efficient formation of heterochromatin with densely packed hypoacetylated nucleosomes and the rapid termination of gene transcription.\r\nIn addition to the well-described core subunits, a large number of proteins have been reported to interact with the NuRD complex, like  DOC1 (O14519), KPNA2 (P52292), ZMYND8(Q9ULU4), ZNF512B/532/592/687(Q96KM6, Q9HCE3, Q92610, Q8N1G0),  SALL4 (Q9UJQ4), PRMT5 (O14744), MEP50 (Q9BQA1). They also contribute to dictate the different biological functions of the NuRD complex.","predictedComplex":false,"interactors":[{"ac":"EBI-1783035","identifier":"O94776","identifierLink":"https://www.uniprot.org/uniprotkb/O94776/entry","name":"MTA2","description":"Metastasis-associated protein MTA2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10865","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2461787","identifier":"Q9BTC8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BTC8/entry","name":"MTA3","description":"Metastasis-associated protein MTA3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10865","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301821","identifier":"Q92769","identifierLink":"https://www.uniprot.org/uniprotkb/Q92769/entry","name":"HDAC2","description":"Histone deacetylase 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301834","identifier":"Q13547","identifierLink":"https://www.uniprot.org/uniprotkb/Q13547/entry","name":"HDAC1","description":"Histone deacetylase 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352227","identifier":"Q16576","identifierLink":"https://www.uniprot.org/uniprotkb/Q16576/entry","name":"RBBP7","description":"Histone-binding protein RBBP7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372916","identifier":"Q14839","identifierLink":"https://www.uniprot.org/uniprotkb/Q14839/entry","name":"CHD4","description":"Chromodomain-helicase-DNA-binding protein 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45623","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-523590","identifier":"Q12873","identifierLink":"https://www.uniprot.org/uniprotkb/Q12873/entry","name":"CHD3","description":"Chromodomain-helicase-DNA-binding protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45623","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-620823","identifier":"Q09028","identifierLink":"https://www.uniprot.org/uniprotkb/Q09028/entry","name":"RBBP4","description":"Histone-binding protein RBBP4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714236","identifier":"Q13330","identifierLink":"https://www.uniprot.org/uniprotkb/Q13330/entry","name":"MTA1","description":"Metastasis-associated protein MTA1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10865","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-726224","identifier":"Q86YP4","identifierLink":"https://www.uniprot.org/uniprotkb/Q86YP4/entry","name":"GATAD2A","description":"Transcriptional repressor p66-alpha","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13455","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-923391","identifier":"Q9UBB5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UBB5/entry","name":"MBD2","description":"Methyl-CpG-binding domain protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12396","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-923440","identifier":"Q8WXI9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WXI9/entry","name":"GATAD2B","description":"Transcriptional repressor p66-beta","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13455","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-881","complexName":"Calcineurin-Calmodulin-AKAP5 complex, alpha-R1 variant","organismName":"Mus musculus; 10090","description":"Calcium-dependent, calmodulin-stimulated protein phosphatase calcineurin in complex with plasma-membrane anchor protein Akap5. Calcineurin is important for cardiac development and pathophysiology, for nervous-system development and for some of the plastic changes in neurons that are believed to underlie learning and memory. Akap5 recruits calcineurin to the vicinity of L-type Ca2+ channels for their activation by elevated Ca2+ entering the cell. Akap5 balances the opposing effects of calcineurin and protein kinase A (PKA) (P05132) on neuronal voltage-gated L-type Ca2+ channels and coordinates the activities of calcineurin, PKA and PKC on a number of other channels and receptors. Despite its atypical PxIxIT calcineurin-recognition motif that confers stronger binding affinity by calcineurin than other substrates, it allows for effective disengagement of calcineurin to couple channel activation with downstream signaling events. The calcineurin-Akap5 complex has been shown to promote NFAT signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-397208","identifier":"P63328","identifierLink":"https://www.uniprot.org/uniprotkb/P63328/entry","name":"Ppp3ca","description":"Protein phosphatase 3 catalytic subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397460","identifier":"P62204","identifierLink":"https://www.uniprot.org/uniprotkb/P62204/entry","name":"Calm1","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-6666164","identifier":"Q63810","identifierLink":"https://www.uniprot.org/uniprotkb/Q63810/entry","name":"Ppp3r1","description":"Calcineurin subunit B type 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7091108","identifier":"D3YVF0","identifierLink":"https://www.uniprot.org/uniprotkb/D3YVF0/entry","name":"Akap5","description":"A-kinase anchor protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15182","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-884","complexName":"LIN-10-LIN-2-LIN-7 complex, LIN7B variant","organismName":"Mus musculus; 10090","description":"Scaffolding complex which appears to act as a major organization hub for modulating cellular functions, such as neuronal synaptic transmission, and cell polarity establishment and maintenance, with four PDZ domains, an SH3-GK tandem, and a PTB domain not involved in complex formation and thus available for binding to various target proteins.  May associate with the motor protein Kif17 (Q99PW8) to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B (Q01097) along microtubules..","predictedComplex":false,"interactors":[{"ac":"EBI-771402","identifier":"O70589","identifierLink":"https://www.uniprot.org/uniprotkb/O70589/entry","name":"Cask","description":"Peripheral plasma membrane protein CASK","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23122","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-775103","identifier":"O88951","identifierLink":"https://www.uniprot.org/uniprotkb/O88951/entry","name":"Lin7b","description":"Protein lin-7 homolog B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14063","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8840254","identifier":"B2RUJ5","identifierLink":"https://www.uniprot.org/uniprotkb/B2RUJ5/entry","name":"Apba1","description":"Amyloid-beta A4 precursor protein-binding family A member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12345","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-885","complexName":"MTERF4-NSUN4 mitochondrial ribosomal assembly complex","organismName":"Homo sapiens; 9606","description":"Sequester helices H68-71 of the 16S rRNA and maintains this in an open, immature conformation, exposing the functionally important regions of rRNA for modification by the MRM2 methyltransferase (Q9UI43) and quality control interactions with the conserved mitochondrial GTPase MTG2 (Q9H4K7). NSUN4 has 5-methylcytosine rRNA methyltransferase complex which targets C911 of the 12S rRNA in the 28S small ribosomal subunit (CPX-5225) but this may be independent of complex formation.","predictedComplex":false,"interactors":[{"ac":"EBI-744435","identifier":"Q96CB9","identifierLink":"https://www.uniprot.org/uniprotkb/Q96CB9/entry","name":"NSUN4","description":"5-cytosine rRNA methyltransferase NSUN4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22808","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-948435","identifier":"Q7Z6M4","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z6M4/entry","name":"MTERF4","description":"Transcription termination factor 4, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-980183","identifier":"CHEBI:15414","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15414","name":"s-adenosyl-l-methionine","description":"S adenosyl Methionine","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-888","complexName":"Keratin-5 - Keratin-14 dimer complex","organismName":"Homo sapiens; 9606","description":"Part of the intermediate filaments of the cytoskeleton. Mostly found in skin. \r\n\r\nMutations in either KRT5 or KRT14 can result in epidermolysis bullosa simplex (EBS).","predictedComplex":false,"interactors":[{"ac":"EBI-702178","identifier":"P02533","identifierLink":"https://www.uniprot.org/uniprotkb/P02533/entry","name":"KRT14","description":"Keratin, type I cytoskeletal 14","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-702187","identifier":"P13647","identifierLink":"https://www.uniprot.org/uniprotkb/P13647/entry","name":"KRT5","description":"Keratin, type II cytoskeletal 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45616","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-889","complexName":"NONO-PSPC1 RNA-binding complex","organismName":"Homo sapiens; 9606","description":"RNA-binding complex which is a core component of paraspeckles, discrete subnuclear bodies in the interchromatin nucleoplasmic space, often located adjacent to nuclear specks. Biogenesis and structural integrity of paraspeckles mainly depend on the interaction of NONO, SFPQ, and PSPC1 homo/heterodimers with the long non-coding RNA nuclear-enriched autosomal non-coding transcripts (NEAT1). The complex plays a role in several nuclear processes, such as pre-mRNA splicing, DNA repair, and transcriptional regulation","predictedComplex":false,"interactors":[{"ac":"EBI-1392258","identifier":"Q8WXF1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WXF1/entry","name":"PSPC1","description":"Paraspeckle component 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23189","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350527","identifier":"Q15233","identifierLink":"https://www.uniprot.org/uniprotkb/Q15233/entry","name":"NONO","description":"Non-POU domain-containing octamer-binding protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23189","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-890","complexName":"C3PO endoribonuclease complex","organismName":"Homo sapiens; 9606","description":"Endoribonuclease complex which functions as the component 3 promoter of RISC (RNA-induced silencing complex). Cleaves the fragmented siRNA passenger strands and facilitates the activation of RNA-induced silencing complex (RISC), the effector complex of RNA interference (RNAi), and thus plays a role in post-transcriptional repression of gene expression through down-regulation of translation or induction of mRNA degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-1044160","identifier":"Q15631","identifierLink":"https://www.uniprot.org/uniprotkb/Q15631/entry","name":"TSN","description":"Translin","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10741","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21353855","identifier":"Q99598","identifierLink":"https://www.uniprot.org/uniprotkb/Q99598/entry","name":"TSNAX","description":"Translin-associated protein X","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10741","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-891","complexName":"DSIF transcription elongation factor complex","organismName":"Homo sapiens; 9606","description":"An essential RNA polymerase II elongation factor which functions in the control of RNAP II processivity. Mediates both activation and inhibition of transcription elongation, and plays a role in pre-mRNA processing. Required for promoter-proximal pausing when elongating Pol II pauses near the promoter, about 20-60 base pairs downstream of the transcription start site, a key event in post-initiation regulation of transcription. SUPT5H docks DSIF to Pol II near the RNA exit channel where it facilitates capping of the nascent RNA . The negative elongation factor (NELF, CPX-6267) complex then recognizes the Pol II-SUPT5H interface and associates with the elongation complex as it transcribes through the promoter-proximal region. Phosphorylation of SUPT5H by P-TEFb (CPX-222/CPX-321/CPX-322) appears to trigger dissociation of NELF from Pol II, enabling Pol II reactivation and resumption of elongation.","predictedComplex":false,"interactors":[{"ac":"EBI-710464","identifier":"O00267","identifierLink":"https://www.uniprot.org/uniprotkb/O00267/entry","name":"SUPT5H","description":"Transcription elongation factor SPT5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11125","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727250","identifier":"P63272","identifierLink":"https://www.uniprot.org/uniprotkb/P63272/entry","name":"SUPT4H1","description":"Transcription elongation factor SPT4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12882","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-892","complexName":"TLR2-TLR6 toll-like receptor complex","organismName":"Homo sapiens; 9606","description":"Type I membrane receptor that plays a crucial role in innate immunity by recognizing conserved patterns in diverse microbial molecules including lipoproteins, lipopeptides, lipopolysaccharide, flagellin, and nucleic acids.TLR1-TLR6 mainly recognizes diacylated lipopeptides deriving from microorganisms, in particular bacteria and viruses. Ligand binding triggers conformational changes and subsequent recruitment of adaptor proteins which execute downstream signal transduction.","predictedComplex":false,"interactors":[{"ac":"EBI-13940779","identifier":"Q9Y2C9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2C9/entry","name":"TLR6","description":"Toll-like receptor 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24365","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-973722","identifier":"O60603","identifierLink":"https://www.uniprot.org/uniprotkb/O60603/entry","name":"TLR2","description":"Toll-like receptor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24365","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-893","complexName":"TLR1-TLR2 toll-like receptor complex","organismName":"Homo sapiens; 9606","description":"Type I membrane receptor that plays a crucial role in innate immunity by recognizing conserved patterns in diverse microbial molecules including lipoproteins, lipopeptides, lipopolysaccharide, flagellin, and nucleic acids. TLR1-TLR2 mainly recognizes triacylated lipopeptides deriving from microorganisms. Ligand binding triggers conformational changes and subsequent recruitment of adaptor proteins which execute downstream signal transduction.","predictedComplex":false,"interactors":[{"ac":"EBI-9009517","identifier":"Q15399","identifierLink":"https://www.uniprot.org/uniprotkb/Q15399/entry","name":"TLR1","description":"Toll-like receptor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24365","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-973722","identifier":"O60603","identifierLink":"https://www.uniprot.org/uniprotkb/O60603/entry","name":"TLR2","description":"Toll-like receptor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24365","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-898","complexName":"Annexin A2 - S100-A10 complex","organismName":"Mus musculus; 10090","description":"Calcium-dependent membrane-tethering complex that acts on ruptured membranes and aids general membrane organisation. Annexin A2 binds to negatively charged phospholipids at rupture sites while the S100-A10 dimer binds one molecule of annexin A2 at each end forming a junctions between adjacent bilayers. Rapid influx of Ca2+ at the rupture site activates complex formation by Ca2+ binding to Annexin A2. Membrane tethering is further aided by additional proteins forming larger complexes, such as the AHNAK - Annexin A2 - S100-A10 complex (CPX-905) or the SMARCA3 - Annexin A2 - S100-A10 complex (CPX-899); repair activity may also require dysferlin (Q9ESD7). \r\n\r\nAlso plays a role in the organization of membrane-associated actin at sites of cholesterol-rich membrane domains. Found at sites of plasma membrane/secretory granule membrane contact and intergranule contact and therefore possibly involved in exocytotic processes and vesicles aggregation. Can indirectly affect a number of membrane transport events. Linked to Cl− channel regulation. As an extracellular complex, it regulates the stimulation of t-PA-dependent activation of plasminogen.","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-643986","identifier":"P08207","identifierLink":"https://www.uniprot.org/uniprotkb/P08207/entry","name":"S100a10","description":"Protein S100-A10","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-738510","identifier":"P07356","identifierLink":"https://www.uniprot.org/uniprotkb/P07356/entry","name":"Anxa2","description":"Annexin A2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10502","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-899","complexName":"SMARCA3 - Annexin A2 - S100-A10 complex","organismName":"Mus musculus; 10090","description":"A transcription factor complex that mediates neurogenic and behavioral responses to selective antidepressant serotonin-reuptake inhibitors. The core tetramer of annexin A2 - S100A10 (CPX-898) anchors the complex to the inner nuclear membrane while Hltf/Smarca3 binds to promoter sequences. Hltf's DNA binding affinity is enhanced by the interaction with annexin A2 and S100-A10.","predictedComplex":false,"interactors":[{"ac":"EBI-643986","identifier":"P08207","identifierLink":"https://www.uniprot.org/uniprotkb/P08207/entry","name":"S100a10","description":"Protein S100-A10","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6869770","identifier":"Q6PCN7","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PCN7/entry","name":"Hltf","description":"Helicase-like transcription factor","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45626","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-738510","identifier":"P07356","identifierLink":"https://www.uniprot.org/uniprotkb/P07356/entry","name":"Anxa2","description":"Annexin A2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10502","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-902","complexName":"Kv7.1 channel complex","organismName":"Homo sapiens; 9606","description":"Voltage-dependent potassium channels that plays major roles in tuning neuronal and cardiomyocyte excitability by acting as a brake for neuronal firing and by controlling cardiomyocyte repolarization. Calmodulin acts as obligate subunit of the Kv7.1 channel.","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-359667","identifier":"P51787","identifierLink":"https://www.uniprot.org/uniprotkb/P51787/entry","name":"KCNQ1","description":"Potassium voltage-gated channel subfamily KQT member 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11537","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397435","identifier":"P62158","identifierLink":"https://www.uniprot.org/uniprotkb/P62158/entry","name":"calm_human","description":"Calmodulin","stochiometry":"minValue: 2, maxValue: 2","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-903","complexName":"TFTC histone acetylation complex","organismName":"Homo sapiens; 9606","description":"A chromatin-acetylating transcription coactivator with histone acetyltransferase activity. TFTC is a TBP (TATA binding protein) independent transcription initiation factor, able to nucleate RNA polymerase II transcription. It acetylates histone H3 in both a free and a nucleosomal context, but preferentially in nucleosomes assembled on UV-irradiated DNA, indicating that TFTC may also function as a facilitator of DNA repair. It interacts with the splicing factor SF3B3 (Q15393). The complex also has histone H2A and H2B deubiquitinase activity which counteracts heterochromatin silencing. May include TAF6L (Q9Y6J9).\r\nBecause of the similar subunit composition between the TFTC complex and the SAGA (also called STAGA) complex, it has been considered as the same complex in some publications (PMID:19114550, 25111486, 18206972, 15115762).","predictedComplex":false,"interactors":[{"ac":"EBI-1034238","identifier":"Q16514","identifierLink":"https://www.uniprot.org/uniprotkb/Q16514/entry","name":"TAF12","description":"Transcription initiation factor TFIID subunit 12","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1034261","identifier":"O00268","identifierLink":"https://www.uniprot.org/uniprotkb/O00268/entry","name":"TAF4","description":"Transcription initiation factor TFIID subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15138","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12603476","identifier":"CHEBI:27363","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:27363","name":"zinc atom","description":"zinc atom","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1560063","identifier":"Q6P1X5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P1X5/entry","name":"TAF2","description":"Transcription initiation factor TFIID subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15137","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1560145","identifier":"Q15542","identifierLink":"https://www.uniprot.org/uniprotkb/Q15542/entry","name":"TAF5","description":"Transcription initiation factor TFIID subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19879","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1560194","identifier":"Q15545","identifierLink":"https://www.uniprot.org/uniprotkb/Q15545/entry","name":"TAF7","description":"Transcription initiation factor TFIID subunit 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12228","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1560206","identifier":"P49848","identifierLink":"https://www.uniprot.org/uniprotkb/P49848/entry","name":"TAF6","description":"Transcription initiation factor TFIID subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10221","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1785876","identifier":"O75529","identifierLink":"https://www.uniprot.org/uniprotkb/O75529/entry","name":"TAF5L","description":"TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19879","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-399128","identifier":"Q9Y4A5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4A5/entry","name":"TRRAP","description":"Transformation/transcription domain-associated protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-473249","identifier":"O75528","identifierLink":"https://www.uniprot.org/uniprotkb/O75528/entry","name":"TADA3","description":"Transcriptional adapter 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13556","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-477622","identifier":"Q92830","identifierLink":"https://www.uniprot.org/uniprotkb/Q92830/entry","name":"KAT2A","description":"Histone acetyltransferase KAT2A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45750","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-708350","identifier":"O15265","identifierLink":"https://www.uniprot.org/uniprotkb/O15265/entry","name":"ATXN7","description":"Ataxin-7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-708376","identifier":"Q12962","identifierLink":"https://www.uniprot.org/uniprotkb/Q12962/entry","name":"TAF10","description":"Transcription initiation factor TFIID subunit 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21242","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712521","identifier":"Q16594","identifierLink":"https://www.uniprot.org/uniprotkb/Q16594/entry","name":"TAF9","description":"Transcription initiation factor TFIID subunit 9","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-719226","identifier":"Q9NPA8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPA8/entry","name":"ENY2","description":"Transcription and mRNA export factor ENY2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12514","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-723510","identifier":"Q9UPT9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UPT9/entry","name":"USP22","description":"Ubiquitin carboxyl-terminal hydrolase 22","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21646","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-896640","identifier":"O75486","identifierLink":"https://www.uniprot.org/uniprotkb/O75486/entry","name":"SUPT3H","description":"Transcription initiation protein SPT3 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11380","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-949215","identifier":"Q14CW9","identifierLink":"https://www.uniprot.org/uniprotkb/Q14CW9/entry","name":"ATXN7L3","description":"Ataxin-7-like protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46367","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-905","complexName":"AHNAK - Annexin A2 - S100-A10 complex","organismName":"Mus musculus; 10090","description":"Calcium-dependent membrane-tethering complex that acts on ruptured membranes and aids general membrane organisation. Rapid influx of Ca2+ at the rupture site activates complex formation by Ca2+ binding to Annexin A2; repair activity may also require dysferlin (O75923).","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-12601627","identifier":"E9Q616","identifierLink":"https://www.uniprot.org/uniprotkb/E9Q616/entry","name":"Ahnak","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23348","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-643986","identifier":"P08207","identifierLink":"https://www.uniprot.org/uniprotkb/P08207/entry","name":"S100a10","description":"Protein S100-A10","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11639","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-738510","identifier":"P07356","identifierLink":"https://www.uniprot.org/uniprotkb/P07356/entry","name":"Anxa2","description":"Annexin A2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10502","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-909","complexName":"NLGN1(-SSA-SSB) - NRXN1-beta(-SS4) complex","organismName":"Homo sapiens; 9606","description":"A cell adhesion complex that forms at synaptic clefts and mediates trans-synaptic signaling. Composed by binding of the extracellular domains of two presynaptic neurexin proteins and two postsynaptic neuroligin proteins. \r\n\r\nExpression of both subunits is regulated by neuronal activity. \r\n\r\nRequired for synaptic differentiation, maturation and maintenance, dendritic spine remodelling and axon arborisation. Possibly required for synapse formation. Mediates bidirectional synaptic signalling and coupling of presynaptic, Ca2+-dependent synaptic vesicle exocytosis (= neurotransmitter release) with postsynaptic neurotransmitter receptor recruitment. \r\n\r\nActs as a molecular switch between excitatory and inhibitory synapses: this complex acts primarily, but not exclusively, on GABAergic, inhibitory synapses that mainly release neurotransmitters GABA and glycine. \r\n\r\nMainly found in synaptic clefts of the central nervous system but also at neuromuscular junctions (particularly alpha neurexin-containing complexes). \r\n\r\nMutations in the neuroligin dimer interface as well as allosteric affects of mutation in both subunits affect spacial and fear-associated memory and result in autism-related disorders, mental retardation disorders and schizophrenia.","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-16513622","identifier":"P58400-1","identifierLink":"https://www.uniprot.org/uniprotkb/P58400-1/entry","name":"NRXN1","description":"Neurexin-1-beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-8287193","identifier":"Q8N2Q7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N2Q7/entry","name":"NLGN1","description":"Neuroligin-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43903","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-912","complexName":"bZIP transcription factor complex, CEBPE-CEBPE","organismName":"Homo sapiens; 9606","description":"Transcription factor complex which binds to a specific DNA consensus sequence to regulate transcription. Required for the terminal differentiation of neutrophils, promyelocyte-myelocyte transition in myeloid differentiation, regulating the expression of neutrophil-specific granule proteins such as lactotransferrin (P02788).","predictedComplex":false,"interactors":[{"ac":"EBI-3907048","identifier":"Q15744","identifierLink":"https://www.uniprot.org/uniprotkb/Q15744/entry","name":"CEBPE","description":"CCAAT/enhancer-binding protein epsilon","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23334","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-914","complexName":"Casein kinase II complex, CSNK2A1 variant","organismName":"Homo sapiens; 9606","description":"Serine/threonine-protein kinase that phosphorylates substrates containing acidic residues both N- and C-terminal to the phosphorylated serine or threonine.","predictedComplex":false,"interactors":[{"ac":"EBI-347804","identifier":"P68400","identifierLink":"https://www.uniprot.org/uniprotkb/P68400/entry","name":"CSNK2A1","description":"Casein kinase II subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24054","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348169","identifier":"P67870","identifierLink":"https://www.uniprot.org/uniprotkb/P67870/entry","name":"CSNK2B","description":"Casein kinase II subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-915","complexName":"General transcription factor complex TFIID","organismName":"Homo sapiens; 9606","description":"General transcription factor complex that acts as the primary core promoter recognition factor in the initiation of RNA polymerase II (Pol II)-dependent transcription. The TBP subunit of TFIID recognizes and binds to the TATA box (if present), while TAF1 and TAF2 interact with the Initiator element (Inr), and TAF1 and the TAF6-TAF9 module recognizes the downstream core promoter element (DPE). Other core promoter elements, such as the motif ten element (MTE), may also be involved. Binding of the general transcription factor complex TFIIA (CPX-519) enhances binding of TFIID to the core promoter and nucleates  pre-initiation complex (PIC) assembly. Following recruitment of TFIIA to TFIID, TFIIB, TFIIF (CPX-79), Pol II, TFIIE and TFIIH are successively assembled at the core promoter, allowing the PIC to initiate Pol II transcription. While TFIID is essential for transcription and its post-mitotic reinitiation, the loss of one or more subunits does not harm ongoing transcription during any given cell cycle. \r\n\r\nTFIID promoter binding appears to be regulated by histone modifications: TAF1 bromodomains (1361-1617 aa, IPR001487) bind the modified histone tails of acetylated H4K16, H4K5/K12 and H4K8/K16. TAF1 also appears to exhibit histone acetyltransferase activity towards histones H3 and H4. TAF3 and the PHD domains of other TFIID subunits  bind modified histone tails carrying trimethylated H3K4 in combination with acetylated H3K9 and H3K14. \r\n\r\nTAF1 phosphorylates TP53 (P04637) on Thr-55, leading to TP53 degradation and G1 cell cycle progression. \r\n\r\nSpermatocytes contain variants of TAF-containing complexes, including the TAF4B variant (CPX-930).","predictedComplex":false,"interactors":[{"ac":"EBI-1026992","identifier":"Q15543","identifierLink":"https://www.uniprot.org/uniprotkb/Q15543/entry","name":"TAF13","description":"Transcription initiation factor TFIID subunit 13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11380","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1027005","identifier":"Q15544","identifierLink":"https://www.uniprot.org/uniprotkb/Q15544/entry","name":"TAF11","description":"Transcription initiation factor TFIID subunit 11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13218","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1034238","identifier":"Q16514","identifierLink":"https://www.uniprot.org/uniprotkb/Q16514/entry","name":"TAF12","description":"Transcription initiation factor TFIID subunit 12","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1034261","identifier":"O00268","identifierLink":"https://www.uniprot.org/uniprotkb/O00268/entry","name":"TAF4","description":"Transcription initiation factor TFIID subunit 4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15138","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1560063","identifier":"Q6P1X5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P1X5/entry","name":"TAF2","description":"Transcription initiation factor TFIID subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15137","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1560087","identifier":"Q5VWG9","identifierLink":"https://www.uniprot.org/uniprotkb/Q5VWG9/entry","name":"TAF3","description":"Transcription initiation factor TFIID subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46452","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1560145","identifier":"Q15542","identifierLink":"https://www.uniprot.org/uniprotkb/Q15542/entry","name":"TAF5","description":"Transcription initiation factor TFIID subunit 5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19879","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1560194","identifier":"Q15545","identifierLink":"https://www.uniprot.org/uniprotkb/Q15545/entry","name":"TAF7","description":"Transcription initiation factor TFIID subunit 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12228","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1560206","identifier":"P49848","identifierLink":"https://www.uniprot.org/uniprotkb/P49848/entry","name":"TAF6","description":"Transcription initiation factor TFIID subunit 6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10221","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1560220","identifier":"Q7Z7C8","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z7C8/entry","name":"TAF8","description":"Transcription initiation factor TFIID subunit 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46469","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355371","identifier":"P20226","identifierLink":"https://www.uniprot.org/uniprotkb/P20226/entry","name":"TBP","description":"TATA-box-binding protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10126","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-491289","identifier":"P21675","identifierLink":"https://www.uniprot.org/uniprotkb/P21675/entry","name":"TAF1","description":"Transcription initiation factor TFIID subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13900","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-708376","identifier":"Q12962","identifierLink":"https://www.uniprot.org/uniprotkb/Q12962/entry","name":"TAF10","description":"Transcription initiation factor TFIID subunit 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21242","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712521","identifier":"Q16594","identifierLink":"https://www.uniprot.org/uniprotkb/Q16594/entry","name":"TAF9","description":"Transcription initiation factor TFIID subunit 9","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-916","complexName":"TFTC histone acetylation complex","organismName":"Mus musculus; 10090","description":"A chromatin-acetylating transcription coactivator with histone acetyltransferase activity. TFTC is a TBP (TATA binding protein) independent transcription initiation factor, able to nucleate RNA polymerase II transcription. It acetylates histone H3 in both a free and a nucleosomal context, but preferentially in nucleosomes assembled on UV-irradiated DNA, indicating that TFTC may also function as a facilitator of DNA repair. It interacts with the splicing factor Sf3b3 (Q921M3). The complex also has histone H2A and H2B deubiquitinase activity which counteracts heterochromatin silencing. May include TAF6L (Q8R2K4).\r\nBecause of the similar subunit composition between the TFTC complex and the SAGA (also called STAGA) complex, it has been considered as the same complex in some publications (PMID:19114550, 25111486, 18206972, 15115762).","predictedComplex":false,"interactors":[{"ac":"EBI-12603476","identifier":"CHEBI:27363","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:27363","name":"zinc atom","description":"zinc atom","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-12667195","identifier":"B0QZW4","identifierLink":"https://www.uniprot.org/uniprotkb/B0QZW4/entry","name":"Supt3","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-12667225","identifier":"Q8C176","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C176/entry","name":"Taf2","description":"Transcription initiation factor TFIID subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15137","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12667248","identifier":"Q8C092","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C092/entry","name":"Taf5","description":"Transcription initiation factor TFIID subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR19879","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942477","identifier":"Q80YV3","identifierLink":"https://www.uniprot.org/uniprotkb/Q80YV3/entry","name":"Trrap","description":"Transformation/transcription domain-associated protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2943116","identifier":"Q9JHD2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JHD2/entry","name":"Kat2a","description":"Histone acetyltransferase KAT2A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45750","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2943161","identifier":"Q91WQ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q91WQ5/entry","name":"Taf5l","description":"TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR19879","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2943209","identifier":"Q8R0L9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R0L9/entry","name":"Tada3","description":"Transcriptional adapter 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13556","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2943311","identifier":"Q8VI33","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VI33/entry","name":"Taf9","description":"Transcription initiation factor TFIID subunit 9","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR48068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5744190","identifier":"Q62311","identifierLink":"https://www.uniprot.org/uniprotkb/Q62311/entry","name":"Taf6","description":"Transcription initiation factor TFIID subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10221","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5744209","identifier":"Q8K0H5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K0H5/entry","name":"Taf10","description":"Transcription initiation factor TFIID subunit 10","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21242","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6260765","identifier":"Q9R1C0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R1C0/entry","name":"Taf7","description":"Transcription initiation factor TFIID subunit 7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12228","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7990620","identifier":"A2AWT3","identifierLink":"https://www.uniprot.org/uniprotkb/A2AWT3/entry","name":"Atxn7l3","description":"Ataxin-7-like protein 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46367","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7990691","identifier":"Q5DU02","identifierLink":"https://www.uniprot.org/uniprotkb/Q5DU02/entry","name":"Usp22","description":"Ubiquitin carboxyl-terminal hydrolase 22","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21646","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7990748","identifier":"Q8R4I1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R4I1/entry","name":"Atxn7","description":"Ataxin-7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7990784","identifier":"Q8VE65","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VE65/entry","name":"Taf12","description":"Transcription initiation factor TFIID subunit 12","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8338402","identifier":"Q9JIX0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JIX0/entry","name":"Eny2","description":"Transcription and mRNA export factor ENY2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12514","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8663048","identifier":"E9QAP7","identifierLink":"https://www.uniprot.org/uniprotkb/E9QAP7/entry","name":"Taf4","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15138","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-922","complexName":"MBD3/NuRD nucleosome remodeling and deacetylase complex","organismName":"Homo sapiens; 9606","description":"Corepressor complex that couples histone deacetylase and ATP-dependent chromatin remodeling activities. It regulates the higher-order structure of chromatin, making chromatin more compact by removing acetyl groups from nucleosomes, and has important roles in the regulation of gene expression, DNA damage repair and cell differentiation.\r\nThe core of the complex is composed of six groups of proteins, each one with several  paralogues (HDAC1/2, MTA1/2/3, RBBP4/7, GATAD2A/B, MBD3, and CHD3/4). Combinatorial assembly of these isoforms contributes to the targeting and function of the complex.\r\nIt is currently not known whether GATAD2A/GATAD2B, RBBP4/RBBP7, and MTA1/MTA2/MTA3 form heterodimers/trimers or mutually exclusive homodimers/trimers. The  CHD3/4 ATPase, utilizes energy derived from hydrolysis of ATP for DNA sliding and repositioning of nucleosomes. The second catalytic subunit, HDAC1/2 (histone deacetylase), deacetylates acetylated lysine residues of histone and non-histone proteins. This dual enzymatic activity is proposed to be important for the efficient formation of heterochromatin with densely packed hypoacetylated nucleosomes and the rapid termination of gene transcription.\r\nIn addition to the well-described core subunits, a large number of proteins have been reported to interact with the NuRD complex, like  DOC1 (O14519), KPNA2 (P52292), ZMYND8(Q9ULU4), ZNF512B/532/592/687(Q96KM6, Q9HCE3, Q92610, Q8N1G0),  SALL4 (Q9UJQ4), PRMT5 (O14744), MEP50 (Q9BQA1). They also contribute to dictate the different biological functions of the NuRD complex.","predictedComplex":false,"interactors":[{"ac":"EBI-1783035","identifier":"O94776","identifierLink":"https://www.uniprot.org/uniprotkb/O94776/entry","name":"MTA2","description":"Metastasis-associated protein MTA2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10865","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1783068","identifier":"O95983","identifierLink":"https://www.uniprot.org/uniprotkb/O95983/entry","name":"MBD3","description":"Methyl-CpG-binding domain protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12396","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2461787","identifier":"Q9BTC8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BTC8/entry","name":"MTA3","description":"Metastasis-associated protein MTA3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10865","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301821","identifier":"Q92769","identifierLink":"https://www.uniprot.org/uniprotkb/Q92769/entry","name":"HDAC2","description":"Histone deacetylase 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301834","identifier":"Q13547","identifierLink":"https://www.uniprot.org/uniprotkb/Q13547/entry","name":"HDAC1","description":"Histone deacetylase 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352227","identifier":"Q16576","identifierLink":"https://www.uniprot.org/uniprotkb/Q16576/entry","name":"RBBP7","description":"Histone-binding protein RBBP7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372916","identifier":"Q14839","identifierLink":"https://www.uniprot.org/uniprotkb/Q14839/entry","name":"CHD4","description":"Chromodomain-helicase-DNA-binding protein 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45623","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-523590","identifier":"Q12873","identifierLink":"https://www.uniprot.org/uniprotkb/Q12873/entry","name":"CHD3","description":"Chromodomain-helicase-DNA-binding protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45623","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-620823","identifier":"Q09028","identifierLink":"https://www.uniprot.org/uniprotkb/Q09028/entry","name":"RBBP4","description":"Histone-binding protein RBBP4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714236","identifier":"Q13330","identifierLink":"https://www.uniprot.org/uniprotkb/Q13330/entry","name":"MTA1","description":"Metastasis-associated protein MTA1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10865","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-726224","identifier":"Q86YP4","identifierLink":"https://www.uniprot.org/uniprotkb/Q86YP4/entry","name":"GATAD2A","description":"Transcriptional repressor p66-alpha","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13455","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-923440","identifier":"Q8WXI9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WXI9/entry","name":"GATAD2B","description":"Transcriptional repressor p66-beta","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13455","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-923","complexName":"Nuclear cap-binding complex","organismName":"Mus musculus; 10090","description":"Binds co-transcriptionally to the 5-prime, m7GpppG-cap (m7G-cap) structures of all RNA polymerase II transcripts (pre-mRNAs and pre-miRNAs). Required for processes such as transcription elongation, pre-mRNA splicing through commitment and NELF complexes and spliceosome formation, classic mRNA 3-prime end processing, suppression of poly-A tail formation in histone 3-prime end pre-mRNA processing in complex with serrate (Srrt/Ars2, Q99MR6) and NELF complex, nuclear export of mRNAs and U snRNAs in complex with importin-alpha and either Alyref2 (Q9JJW6) and TREX complex (mRNAs) or Phax-Xpo1/Crm1-Ran.GTP complex (U snRNAs), degradation of nuclear mRNAs via nonsense-mediated decay (NMD), primary miRNA processing in complex with serrate (Srrt/Ars2), miRNA-mediated RNA interference and the pioneer round of translation. During the pioneer round of translation it interacts with Ctif (Q6PEE2) which facilitates the eventual release of CBC from the transcript and its replacement by the cytoplasmic cap-binding complex eIF4F. In the cytosol, importin-beta interacts with CBC-bound importin-alpha and promotes the dissociation of the RNA from CBC. Importin-complex-bound CBC gets reimported into the nucleus for reuse. Ncbp1 phosphorylation correlate with increased cap-dependent splicing activity. Histone pre-mRNA processing and the pioneer round of translation may be restricted to mammalian CBC.","predictedComplex":false,"interactors":[{"ac":"EBI-16747696","identifier":"Q3UYV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q3UYV9/entry","name":"Ncbp1","description":"Nuclear cap-binding protein subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8586642","identifier":"Q9CQ49","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQ49/entry","name":"Ncbp2","description":"Nuclear cap-binding protein subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-925","complexName":"NXF2-NXT1 mRNA nuclear export factor complex","organismName":"Homo sapiens; 9606","description":"Mediates the export of bulk mRNA through direct interactions with both the mRNA cargo and nuclear pore proteins that contain characteristic phenylalanine-glycine repeating sequence motifs (FG-nucleoporins or FG-nups).","predictedComplex":false,"interactors":[{"ac":"EBI-301889","identifier":"Q9UKK6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UKK6/entry","name":"NXT1","description":"NTF2-related export protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12612","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-444173","identifier":"Q9GZY0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9GZY0/entry","name":"NXF2B","description":"Nuclear RNA export factor 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10662","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-928","complexName":"Soluble guanylate cyclase complex, SGCalpha1-SGCbeta1 variant","organismName":"Homo sapiens; 9606","description":"Catalyses the the conversion of GTP to the secondary messenger cyclic GMP in response to nitric oxide.","predictedComplex":false,"interactors":[{"ac":"EBI-3910037","identifier":"Q02108","identifierLink":"https://www.uniprot.org/uniprotkb/Q02108/entry","name":"GUCY1A1","description":"Guanylate cyclase soluble subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45655","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-6911707","identifier":"Q02153","identifierLink":"https://www.uniprot.org/uniprotkb/Q02153/entry","name":"GUCY1B1","description":"Guanylate cyclase soluble subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45655","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-929","complexName":"Coagulation factor VIIIa complex, heavy chain variant 1","organismName":"Homo sapiens; 9606","description":"Part of the intrinsic blood coagulation pathway (contact activation pathway). When bound to factor IXa (CPX-4945) forms the intrinsic tenase complex that cleaves Arg-|-Ile bonds of factor X (P00742) by limited proteolysis to form active factor Xa (CPX-6215) in the presence of vitamin K, Ca2+ ions, phospholipids and factor VII (P08709). The coagulation pathway is terminated when fibrinogen is cleaved to fibrin which in turn polymerizes to produce a clot. \r\n\r\nIts zymogen form is activated by limited proteolysis by thrombin (FIIa, P00734) to form active factor VIIIa. Inhibited by Active Protein C (APC, P04070). \r\n\r\nMutations in factor VIII gene lead to hemophilia A.","predictedComplex":false,"interactors":[{"ac":"EBI-12684033","identifier":"P00451-PRO_0000002971","identifierLink":"https://www.uniprot.org/uniprotkb/P00451-PRO_0000002971/entry","name":"F8","description":"Factor VIIIa light chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-12684039","identifier":"P00451-PRO_0000002969","identifierLink":"https://www.uniprot.org/uniprotkb/P00451-PRO_0000002969/entry","name":"F8","description":"Factor VIIIa heavy chain, 92 kDa isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-930","complexName":"General transcription factor complex TFIID, TAF4B variant","organismName":"Homo sapiens; 9606","description":"General transcription factor complex primarily found in spermatocytes that acts as the primary core promoter recognition factor in the initiation of RNA polymerase II (Pol II)-dependent transcription. The TBP subunit of TFIID recognizes and binds to the TATA box (if present), while TAF1 and TAF2 interact with the Initiator element (Inr), and TAF1 and the TAF6-TAF9 module recognizes the downstream core promoter element (DPE). Other core promoter elements, such as the motif ten element (MTE), may also be involved. Binding of the general transcription factor complex TFIIA (CPX-519) enhances binding of TFIID to the core promoter and nucleates  pre-initiation complex (PIC) assembly. Following recruitment of TFIIA to TFIID, TFIIB, TFIIF (CPX-79), Pol II, TFIIE and TFIIH are successively assembled at the core promoter, allowing the PIC to initiate Pol II transcription. While TFIID is essential for transcription and its post-mitotic reinitiation, the loss of one or more subunits does not harm ongoing transcription during any given cell cycle. \r\n\r\nTFIID promoter binding appears to be regulated by histone modifications: TAF1 bromodomains (1361-1617 aa, IPR001487) bind the modified histone tails of acetylated H4K16, H4K5/K12 and H4K8/K16. TAF1 also appears to exhibit histone acetyltransferase activity towards histones H3 and H4. TAF3 and the PHD domains of other TFIID subunits  bind modified histone tails carrying trimethylated H3K4 in combination with acetylated H3K9 and H3K14. \r\n\r\nTAF1 phosphorylates TP53 (P046370) on Thr-55, leading to TP53 degradation and G1 cell cycle progression.","predictedComplex":false,"interactors":[{"ac":"EBI-1026992","identifier":"Q15543","identifierLink":"https://www.uniprot.org/uniprotkb/Q15543/entry","name":"TAF13","description":"Transcription initiation factor TFIID subunit 13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11380","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1027005","identifier":"Q15544","identifierLink":"https://www.uniprot.org/uniprotkb/Q15544/entry","name":"TAF11","description":"Transcription initiation factor TFIID subunit 11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13218","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1034238","identifier":"Q16514","identifierLink":"https://www.uniprot.org/uniprotkb/Q16514/entry","name":"TAF12","description":"Transcription initiation factor TFIID subunit 12","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1560063","identifier":"Q6P1X5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P1X5/entry","name":"TAF2","description":"Transcription initiation factor TFIID subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15137","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1560087","identifier":"Q5VWG9","identifierLink":"https://www.uniprot.org/uniprotkb/Q5VWG9/entry","name":"TAF3","description":"Transcription initiation factor TFIID subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46452","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1560111","identifier":"Q92750","identifierLink":"https://www.uniprot.org/uniprotkb/Q92750/entry","name":"TAF4B","description":"Transcription initiation factor TFIID subunit 4B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15138","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1560145","identifier":"Q15542","identifierLink":"https://www.uniprot.org/uniprotkb/Q15542/entry","name":"TAF5","description":"Transcription initiation factor TFIID subunit 5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19879","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1560194","identifier":"Q15545","identifierLink":"https://www.uniprot.org/uniprotkb/Q15545/entry","name":"TAF7","description":"Transcription initiation factor TFIID subunit 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12228","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1560206","identifier":"P49848","identifierLink":"https://www.uniprot.org/uniprotkb/P49848/entry","name":"TAF6","description":"Transcription initiation factor TFIID subunit 6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10221","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1560220","identifier":"Q7Z7C8","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z7C8/entry","name":"TAF8","description":"Transcription initiation factor TFIID subunit 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46469","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355371","identifier":"P20226","identifierLink":"https://www.uniprot.org/uniprotkb/P20226/entry","name":"TBP","description":"TATA-box-binding protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10126","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-491289","identifier":"P21675","identifierLink":"https://www.uniprot.org/uniprotkb/P21675/entry","name":"TAF1","description":"Transcription initiation factor TFIID subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13900","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-708376","identifier":"Q12962","identifierLink":"https://www.uniprot.org/uniprotkb/Q12962/entry","name":"TAF10","description":"Transcription initiation factor TFIID subunit 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21242","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712521","identifier":"Q16594","identifierLink":"https://www.uniprot.org/uniprotkb/Q16594/entry","name":"TAF9","description":"Transcription initiation factor TFIID subunit 9","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-932","complexName":"General transcription factor complex TFIID","organismName":"Mus musculus; 10090","description":"General transcription factor complex that acts as the primary core promoter recognition factor in the initiation of RNA polymerase II (Pol II)-dependent transcription. The TBP subunit of TFIID recognizes and binds to the TATA box (if present), while Taf1 and Taf2 interact with the Initiator element (Inr), and Taf1 and the Taf6-Taf9 module recognizes the downstream core promoter element (DPE). Other core promoter elements, such as the motif ten element (MTE), may also be involved. Binding of the general transcription factor complex TFIIA (CPX-743) enhances binding of TFIID to the core promoter and nucleates  pre-initiation complex (PIC) assembly. Following recruitment of TFIIA to TFIID, TFIIB, TFIIF (CPX-83), Pol II, TFIIE and TFIIH are successively assembled at the core promoter, allowing the PIC to initiate Pol II transcription. While TFIID is essential for transcription and its post-mitotic reinitiation, the loss of one or more subunits does not harm ongoing transcription during any given cell cycle. \r\n\r\nTFIID promoter binding appears to be regulated by histone modifications: Taf1 bromodomains (1382-1638 aa, IPR001487) bind the modified histone tails of acetylated H4K16, H4K5/K12 and H4K8/K16. Taf1 also appears to exhibit histone acetyltransferase activity towards histones H3 and H4. Taf3 and the PHD domains of other TFIID subunits  bind modified histone tails carrying trimethylated H3K4 in combination with acetylated H3K9 and H3K14. \r\n\r\nTaf1 phosphorylates TP53 (P02340), leading to TP53 degradation and G1 cell cycle progression. \r\n\r\nSpermatocytes contain variants of TAF-containing complexes and may therefore lack fully functional TFIID.","predictedComplex":false,"interactors":[{"ac":"EBI-12667225","identifier":"Q8C176","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C176/entry","name":"Taf2","description":"Transcription initiation factor TFIID subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15137","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12667248","identifier":"Q8C092","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C092/entry","name":"Taf5","description":"Transcription initiation factor TFIID subunit 5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR19879","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12672261","identifier":"Q9EQH4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9EQH4/entry","name":"Taf8","description":"Transcription initiation factor TFIID subunit 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46469","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12684655","identifier":"Q80UV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q80UV9/entry","name":"Taf1","description":"Transcription initiation factor TFIID subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13900","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1561080","identifier":"Q5HZG4","identifierLink":"https://www.uniprot.org/uniprotkb/Q5HZG4/entry","name":"Taf3","description":"Transcription initiation factor TFIID subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46452","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2943311","identifier":"Q8VI33","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VI33/entry","name":"Taf9","description":"Transcription initiation factor TFIID subunit 9","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR48068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-309424","identifier":"P61216","identifierLink":"https://www.uniprot.org/uniprotkb/P61216/entry","name":"Taf13","description":"Transcription initiation factor TFIID subunit 13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11380","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-309427","identifier":"Q99JX1","identifierLink":"https://www.uniprot.org/uniprotkb/Q99JX1/entry","name":"Taf11","description":"Transcription initiation factor TFIID subunit 11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13218","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4399956","identifier":"P29037","identifierLink":"https://www.uniprot.org/uniprotkb/P29037/entry","name":"Tbp","description":"TATA-box-binding protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10126","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5744190","identifier":"Q62311","identifierLink":"https://www.uniprot.org/uniprotkb/Q62311/entry","name":"Taf6","description":"Transcription initiation factor TFIID subunit 6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10221","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5744209","identifier":"Q8K0H5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K0H5/entry","name":"Taf10","description":"Transcription initiation factor TFIID subunit 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21242","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6260765","identifier":"Q9R1C0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R1C0/entry","name":"Taf7","description":"Transcription initiation factor TFIID subunit 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12228","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7990784","identifier":"Q8VE65","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VE65/entry","name":"Taf12","description":"Transcription initiation factor TFIID subunit 12","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8663048","identifier":"E9QAP7","identifierLink":"https://www.uniprot.org/uniprotkb/E9QAP7/entry","name":"Taf4","description":null,"stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15138","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-936","complexName":"HOPS tethering complex","organismName":"Drosophila melanogaster; 7227","description":"Multisubunit tethering complex involved in endo-lysosomal vesicle trafficking and lysosome biogenesis by cross-linking two membranes, and facilitating the formation of a SNARE complex during fusion. Required for the delivery of vacuolar proteins and homotypic fusion of vacuoles and controls the clearance of late endosomes and autophagosomes during heterophagy and autophagy through promoting fusion of these vesicles with the vacuole. Appears to instigate autophagosome-lysosome fusion by binding autophagosome associated Syx17 (Q9VZC9) and promoting assembly of a trans-SNARE complex Plays a role in crinophagy and eye pigment granule biogenesis.","predictedComplex":false,"interactors":[{"ac":"EBI-103836","identifier":"Q7PL76","identifierLink":"https://www.uniprot.org/uniprotkb/Q7PL76/entry","name":"lt","description":"Vacuolar protein sorting-associated protein 41 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12616","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-135345","identifier":"Q9VEA2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VEA2/entry","name":"Vps39","description":"Vacuolar protein sorting-associated protein 39 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-187940","identifier":"Q9VHG1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VHG1/entry","name":"Vps16A","description":"Vacuolar protein sorting-associated protein 16 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12811","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3423413","identifier":"Q8SX81","identifierLink":"https://www.uniprot.org/uniprotkb/Q8SX81/entry","name":"Vps11","description":"Vacuolar protein sorting-associated protein 11 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23323","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-421908","identifier":"Q24314","identifierLink":"https://www.uniprot.org/uniprotkb/Q24314/entry","name":"dor","description":"Vacuolar protein sorting-associated protein 18 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23323","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9924110","identifier":"Q9Y1I2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y1I2/entry","name":"car","description":"Vacuolar protein sorting-associated protein 33A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11679","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-937","complexName":"CSL-NOTCH1-MAML transcriptional activation complex","organismName":"Homo sapiens; 9606","description":"Transcriptional activation complex. Assembles in the nucleus following engagement of a Notch receptor ligand which results in the release of the intracellular portion of Notch (ICN, NICD or Notch-Intra) from the membrane allowing this to translocate to the nucleus. The complex binds to the promoter of genes containing a conserved pair of CSL binding sites in a psuedo-symmetrical head-to-head orientation that are separated by 15-19 base pairs - a Su(H)-paired site or sequence paired site (SPS).","predictedComplex":false,"interactors":[{"ac":"EBI-632552","identifier":"Q06330","identifierLink":"https://www.uniprot.org/uniprotkb/Q06330/entry","name":"RBPJ","description":"Recombining binding protein suppressor of hairless","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10665","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-636374","identifier":"P46531","identifierLink":"https://www.uniprot.org/uniprotkb/P46531/entry","name":"NOTCH1","description":"Neurogenic locus notch homolog protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45836","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-908250","identifier":"Q92585","identifierLink":"https://www.uniprot.org/uniprotkb/Q92585/entry","name":"MAML1","description":"Mastermind-like protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15692","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-941","complexName":"mRNA cleavage factor I(m) complex, CPSF6 variant","organismName":"Homo sapiens; 9606","description":"Required for the post-transcriptional cleavage of 3' mRNA as part of its maturation process. Recognises and binds auxiliary UGUA sequence elements localized near the cleavage and polyadenylation signals in the 3'-untranslated region of pre-mRNAs and appears to determine which is the terminal exon. Recruits additional complexes which promote RNA looping.","predictedComplex":false,"interactors":[{"ac":"EBI-355720","identifier":"O43809","identifierLink":"https://www.uniprot.org/uniprotkb/O43809/entry","name":"NUDT21","description":"Cleavage and polyadenylation specificity factor subunit 5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13047","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358410","identifier":"Q16630","identifierLink":"https://www.uniprot.org/uniprotkb/Q16630/entry","name":"CPSF6","description":"Cleavage and polyadenylation specificity factor subunit 6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23204","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-943","complexName":"Insulin complex","organismName":"Homo sapiens; 9606","description":"Insulin is a protein hormone that regulates the metabolism of carbohydrates, fats and protein by promoting the absorption of glucose from the blood into liver, fat and skeletal muscle cells","predictedComplex":false,"interactors":[{"ac":"EBI-12685818","identifier":"P01308-PRO_0000015821","identifierLink":"https://www.uniprot.org/uniprotkb/P01308-PRO_0000015821/entry","name":"INS","description":"Insulin A chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-12685833","identifier":"P01308-PRO_0000015819","identifierLink":"https://www.uniprot.org/uniprotkb/P01308-PRO_0000015819/entry","name":"INS","description":"Insulin B chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-944","complexName":"DNA (cytosine-5)-methyltransferase 3A complex","organismName":"Homo sapiens; 9606","description":"DNA methyltransferase which methylates DNA by a cooperative mechanism via multimerization on DNA forming nucleoprotein filaments.  Required for genome-wide de novo methylation, a  major epigenetic mechanism that controls gene expression, genomic stability, and cell differentiation.  Predominantly occurs at the C-5 position of cytosine within the symmetric CpG dinucleotide, affecting approximately 70-80% of the CpG sites throughout the genome. Also responsible fornon-CpG methylation (mainly CpA ) in oocytes, embryonic stem cells, and neural cells DNA  the DNMT3A-3L complex is critical for establishing methylation at major satellite repeats and allele-specific imprinting during gametogenesis. Plays a role in paternal and maternal imprinting and is required for methylation of most imprinted loci in germ cells.","predictedComplex":false,"interactors":[{"ac":"EBI-740967","identifier":"Q9UJW3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UJW3/entry","name":"DNMT3L","description":"DNA (cytosine-5)-methyltransferase 3-like","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-923653","identifier":"Q9Y6K1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6K1/entry","name":"DNMT3A","description":"DNA (cytosine-5)-methyltransferase 3A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-945","complexName":"TLR4-TLR6 toll-like receptor complex","organismName":"Homo sapiens; 9606","description":"Type I membrane receptor that plays a crucial role in innate immunity by recognizing conserved patterns in diverse microbial molecules including lipoproteins, lipopeptides, lipopolysaccharide, flagellin, and nucleic acids. Initiates   innate immune activation of macrophages and microglia.through binding of atherogenic lipids susch as oxidised LDL (CHEBI:60151) or beta-amyloid 42 complex (CPX-1070) to a shared receptor, CD36 (P16671), that provides the proximal signalling event required for TLR4-TLR6 activation","predictedComplex":false,"interactors":[{"ac":"EBI-13940779","identifier":"Q9Y2C9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2C9/entry","name":"TLR6","description":"Toll-like receptor 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24365","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-528701","identifier":"O00206","identifierLink":"https://www.uniprot.org/uniprotkb/O00206/entry","name":"TLR4","description":"Toll-like receptor 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24365","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-948","complexName":"S-adenosylmethionine synthase, MAT2A-MAT2B variant","organismName":"Homo sapiens; 9606","description":"Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises of two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate. The complex is present  in nearly all tissues and is thought to be essential in providing the necessary SAM flux for methylation of DNA and various proteins including histones. The  Vmax of the MAT2A-2A complex is three- to four fold higher than the MAT2A heterotetramer (CPX-3168).","predictedComplex":false,"interactors":[{"ac":"EBI-10317491","identifier":"Q9NZL9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZL9/entry","name":"MAT2B","description":"Methionine adenosyltransferase 2 subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10491","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1050743","identifier":"P31153","identifierLink":"https://www.uniprot.org/uniprotkb/P31153/entry","name":"MAT2A","description":"S-adenosylmethionine synthase isoform type-2","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-949","complexName":"Mitochondrial 3-oxoacyl-[acyl-carrier-protein] reductase","organismName":"Homo sapiens; 9606","description":"Catalyses the second step of the mitochondrial fatty acid synthesis (mtFAS) pathway, reducing 3-oxoacyl-[ACP] to (3R)-hydroxyacyl-[ACP] in a NADPH-dependent manner with no chain length preference, thereby participating in mitochondrial fatty acid biosynthesis. The.mtFAS pathway is essential for mammalian embryonic survival and provides the precursor of mitochondrially synthesized aloha-lipoic acid, a key cofactor for oxidative decarboxylation of alpha-keto acids and glycine within eukaryotic cells. Deficiency of mtFAS leads to respiratory chain defects and mitochondrial dysfunction.","predictedComplex":false,"interactors":[{"ac":"EBI-10897344","identifier":"Q8N4T8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N4T8/entry","name":"CBR4","description":"3-oxoacyl-[acyl-carrier-protein] reductase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR42760","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32717409","identifier":"CHEBI:57540","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57540","name":"nad(1-)","description":"NAD(1-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-44435158","identifier":"CHEBI:58349","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58349","name":"nadp3+","description":"NADP3+","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-5461137","identifier":"Q92506","identifierLink":"https://www.uniprot.org/uniprotkb/Q92506/entry","name":"HSD17B8","description":"(3R)-3-hydroxyacyl-CoA dehydrogenase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR42760","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-951","complexName":"mRNA cleavage factor I(m) complex, CPSF7 variant","organismName":"Homo sapiens; 9606","description":"Required for the post-transcriptional cleavage of 3' mRNA as part of its maturation process. Recognises and binds auxiliary UGUA sequence elements localized near the cleavage and polyadenylation signals in the 3'-untranslated region of pre-mRNAs and appears to determine which is the terminal exon. Recruits additional complexes which promote RNA looping.","predictedComplex":false,"interactors":[{"ac":"EBI-355720","identifier":"O43809","identifierLink":"https://www.uniprot.org/uniprotkb/O43809/entry","name":"NUDT21","description":"Cleavage and polyadenylation specificity factor subunit 5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13047","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-746909","identifier":"Q8N684","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N684/entry","name":"CPSF7","description":"Cleavage and polyadenylation specificity factor subunit 7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23204","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-952","complexName":"Caspase-1 complex","organismName":"Homo sapiens; 9606","description":"A pro-inflammatory thiol protease complex that is activated in response to pathogen infections and toxins. Primarily acts in monocytes and macrophages. \r\n\r\nActivation by autocatalytic cleavage is an ATP-dependent reaction and occurs within an activation platform, the Inflammasome (CPX-4141, CPX-4082, CPX-4144, CPX-4142 and CPX-4143). \r\n\r\nOnce activated, it has a strict requirement for an Asp residue at position P1 and preferred cleavage sequence of Asp-Glu-Val-Asp-|-. It cleaves interleukins 1beta (IL1B, P01584) and IL18 (Q14116) between an Asp and an Ala, releasing the mature cytokines which are involved in a variety of inflammatory processes. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Related to, but independent of, IL1B activation it is also involved in pyroptosis of macrophages, a special case of cell death, associated with infection by intracellular pathogens where it cleaves GSDMD (P57764). However, as a side effect of pyroptosis active IL1B is often released form the dead cells and therefore some link exists between both activities. While primarily a pro-inflammatory caspase it can also promote apoptosis in non-immune cells, especially in response to brain, kidney and renal cell injury.\r\n\r\nCaspase-1-deficient mice are protected from several acute and chronic inflammatory diseases, including sepsis and colitis.","predictedComplex":false,"interactors":[{"ac":"EBI-12685775","identifier":"P29466-PRO_0000004524","identifierLink":"https://www.uniprot.org/uniprotkb/P29466-PRO_0000004524/entry","name":"CASP1","description":"Caspase-1 subunit p10","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-1749839","identifier":"P29466-PRO_0000004522","identifierLink":"https://www.uniprot.org/uniprotkb/P29466-PRO_0000004522/entry","name":"CASP1","description":"Caspase-1 subunit p20","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-953","complexName":"MBD2/NuRD nucleosome remodeling and deacetylase complex","organismName":"Mus musculus; 10090","description":"Corepressor complex that couples histone deacetylase and ATP-dependent chromatin remodeling activities. It regulates the higher-order structure of chromatin, making chromatin more compact by removing acetyl groups from nucleosomes, and has important roles in the regulation of gene expression and DNA damage repair.\r\nThe core of the complex is composed of six groups of proteins, each one with several paralogues (Hdac1/2, Mta1/2/3, Rbbp4/7, Gatad2a/b, Mbd2, and Chd3/4). Combinatorial assembly of these isoforms contributes to the targeting and function of the complex.\r\nIt is currently not known whether Gatad2a/Gatad2b, Rbbp4/Rbbp7, and Mta1/Mta2/Mta3 form heterodimers/trimers or mutually exclusive homodimers/trimers. The  Chd3/4 ATPase, utilizes energy derived from hydrolysis of ATP for DNA sliding and repositioning of nucleosomes. The second catalytic subunit, Hdac1/2 (histone deacetylase), deacetylates acetylated lysine residues of histone and non-histone proteins. This dual enzymatic activity is proposed to be important for the efficient formation of heterochromatin with densely packed hypoacetylated nucleosomes and the rapid termination of gene transcription.\r\nIn addition to the well-described core subunits, a large number of proteins have been reported to interact with the NuRD complex, like  Doc1 (O35207), Kpna2 (P52293), Zmynd8 (A2A484), Znf512b/532/592/687(Q6PHP4, Q6NXK2 , Q8BHZ4, Q9D2D7),  Sall4 (Q8BX22), Prmt5 (Q8CIG8), Mep50 (Q99J09). They also contribute to dictate the different biological functions of the NuRD complex.","predictedComplex":false,"interactors":[{"ac":"EBI-1216353","identifier":"Q8K4B0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K4B0/entry","name":"Mta1","description":"Metastasis-associated protein MTA1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10865","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301912","identifier":"O09106","identifierLink":"https://www.uniprot.org/uniprotkb/O09106/entry","name":"Hdac1","description":"Histone deacetylase 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302251","identifier":"P70288","identifierLink":"https://www.uniprot.org/uniprotkb/P70288/entry","name":"Hdac2","description":"Histone deacetylase 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302291","identifier":"Q60972","identifierLink":"https://www.uniprot.org/uniprotkb/Q60972/entry","name":"Rbbp4","description":"Histone-binding protein RBBP4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302297","identifier":"Q60973","identifierLink":"https://www.uniprot.org/uniprotkb/Q60973/entry","name":"Rbbp7","description":"Histone-binding protein RBBP7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3043849","identifier":"B1AR17","identifierLink":"https://www.uniprot.org/uniprotkb/B1AR17/entry","name":"Chd3","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45623","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3043852","identifier":"Q6PDQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDQ2/entry","name":"Chd4","description":"Chromodomain-helicase-DNA-binding protein 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45623","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3043877","identifier":"Q8CHY6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CHY6/entry","name":"Gatad2a","description":"Transcriptional repressor p66 alpha","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13455","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3043880","identifier":"Q8VHR5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VHR5/entry","name":"Gatad2b","description":"Transcriptional repressor p66-beta","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13455","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3043925","identifier":"Q924K8","identifierLink":"https://www.uniprot.org/uniprotkb/Q924K8/entry","name":"Mta3","description":"Metastasis-associated protein MTA3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10865","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5716946","identifier":"Q9Z2E1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z2E1/entry","name":"Mbd2","description":"Methyl-CpG-binding domain protein 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12396","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-904134","identifier":"Q9R190","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R190/entry","name":"Mta2","description":"Metastasis-associated protein MTA2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10865","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-954","complexName":"MBD3/NuRD nucleosome remodeling and deacetylase complex","organismName":"Mus musculus; 10090","description":"Corepressor complex that couples histone deacetylase and ATP-dependent chromatin remodeling activities. It regulates the higher-order structure of chromatin, making chromatin more compact by removing acetyl groups from nucleosomes, and has important roles in the regulation of gene expression, DNA damage repair and cell differentiation.\r\nThe core of the complex is composed of six groups of proteins, each one with several  paralogues (Hdac1/2, Mta1/2/3, Rbbp4/7, Gatad2a/b, Mbd3, and Chd3/4). Combinatorial assembly of these isoforms contributes to the targeting and function of the complex.\r\nIt is currently not known whether Gatad2a/Gatad2b, Rbbp4/Rbbp7, and Mta1/Mta2/Mta3 form heterodimers/trimers or mutually exclusive homodimers/trimers. The  Chd3/4 ATPase, utilizes energy derived from hydrolysis of ATP for DNA sliding and repositioning of nucleosomes. The second catalytic subunit, Hdac1/2 (histone deacetylase), deacetylates acetylated lysine residues of histone and non-histone proteins. This dual enzymatic activity is proposed to be important for the efficient formation of heterochromatin with densely packed hypoacetylated nucleosomes and the rapid termination of gene transcription.\r\nIn addition to the well-described core subunits, a large number of proteins have been reported to interact with the NuRD complex, like  Doc1 (O35207), Kpna2 (P52293), Zmynd8 (A2A484), Znf512b/532/592/687(Q6PHP4, Q6NXK2 , Q8BHZ4, Q9D2D7),  Sall4 (Q8BX22), Prmt5 (Q8CIG8), Mep50 (Q99J09). They also contribute to dictate the different biological functions of the NuRD complex.","predictedComplex":false,"interactors":[{"ac":"EBI-1216353","identifier":"Q8K4B0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K4B0/entry","name":"Mta1","description":"Metastasis-associated protein MTA1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10865","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1994548","identifier":"Q9Z2D8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z2D8/entry","name":"Mbd3","description":"Methyl-CpG-binding domain protein 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12396","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-301912","identifier":"O09106","identifierLink":"https://www.uniprot.org/uniprotkb/O09106/entry","name":"Hdac1","description":"Histone deacetylase 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302251","identifier":"P70288","identifierLink":"https://www.uniprot.org/uniprotkb/P70288/entry","name":"Hdac2","description":"Histone deacetylase 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302291","identifier":"Q60972","identifierLink":"https://www.uniprot.org/uniprotkb/Q60972/entry","name":"Rbbp4","description":"Histone-binding protein RBBP4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302297","identifier":"Q60973","identifierLink":"https://www.uniprot.org/uniprotkb/Q60973/entry","name":"Rbbp7","description":"Histone-binding protein RBBP7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3043849","identifier":"B1AR17","identifierLink":"https://www.uniprot.org/uniprotkb/B1AR17/entry","name":"Chd3","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45623","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3043852","identifier":"Q6PDQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDQ2/entry","name":"Chd4","description":"Chromodomain-helicase-DNA-binding protein 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45623","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3043877","identifier":"Q8CHY6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CHY6/entry","name":"Gatad2a","description":"Transcriptional repressor p66 alpha","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13455","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3043880","identifier":"Q8VHR5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VHR5/entry","name":"Gatad2b","description":"Transcriptional repressor p66-beta","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13455","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3043925","identifier":"Q924K8","identifierLink":"https://www.uniprot.org/uniprotkb/Q924K8/entry","name":"Mta3","description":"Metastasis-associated protein MTA3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10865","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-904134","identifier":"Q9R190","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R190/entry","name":"Mta2","description":"Metastasis-associated protein MTA2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10865","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-955","complexName":"BRCC E3 ubiquitin ligase complex","organismName":"Homo sapiens; 9606","description":"A Ubc5-dependent E3 ubiquitin ligase complex involved in DNA repair, potentially by regulating factors involved in the process. It has a defined substrate specificity, with a strong preference for the nucleosome core histones H2A, H2B, H3 and H4. It co-localizes with, and efficiently ubiquitylates, the histone variant H2AX at sites of DNA damage.","predictedComplex":false,"interactors":[{"ac":"EBI-297202","identifier":"Q06609","identifierLink":"https://www.uniprot.org/uniprotkb/Q06609/entry","name":"RAD51","description":"DNA repair protein RAD51 homolog 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-349905","identifier":"P38398","identifierLink":"https://www.uniprot.org/uniprotkb/P38398/entry","name":"BRCA1","description":"Breast cancer type 1 susceptibility protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13763","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-473181","identifier":"Q99728","identifierLink":"https://www.uniprot.org/uniprotkb/Q99728/entry","name":"BARD1","description":"BRCA1-associated RING domain protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24171","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-750352","identifier":"P46736","identifierLink":"https://www.uniprot.org/uniprotkb/P46736/entry","name":"BRCC3","description":"Lys-63-specific deubiquitinase BRCC36","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10410","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-79792","identifier":"P51587","identifierLink":"https://www.uniprot.org/uniprotkb/P51587/entry","name":"BRCA2","description":"Breast cancer type 2 susceptibility protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11289","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-949389","identifier":"Q9NXR7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NXR7/entry","name":"BABAM2","description":"BRISC and BRCA1-A complex member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15189","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-957","complexName":"Nuclear cap-binding complex","organismName":"Caenorhabditis elegans; 6239","description":"Binds co-transcriptionally to the 5-prime, m7GpppG-cap (m7G-cap) structures of all RNA polymerase II transcripts (mRNAs and pre-miRNAs). Required for various processes such as pre-mRNA splicing through commitment complex and spliceosome formation, export of mRNA out of the nucleus, degradation of nuclear mRNAs, primary miRNA processing and miRNA-mediated RNA interference. In the cytosol, importin-beta interacts with CBC-bound importin-alpha and promotes the dissociation of the RNA from CBC. Importin-complex-bound CBC gets reimported into the nucleus for reuse.","predictedComplex":false,"interactors":[{"ac":"EBI-12687361","identifier":"O01763","identifierLink":"https://www.uniprot.org/uniprotkb/O01763/entry","name":"ncbp-1","description":"Nuclear cap-binding protein subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12687395","identifier":"Q93594","identifierLink":"https://www.uniprot.org/uniprotkb/Q93594/entry","name":"ncbp-2","description":"Nuclear cap-binding protein subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR18847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-958","complexName":"SCF-rpm-1 ubiquitin ligase complex","organismName":"Caenorhabditis elegans; 6239","description":"SCF-rpm-1 is a member of the SCF (Skp1-Cullin-F-box) E3 ubiquitin ligase family, in which the F-box protein, rpm-1, forms the substrate recognition subunit. The complex mediates the ubiquitination and subsequent proteasomal degradation of target proteins. \r\n\r\nThe complex is formed at presynaptic periactive zones along dorsal and ventral nerve cords and targets proteins such as scd-2, an ALK tyrosine kinase receptor, to stabilize synapse formation. Required for the restriction and/or maturation of synapses in GABAergic neuromuscular junction (NMJ) presynaptic neurons.","predictedComplex":false,"interactors":[{"ac":"EBI-12687470","identifier":"Q17389","identifierLink":"https://www.uniprot.org/uniprotkb/Q17389/entry","name":"cul-1","description":"Cullin-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2003744","identifier":"Q18223","identifierLink":"https://www.uniprot.org/uniprotkb/Q18223/entry","name":"fsn-1","description":"F-box/SPRY domain-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12245","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-323117","identifier":"G5ECU1","identifierLink":"https://www.uniprot.org/uniprotkb/G5ECU1/entry","name":"skr-1","description":"Skp1-related protein","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6920110","identifier":"Q17551","identifierLink":"https://www.uniprot.org/uniprotkb/Q17551/entry","name":"rpm-1","description":"E3 ubiquitin-protein ligase rpm-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45943","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-959","complexName":"General transcription factor complex TFIID, Taf4b variant","organismName":"Mus musculus; 10090","description":"General transcription factor complex primarily found in spermatocytes that acts as the primary core promoter recognition factor in the initiation of RNA polymerase II (Pol II)-dependent transcription. The TBP subunit of TFIID recognizes and binds to the TATA box (if present), while Taf1 and Taf2 interact with the Initiator element (Inr), and Taf1 and the Taf6-Taf9 module recognizes the downstream core promoter element (DPE). Other core promoter elements, such as the motif ten element (MTE), may also be involved. Binding of the general transcription factor complex TFIIA (CPX-743) enhances binding of TFIID to the core promoter and nucleates  pre-initiation complex (PIC) assembly. Following recruitment of TFIIA to TFIID, TFIIB, TFIIF (CPX-83), Pol II, TFIIE and TFIIH are successively assembled at the core promoter, allowing the PIC to initiate Pol II transcription. While TFIID is essential for transcription and its post-mitotic reinitiation, the loss of one or more subunits does not harm ongoing transcription during any given cell cycle. \r\n\r\nTFIID promoter binding appears to be regulated by histone modifications: Taf1 bromodomains (1382-1638 aa, IPR001487) bind the modified histone tails of acetylated H4K16, H4K5/K12 and H4K8/K16. Taf1 also appears to exhibit histone acetyltransferase activity towards histones H3 and H4. Taf3 and the PHD domains of other TFIID subunits  bind modified histone tails carrying trimethylated H3K4 in combination with acetylated H3K9 and H3K14. \r\n\r\nTaf1 phosphorylates TP53 (P02340), leading to TP53 degradation and G1 cell cycle progression.","predictedComplex":false,"interactors":[{"ac":"EBI-12667225","identifier":"Q8C176","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C176/entry","name":"Taf2","description":"Transcription initiation factor TFIID subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15137","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12667248","identifier":"Q8C092","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C092/entry","name":"Taf5","description":"Transcription initiation factor TFIID subunit 5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR19879","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12672261","identifier":"Q9EQH4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9EQH4/entry","name":"Taf8","description":"Transcription initiation factor TFIID subunit 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46469","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12684655","identifier":"Q80UV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q80UV9/entry","name":"Taf1","description":"Transcription initiation factor TFIID subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13900","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12688342","identifier":"G5E8Z2","identifierLink":"https://www.uniprot.org/uniprotkb/G5E8Z2/entry","name":"Taf4b","description":"Transcription initiation factor TFIID subunit 4B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15138","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1561080","identifier":"Q5HZG4","identifierLink":"https://www.uniprot.org/uniprotkb/Q5HZG4/entry","name":"Taf3","description":"Transcription initiation factor TFIID subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46452","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2943311","identifier":"Q8VI33","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VI33/entry","name":"Taf9","description":"Transcription initiation factor TFIID subunit 9","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR48068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-309424","identifier":"P61216","identifierLink":"https://www.uniprot.org/uniprotkb/P61216/entry","name":"Taf13","description":"Transcription initiation factor TFIID subunit 13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11380","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-309427","identifier":"Q99JX1","identifierLink":"https://www.uniprot.org/uniprotkb/Q99JX1/entry","name":"Taf11","description":"Transcription initiation factor TFIID subunit 11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13218","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4399956","identifier":"P29037","identifierLink":"https://www.uniprot.org/uniprotkb/P29037/entry","name":"Tbp","description":"TATA-box-binding protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10126","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5744190","identifier":"Q62311","identifierLink":"https://www.uniprot.org/uniprotkb/Q62311/entry","name":"Taf6","description":"Transcription initiation factor TFIID subunit 6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10221","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5744209","identifier":"Q8K0H5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K0H5/entry","name":"Taf10","description":"Transcription initiation factor TFIID subunit 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21242","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6260765","identifier":"Q9R1C0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R1C0/entry","name":"Taf7","description":"Transcription initiation factor TFIID subunit 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12228","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7990784","identifier":"Q8VE65","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VE65/entry","name":"Taf12","description":"Transcription initiation factor TFIID subunit 12","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-960","complexName":"Collagen type II trimer","organismName":"Gallus gallus; 9031","description":"The major component of cartilage.","predictedComplex":false,"interactors":[{"ac":"EBI-1636115","identifier":"P02460","identifierLink":"https://www.uniprot.org/uniprotkb/P02460/entry","name":"COL2A1","description":"Collagen alpha-1(II) chain","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Gallus gallus; 9031","xrefs":[]}]},{"complexAC":"CPX-965","complexName":"E2F1-DP1 transcription factor complex","organismName":"Caenorhabditis elegans; 6239","description":"Transcription factor complex which binds DNA through the E2 recognition site, 5'-TTTC[CG]CGC-3', typically associated with the promoters of genes active in S phase. Activates genes that stimulate DNA synthesis and cell cycle advancement. The complex positively and negatively regulates the transcription of genes required for centriole duplication and assembly.","predictedComplex":false,"interactors":[{"ac":"EBI-324825","identifier":"Q22703","identifierLink":"https://www.uniprot.org/uniprotkb/Q22703/entry","name":"dpl-1","description":"Transcription factor dpl-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12548","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-331564","identifier":"G5EF11","identifierLink":"https://www.uniprot.org/uniprotkb/G5EF11/entry","name":"efl-1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12081","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-966","complexName":"PAF1 complex","organismName":"Caenorhabditis elegans; 6239","description":"A multifunctional complex involved in  many aspects of RNA polymerase II (Pol II) transcriptional regulation, including transcriptional elongation, 3'-terminal end processing, and histone modification.\r\n\r\nRole in 3'-end formation of mRNAs, required for the recruitment of cleavage and polyadenylation factors to Pol II. Also involved in gene regulation of embryonic epidermal morphogenesis.","predictedComplex":false,"interactors":[{"ac":"EBI-12734514","identifier":"Q03560","identifierLink":"https://www.uniprot.org/uniprotkb/Q03560/entry","name":"ctr-9","description":"RNA polymerase-associated protein CTR9","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR14027","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12734541","identifier":"Q17431","identifierLink":"https://www.uniprot.org/uniprotkb/Q17431/entry","name":"leo-1","description":"RNA polymerase-associated protein LEO1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR23146","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-314207","identifier":"G5EBY0","identifierLink":"https://www.uniprot.org/uniprotkb/G5EBY0/entry","name":"rtfo-1","description":"RNA polymerase-associated protein RTF1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-321153","identifier":"Q9N5U5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9N5U5/entry","name":"cdc-73","description":"Cell division cycle protein 73","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12466","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-323546","identifier":"P90783","identifierLink":"https://www.uniprot.org/uniprotkb/P90783/entry","name":"pafo-1","description":"RNA polymerase II-associated factor 1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR23188","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-967","complexName":"Nuclear mitotic cohesin complex","organismName":"Caenorhabditis elegans; 6239","description":"Required for sister chromatid cohesion during cell division, which enables cells to attach sister kinetochores to microtubules with opposing polarity (bi-orientation) and subsequently resists the tendency of these microtubules to pull chromatids toward opposite spindle poles. Before the commencement of replication, the cohesin complex is loaded onto DNA. The arms of the him-1 and smc-3 molecules embrace the DNA, thereby forming a ring. The head domains of him-1 and smc-3 are locked together by scc-1. Cohesion might be generated as the replication fork passes through the ring, entrapping both sister chromatids inside. At the metaphase to anaphase transition, scc-1 is cleaved by separase, thereby opening the lock of the him-1 and smc-3 head domains. The ring opens and sister chromatids can be pulled to opposite spindle poles.","predictedComplex":false,"interactors":[{"ac":"EBI-12734598","identifier":"O01789","identifierLink":"https://www.uniprot.org/uniprotkb/O01789/entry","name":"him-1","description":"Structural maintenance of chromosomes protein 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR18937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12734629","identifier":"B2FDA8","identifierLink":"https://www.uniprot.org/uniprotkb/B2FDA8/entry","name":"smc-3","description":"Structural maintenance of chromosomes protein 3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR43977","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-319347","identifier":"Q19325","identifierLink":"https://www.uniprot.org/uniprotkb/Q19325/entry","name":"scc-1","description":"Sister chromatid cohesion protein 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12585","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-319920","identifier":"Q19555","identifierLink":"https://www.uniprot.org/uniprotkb/Q19555/entry","name":"scc-3","description":"Cohesin subunit scc-3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11199","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-968","complexName":"Oligosaccharyltransferase complex","organismName":"Caenorhabditis elegans; 6239","description":"Transfers the dolicholphosphate-linked core oligosaccharide to selected Asn-X-Ser/Thr sequences of the nascent polypeptide chain, a key step in N-glycosylation of secretory and membrane-bound proteins in the lumen of the endoplasmic reticulum.","predictedComplex":false,"interactors":[{"ac":"EBI-12734809","identifier":"P45971","identifierLink":"https://www.uniprot.org/uniprotkb/P45971/entry","name":"ostb-1","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10830","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12734822","identifier":"Q9GZH4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9GZH4/entry","name":"ribo-1","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR21049","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12734834","identifier":"P91390","identifierLink":"https://www.uniprot.org/uniprotkb/P91390/entry","name":"ostd-1","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-322688","identifier":"P46975","identifierLink":"https://www.uniprot.org/uniprotkb/P46975/entry","name":"stt-3","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt-3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13872","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-323348","identifier":"P52872","identifierLink":"https://www.uniprot.org/uniprotkb/P52872/entry","name":"dad-1","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit dad-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10705","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-328011","identifier":"P34669","identifierLink":"https://www.uniprot.org/uniprotkb/P34669/entry","name":"ost3","description":"Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12692","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-969","complexName":"Caspase-2 complex","organismName":"Homo sapiens; 9606","description":"Thiol-dependent aspartate-specific protease complex possessing features of both initiator and executioner caspases and required in stress-induced apoptosis. Genotoxic stress, mitotic catastrophe, heat shock, ER stress or bacterial toxins can stimulate Caspase-2 activation. It is activated by autocatalytic cleavage in the Caspase-2-PIDDosome (CPX-3905). Once activated, it is released from the PIDDosome and induces BID (P55957) cleavage, BAX (Q07812) translocation to mitochondria, subsequent Cytochrome c (P99999) release and consequent activation of the apoptotic process. Specifically cleaves substrates with an aspartic acid residue at position P1 and has a preferred cleavage sequence of Val-Asp-Val-Ala-Asp-|-. \r\n\r\nIn addition, Caspase-2 has been reported to be a negative regulator of necroptosis and to be indispensable for correct cell proliferation and genomic stability acting as a potential tumor suppressor factor. \r\n\r\nCaspase-2 is negatively regulated by phosphorylation at distinct sites (Ser157 and Ser340) during cell division and in nutrient abundance conditions. In response to heat shock, Caspase-2 activity is suppressed by the chaperone HSP90AA1(P07900).\r\n\r\nDecreased level of Caspase-2 associated with childhood forms of drug-resistance acute lymphoblastic leukaemia and decreased Caspase-2 expression was observed in mantle cell lymphoma tumor samples.\r\nCaspase-2 is associated with neurodegenerative disorders such as Alzheimer's and Huntington'd diseases.","predictedComplex":false,"interactors":[{"ac":"EBI-12735018","identifier":"P42575-PRO_0000004542","identifierLink":"https://www.uniprot.org/uniprotkb/P42575-PRO_0000004542/entry","name":"CASP2","description":"Caspase-2 subunit p18","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-12735025","identifier":"P42575-PRO_0000004545","identifierLink":"https://www.uniprot.org/uniprotkb/P42575-PRO_0000004545/entry","name":"CASP2","description":"Caspase-2 subunit p12","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-970","complexName":"Caspase-3 complex","organismName":"Homo sapiens; 9606","description":"A thiol protease complex that is activated by caspase-9 (CPX-3762 and CPX-991) and is one of the main effector caspases in mammalian cells. Cleaves and activates Caspase-6 (CPX-971), Caspase-7 (CPX-2862) and Caspase-9. \r\nAt the onset of apoptosis it proteolytically cleaves poly[ADP-ribose] polymerase 1 (PARP1, P09874) at a '216-Asp-|-Gly-217' bond. It is also the primary activator of apoptotic DNA fragmentation through inactivation of DNA fragmentation factor subunit alpha (DFFA - O00273).","predictedComplex":false,"interactors":[{"ac":"EBI-11619259","identifier":"P42574-PRO_0000004572","identifierLink":"https://www.uniprot.org/uniprotkb/P42574-PRO_0000004572/entry","name":"CASP3","description":"Caspase-3 subunit p12","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-11619267","identifier":"P42574-PRO_0000004571","identifierLink":"https://www.uniprot.org/uniprotkb/P42574-PRO_0000004571/entry","name":"CASP3","description":"Caspase-3 subunit p17","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-971","complexName":"Caspase-6 complex","organismName":"Homo sapiens; 9606","description":"A cysteine protease complex that specifically cleaves substrates with an aspartic acid residue at position P1 and has a preferred cleavage sequence of Val-Glu-His-Asp-|-. Caspase-6 is an initiator enzyme involved in the activation cascade of caspases responsible for apoptosis execution. \r\n\r\nCaspase-6 is capable of autoactivation and/or may be activated via proteolytic cleavage by Caspase-3 (CPX-970), Caspase-8 (CPX-975) or Caspase-10 (Q92851). Once activated it cleaves pro-Caspase-2 (P42575), pro-Caspase-8 (Q14790) and pro-Caspase-10 allowing their oligomerization into active Caspase-2 (CPX-969), Caspase-8 and Caspase-10. Caspase-6 induces mitochondrial permeabilisation, which leads to cytochrome c release and activation of the Apotosome (CPX-3762).\r\n\r\nCaspase-6 plays a role in neurodegenerative disease such as Huntigton disease (HD) and Alzheimer's disease. In HD, a mutant huntingtin (mHTT) protein features expanded polyglutamine repeats at its N-terminus. Caspase-6 is a key processing enzyme responsible for the cleavage of mHTT.","predictedComplex":false,"interactors":[{"ac":"EBI-12735154","identifier":"P55212-PRO_0000004611","identifierLink":"https://www.uniprot.org/uniprotkb/P55212-PRO_0000004611/entry","name":"CASP6","description":"Caspase-6 subunit p11","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-12735160","identifier":"P55212-PRO_0000004609","identifierLink":"https://www.uniprot.org/uniprotkb/P55212-PRO_0000004609/entry","name":"CASP6","description":"Caspase-6 subunit p18","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-972","complexName":"BRCC ubiquitin ligase complex","organismName":"Mus musculus; 10090","description":"A Ubc5-dependent E3 ubiquitin ligase complex involved in DNA repair, potentially by regulating factors involved in the process. It has a defined substrate specificity, with a strong preference for the nucleosome core histones H2A, H2B, H3 and H4. It co-localizes with and efficiently ubiquitylates, the histone variant H2AX at sites of DNA damage.","predictedComplex":false,"interactors":[{"ac":"EBI-1034100","identifier":"P97929","identifierLink":"https://www.uniprot.org/uniprotkb/P97929/entry","name":"Brca2","description":"Breast cancer type 2 susceptibility protein homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11289","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12735562","identifier":"Q8K3W0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K3W0/entry","name":"Babam2","description":"BRISC and BRCA1-A complex member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15189","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1790207","identifier":"O70445","identifierLink":"https://www.uniprot.org/uniprotkb/O70445/entry","name":"Bard1","description":"BRCA1-associated RING domain protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24171","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-309897","identifier":"Q08297","identifierLink":"https://www.uniprot.org/uniprotkb/Q08297/entry","name":"Rad51","description":"DNA repair protein RAD51 homolog 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6876136","identifier":"P48754","identifierLink":"https://www.uniprot.org/uniprotkb/P48754/entry","name":"Brca1","description":"Breast cancer type 1 susceptibility protein homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13763","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8360920","identifier":"P46737","identifierLink":"https://www.uniprot.org/uniprotkb/P46737/entry","name":"Brcc3","description":"Lys-63-specific deubiquitinase BRCC36","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10410","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-973","complexName":"Complement C3b complex","organismName":"Homo sapiens; 9606","description":"A protein complex of the alternative pathway of complement activation of the innate immune system. Complement C3 precursor is activated by cleavage into C3a and C3b by C3 convertases, either C4bC2a in the classical and lectin pathways or C3(H2O)Bb, C3bBb, C3bBbC3b, C3bBbP or C3bBbC3bP in the alternative pathway. \r\n\r\nC3b acts as an opsonin and interacts with glycoproteins and carbohydrates on pathogenic or apoptotic target cell surfaces through its reactive thioester moiety. Opsonization of target cells leads to enhanced phagocytosis, lysis of target cells via membrane attack complex (CPX-6159) assembly, clearance of antibody-antigen complexes and up-regulation of the adaptive response. \r\n\r\nActivation of C3b leads to an amplification cascade that generates more C3 convertase, deposits more C3b at the local site and switches C3 convertases to C5 convertases. \r\n\r\nTo protect host cells from inadvertent complement activation the activation of C3b is tightly regulated by either disrupting the C3 convertases or aiding in the proteolytic degradation of C3b. Bacteria and viruses possess C3b proteases to evade the complement response. \r\n\r\nLack of protection, due to familial mutations in the complement genes or the presence of autoantibodies against regulators has been linked to atypical hemolytic uremic syndrome (aHUS) and C3 glomerulopathies (C3G) in kidneys and age-related macular degeneration (AMD) in eyes. Conditions of chronic and acute inflammations, as in rheumatoid arthritis, strokes, and heart attacks, become aggravated by complement activation against the disturbed tissue.","predictedComplex":false,"interactors":[{"ac":"EBI-12735725","identifier":"P01024-PRO_0000005911","identifierLink":"https://www.uniprot.org/uniprotkb/P01024-PRO_0000005911/entry","name":"C3","description":"Complement C3b","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-6863145","identifier":"P01024-PRO_0000005908","identifierLink":"https://www.uniprot.org/uniprotkb/P01024-PRO_0000005908/entry","name":"C3","description":"Complement C3 beta chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-974","complexName":"SRCAP chromatin remodeling complex","organismName":"Homo sapiens; 9606","description":"ATP-dependent chromatin remodeling complex that catalyzes the exchange of H2A/H2B for H2A.Z/H2B in nucleosomes, thus regulating transcription of a specific subset of genes. \r\nWhether VPS72 and ZNHIT1 are part of  the core complex is unclear.  The first study (PMID:16634648) to show the histone exchange activity were not able to identify these two proteins in the purified active complex, whereas a previous study (PMID:15647280) purified a complex that contained the two proteins, but showed no functional activity in the exchange assay. A recent study (PMID: 25176633) claimed that the SRCAP complex may also be involved in double strand DNA repair by  homologous recombination. However, this was only demonstrated for the SRCAP protein, and not the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-347522","identifier":"O43257","identifierLink":"https://www.uniprot.org/uniprotkb/O43257/entry","name":"ZNHIT1","description":"Zinc finger HIT domain-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352939","identifier":"Q9Y230","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y230/entry","name":"RUVBL2","description":"RuvB-like 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353675","identifier":"Q9Y265","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y265/entry","name":"RUVBL1","description":"RuvB-like 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355018","identifier":"O96019","identifierLink":"https://www.uniprot.org/uniprotkb/O96019/entry","name":"ACTL6A","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-399105","identifier":"Q9NPF5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPF5/entry","name":"DMAP1","description":"DNA methyltransferase 1-associated protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12855","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-399189","identifier":"Q15906","identifierLink":"https://www.uniprot.org/uniprotkb/Q15906/entry","name":"VPS72","description":"Vacuolar protein sorting-associated protein 72 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13275","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-399269","identifier":"O95619","identifierLink":"https://www.uniprot.org/uniprotkb/O95619/entry","name":"YEATS4","description":"YEATS domain-containing protein 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23195","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-769316","identifier":"Q6ZRS2","identifierLink":"https://www.uniprot.org/uniprotkb/Q6ZRS2/entry","name":"SRCAP","description":"Helicase SRCAP","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45685","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-769329","identifier":"Q9GZN1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9GZN1/entry","name":"ACTR6","description":"Actin-related protein 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-975","complexName":"Caspase-8 complex","organismName":"Homo sapiens; 9606","description":"Cysteine protease that specifically cleaves substrates with an aspartic acid residue at the P(1) position and has an optimal recognition motif that incorporates four amino acid residues N-terminal to the cleavage site. Caspase-8 is an initiator enzyme in death receptors induced pathways of which the downstream executioner Caspase-3 (CPX-970) is a physiological target. It is activated via proteolytic cleavage by the DISC complex. Once activated, Caspase-8 cleaves and activates Caspase-3, Caspase-4 (P49662), Caspase-6 (CPX-971), Caspase-7 (CPX-2862), Caspase-9 (CPX-991 and CPX-3762) and Caspase-10 (Q92851). Deficiency leads to autoimmune lymphoproliferative syndrome (ALPS).","predictedComplex":false,"interactors":[{"ac":"EBI-12736099","identifier":"Q14790-PRO_0000004631","identifierLink":"https://www.uniprot.org/uniprotkb/Q14790-PRO_0000004631/entry","name":"CASP8","description":"Caspase-8 subunit p10","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-4478080","identifier":"Q14790-PRO_0000004629","identifierLink":"https://www.uniprot.org/uniprotkb/Q14790-PRO_0000004629/entry","name":"CASP8","description":"Caspase-8 subunit p18","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-976","complexName":"SRCAP chromatin remodeling complex","organismName":"Mus musculus; 10090","description":"ATP-dependent chromatin remodeling complex that catalyzes the exchange of H2a/H2b for H2a.z/H2b in nucleosomes, thus regulating transcription of a specific subset of genes. \r\nWhether Vps72 and Znhit1 are part of  the core complex is unclear.  The first study (PMID:16634648) to show the histone exchange activity were not able to identify these two proteins in the purified active complex, whereas a previous study (PMID:15647280) purified a complex that contained the two proteins, but showed no functional activity in the exchange assay. A recent study (PMID: 25176633) claimed that the SRCAP complex may also be involved in double strand DNA repair by  homologous recombination. However, this was only demonstrated for the SRCAP protein, and not the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-12736753","identifier":"A0A087WQ44","identifierLink":"https://www.uniprot.org/uniprotkb/A0A087WQ44/entry","name":"Srcap","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45685","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12736786","identifier":"Q8R331","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R331/entry","name":"Znhit1","description":"Zinc finger HIT domain-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1634999","identifier":"P60122","identifierLink":"https://www.uniprot.org/uniprotkb/P60122/entry","name":"Ruvbl1","description":"RuvB-like 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2549911","identifier":"Q9WTM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WTM5/entry","name":"Ruvbl2","description":"RuvB-like 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942577","identifier":"Q9JI44","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JI44/entry","name":"Dmap1","description":"DNA methyltransferase 1-associated protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12855","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942759","identifier":"Q9Z2N8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z2N8/entry","name":"Actl6a","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942848","identifier":"Q9CR11","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CR11/entry","name":"Yeats4","description":"YEATS domain-containing protein 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23195","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942867","identifier":"Q9D864","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D864/entry","name":"Actr6","description":"Actin-related protein 6","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942880","identifier":"Q62481","identifierLink":"https://www.uniprot.org/uniprotkb/Q62481/entry","name":"Vps72","description":"Vacuolar protein sorting-associated protein 72 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13275","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-977","complexName":"CDC24-FAR1-Gbetagamma complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for oriented growth of haploid cells in response to a pheromone gradient created by a mating partner of the opposite mating type. Forms at the cell cortex during mating, when a Far1-Cdc24 complex translocates from the nucleus. Recruits Cdc42 (P19073) and Bem1 (P29366) away from the bud site, thus providing the switch from bud growth to polarized growth, enabling the cell to project a shmoo towards the source of a pheromone gradient, and thus grow towards the mating partner. Binding to Gbetagamma may trigger a conformational change in Far1 that is required for its ability to activate Cdc24.","predictedComplex":false,"interactors":[{"ac":"EBI-4220","identifier":"P11433","identifierLink":"https://www.uniprot.org/uniprotkb/P11433/entry","name":"CDC24","description":"Cell division control protein 24","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47339","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6780","identifier":"P21268","identifierLink":"https://www.uniprot.org/uniprotkb/P21268/entry","name":"FAR1","description":"Cyclin-dependent kinase inhibitor FAR1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-7390","identifier":"P18851","identifierLink":"https://www.uniprot.org/uniprotkb/P18851/entry","name":"STE4","description":"Guanine nucleotide-binding protein subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7397","identifier":"P18852","identifierLink":"https://www.uniprot.org/uniprotkb/P18852/entry","name":"STE18","description":"Guanine nucleotide-binding protein subunit gamma","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28189","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-978","complexName":"NuA4 histone acetyltransferase complex","organismName":"Homo sapiens; 9606","description":"Histone acetyl transferase (HAT) complex involved in transcriptional activation of selected genes, mostly involved in apoptosis, cell-cycle regulation and hypoxia. Examples of regulated genes include TP53 (P04637)-dependent transcription genes, those containing promoters regulated by MYC (P01106) and highly transcribed genes such as those encoding ribosomal proteins. The major acetylation targets are lysines-5, 8, and 12 on nucleosomal H4, K5 and K15 on H2A, histone variants H2AZ and H2AX, as well as non-histone substrates such as TP53. The NuA4 complex can also acetylate H3 in free histones. A core complex formed by the subunits KAT5, EPC1, and ING3  is  sufficient  to  enable  strong  HAT  activity on  nucleosomal templates (Piccolo NuA4 CPX-709).\r\nThe  NuA4 complex is rapidly recruited at double-strand breaks (DSBs) during double strand break repair  to acetylate H4, H2A, and H2AX, thereby facilitating chromatin opening.","predictedComplex":false,"interactors":[{"ac":"EBI-352939","identifier":"Q9Y230","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y230/entry","name":"RUVBL2","description":"RuvB-like 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353675","identifier":"Q9Y265","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y265/entry","name":"RUVBL1","description":"RuvB-like 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355018","identifier":"O96019","identifierLink":"https://www.uniprot.org/uniprotkb/O96019/entry","name":"ACTL6A","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-399076","identifier":"Q9NV56","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NV56/entry","name":"MRGBP","description":"MRG/MORF4L-binding protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13581","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-399080","identifier":"Q92993","identifierLink":"https://www.uniprot.org/uniprotkb/Q92993/entry","name":"KAT5","description":"Histone acetyltransferase KAT5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-399105","identifier":"Q9NPF5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPF5/entry","name":"DMAP1","description":"DNA methyltransferase 1-associated protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12855","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-399128","identifier":"Q9Y4A5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4A5/entry","name":"TRRAP","description":"Transformation/transcription domain-associated protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-399163","identifier":"Q96L91","identifierLink":"https://www.uniprot.org/uniprotkb/Q96L91/entry","name":"EP400","description":"E1A-binding protein p400","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46459","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-399189","identifier":"Q15906","identifierLink":"https://www.uniprot.org/uniprotkb/Q15906/entry","name":"VPS72","description":"Vacuolar protein sorting-associated protein 72 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13275","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-399246","identifier":"Q9UBU8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UBU8/entry","name":"MORF4L1","description":"Mortality factor 4-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10880","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-399257","identifier":"Q15014","identifierLink":"https://www.uniprot.org/uniprotkb/Q15014/entry","name":"MORF4L2","description":"Mortality factor 4-like protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10880","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-399266","identifier":"Q9HAF1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HAF1/entry","name":"MEAF6","description":"Chromatin modification-related protein MEAF6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-399269","identifier":"O95619","identifierLink":"https://www.uniprot.org/uniprotkb/O95619/entry","name":"YEATS4","description":"YEATS domain-containing protein 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23195","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5666902","identifier":"Q05BQ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q05BQ5/entry","name":"MBTD1","description":"MBT domain-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12247","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-769266","identifier":"Q9H0E9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H0E9/entry","name":"BRD8","description":"Bromodomain-containing protein 8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15398","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-769270","identifier":"Q9H2F5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H2F5/entry","name":"EPC1","description":"Enhancer of polycomb homolog 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14898","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-769498","identifier":"Q52LR7","identifierLink":"https://www.uniprot.org/uniprotkb/Q52LR7/entry","name":"EPC2","description":"Enhancer of polycomb homolog 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14898","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-769503","identifier":"Q9NXR8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NXR8/entry","name":"ING3","description":"Inhibitor of growth protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-979","complexName":"Condensin I complex","organismName":"Homo sapiens; 9606","description":"Involved in chromosome condensation and segregation, both in meiosis and mitosis. Assembles in alternating pattern with Condensin II (CPX-985) complex along metaphase chromosomes with fully resolved sister chromatids. Also affects nuclear architecture and chromosome stability during interphase. Defects in Condensin complexes lead to anaphase bridges and apoptosis. In meiosis, only stably associates with chromosomes after anaphase I.","predictedComplex":false,"interactors":[{"ac":"EBI-1044041","identifier":"Q15021","identifierLink":"https://www.uniprot.org/uniprotkb/Q15021/entry","name":"NCAPD2","description":"Condensin complex subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1046410","identifier":"Q15003","identifierLink":"https://www.uniprot.org/uniprotkb/Q15003/entry","name":"NCAPH","description":"Condensin complex subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13108","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355822","identifier":"O95347","identifierLink":"https://www.uniprot.org/uniprotkb/O95347/entry","name":"SMC2","description":"Structural maintenance of chromosomes protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43941","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356173","identifier":"Q9NTJ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NTJ3/entry","name":"SMC4","description":"Structural maintenance of chromosomes protein 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43939","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-970214","identifier":"Q9BPX3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BPX3/entry","name":"NCAPG","description":"Condensin complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14418","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-980","complexName":"Condensin I complex","organismName":"Mus musculus; 10090","description":"Involved in chromosome condensation and segregation, both in meiosis and mitosis. Assembles in alternating pattern with Condensin II (CPX-986) complex along metaphase chromosomes with fully resolved sister chromatids. Also affects nuclear architecture and chromosome stability during interphase. Defects in Condensin complexes lead to anaphase bridges and apoptosis. In meiosis, only stably associates with chromosomes after anaphase I.","predictedComplex":false,"interactors":[{"ac":"EBI-12602144","identifier":"Q8K2Z4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8K2Z4/entry","name":"Ncapd2","description":"Condensin complex subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12738682","identifier":"E9PWG6","identifierLink":"https://www.uniprot.org/uniprotkb/E9PWG6/entry","name":"Ncapg","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14418","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-643436","identifier":"Q8CG48","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CG48/entry","name":"Smc2","description":"Structural maintenance of chromosomes protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR43941","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6921492","identifier":"Q8C156","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C156/entry","name":"Ncaph","description":"Condensin complex subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13108","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6921575","identifier":"Q8CG47","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CG47/entry","name":"Smc4","description":"Structural maintenance of chromosomes protein 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR43939","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-983","complexName":"ICAP1-KRIT1 integrin activation complex","organismName":"Homo sapiens; 9606","description":"Complex formation prevents the beta1-integrin binding protein ICAP1 from binding to, and limiting the activation of, beta1-integrin.  ICAP1 is a known suppressor of integrin activation believed to act by competing with the integrin activators talin (Q9Y490) and kindlin (Q9BQL6)  by competitively binding to the integrin beta1 cytoplasmic tail. Complex formation may also sequester ICAP1 to the nucleus.","predictedComplex":false,"interactors":[{"ac":"EBI-1573121","identifier":"O00522","identifierLink":"https://www.uniprot.org/uniprotkb/O00522/entry","name":"KRIT1","description":"Krev interaction trapped protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13283","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2127319","identifier":"O14713","identifierLink":"https://www.uniprot.org/uniprotkb/O14713/entry","name":"ITGB1BP1","description":"Integrin beta-1-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32055","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-984","complexName":"CCM endothelial permeability complex","organismName":"Homo sapiens; 9606","description":"Forms a signalling platform, responsible for maintaining integrity of endothelial permeability. Plays a key role in the integrity of the endothelial tubule networks at the initial stages of vasculogenesis. Appears to act primarily by inhibiting RhoA-associated kinase (ROCK) activation and thus regulating  RhoA signaling however distinct patterns of interacting proteins for each CCM protein has been observed.","predictedComplex":false,"interactors":[{"ac":"EBI-1573056","identifier":"Q9BSQ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BSQ5/entry","name":"CCM2","description":"Cerebral cavernous malformations 2 protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21642","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1573121","identifier":"O00522","identifierLink":"https://www.uniprot.org/uniprotkb/O00522/entry","name":"KRIT1","description":"Krev interaction trapped protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13283","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-740195","identifier":"Q9BUL8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BUL8/entry","name":"PDCD10","description":"Programmed cell death protein 10","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13250","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-985","complexName":"Condensin II complex","organismName":"Homo sapiens; 9606","description":"Involved in chromosome condensation and segregation, both in meiosis and mitosis. Assembles in alternating pattern with Condensin I (CPX-979) complex along metaphase chromosomes with fully resolved sister chromatids. Also affects nuclear architecture and chromosome stability during interphase. Defects in Condensin complexes lead to anaphase bridges and apoptosis. In meiosis, only stably associates with chromosomes after anaphase I.","predictedComplex":false,"interactors":[{"ac":"EBI-1047404","identifier":"Q86XI2","identifierLink":"https://www.uniprot.org/uniprotkb/Q86XI2/entry","name":"NCAPG2","description":"Condensin-2 complex subunit G2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16199","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2548296","identifier":"Q6IBW4","identifierLink":"https://www.uniprot.org/uniprotkb/Q6IBW4/entry","name":"NCAPH2","description":"Condensin-2 complex subunit H2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14324","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355822","identifier":"O95347","identifierLink":"https://www.uniprot.org/uniprotkb/O95347/entry","name":"SMC2","description":"Structural maintenance of chromosomes protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43941","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356173","identifier":"Q9NTJ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NTJ3/entry","name":"SMC4","description":"Structural maintenance of chromosomes protein 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43939","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-722805","identifier":"P42695","identifierLink":"https://www.uniprot.org/uniprotkb/P42695/entry","name":"NCAPD3","description":"Condensin-2 complex subunit D3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-986","complexName":"Condensin II complex","organismName":"Mus musculus; 10090","description":"Involved in chromosome condensation and segregation, both in meiosis and mitosis. Assembles in alternating pattern with Condensin I (CPX-980) complex along metaphase chromosomes with fully resolved sister chromatids. Also affects nuclear architecture and chromosome stability during interphase. Defects in Condensin complexes lead to anaphase bridges and apoptosis. In meiosis, only stably associates with chromosomes after anaphase I.","predictedComplex":false,"interactors":[{"ac":"EBI-11150710","identifier":"Q6DFV1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6DFV1/entry","name":"Ncapg2","description":"Condensin-2 complex subunit G2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16199","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11568170","identifier":"Q8BSP2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BSP2/entry","name":"Ncaph2","description":"Condensin-2 complex subunit H2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14324","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12739065","identifier":"Q6ZQK0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6ZQK0/entry","name":"Ncapd3","description":"Condensin-2 complex subunit D3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-643436","identifier":"Q8CG48","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CG48/entry","name":"Smc2","description":"Structural maintenance of chromosomes protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR43941","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6921575","identifier":"Q8CG47","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CG47/entry","name":"Smc4","description":"Structural maintenance of chromosomes protein 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR43939","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-988","complexName":"Complement C3b complex","organismName":"Mus musculus; 10090","description":"A protein complex of the alternative pathway of complement activation of the innate immune system. Complement C3 precurser is activated by cleavage into C3a and C3b by C3 convertases, either C4bC2a in the classical and lectin pathways or C3(H2O)Bb, C3bBb, C3bBbC3b, C3bBbP or C3bBbC3bP in the alternative pathway. \r\n\r\nC3b acts as an opsonin and interacts with glycoproteins and carbohydrates on pathogenic or apoptotic target cell surfaces through its reactive thioester moiety. Opsonization of target cells leads to enhanced phagocytosis, lysis of target cells via membrane attack complex (CPX-6159) assembly, clearance of antibody-antigen complexes and upregulation of the adaptive response. \r\n\r\nActivation of C3b leads to an amplification cascade that generates more C3 convertase, deposits more C3b at the local site and switches C3 convertases to C5 convertases. \r\n\r\nTo protect host cells from inadvertent complement activation the activation of C3b is tightly regulated by either disrupting the C3 convertases or aiding in the proteolytic degradation of C3b. Bacteria and viruses possess C3b proteases to evade the complement response.","predictedComplex":false,"interactors":[{"ac":"EBI-12739639","identifier":"P01027-PRO_0000005918","identifierLink":"https://www.uniprot.org/uniprotkb/P01027-PRO_0000005918/entry","name":"C3","description":"Complement C3 beta chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-12739644","identifier":"P01027-PRO_0000005921","identifierLink":"https://www.uniprot.org/uniprotkb/P01027-PRO_0000005921/entry","name":"C3","description":"Complement C3b","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-989","complexName":"PCAF histone acetylase complex","organismName":"Homo sapiens; 9606","description":"A histone acetyl transferase complex that plays a role in regulation of transcription of a specific group of genes by increasing the decompaction of chromatin to facilitate the access of transcription factors to promoter regions. It preferentially acetylates a single residue of Histone H3 (Lys-14) and is only able to weakly acetylate a single residue of Histone H4 (Lys-8) within nucleosomal substrates. The complex may also acetylate non-histone proteins, such as transcription factors.\r\n.","predictedComplex":false,"interactors":[{"ac":"EBI-1034238","identifier":"Q16514","identifierLink":"https://www.uniprot.org/uniprotkb/Q16514/entry","name":"TAF12","description":"Transcription initiation factor TFIID subunit 12","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1785876","identifier":"O75529","identifierLink":"https://www.uniprot.org/uniprotkb/O75529/entry","name":"TAF5L","description":"TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19879","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-399128","identifier":"Q9Y4A5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4A5/entry","name":"TRRAP","description":"Transformation/transcription domain-associated protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-473249","identifier":"O75528","identifierLink":"https://www.uniprot.org/uniprotkb/O75528/entry","name":"TADA3","description":"Transcriptional adapter 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13556","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-477430","identifier":"Q92831","identifierLink":"https://www.uniprot.org/uniprotkb/Q92831/entry","name":"KAT2B","description":"Histone acetyltransferase KAT2B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45750","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-708376","identifier":"Q12962","identifierLink":"https://www.uniprot.org/uniprotkb/Q12962/entry","name":"TAF10","description":"Transcription initiation factor TFIID subunit 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21242","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712521","identifier":"Q16594","identifierLink":"https://www.uniprot.org/uniprotkb/Q16594/entry","name":"TAF9","description":"Transcription initiation factor TFIID subunit 9","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48068","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742268","identifier":"O75478","identifierLink":"https://www.uniprot.org/uniprotkb/O75478/entry","name":"TADA2A","description":"Transcriptional adapter 2-alpha","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12374","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743984","identifier":"Q9Y6J9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6J9/entry","name":"TAF6L","description":"TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10221","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-896640","identifier":"O75486","identifierLink":"https://www.uniprot.org/uniprotkb/O75486/entry","name":"SUPT3H","description":"Transcription initiation protein SPT3 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11380","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-990","complexName":"NuA4 histone acetyltransferase complex","organismName":"Mus musculus; 10090","description":"Histone acetyl transferase (HAT) complex involved in transcriptional activation of selected genes, mostly involved in apoptosis, cell-cycle regulation and hypoxia. Examples of regulated genes include Tp53 (P02340)-dependent transcription genes, those containing promoters regulated by Myc (P01108) and highly transcribed genes such as those encoding ribosomal proteins. The major acetylation targets are lysines-5, 8, and 12 on nucleosomal H4, K5 and K15 on H2A, histone variants H2AZ and H2AX, as well as non-histone substrates such as Tp53. The NuA4 complex can also acetylate H3 in free histones. A core complex formed by the subunits Kat5, Epc1, and Ing3  is  sufficient  to  enable  strong  HAT  activity on  nucleosomal templates (Piccolo NuA4 CPX-747).\r\nThe  NuA4 complex is rapidly recruited at double-strand breaks (DSBs) during double strand break repair  to acetylate H4, H2A, and H2AX, thereby facilitating chromatin opening.","predictedComplex":false,"interactors":[{"ac":"EBI-1169948","identifier":"Q8CHK4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CHK4/entry","name":"Kat5","description":"Histone acetyltransferase KAT5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1634999","identifier":"P60122","identifierLink":"https://www.uniprot.org/uniprotkb/P60122/entry","name":"Ruvbl1","description":"RuvB-like 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2549911","identifier":"Q9WTM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WTM5/entry","name":"Ruvbl2","description":"RuvB-like 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11093","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942477","identifier":"Q80YV3","identifierLink":"https://www.uniprot.org/uniprotkb/Q80YV3/entry","name":"Trrap","description":"Transformation/transcription domain-associated protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942504","identifier":"Q8CHI8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CHI8/entry","name":"Ep400","description":"E1A-binding protein p400","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46459","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942577","identifier":"Q9JI44","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JI44/entry","name":"Dmap1","description":"DNA methyltransferase 1-associated protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12855","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942609","identifier":"Q8R3B7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8R3B7/entry","name":"Brd8","description":"Bromodomain-containing protein 8","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15398","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942636","identifier":"Q8C9X6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C9X6/entry","name":"Epc1","description":"Enhancer of polycomb homolog 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14898","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942663","identifier":"Q8C0I4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C0I4/entry","name":"Epc2","description":"Enhancer of polycomb homolog 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14898","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942759","identifier":"Q9Z2N8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z2N8/entry","name":"Actl6a","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942848","identifier":"Q9CR11","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CR11/entry","name":"Yeats4","description":"YEATS domain-containing protein 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23195","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942880","identifier":"Q62481","identifierLink":"https://www.uniprot.org/uniprotkb/Q62481/entry","name":"Vps72","description":"Vacuolar protein sorting-associated protein 72 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13275","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942903","identifier":"Q8VEK6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VEK6/entry","name":"Ing3","description":"Inhibitor of growth protein 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2943018","identifier":"P60762","identifierLink":"https://www.uniprot.org/uniprotkb/P60762/entry","name":"Morf4l1","description":"Mortality factor 4-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10880","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5736761","identifier":"Q9DAT2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DAT2/entry","name":"Mrgbp","description":"MRG/MORF4L-binding protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13581","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8338571","identifier":"Q2VPQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q2VPQ9/entry","name":"Meaf6","description":"Chromatin modification-related protein MEAF6","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13476","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8820711","identifier":"Q6P5G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P5G3/entry","name":"Mbtd1","description":"MBT domain-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12247","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9989979","identifier":"Q9R0Q4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9R0Q4/entry","name":"Morf4l2","description":"Mortality factor 4-like protein 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10880","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-991","complexName":"Caspase-9 complex","organismName":"Homo sapiens; 9606","description":"A cysteine protease complex that is an apical protease of the intrinsic apoptosis pathway. Generates the active forms of Caspase-3 (CPX-970) and Caspase-7 (CPX-2862) by limited proteolysis, and thereby transmit the apoptotic signal to the execution phase. Caspase-9 is mostly active as part of a multicomponent complex known as the apoptosome (CPX-3762), however it has residual catalytic activity on its own.","predictedComplex":false,"interactors":[{"ac":"EBI-13635286","identifier":"P55211-PRO_0000004643","identifierLink":"https://www.uniprot.org/uniprotkb/P55211-PRO_0000004643/entry","name":"CASP9","description":"Caspase-9 subunit p10","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-516799","identifier":"P55211","identifierLink":"https://www.uniprot.org/uniprotkb/P55211/entry","name":"CASP9","description":"Caspase-9","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10454","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-994","complexName":"DNA polymerase zeta complex","organismName":"Homo sapiens; 9606","description":"Error prone DNA polymerase active in  translesion DNA synthesis in response to stalled DNA replication forks, for example at sites of covalent DNA lesions such as UV radiation-induced photo-products.","predictedComplex":false,"interactors":[{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2871302","identifier":"O60673","identifierLink":"https://www.uniprot.org/uniprotkb/O60673/entry","name":"REV3L","description":"DNA polymerase zeta catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45812","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372354","identifier":"P49005","identifierLink":"https://www.uniprot.org/uniprotkb/P49005/entry","name":"POLD2","description":"DNA polymerase delta subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-77889","identifier":"Q9UI95","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UI95/entry","name":"MAD2L2","description":"Mitotic spindle assembly checkpoint protein MAD2B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-864956","identifier":"Q15054","identifierLink":"https://www.uniprot.org/uniprotkb/Q15054/entry","name":"POLD3","description":"DNA polymerase delta subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR17598","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-995","complexName":"KEOPS tRNA N6-adenosine threonylcarbamoyltransferase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyses the transfer of the threonylcarbamoyl-moiety of threonylcarbamoyladenylate (TCA) onto A37 of substrate tRNA in the cytoplasm. The N6-threonylcarbamoyladenosine (t6A) modification is present at position 37 of tRNAs that recognize ANN-codons, with N being any nucleotide, enhancing the codon-anti-codon interaction and is required for recognition of the AUG start codon. The modification is thus important for maintaining translational fidelity and also appears to play a role in transcription and telomere homeostasis. The unstable TCA intermediate is synthesised from ATP, threonine and bicarbonate by the SUA5 (P32579) enzyme.","predictedComplex":false,"interactors":[{"ac":"EBI-1200990","identifier":"Q3E833","identifierLink":"https://www.uniprot.org/uniprotkb/Q3E833/entry","name":"PCC1","description":"EKC/KEOPS complex subunit PCC1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31283","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26178","identifier":"P46984","identifierLink":"https://www.uniprot.org/uniprotkb/P46984/entry","name":"GON7","description":"EKC/KEOPS complex subunit GON7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-26411","identifier":"P36132","identifierLink":"https://www.uniprot.org/uniprotkb/P36132/entry","name":"KAE1","description":"tRNA N6-adenosine threonylcarbamoyltransferase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11735","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3809","identifier":"P53323","identifierLink":"https://www.uniprot.org/uniprotkb/P53323/entry","name":"BUD32","description":"EKC/KEOPS complex subunit BUD32","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12209","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9097897","identifier":"CHEBI:60240","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60240","name":"divalent metal cation","description":"divalent metal cation","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-912262","identifier":"Q03705","identifierLink":"https://www.uniprot.org/uniprotkb/Q03705/entry","name":"CGI121","description":"EKC/KEOPS complex subunit CGI121","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15840","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-996","complexName":"Cas1-Cas2 complex","organismName":"Escherichia coli (strain K12); 83333","description":"CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). The system memorizes previous infections by integrating short sequences of invading genomes (spacers) into the CRISPR locus. The spacers, interspaced with repeats, are expressed as small guide CRISPR RNAs (crRNAs) that are employed by Cas proteins to target invaders sequence-specifically upon a reoccurring infection. The Cas1-Cas 2 complex is essential for the incorporation of 33-bp long sequence-variable foreign DNA protospacers into the host CRISPR locus. CRISPR transcripts generated from the loci assemble with Cas proteins to detect and cleave foreign nucleic acids bearing sequence complementarity to the spacer segment. Cas1 is the probable nuclease that catalyzes the integration reaction, whilst Cas2 may provide a structural scaffold and stimulate the catalytic activity of Cas1","predictedComplex":false,"interactors":[{"ac":"EBI-1130209","identifier":"Q46896","identifierLink":"https://www.uniprot.org/uniprotkb/Q46896/entry","name":"ygbT","description":"CRISPR-associated endonuclease Cas1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR34353","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9150552","identifier":"P45956","identifierLink":"https://www.uniprot.org/uniprotkb/P45956/entry","name":"ygbF","description":"CRISPR-associated endoribonuclease Cas2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-997","complexName":"GCN5-containing ATAC complex","organismName":"Homo sapiens; 9606","description":"A histone acetyl transferase complex that plays a role in regulation of transcription of a specific group of genes by increasing the decompaction of chromatin to facilitate the access of transcription factors to promoter regions. It preferentially acetylates  a single residue of Histone H3 (Lys-14) and only weakly acetylates Histone H4. Recruited to the promoters of the IE (immediate early) gene FOS (P01100), FOSL1 (P15407), EGR1 (P18146). The complex also regulates the activity of non-histone targets and orchestrates mitotic progression by regulating Cyclin A degradation through acetylation.Cyclin A/CDK2 kinase is essential for correct centrosome formation and inhibits SIRT2 (Q8IXJ6) function.","predictedComplex":false,"interactors":[{"ac":"EBI-2795509","identifier":"Q9ULM3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ULM3/entry","name":"YEATS2","description":"YEATS domain-containing protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23195","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2795524","identifier":"Q8IYH5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IYH5/entry","name":"ZZZ3","description":"ZZ-type zinc finger-containing protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22705","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-473249","identifier":"O75528","identifierLink":"https://www.uniprot.org/uniprotkb/O75528/entry","name":"TADA3","description":"Transcriptional adapter 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13556","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-477622","identifier":"Q92830","identifierLink":"https://www.uniprot.org/uniprotkb/Q92830/entry","name":"KAT2A","description":"Histone acetyltransferase KAT2A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45750","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-540834","identifier":"P61964","identifierLink":"https://www.uniprot.org/uniprotkb/P61964/entry","name":"WDR5","description":"WD repeat-containing protein 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-741953","identifier":"Q9NS73","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NS73/entry","name":"MBIP","description":"MAP3K12-binding inhibitory protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23404","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742268","identifier":"O75478","identifierLink":"https://www.uniprot.org/uniprotkb/O75478/entry","name":"TADA2A","description":"Transcriptional adapter 2-alpha","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12374","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743117","identifier":"Q96ES7","identifierLink":"https://www.uniprot.org/uniprotkb/Q96ES7/entry","name":"SGF29","description":"SAGA-associated factor 29","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21539","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-750300","identifier":"Q01658","identifierLink":"https://www.uniprot.org/uniprotkb/Q01658/entry","name":"DR1","description":"Protein Dr1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46138","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-750907","identifier":"Q9H8E8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H8E8/entry","name":"KAT14","description":"Cysteine-rich protein 2-binding protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20916","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-998","complexName":"Calcineurin-Calmodulin-AKAP5 complex, beta-R1 variant","organismName":"Homo sapiens; 9606","description":"Calcium-dependent, calmodulin-stimulated protein phosphatase calcineurin in complex with plasma-membrane anchor protein AKAP5. 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The calcineurin-AKAP5 complex has been shown to promote NFAT signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1759540","identifier":"P16298","identifierLink":"https://www.uniprot.org/uniprotkb/P16298/entry","name":"PPP3CB","description":"Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397435","identifier":"P62158","identifierLink":"https://www.uniprot.org/uniprotkb/P62158/entry","name":"calm_human","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-703640","identifier":"P24588","identifierLink":"https://www.uniprot.org/uniprotkb/P24588/entry","name":"AKAP5","description":"A-kinase anchor protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15182","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-915984","identifier":"P63098","identifierLink":"https://www.uniprot.org/uniprotkb/P63098/entry","name":"PPP3R1","description":"Calcineurin subunit B type 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1113","complexName":"Calcineurin-Calmodulin-AKAP5 complex, gamma-R1 variant","organismName":"Mus musculus; 10090","description":"Calcium-dependent, calmodulin-stimulated protein phosphatase calcineurin in complex with plasma-membrane anchor protein Akap5. 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The calcineurin-Akap5 complex has been shown to promote NFAT signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-397460","identifier":"P62204","identifierLink":"https://www.uniprot.org/uniprotkb/P62204/entry","name":"Calm1","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-6271683","identifier":"P48455","identifierLink":"https://www.uniprot.org/uniprotkb/P48455/entry","name":"Ppp3cc","description":"Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6666164","identifier":"Q63810","identifierLink":"https://www.uniprot.org/uniprotkb/Q63810/entry","name":"Ppp3r1","description":"Calcineurin subunit B type 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7091108","identifier":"D3YVF0","identifierLink":"https://www.uniprot.org/uniprotkb/D3YVF0/entry","name":"Akap5","description":"A-kinase anchor protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15182","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1114","complexName":"Calcineurin-Calmodulin-AKAP5 complex, alpha-R2 variant","organismName":"Homo sapiens; 9606","description":"Calcium-dependent, calmodulin-stimulated protein phosphatase calcineurin in complex with plasma-membrane anchor protein AKAP5. 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The calcineurin-AKAP5 complex has been shown to promote NFAT signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-352922","identifier":"Q08209","identifierLink":"https://www.uniprot.org/uniprotkb/Q08209/entry","name":"PPP3CA","description":"Protein phosphatase 3 catalytic subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3906025","identifier":"Q96LZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96LZ3/entry","name":"PPP3R2","description":"Calcineurin subunit B type 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397435","identifier":"P62158","identifierLink":"https://www.uniprot.org/uniprotkb/P62158/entry","name":"calm_human","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-703640","identifier":"P24588","identifierLink":"https://www.uniprot.org/uniprotkb/P24588/entry","name":"AKAP5","description":"A-kinase anchor protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15182","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1115","complexName":"Calcineurin-Calmodulin-AKAP5 complex, alpha-R2 variant","organismName":"Mus musculus; 10090","description":"Calcium-dependent, calmodulin-stimulated protein phosphatase calcineurin in complex with plasma-membrane anchor protein Akap5. 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Calcineurin is important for cardiac development and pathophysiology, for nervous-system development and for some of the plastic changes in neurons that are believed to underlie learning and memory. AKAP5 recruits calcineurin to the vicinity of L-type Ca2+ channels for their activation by elevated Ca2+ entering the cell. AKAP5 balances the opposing effects of calcineurin and protein kinase A (PKA) (P17612) on neuronal voltage-gated L-type Ca2+ channels and coordinates the activities of calcineurin, PKA and PKC on a number of other channels and receptors. Despite its atypical PxIxIT calcineurin-recognition motif that confers stronger binding affinity by calcineurin than other substrates it allows for effective disengagement of calcineurin to couple channel activation with downstream signaling events. The calcineurin-AKAP5 complex has been shown to promote NFAT signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1759540","identifier":"P16298","identifierLink":"https://www.uniprot.org/uniprotkb/P16298/entry","name":"PPP3CB","description":"Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3906025","identifier":"Q96LZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96LZ3/entry","name":"PPP3R2","description":"Calcineurin subunit B type 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397435","identifier":"P62158","identifierLink":"https://www.uniprot.org/uniprotkb/P62158/entry","name":"calm_human","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-703640","identifier":"P24588","identifierLink":"https://www.uniprot.org/uniprotkb/P24588/entry","name":"AKAP5","description":"A-kinase anchor protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15182","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1117","complexName":"Calcineurin-Calmodulin-AKAP5 complex, beta-R2 variant","organismName":"Mus musculus; 10090","description":"Calcium-dependent, calmodulin-stimulated protein phosphatase calcineurin in complex with plasma-membrane anchor protein Akap5. Calcineurin is important for cardiac development and pathophysiology, for nervous-system development and for some of the plastic changes in neurons that are believed to underlie learning and memory. Akap5 recruits calcineurin to the vicinity of L-type Ca2+ channels for their activation by elevated Ca2+ entering the cell. Akap5 balances the opposing effects of calcineurin and protein kinase A (PKA) (P05132) on neuronal voltage-gated L-type Ca2+ channels and coordinates the activities of calcineurin, PKA and PKC on a number of other channels and receptors. Despite its atypical PxIxIT calcineurin-recognition motif that confers stronger binding affinity by calcineurin than other substrates it allows for effective disengagement of calcineurin to couple channel activation with downstream signaling events. The calcineurin-Akap5 complex has been shown to promote NFAT signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-13916676","identifier":"Q63811","identifierLink":"https://www.uniprot.org/uniprotkb/Q63811/entry","name":"Ppp3r2","description":"Calcineurin subunit B type 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397460","identifier":"P62204","identifierLink":"https://www.uniprot.org/uniprotkb/P62204/entry","name":"Calm1","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-642618","identifier":"P48453","identifierLink":"https://www.uniprot.org/uniprotkb/P48453/entry","name":"Ppp3cb","description":"Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7091108","identifier":"D3YVF0","identifierLink":"https://www.uniprot.org/uniprotkb/D3YVF0/entry","name":"Akap5","description":"A-kinase anchor protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15182","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1118","complexName":"Calcineurin-Calmodulin-AKAP5 complex, gamma-R2 variant","organismName":"Homo sapiens; 9606","description":"Calcium-dependent, calmodulin-stimulated protein phosphatase calcineurin in complex with plasma-membrane anchor protein AKAP5. Calcineurin is important for cardiac development and pathophysiology, for nervous-system development and for some of the plastic changes in neurons that are believed to underlie learning and memory. AKAP5 recruits calcineurin to the vicinity of L-type Ca2+ channels for their activation by elevated Ca2+ entering the cell. AKAP5 balances the opposing effects of calcineurin and protein kinase A (PKA) (P17612) on neuronal voltage-gated L-type Ca2+ channels and coordinates the activities of calcineurin, PKA and PKC on a number of other channels and receptors. Despite its atypical PxIxIT calcineurin-recognition motif that confers stronger binding affinity by calcineurin than other substrates it allows for effective disengagement of calcineurin to couple channel activation with downstream signaling events. The calcineurin-AKAP5 complex has been shown to promote NFAT signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2827192","identifier":"P48454","identifierLink":"https://www.uniprot.org/uniprotkb/P48454/entry","name":"PPP3CC","description":"Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3906025","identifier":"Q96LZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96LZ3/entry","name":"PPP3R2","description":"Calcineurin subunit B type 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397435","identifier":"P62158","identifierLink":"https://www.uniprot.org/uniprotkb/P62158/entry","name":"calm_human","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-703640","identifier":"P24588","identifierLink":"https://www.uniprot.org/uniprotkb/P24588/entry","name":"AKAP5","description":"A-kinase anchor protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15182","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1119","complexName":"Calcineurin-Calmodulin-AKAP5 complex, gamma-R2 variant","organismName":"Mus musculus; 10090","description":"Calcium-dependent, calmodulin-stimulated protein phosphatase calcineurin in complex with plasma-membrane anchor protein Akap5. Calcineurin is important for cardiac development and pathophysiology, for nervous-system development and for some of the plastic changes in neurons that are believed to underlie learning and memory. Akap5 recruits calcineurin to the vicinity of L-type Ca2+ channels for their activation by elevated Ca2+ entering the cell. Akap5 balances the opposing effects of calcineurin and protein kinase A (PKA) (P05132) on neuronal voltage-gated L-type Ca2+ channels and coordinates the activities of calcineurin, PKA and PKC on a number of other channels and receptors. Despite its atypical PxIxIT calcineurin-recognition motif that confers stronger binding affinity by calcineurin than other substrates it allows for effective disengagement of calcineurin to couple channel activation with downstream signaling events. The calcineurin-Akap5 complex has been shown to promote NFAT signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 8, maxValue: 8","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-13916676","identifier":"Q63811","identifierLink":"https://www.uniprot.org/uniprotkb/Q63811/entry","name":"Ppp3r2","description":"Calcineurin subunit B type 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397460","identifier":"P62204","identifierLink":"https://www.uniprot.org/uniprotkb/P62204/entry","name":"Calm1","description":"Calmodulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-6271683","identifier":"P48455","identifierLink":"https://www.uniprot.org/uniprotkb/P48455/entry","name":"Ppp3cc","description":"Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7091108","identifier":"D3YVF0","identifierLink":"https://www.uniprot.org/uniprotkb/D3YVF0/entry","name":"Akap5","description":"A-kinase anchor protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15182","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1120","complexName":"Amyloid-beta protein 40/42 oligomeric complex","organismName":"Homo sapiens; 9606","description":"Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. May have a role in depressing synaptic activity thus preventing excitotoxicity. Influences synaptic plasticity through various receptors, including NMDAR, mGluR and alpha7 nicotinic acetylcholine receptors (CPX-236). Mediates dendritic spine loss leading to decreased synapse density, inhibition of long-term potentiation (LTP), enhancement of long-term depression (LTD), excessive calcium influx, mitochondrial impairment, endoplasmic reticulum stress and activation of apoptotic processes. May bind plasma membrane lipids affecting their stability and leading to cytotoxicity. May affect metal ion homeostasis by chelating synaptic copper, zinc or iron ions. Oligomers of protein 42 only may have positive neurogenetic effects by activating synaptic protein kinases. Mostly found in the extracellular space with a small proportion occurring as membrane-bound species. Dimers (CPX-1062) and oligomers of soluble amyloid-beta peptides are the main pathogenic species linked to Alzheimer's disease. Cellular prion protein (PrPC/PRNP, P04156) binds amyloid-beta oligomers mediating their synaptic dysfunction. Insoluble fibrils and plaques form during the latter stages of the disease. Chaperones, such as alphaB-crystallins or clusterin (P10909), bind to misfolded oligomeric species and form long-lived complexes, thereby preventing both their further growth into fibrils and their dissociation into synaptotoxic dimers. \r\n\r\nAmyloid-beta peptide may act as transcription factor for its own precursor protein APP and its cleavage enzyme BACE1 (P56817) initiating a positive feedback mechanism that ultimately leads to amyloidogenesis and Alzheimer's disease.","predictedComplex":false,"interactors":[{"ac":"EBI-2431589","identifier":"P05067-PRO_0000000093","identifierLink":"https://www.uniprot.org/uniprotkb/P05067-PRO_0000000093/entry","name":"APP","description":"Amyloid-beta protein 40","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-821758","identifier":"P05067-PRO_0000000092","identifierLink":"https://www.uniprot.org/uniprotkb/P05067-PRO_0000000092/entry","name":"APP","description":"Amyloid-beta protein 42","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-1121","complexName":"Amyloid-beta protein 40/42 oligomeric complex","organismName":"Mus musculus; 10090","description":"Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. May have a role in depressing synaptic activity thus preventing excitotoxicity. Influences synaptic plasticity through various receptors, including NMDAR, mGluR and alpha7 nicotinic acetylcholine receptors (CPX-234). Mediates dendritic spine loss leading to decreased synapse density, inhibition of long-term potentiation (LTP), enhancement of long-term depression (LTD), excessive calcium influx, mitochondrial impairment, endoplasmic reticulum stress and activation of apoptotic processes. May bind plasma membrane lipids affecting their stability and leading to cytotoxicity. May affect metal ion homeostasis by chelating synaptic copper, zinc or iron ions. Oligomers of protein 42 only may have positive neurogenetic effects by activating synaptic protein kinases. Mostly found in the extracellular space with a small proportion occurring as membrane-bound species. Dimers (CPX-1105) and oligomers of soluble amyloid-beta peptides are the main pathogenic species linked to Alzheimer's disease. Cellular prion protein (PrPC/Prnp, P04925) binds amyloid-beta oligomers mediating their synaptic dysfunction. Insoluble fibrils and plaques form during the latter stages of the disease. Chaperones, such as alphaB-crystallins or clusterin (Q06890), bind to misfolded oligomeric species and form long-lived complexes, thereby preventing both their further growth into fibrils and their dissociation into synaptotoxic dimers. \r\n\r\nAmyloid-beta peptide may act as transcription factor for its own precursor protein APP and its cleavage enzyme BACE1 (P56818) initiating a positive feedback mechanism that ultimately leads to amyloidogenesis and Alzheimer's disease.","predictedComplex":false,"interactors":[{"ac":"EBI-14022231","identifier":"P12023-PRO_0000000118","identifierLink":"https://www.uniprot.org/uniprotkb/P12023-PRO_0000000118/entry","name":"App","description":"Amyloid-beta protein 42","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-14022236","identifier":"P12023-PRO_0000000119","identifierLink":"https://www.uniprot.org/uniprotkb/P12023-PRO_0000000119/entry","name":"App","description":"Amyloid-beta protein 40","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-1122","complexName":"UV DNA damage recognition complex DBB1-DBB2","organismName":"Mus musculus; 10090","description":"Mediates the initial detection of UV light-induced cyclobutane pyrimidine photodimers as part of the nucleotide excision repair (NER) process. Performs a 3D search mechanism, examining sites on DNA in discrete steps before binding as long-lived, non-motile dimers at sites of damage. The complex then constitutively associates with Cullin4A or 4B and Rbx1 to form an E3 ligase (CPX-650/CPX-651).","predictedComplex":false,"interactors":[{"ac":"EBI-12510080","identifier":"Q99J79","identifierLink":"https://www.uniprot.org/uniprotkb/Q99J79/entry","name":"Ddb2","description":"DNA damage-binding protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15169","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2552275","identifier":"Q3U1J4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3U1J4/entry","name":"Ddb1","description":"DNA damage-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1123","complexName":"FOXO3-MYC complex","organismName":"Homo sapiens; 9606","description":"A transcription factor repressor complex involved in regulating cell proliferation by repressing transcription of genes involved in negative regulation of mitotic cell cycle. The interaction of MYC with FOXO3 is likely to occur at the target gene promoter and inhibits FOXO3s activating effect on target gene transcription. The half life of the FOXO3-MYC complex is not known, but most likely to be of limited time span, in line with rapid dynamics of changes in transcription regulation in response to internal and external cues. Another variant of FOXO3-MYC interaction has been observed where FOXO3 seems to facilitate displacement of MYC from its promoters, thereby antagonizing MYC function in metabolic adaption to hypoxia.","predictedComplex":false,"interactors":[{"ac":"EBI-1644164","identifier":"O43524","identifierLink":"https://www.uniprot.org/uniprotkb/O43524/entry","name":"FOXO3","description":"Forkhead box protein O3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-447544","identifier":"P01106","identifierLink":"https://www.uniprot.org/uniprotkb/P01106/entry","name":"MYC","description":"Myc proto-oncogene protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45851","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1124","complexName":"Telomerase holoenzyme complex","organismName":"Mus musculus; 10090","description":"A reverse transcriptase complex that is essential for maintenance of telomeres. \r\n\r\nCatalytic subunit Tert and RNA template terc (CPX-19) are essential for telomerase activity. \r\n\r\nElongates the single-stranded G-rich 3-prime protruding ends of chromosomal DNA using Terc RNA as a template. \r\n\r\nTerc, Dkc1, Gar1, Nhp2 & Nop10 form the box H/ACA telomerase ribonucleoprotein (RNP) complex which then binds to Tert forming the telomerase holoenzyme complex. \r\n\r\nWrap53 (also known as Tcab1, Q8VC51) binds to the CAB box in Terc and facilitates localization of the telomerase complex to Cajal bodies. In S-phase, telomerase holoenzyme complex is targeted from Cajal bodies to telomeres by binding of Tert to the shelterin subunit, Acd (Q5EE38).","predictedComplex":false,"interactors":[{"ac":"EBI-10046300","identifier":"URS00004A29D0_10090","identifierLink":"http://rnacentral.org/rna/URS00004A29D0_10090","name":"terc_mouse_rna","description":"Mouse telomerase RNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"ribonucleic acid","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-6260856","identifier":"Q9CY66","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CY66/entry","name":"Gar1","description":"H/ACA ribonucleoprotein complex subunit 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23237","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8339277","identifier":"Q9ESX5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ESX5/entry","name":"Dkc1","description":"H/ACA ribonucleoprotein complex subunit DKC1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23127","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8340560","identifier":"Q9CQS2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQS2/entry","name":"Nop10","description":"H/ACA ribonucleoprotein complex subunit 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8340718","identifier":"Q9CRB2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CRB2/entry","name":"Nhp2","description":"H/ACA ribonucleoprotein complex subunit 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9662790","identifier":"O70372","identifierLink":"https://www.uniprot.org/uniprotkb/O70372/entry","name":"Tert","description":"Telomerase reverse transcriptase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12066","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1125","complexName":"BUG1-GRH1 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Appears to play a role in the tethering of COPII (CPX-2523), though an interaction with Sec23/24, and thus formation of the cis-Golgi and endoplasmic reticulum to Golgi vesicle-mediated transport. The complex is anchored to membranes through an acetylated amino-terminal region in Grh1.","predictedComplex":false,"interactors":[{"ac":"EBI-32083","identifier":"Q04410","identifierLink":"https://www.uniprot.org/uniprotkb/Q04410/entry","name":"GRH1","description":"GRASP65 homolog protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12893","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32271","identifier":"Q12191","identifierLink":"https://www.uniprot.org/uniprotkb/Q12191/entry","name":"BUG1","description":"Binder of USO1 and GRH1 protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1126","complexName":"Cyclin cyd-1-cdk4 complex","organismName":"Caenorhabditis elegans; 6239","description":"Cyclin-dependent protein kinase activity. Required for G1 to S phase transition of the mitotic cell cycle. Cdk-4 phosphorylates the Rb protein lin-35 at Ser-714 and Thr-719 which inhibits the transcriptional repressor activity of lin-35 and allows for progression through the G1 phase of the cell cycle during postembryonic development.\r\n\r\nThe complex also regulates the asymmetric division of the somatic gonadal precursor cell to determine sex during gonadogenesis and controls the expression of growth and metabolic genes in muscle cells, in addition to cell cycle genes.","predictedComplex":false,"interactors":[{"ac":"EBI-14063019","identifier":"Q9XTR1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XTR1/entry","name":"cdk-4","description":"Cyclin-dependent kinase 4 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2420074","identifier":"Q9U2M5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9U2M5/entry","name":"cyd-1","description":"G1/S-specific cyclin-D","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1127","complexName":"Cyclin cye-1-cdk2 complex","organismName":"Caenorhabditis elegans; 6239","description":"Cyclin-dependent protein kinase complex. Required for G1 to S phase transition of the mitotic cell cycle. Hyper-phosphorylation of Rb proteins by the complex leads to their inactivation which allows transcription of E2F-controlled genes.\r\n\r\nRegulates proliferation, quiescent state and cell fate during the development of several cell lineages. \r\n\r\nPhosphorylates and inhibits the translational repressor gld-1 and thus prevents entry into meiosis in order to regulate the pool of germline stem cells and the size of the mitotic zone in the gonads.","predictedComplex":false,"interactors":[{"ac":"EBI-14063070","identifier":"O61847","identifierLink":"https://www.uniprot.org/uniprotkb/O61847/entry","name":"cdk-2","description":"Cyclin-dependent kinase 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6499833","identifier":"O01501","identifierLink":"https://www.uniprot.org/uniprotkb/O01501/entry","name":"cye-1","description":"G1/S-specific cyclin-E","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1128","complexName":"Calcineurin-Calmodulin complex","organismName":"Caenorhabditis elegans; 6239","description":"A calcium-dependent, calmodulin-stimulated serine/threonine protein phosphatase complex that is activated by elevated cytoplasmic calcium ion concentrations.  Important for many cellular processes including development, egg-laying, fertility, cuticle formation, proliferation, thermotaxis, behaviour and lifespan.","predictedComplex":false,"interactors":[{"ac":"EBI-11178149","identifier":"CHEBI:29034","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29034","name":"iron(3+)","description":"iron(3+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-14063206","identifier":"G5EDN6","identifierLink":"https://www.uniprot.org/uniprotkb/G5EDN6/entry","name":"cnb-1","description":"Protein phosphatase 2B regulatory subunit cnb-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45942","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-317271","identifier":"O16305","identifierLink":"https://www.uniprot.org/uniprotkb/O16305/entry","name":"cmd-1","description":"Calmodulin","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR23050","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-323063","identifier":"Q0G819","identifierLink":"https://www.uniprot.org/uniprotkb/Q0G819/entry","name":"tax-6","description":"Serine/threonine-protein phosphatase 2B catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1129","complexName":"Atk-1/Akt-2/Sgk-1 protein kinase complex","organismName":"Caenorhabditis elegans; 6239","description":"Serine/threonine protein kinase complex. Component of the daf-2 insulin receptor-like signalling cascade that controls daf-16-mediated gene expression.  The forkhead transcription factor daf-16 regulates the expression of genes involved in metabolism, development, dauer formation, longevity and the response to stress. The complex functions downstream of pkd-1 in the signalling cascade to antagonize daf-16 by phosphorylation. The complex is activated by pdk-1 phosphorylation. The activated complex then controls the intracellular localisation and activation of daf-16.","predictedComplex":false,"interactors":[{"ac":"EBI-1770718","identifier":"Q17941","identifierLink":"https://www.uniprot.org/uniprotkb/Q17941/entry","name":"akt-1","description":"Serine/threonine-protein kinase akt-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24356","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1770776","identifier":"Q2PJ68","identifierLink":"https://www.uniprot.org/uniprotkb/Q2PJ68/entry","name":"sgk-1","description":"Serine/threonine-protein kinase sgk-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24356","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-320656","identifier":"Q9XTG7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XTG7/entry","name":"akt-2","description":"Serine/threonine-protein kinase akt-2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24356","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1130","complexName":"Beta-catenin-lit-1 complex","organismName":"Caenorhabditis elegans; 6239","description":"Serine/threonine protein kinase complex. Acts as an effector in the wnt signalling pathway to control the asymmetry of cell divisions in embryogenesis by down-regulating pop-1 activity. pop-1 is a protein related to the vertebrate TCF/LEF transcription factors, and is required for cell fate decisions and in particular, for anterior/posterior cell divisions. The complex regulates pop-1 localization and is required for the pop-1/par-5 interaction. Specifically lit-1 Interacts with wrm-1 (via N-terminus); activates lit-1 kinase activity and the lit-1/wrm-1 dimer phosphorylates pop-1 at Ser-118 and Ser-127. This promotes pop-1 interaction with par-5 and translocation of pop-1 from the nucleus to the cytoplasm.","predictedComplex":false,"interactors":[{"ac":"EBI-2530558","identifier":"Q10953","identifierLink":"https://www.uniprot.org/uniprotkb/Q10953/entry","name":"wrm-1","description":"Armadillo repeat-containing protein wrm-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR45976","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-318513","identifier":"Q9U9Y8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9U9Y8/entry","name":"lit-1","description":"Serine/threonine kinase NLK","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24055","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1131","complexName":"Prmt-5-cep-1-cbp-1 complex","organismName":"Caenorhabditis elegans; 6239","description":"Represses transcriptional activation in response to DNA damage.  prmt-5 interacts with, but does not methylate, cep-1 and with cbp-1 which results in the methylation of cbp-1. Cep-1 transcriptional activity may be inhibited by its interaction with methylated cbp-1. The formation of this complex may prevent apoptosis by repressing the capacity of cbp-1 to enhance cep-1 dependent transcriptional activation of the programmed cell death activator egl-1.","predictedComplex":false,"interactors":[{"ac":"EBI-14063756","identifier":"P34545","identifierLink":"https://www.uniprot.org/uniprotkb/P34545/entry","name":"cbp-1","description":"Protein cbp-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13808","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6741131","identifier":"P46580","identifierLink":"https://www.uniprot.org/uniprotkb/P46580/entry","name":"prmt-5","description":"Protein arginine N-methyltransferase 5","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10738","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6768115","identifier":"Q20646","identifierLink":"https://www.uniprot.org/uniprotkb/Q20646/entry","name":"cep-1","description":"Transcription factor cep-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]}]},{"complexAC":"CPX-1132","complexName":"gls-1-gld-3 complex","organismName":"Caenorhabditis elegans; 6239","description":"Translation regulator complex which, in early embryos, promotes the expression of mRNAs that encode germline survival factors.\r\n\r\nDuring hermaphrodite development, the complex promotes the sperm/oocyte switch by freeing the translational repressor fbf-1 to turn off sperm promoting factors.\r\n\r\nThe complex is essential for germline survival during post-embryonic germline development. Upon dissociation of the complex, germ cells fail to survive into adulthood.","predictedComplex":false,"interactors":[{"ac":"EBI-317828","identifier":"Q95ZK7","identifierLink":"https://www.uniprot.org/uniprotkb/Q95ZK7/entry","name":"gld-3","description":"Defective in germ line development protein 3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10627","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-322416","identifier":"Q8I4M5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8I4M5/entry","name":"gls-1","description":"Germline survival defective-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]}]},{"complexAC":"CPX-1133","complexName":"B-WICH chromatin remodelling complex","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex that exposes DNA by sliding away histone octamers. Positively regulates histone H3 acetylation, in particular H3K9, by recruiting several histone acetyltransferases (HATs), such as Kat2b (Pcaf, Q9JHD1), p300 (B2RWS6), and Kat2a (Gcn5, Q9JHD2). Binds to both ribosomal DNA promoters and coding regions. Facilitates RNA polymerase I and III transcription by preventing compaction of chromatin at rDNA loci allowing HATs to assemble. An open chromatin structure is a prerequisite for the binding of the RNA polymerase machinery and also the regulatory factor Myc (P01108), which activates both RNA pol I genes and RNA pol III genes. May also activate RNA polymerase II gene transcription. The different subunits of the complex potentially have specific roles that lead to the stepwise modification of chromatin, and may not all associate simultaneously with the Baz1b-Smarca5 core. The B-WICH assembly may thus represent a number of smaller complexes. At the start of the cell division process, when Pol I transcription is arrested, B-WICH is in a disassembled state due to the phosphorylation of Baz1b. The complex assembles on the active gene during early G1 phase. Polymeric actin interacts with Pol I, an interaction that is required for transcription. One speculative model is that Nm1 (Q9WTI7-3) interacts with actin and the rDNA via its C-terminus, generating local force that pulls the polymerase along the active gene. Once dissociated from actin, Nm1 interacts with Smarca5 in a Baz1b-dependent manner, a mechanism that stabilizes the complex on the rDNA. Additional components then assemble into the B-WICH complex(es) mediated by specific RNA species. \r\n\r\nParticularly important during embryonic and neonatal development, especially for craniofacial features.","predictedComplex":false,"interactors":[{"ac":"EBI-11517516","identifier":"Q9WTI7-3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WTI7-3/entry","name":"Myo1c","description":"Unconventional myosin-Ic","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-1373622","identifier":"Q7TPV4","identifierLink":"https://www.uniprot.org/uniprotkb/Q7TPV4/entry","name":"Mybbp1a","description":"Myb-binding protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13213","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14063885","identifier":"F8VPZ5","identifierLink":"https://www.uniprot.org/uniprotkb/F8VPZ5/entry","name":"Ercc6","description":"DNA excision repair protein ERCC-6","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45629","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2551674","identifier":"Q9JIK5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JIK5/entry","name":"Ddx21","description":"Nucleolar RNA helicase 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR47958","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-688642","identifier":"Q99NB9","identifierLink":"https://www.uniprot.org/uniprotkb/Q99NB9/entry","name":"Sf3b1","description":"Splicing factor 3B subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8340579","identifier":"Q7TNV0","identifierLink":"https://www.uniprot.org/uniprotkb/Q7TNV0/entry","name":"Dek","description":"Protein DEK","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13468","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-927547","identifier":"Q91ZW3","identifierLink":"https://www.uniprot.org/uniprotkb/Q91ZW3/entry","name":"Smarca5","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-927576","identifier":"Q9Z277","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z277/entry","name":"Baz1b","description":"Tyrosine-protein kinase BAZ1B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9494077","identifier":"CHEBI:18111","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18111","name":"ribosomal rna","description":"ribosomal RNA","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1134","complexName":"Amyloid-beta protein 42 oligomeric complex","organismName":"Homo sapiens; 9606","description":"Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. This oligomer of protein 42 only has positive neurogenetic effects by activating synaptic protein kinases. May have a role in depressing synaptic activity thus preventing excitotoxicity. Influences synaptic plasticity through various receptors, including NMDAR, mGluR and alpha7 nicotinic acetylcholine receptors (CPX-236). Mediates dendritic spine loss leading to decreased synapse density, inhibition of long-term potentiation (LTP), enhancement of long-term depression (LTD), excessive calcium influx, mitochondrial impairment, endoplasmic reticulum stress and activation of apoptotic processes. May bind plasma membrane lipids affecting their stability and leading to cytotoxicity. May affect metal ion homeostasis by chelating synaptic copper, zinc or iron ions. Mostly found in the extracellular space with a small proportion occurring as membrane-bound species. Dimers (CPX-1062) and oligomers of soluble amyloid-beta peptides are the main pathogenic species linked to Alzheimer's disease. Cellular prion protein (PrPC/PRNP, P04156) binds amyloid-beta oligomers mediating their synaptic dysfunction. Insoluble fibrils and plaques form during the latter stages of the disease. Chaperones, such as alphaB-crystallins or clusterin (P10909), bind to misfolded oligomeric species and form long-lived complexes, thereby preventing both their further growth into fibrils and their dissociation into synaptotoxic dimers. \r\n\r\nAmyloid-beta peptide may act as transcription factor for its own precursor protein APP and its cleavage enzyme BACE1 (P56817) initiating a positive feedback mechanism that ultimately leads to amyloidogenesis and Alzheimer's disease.","predictedComplex":false,"interactors":[{"ac":"EBI-821758","identifier":"P05067-PRO_0000000092","identifierLink":"https://www.uniprot.org/uniprotkb/P05067-PRO_0000000092/entry","name":"APP","description":"Amyloid-beta protein 42","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-1135","complexName":"Sand-1-ccz-1 complex","organismName":"Caenorhabditis elegans; 6239","description":"Critical role in maintaining proper vacuole morphology in vacuole delivery pathways by regulating fusion of vesicles with the vacuole at the tethering/docking stage. Regulates the SNARE complex during the coordinated priming and docking stages of fusion.\r\n\r\nPlays a role in endosome-lysosome fusion. The complex acts as an guanine nucleotide exchange factor for rab-7 to promote the activity of the HOPS complex (CPX-1136) in rab-5-to-rab-7 endosome conversion. May play a role in early-to-late endosome conversion.","predictedComplex":false,"interactors":[{"ac":"EBI-323404","identifier":"Q9XVL8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XVL8/entry","name":"ccz-1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-328112","identifier":"Q9BI89","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BI89/entry","name":"sand-1","description":"Vacuolar fusion protein MON1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13027","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1136","complexName":"HOPS tethering complex","organismName":"Caenorhabditis elegans; 6239","description":"Multisubunit tethering complex involved in endo-lysosomal vesicle trafficking and lysosome biogenesis by cross-linking two membranes, and facilitating the formation of a SNARE complex during fusion. Required for the delivery of vacuolar proteins and homotypic fusion of vacuoles and controls the clearance of late endosomes and autophagosomes during heterophagy and autophagy through promoting fusion of these vesicles with the vacuole. Controls homotypic vacuole-vacuole fusion by regulating vesicle docking to the vacuole through its interaction with soluble SNAREs, the GTP-bound form of the Rab protein rab-7 and phosphoinositides.\r\n\r\nProposed to be involved in the rab-5-to-rab-7 endosome conversion probably by the sand-1/ccz-1 complex (CPX-1135), and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. Functions in late endosomes/lysosomes and during endosome maturation, replaces the early endosome tethering complex CORVET (CPX-1137).","predictedComplex":false,"interactors":[{"ac":"EBI-14973839","identifier":"Q09600","identifierLink":"https://www.uniprot.org/uniprotkb/Q09600/entry","name":"vps-11","description":"Vacuolar protein sorting-associated protein 11 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR23323","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14973864","identifier":"Q11182","identifierLink":"https://www.uniprot.org/uniprotkb/Q11182/entry","name":"vps-16","description":"Vacuolar protein sorting-associated protein 16 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12811","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14973887","identifier":"Q23194","identifierLink":"https://www.uniprot.org/uniprotkb/Q23194/entry","name":"vps-18","description":"Vacuolar protein sorting-associated protein 18 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR23323","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14973931","identifier":"Q19954","identifierLink":"https://www.uniprot.org/uniprotkb/Q19954/entry","name":"vps-41","description":"Vacuolar protein sorting-associated protein 41 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12616","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-312046","identifier":"P34260","identifierLink":"https://www.uniprot.org/uniprotkb/P34260/entry","name":"vps-33.1","description":"Vacuolar protein sorting-associated protein 33A","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11679","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-318975","identifier":"Q1ZXS5","identifierLink":"https://www.uniprot.org/uniprotkb/Q1ZXS5/entry","name":"vps-39","description":"Vacuolar protein sorting-associated protein 39 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1137","complexName":"CORVET tethering complex","organismName":"Caenorhabditis elegans; 6239","description":"Multisubunit tethering complex involved in early endosomal fusions by cross-linking two membranes, and facilitating the formation of a SNARE complex during fusion.. Cooperates with Rab GTPases to capture vesicles and trap them prior to the action of SNAREs. During endosome maturation, it is replaced by the late endosomal/lysosomal HOPS complex (CPX-1136).","predictedComplex":false,"interactors":[{"ac":"EBI-14973839","identifier":"Q09600","identifierLink":"https://www.uniprot.org/uniprotkb/Q09600/entry","name":"vps-11","description":"Vacuolar protein sorting-associated protein 11 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR23323","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14973864","identifier":"Q11182","identifierLink":"https://www.uniprot.org/uniprotkb/Q11182/entry","name":"vps-16","description":"Vacuolar protein sorting-associated protein 16 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12811","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14973887","identifier":"Q23194","identifierLink":"https://www.uniprot.org/uniprotkb/Q23194/entry","name":"vps-18","description":"Vacuolar protein sorting-associated protein 18 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR23323","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-317143","identifier":"A3QMB3","identifierLink":"https://www.uniprot.org/uniprotkb/A3QMB3/entry","name":"vps-8","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12616","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-319270","identifier":"Q18891","identifierLink":"https://www.uniprot.org/uniprotkb/Q18891/entry","name":"vps-33.2","description":"Vacuolar protein sorting-associated protein 33B","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR11679","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1138","complexName":"RB1-E2F1-TFDP1 transcription repressor complex","organismName":"Caenorhabditis elegans; 6239","description":"Transcriptional repressor complex involved in the regulation of intestinal cell division during postembryonic development. lin-35 negatively regulates the G1-S transition by binding to the E2F1-DP1 transcription factor complex (CPX-965) and blocking the transactivation domain of efl-1. lin-35 dissociates from the complex following hyperphosphorylation by cyclin-dependent kinases.","predictedComplex":false,"interactors":[{"ac":"EBI-321470","identifier":"G5EDT1","identifierLink":"https://www.uniprot.org/uniprotkb/G5EDT1/entry","name":"lin-35","description":"Retinoblastoma-like protein homolog lin-35","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-324825","identifier":"Q22703","identifierLink":"https://www.uniprot.org/uniprotkb/Q22703/entry","name":"dpl-1","description":"Transcription factor dpl-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12548","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-331564","identifier":"G5EF11","identifierLink":"https://www.uniprot.org/uniprotkb/G5EF11/entry","name":"efl-1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12081","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1139","complexName":"Amyloid-beta protein 42 oligomeric complex","organismName":"Mus musculus; 10090","description":"Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. This oligomer of protein 42 only has positive neurogenetic effects by activating synaptic protein kinases. May have a role in depressing synaptic activity thus preventing excitotoxicity. Influences synaptic plasticity through various receptors, including NMDAR, mGluR and alpha7 nicotinic acetylcholine receptors (CPX-234). Mediates dendritic spine loss leading to decreased synapse density, inhibition of long-term potentiation (LTP), enhancement of long-term depression (LTD), excessive calcium influx, mitochondrial impairment, endoplasmic reticulum stress and activation of apoptotic processes. May bind plasma membrane lipids affecting their stability and leading to cytotoxicity. May affect metal ion homeostasis by chelating synaptic copper, zinc or iron ions. Mostly found in the extracellular space with a small proportion occurring as membrane-bound species. Dimers (CPX-1105) and oligomers of soluble amyloid-beta peptides are the main pathogenic species linked to Alzheimer's disease. Cellular prion protein (PrPC/PRNP, P04925) binds amyloid-beta oligomers mediating their synaptic dysfunction. Insoluble fibrils and plaques form during the latter stages of the disease. Chaperones, such as alphaB-crystallins or clusterin (Q06890), bind to misfolded oligomeric species and form long-lived complexes, thereby preventing both their further growth into fibrils and their dissociation into synaptotoxic dimers. \r\n\r\nAmyloid-beta peptide may act as transcription factor for its own precursor protein APP and its cleavage enzyme BACE1 (P56818) initiating a positive feedback mechanism that ultimately leads to amyloidogenesis and Alzheimer's disease.","predictedComplex":false,"interactors":[{"ac":"EBI-14022231","identifier":"P12023-PRO_0000000118","identifierLink":"https://www.uniprot.org/uniprotkb/P12023-PRO_0000000118/entry","name":"App","description":"Amyloid-beta protein 42","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-1140","complexName":"HICS complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Appears to have a role in cytokinesis. May connect the actin-myosin ring to the plasma membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-18140","identifier":"P40073","identifierLink":"https://www.uniprot.org/uniprotkb/P40073/entry","name":"SHO1","description":"High osmolarity signaling protein SHO1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15735","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28955","identifier":"P53901","identifierLink":"https://www.uniprot.org/uniprotkb/P53901/entry","name":"INN1","description":"Ingression protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47052","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31510","identifier":"Q07533","identifierLink":"https://www.uniprot.org/uniprotkb/Q07533/entry","name":"CYK3","description":"Cytokinesis protein 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5412","identifier":"Q05080","identifierLink":"https://www.uniprot.org/uniprotkb/Q05080/entry","name":"HOF1","description":"Cytokinesis protein 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23065","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1141","complexName":"MOT1-TBP transcription regulation complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Transcriptional regulation complex, formation of which causes the  dissociation of the TATA-binding protein (TBP) from promoters and thereby regulates TBP distribution in the cell. ATP-driven TBP-DNA dissociation by MOT1 involves both the conversion of MOT1 to an open ATPase state to the closed state induced by ATP binding and short range DNA translocation. May form a larger, DNA-dependent, assembly with the NC2 complex (CPX-1662).","predictedComplex":false,"interactors":[{"ac":"EBI-11152","identifier":"P32333","identifierLink":"https://www.uniprot.org/uniprotkb/P32333/entry","name":"MOT1","description":"TATA-binding protein-associated factor MOT1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR36498","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19129","identifier":"P13393","identifierLink":"https://www.uniprot.org/uniprotkb/P13393/entry","name":"SPT15","description":"TATA-box-binding protein","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10126","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1142","complexName":"MEX67-MTR2 mRNA nuclear export factor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Mediates the export of bulk mRNA through direct interactions with both the mRNA cargo and nuclear pore proteins that contain characteristic phenylalanine-glycine repeating sequence motifs (FG-nucleoporins). Also contributes to ribosomal subunit export.","predictedComplex":false,"interactors":[{"ac":"EBI-11585","identifier":"P34232","identifierLink":"https://www.uniprot.org/uniprotkb/P34232/entry","name":"MTR2","description":"mRNA transport regulator MTR2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12612","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11642","identifier":"Q99257","identifierLink":"https://www.uniprot.org/uniprotkb/Q99257/entry","name":"MEX67","description":"mRNA export factor MEX67","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10662","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1143","complexName":"General transcription factor TFIIIB complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Transcription factor complex required for Pol III transcription complex (CPX-2660) assembly which transcribes short noncoding RNA genes. Cooperates with TFIIIC (CPX-1656) to recruit Pol III to different types of gene promoters and form the preinitiation complex (PIC). In the case of PIC formation at transfer DNA (tDNA) genes, TFIIIC recognizes the gene-internal box A and B elements, while TFIIIB localizes further upstream. TFIIIA (P39933) is required only for the transcription of 5S rRNA, where it recognizes the gene-internal control element, box C, to further recruit TFIIIC and TFIIIB. Once assembled upstream of the start site, TFIIIB generates a significant DNA distortion of the class III gene promoter through the SPT15 and BDP1 subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-19129","identifier":"P13393","identifierLink":"https://www.uniprot.org/uniprotkb/P13393/entry","name":"SPT15","description":"TATA-box-binding protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10126","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19142","identifier":"P29056","identifierLink":"https://www.uniprot.org/uniprotkb/P29056/entry","name":"BRF1","description":"Transcription factor IIIB 70 kDa subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11618","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19164","identifier":"P46678","identifierLink":"https://www.uniprot.org/uniprotkb/P46678/entry","name":"BDP1","description":"Transcription factor TFIIIB component B''","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22929","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1144","complexName":"FOXO3-MYC complex","organismName":"Mus musculus; 10090","description":"A transcription factor repressor complex involved in regulating cell proliferation by repressing transcription of genes involved in negative regulation of mitotic cell cycle. The interaction of Myc with Foxo3 is likely to occur at the target gene promoter and inhibits Foxo3s activating effect on target gene transcription. The half life of the Foxo3-Myc complex is not known, but most likely to be of limited time span, in line with rapid dynamics of changes in transcription regulation in response to internal and external cues. Another variant of Foxo3-Myc interaction has been observed where Foxo3 seems to facilitate displacement of Myc from its promoters, thereby antagonizing Myc function in metabolic adaption to hypoxia.","predictedComplex":false,"interactors":[{"ac":"EBI-1183114","identifier":"P01108","identifierLink":"https://www.uniprot.org/uniprotkb/P01108/entry","name":"Myc","description":"Myc proto-oncogene protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45851","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6127038","identifier":"Q9WVH4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WVH4/entry","name":"Foxo3","description":"Forkhead box protein O3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1145","complexName":"E2F2-DP1 transcription factor complex","organismName":"Caenorhabditis elegans; 6239","description":"Probable transcription factor complex which binds DNA through the E2 recognition site, 5'-TTTC[CG]CGC-3', typically associated with the promoters of genes active in S phase, activating genes that stimulate DNA synthesis and cell cycle advancement. Regulates the expression of genes such as ced-3 and ced-4, which are involved in programmed cell death in germ cells.","predictedComplex":false,"interactors":[{"ac":"EBI-322786","identifier":"A5HWA8","identifierLink":"https://www.uniprot.org/uniprotkb/A5HWA8/entry","name":"efl-2","description":"Transcription factor efl-2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12081","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-324825","identifier":"Q22703","identifierLink":"https://www.uniprot.org/uniprotkb/Q22703/entry","name":"dpl-1","description":"Transcription factor dpl-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12548","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1146","complexName":"RB1-E2F2-TFDP1 transcription repressor complex","organismName":"Caenorhabditis elegans; 6239","description":"Probably negatively regulates the G1-S transition by binding to the E2F2-DP1 complex (CPX-1145) and blocking the transactivation domain of efl-2. Lin-35 dissociates from the complex following hyperphosphorylation by cyclin-dependent kinases. Regulates the expression of genes such as ced-3 and ced-4, which are involved in programmed cell death in germ cells.","predictedComplex":false,"interactors":[{"ac":"EBI-321470","identifier":"G5EDT1","identifierLink":"https://www.uniprot.org/uniprotkb/G5EDT1/entry","name":"lin-35","description":"Retinoblastoma-like protein homolog lin-35","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-322786","identifier":"A5HWA8","identifierLink":"https://www.uniprot.org/uniprotkb/A5HWA8/entry","name":"efl-2","description":"Transcription factor efl-2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12081","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-324825","identifier":"Q22703","identifierLink":"https://www.uniprot.org/uniprotkb/Q22703/entry","name":"dpl-1","description":"Transcription factor dpl-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12548","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1147","complexName":"FOXO3-YWHAZ complex","organismName":"Homo sapiens; 9606","description":"Complex formation promotes nuclear export of FOXO3 and increases the half-life of phosphorylated FOXO3 in the cytoplasm. The 14-3-3 zeta /YWHAZ-FOXO3 complex thus  down-regulates FOXO3-mediated transcription of genes encoding anti-proliferative and pro-apoptotic proteins and attenuates anti-viability cellular processes in response to growth factors.","predictedComplex":false,"interactors":[{"ac":"EBI-1644164","identifier":"O43524","identifierLink":"https://www.uniprot.org/uniprotkb/O43524/entry","name":"FOXO3","description":"Forkhead box protein O3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347088","identifier":"P63104","identifierLink":"https://www.uniprot.org/uniprotkb/P63104/entry","name":"YWHAZ","description":"14-3-3 protein zeta/delta","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18860","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1148","complexName":"Foxo3-Ywhaz complex","organismName":"Mus musculus; 10090","description":"Complex formation promotes nuclear export of Foxo3 and increases the half-life of phosphorylated Foxo3 in the cytoplasm. The 14-3-3 zeta/Ywhaz-Foxo3 complex thus  down-regulates Foxo3-mediated transcription of genes encoding anti-proliferative and pro-apoptotic proteins and attenuates anti-viability cellular processes in response to growth factors.","predictedComplex":false,"interactors":[{"ac":"EBI-354751","identifier":"P63101","identifierLink":"https://www.uniprot.org/uniprotkb/P63101/entry","name":"Ywhaz","description":"14-3-3 protein zeta/delta","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR18860","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6127038","identifier":"Q9WVH4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9WVH4/entry","name":"Foxo3","description":"Forkhead box protein O3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1149","complexName":"General transcription factor TFIIF complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"General transcription factor that interacts with RNAPII and can recruit RNAPII to a preinitiation complex containing TFIID and TFIIB. Required for the opening of DNA, to allow transcription initiation. DNA opening occurs around the tip of the Pol II clamp and the TFIIE (CPX-1658) ‘extended winged helix’ domain. TFIIF and TFIIE bind open promoter DNA from opposite sides of the Pol II cleft.  TFIIF adopts an extended induced structure that allows it to retain the upstream DNA–SPT15–TFIIB assembly on the wall and to bind the DNA bubble. TFIIF and TFIIE encircle and retain the DNA and TFIIE may then act to stabilize the open DNA structure.","predictedComplex":false,"interactors":[{"ac":"EBI-18912","identifier":"P41895","identifierLink":"https://www.uniprot.org/uniprotkb/P41895/entry","name":"TFG1","description":"Transcription initiation factor IIF subunit alpha","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13011","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18916","identifier":"P41896","identifierLink":"https://www.uniprot.org/uniprotkb/P41896/entry","name":"TFG2","description":"Transcription initiation factor IIF subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10445","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18920","identifier":"P35189","identifierLink":"https://www.uniprot.org/uniprotkb/P35189/entry","name":"TAF14","description":"Transcription initiation factor TFIID subunit 14","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23195","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1150","complexName":"SWI/SNF chromatin remodelling complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"An ATP-dependent chromatin remodelling complex which disrupts the nucleosome structure, increases the binding of transcription factors to nucleosomes, mobilizes histone octamers along DNA in cis, transfers histone octamers to different DNA fragments, displaces histone H2A/H2B dimers and generates superhelical torsion in DNA. Binds preferentially to four-way DNA and promotes resection initiation at a DNA double-strand break. Binds to DNA and nucleosomes without any DNA sequence specificity.","predictedComplex":false,"interactors":[{"ac":"EBI-17526","identifier":"P22082","identifierLink":"https://www.uniprot.org/uniprotkb/P22082/entry","name":"SNF2","description":"Transcription regulatory protein SNF2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17546","identifier":"P18480","identifierLink":"https://www.uniprot.org/uniprotkb/P18480/entry","name":"SNF5","description":"SWI/SNF chromatin-remodeling complex subunit SNF5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17550","identifier":"P18888","identifierLink":"https://www.uniprot.org/uniprotkb/P18888/entry","name":"SNF6","description":"Transcription regulatory protein SNF6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-17560","identifier":"P38956","identifierLink":"https://www.uniprot.org/uniprotkb/P38956/entry","name":"SNF11","description":"Transcription regulatory protein SNF11","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-17564","identifier":"P53628","identifierLink":"https://www.uniprot.org/uniprotkb/P53628/entry","name":"SNF12","description":"Transcription regulatory protein SNF12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18617","identifier":"P09547","identifierLink":"https://www.uniprot.org/uniprotkb/P09547/entry","name":"SWI1","description":"SWI/SNF chromatin-remodeling complex subunit SWI1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18622","identifier":"P32591","identifierLink":"https://www.uniprot.org/uniprotkb/P32591/entry","name":"SWI3","description":"SWI/SNF complex subunit SWI3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18920","identifier":"P35189","identifierLink":"https://www.uniprot.org/uniprotkb/P35189/entry","name":"TAF14","description":"Transcription initiation factor TFIID subunit 14","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23195","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22851","identifier":"P43554","identifierLink":"https://www.uniprot.org/uniprotkb/P43554/entry","name":"SWP82","description":"SWI/SNF global transcription activator complex subunit SWP82","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22597","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23637","identifier":"P53330","identifierLink":"https://www.uniprot.org/uniprotkb/P53330/entry","name":"RTT102","description":"Regulator of Ty1 transposition protein 102","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-2962","identifier":"Q12406","identifierLink":"https://www.uniprot.org/uniprotkb/Q12406/entry","name":"ARP7","description":"Actin-related protein 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2972","identifier":"Q05123","identifierLink":"https://www.uniprot.org/uniprotkb/Q05123/entry","name":"ARP9","description":"Actin-like protein ARP9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1151","complexName":"N-acetylglutamate synthase NAGS/NAGK complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for the controlling initial step of L-arginine biosynthesis. Forms a metabolon, i.e. a complex formed by the supramolecular association of two sequentially acting enzymes of the pathway that synthesizes N(2)-acetyl-L-ornithine from L-glutamate. Regulated by arginine binding. The ARG5,6 kinase can exist independently of ARG2, ARG2 appears only to exist as a part of the metabolon. ARG5,6 may therefore also act as a chaperone and/or an essential stabilizing agent for ARG2.","predictedComplex":false,"interactors":[{"ac":"EBI-15101247","identifier":"Q01217-PRO_0000002073","identifierLink":"https://www.uniprot.org/uniprotkb/Q01217-PRO_0000002073/entry","name":"ARG5,6","description":"Acetylglutamate kinase","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-25930","identifier":"P40360","identifierLink":"https://www.uniprot.org/uniprotkb/P40360/entry","name":"ARG2","description":"Amino-acid acetyltransferase, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23342","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1152","complexName":"ARGR-MCM1 transcription regulation complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Transcriptional regulation complex which binds, in the presence of arginine, to the promoter regions of genes co-regulated by arginine, repressing the synthesis of five anabolic enzymes, e.g. ornithine carbamoyltransferase and inducing the synthesis of two catabolic enzymes, e.g. arginase. The inositol polyphosphate multikinase, ARG82 appears to be required for the recruitment and stability of complex components but its activity in this complex has not been linked to its enzymatic activity. ARG82 is not required for the formation of an arginine-dependent protein-DNA complex in vitro so may not be a component of the mature complex.","predictedComplex":false,"interactors":[{"ac":"EBI-10528","identifier":"P11746","identifierLink":"https://www.uniprot.org/uniprotkb/P11746/entry","name":"MCM1","description":"Pheromone receptor transcription factor","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR48019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2828","identifier":"P07249","identifierLink":"https://www.uniprot.org/uniprotkb/P07249/entry","name":"ARG80","description":"Arginine metabolism regulation protein I","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR48019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2835","identifier":"P05085","identifierLink":"https://www.uniprot.org/uniprotkb/P05085/entry","name":"ARG81","description":"Arginine metabolism regulation protein II","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31069","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2842","identifier":"P07250","identifierLink":"https://www.uniprot.org/uniprotkb/P07250/entry","name":"ARG82","description":"Inositol polyphosphate multikinase","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12400","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1153","complexName":"BLOC-1 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Endosomal Rab-GAP (GTPase-activating protein) adapter complex which controls the lifetime of active Rab5/Vps21 and thus endosomal maturation along the endocytic pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-22275","identifier":"P40003","identifierLink":"https://www.uniprot.org/uniprotkb/P40003/entry","name":"VAB2","description":"Biogenesis of lysosome-related organelles complex 1 subunit VAB2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-23841","identifier":"P53158","identifierLink":"https://www.uniprot.org/uniprotkb/P53158/entry","name":"KXD1","description":"Biogenesis of lysosome-related organelles complex 1 subunit KXD1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR37787","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26722","identifier":"P35727","identifierLink":"https://www.uniprot.org/uniprotkb/P35727/entry","name":"BLI1","description":"Biogenesis of lysosome-related organelles complex 1 subunit BLI1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-28775","identifier":"P48232","identifierLink":"https://www.uniprot.org/uniprotkb/P48232/entry","name":"SNN1","description":"Biogenesis of lysosome-related organelles complex 1 subunit SNN1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-31100","identifier":"Q06333","identifierLink":"https://www.uniprot.org/uniprotkb/Q06333/entry","name":"CNL1","description":"Biogenesis of lysosome-related organelles complex 1 subunit CNL1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR39145","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3700144","identifier":"Q06071","identifierLink":"https://www.uniprot.org/uniprotkb/Q06071/entry","name":"BLS1","description":"Biogenesis of lysosome-related organelles complex 1 subunit BLS1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1154","complexName":"CPAP-STIL complex","organismName":"Danio rerio; 7955","description":"A protein complex that is required for centriole biogenesis and duplication. \r\n\r\nDuring procentriole formation during G1/S transition, PKL4 (Q7ZVS3) activates STIL by phosphorylating its STAN domain, then activated STIL loads SASS6 and CENPJ (CPAP) to the base of the procentriole to initiate procentriole assembly. Together with CEP135 (Q5RG45), CENPJ and SASS6 form the central scaffolding of the 9-fold symmetry of the procentriole. \r\n\r\nIn the assembled centriole 9 homodimers of SASS6 form the central waggon wheel while CEP135 and CENPJ connect SASS6 to the microtubules. \r\n\r\nLack of the complex or any of its subunits leads to a loss of centriole formation or spindle formation while overexpression leads to overly long centrioles.","predictedComplex":false,"interactors":[{"ac":"EBI-15182913","identifier":"E7FCY1","identifierLink":"https://www.uniprot.org/uniprotkb/E7FCY1/entry","name":"cpap","description":"Centrosomal P4.1-associated protein","stochiometry":null,"interactorType":"protein","organismName":"Danio rerio; 7955","xrefs":[{"identifier":"PTHR10331","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15182936","identifier":"Q8JGS1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8JGS1/entry","name":"stil","description":"SCL-interrupting locus protein homolog","stochiometry":null,"interactorType":"protein","organismName":"Danio rerio; 7955","xrefs":[{"identifier":"PTHR15128","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15188527","identifier":"Q7ZVT3","identifierLink":"https://www.uniprot.org/uniprotkb/Q7ZVT3/entry","name":"sass6","description":"Spindle assembly abnormal protein 6 homolog","stochiometry":null,"interactorType":"protein","organismName":"Danio rerio; 7955","xrefs":[{"identifier":"PTHR44281","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1155","complexName":"CoQ biosynthetic complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for the synthesis of Coenzyme Q (CoQ), an isoprenylated benzoquinone which functions as an electron carrier from complex I or II to complex III in the inner mitochondrial membrane and which also acts as an antioxidant  preventing the oxidation of lipoproteins and the plasma membrane. Assembly of the complex appears to be triggered by 4-hydroxyl-3-hexaprenyl benzoate (HHB) which is a precursor of CoQ.","predictedComplex":false,"interactors":[{"ac":"EBI-11472102","identifier":"CHEBI:24875","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:24875","name":"iron cation","description":"iron cation","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-36932","identifier":"Q05779","identifierLink":"https://www.uniprot.org/uniprotkb/Q05779/entry","name":"COQ9","description":"Ubiquinone biosynthesis protein COQ9, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21427","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4048","identifier":"P41735","identifierLink":"https://www.uniprot.org/uniprotkb/P41735/entry","name":"CAT5","description":"5-demethoxyubiquinone hydroxylase, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11237","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4924","identifier":"P27680","identifierLink":"https://www.uniprot.org/uniprotkb/P27680/entry","name":"COQ3","description":"Ubiquinone biosynthesis O-methyltransferase, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43464","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4930","identifier":"O13525","identifierLink":"https://www.uniprot.org/uniprotkb/O13525/entry","name":"COQ4","description":"Ubiquinone biosynthesis protein COQ4, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12922","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4937","identifier":"P49017","identifierLink":"https://www.uniprot.org/uniprotkb/P49017/entry","name":"COQ5","description":"2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43591","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4943","identifier":"P53318","identifierLink":"https://www.uniprot.org/uniprotkb/P53318/entry","name":"COQ6","description":"Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43876","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1156","complexName":"Central kinetochore CTF19 complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Present in the central kinetochore, where is appears to play a role in the enhancement of cohesin in the pericentromere. May help to mediate the attachment of the centromere to the mitotic spindle by forming interactions between the microtubule-associated outer kinetochore proteins and the centromere-associated inner kinetochore proteins. The COMA subcomplex proteins (CPX-1187) bind to the inner kinetochore proteins whilst the more peripheral proteins do not. Several of the subunits (IML3, CHL4, CTF19, MCM21, CTF3, MCM16 and MCM22) appear to be non-essential although their absence has a significant role in chromosome segregation in meiosis and more limited effects during mitosis. MTW1 is only present in low levels so may only associate with the complex.","predictedComplex":false,"interactors":[{"ac":"EBI-11606","identifier":"P39731","identifierLink":"https://www.uniprot.org/uniprotkb/P39731/entry","name":"MTW1","description":"Kinetochore-associated protein MTW1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1549796","identifier":"CPX-1187","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-1187","name":"COMA complex","description":"COMA complex","stochiometry":null,"interactorType":"stable complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-21579","identifier":"P38265","identifierLink":"https://www.uniprot.org/uniprotkb/P38265/entry","name":"IML3","description":"Inner kinetochore subunit IML3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-25691","identifier":"P47167","identifierLink":"https://www.uniprot.org/uniprotkb/P47167/entry","name":"MCM22","description":"Inner kinetochore subunit MCM22","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-30457","identifier":"Q12748","identifierLink":"https://www.uniprot.org/uniprotkb/Q12748/entry","name":"CTF3","description":"Inner kinetochore subunit CTF3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-31487","identifier":"Q12262","identifierLink":"https://www.uniprot.org/uniprotkb/Q12262/entry","name":"MCM16","description":"Inner kinetochore subunit MCM16","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-34256","identifier":"Q06162","identifierLink":"https://www.uniprot.org/uniprotkb/Q06162/entry","name":"NKP2","description":"Inner kinetochore subunit NKP2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28064","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-35840","identifier":"Q12493","identifierLink":"https://www.uniprot.org/uniprotkb/Q12493/entry","name":"NKP1","description":"Inner kinetochore subunit NKP1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-4606","identifier":"P38907","identifierLink":"https://www.uniprot.org/uniprotkb/P38907/entry","name":"CHL4","description":"Inner kinetochore subunit CHL4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1157","complexName":"CUL8-MMS1-MMS22-ESC4 E3 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Ubiquitin ligase complex required for the ubiquition of acetylated histone H3, thus facilitating nucleosome assembly during replication and promoting replication progression during S-phase. RTT107 may recruit and help load the complex onto a DNA damage site at or near a stalled replication fork.","predictedComplex":false,"interactors":[{"ac":"EBI-24788","identifier":"P38850","identifierLink":"https://www.uniprot.org/uniprotkb/P38850/entry","name":"RTT107","description":"Regulator of Ty1 transposition protein 107","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47667","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25861","identifier":"P47050","identifierLink":"https://www.uniprot.org/uniprotkb/P47050/entry","name":"RTT101","description":"Cullin-8","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31156","identifier":"Q06164","identifierLink":"https://www.uniprot.org/uniprotkb/Q06164/entry","name":"MMS22","description":"E3 ubiquitin-protein ligase substrate receptor MMS22","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28122","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31686","identifier":"Q08273","identifierLink":"https://www.uniprot.org/uniprotkb/Q08273/entry","name":"HRT1","description":"RING-box protein HRT1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-38894","identifier":"Q06211","identifierLink":"https://www.uniprot.org/uniprotkb/Q06211/entry","name":"MMS1","description":"E3 ubiquitin-protein ligase linker protein MMS1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1158","complexName":"GABA-B receptor complex","organismName":"Caenorhabditis elegans; 6239","description":"G-protein-coupled, metabotropic transmembrane receptor for gamma-aminobutyric acid (GABA). Within the heterodimeric GABA receptor, only gbb-1 seems to bind agonists, while gbb-2 mediates coupling to G proteins. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis. Plays a critical role in the fine-tuning of inhibitory synaptic transmission. Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials. May couple to the G(o) alpha G-protein goa-1 (P51875) to negatively regulate cholinergic receptor activity in the presence of high levels of acetylcholine in ventral cord motor neurons. As acetylcholine depolarizes body wall muscles, modulation of acetylcholine levels most likely results in the control of locomotory behavior.","predictedComplex":false,"interactors":[{"ac":"EBI-15188139","identifier":"H2L0Q3","identifierLink":"https://www.uniprot.org/uniprotkb/H2L0Q3/entry","name":"gbb-1","description":"Gamma-aminobutyric acid type B receptor subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10519","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15188159","identifier":"G5ECB2","identifierLink":"https://www.uniprot.org/uniprotkb/G5ECB2/entry","name":"gbb-2","description":"Gamma-aminobutyric acid type B receptor subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10519","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1159","complexName":"CPAP-STIL complex","organismName":"Homo sapiens; 9606","description":"A protein complex that is required for centriole biogenesis and duplication. \r\n\r\nDuring procentriole formation during G1/S transition, PKL4 (O00444) activates STIL by phosphorylating its STAN domain, then activated STIL loads SASS6 and CENPJ (CPAP) to the base of the procentriole to initiate procentriole assembly. Together with CEP135 (Q66GS9), CENPJ and SASS6 form the central scaffolding of the 9-fold symmetry of the procentriole. \r\n\r\nIn the assembled centriole 9 homodimers of SASS6 form the central waggon wheel while CEP135 and CENPJ connect SASS6 to the microtubules. \r\n\r\nLack of the complex or any of its subunits leads to a loss of centriole formation or spindle formation while overexpression leads to overly long centrioles. Patients with autosomal recessive primary microcephaly often present with aberrant spindle positioning in progenitor cells during brain development and mutations in CENPJ or STIL.","predictedComplex":false,"interactors":[{"ac":"EBI-1570153","identifier":"Q6UVJ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6UVJ0/entry","name":"SASS6","description":"Spindle assembly abnormal protein 6 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44281","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7488405","identifier":"Q15468","identifierLink":"https://www.uniprot.org/uniprotkb/Q15468/entry","name":"STIL","description":"SCL-interrupting locus protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15128","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-946194","identifier":"Q9HC77","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HC77/entry","name":"CPAP","description":"Centrosomal P4.1-associated protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10331","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1160","complexName":"CEP152-PLK4 complex","organismName":"Mus musculus; 10090","description":"A protein complex essential for centriole biogenesis; temporarily part of the procentriole to which it recruits further proteins involved in procentriole formation. Snatches PLK4 away from CEP192-PLK4 complex (CPX-1298). \r\n\r\nImpairment of centriole duplication eventually leads to impaired spindle formation and mitosis which is linked to tumorigenesis.","predictedComplex":false,"interactors":[{"ac":"EBI-2552433","identifier":"Q64702","identifierLink":"https://www.uniprot.org/uniprotkb/Q64702/entry","name":"Plk4","description":"Serine/threonine-protein kinase PLK4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24345","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2554268","identifier":"A2AUM9","identifierLink":"https://www.uniprot.org/uniprotkb/A2AUM9/entry","name":"Cep152","description":"Centrosomal protein of 152 kDa","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10337","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1161","complexName":"CEP192-PLK4 complex","organismName":"Homo sapiens; 9606","description":"A protein complex essential for centriole biogenesis; temporarily part of the procentriole to which it recruits further proteins involved in procentriole formation. PLK4 is snatched away from CEP192 (O94986) by CEP152 forming CEP152-PLK4 complex (CPX-1160). \r\n\r\nImpairment of centriole duplication eventually leads to impaired spindle formation and mitosis which is linked to tumorigenesis.","predictedComplex":false,"interactors":[{"ac":"EBI-2339778","identifier":"Q8TEP8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TEP8/entry","name":"CEP192","description":"Centrosomal protein of 192 kDa","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16029","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-746202","identifier":"O00444","identifierLink":"https://www.uniprot.org/uniprotkb/O00444/entry","name":"PLK4","description":"Serine/threonine-protein kinase PLK4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24345","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1163","complexName":"WASH complex, variant WASHC1/WASHC2C","organismName":"Homo sapiens; 9606","description":"Acts as a nucleation-promoting factor to stimulate the Arp2/3 complex to mediate actin polymerisation and create patches of actin filaments on early endosomes that may be involved in the production and/or scission of endosomal tubules. The complex is required for the trafficking of specific  proteins as actin filaments also mediate myosin-driven short-range movement of proteins within endosomal compartments. The WASH complex is recruited to endosomes by the retromer complex. WASH genes duplicated to multiple chromosomal ends during evolution, and the WASH repertoire of humans, and therefore the number of complex variants, may vary among individuals.","predictedComplex":false,"interactors":[{"ac":"EBI-2563783","identifier":"Q2M389","identifierLink":"https://www.uniprot.org/uniprotkb/Q2M389/entry","name":"WASHC4","description":"WASH complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31409","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2563794","identifier":"Q12768","identifierLink":"https://www.uniprot.org/uniprotkb/Q12768/entry","name":"WASHC5","description":"WASH complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6160405","identifier":"A8K0Z3","identifierLink":"https://www.uniprot.org/uniprotkb/A8K0Z3/entry","name":"WASHC1","description":"WASH complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23331","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712969","identifier":"Q9Y3C0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3C0/entry","name":"WASHC3","description":"WASH complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13015","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-948957","identifier":"Q9Y4E1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4E1/entry","name":"WASHC2C","description":"WASH complex subunit 2C","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1164","complexName":"SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nRegulates cell differentiation in several lineages, such as T cells and myocytes, and specific variants exist in embryonic stem cells (esBAF) and neuronal progenitor cells (npBAF). \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional repression is probably driven by the presence of the ARID1A subunit. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, SMARCA2/BRM (this complex) and SMARCA4/BRG1 (CPX-1204) do not co-occur in the same complex. SMARCD1 (BAF60A) and SMARCD2 (BAF60B) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: DPF2/BAF45D (Q92785), BRD9 (Q9H8M2), SS18 (Q15532), BCL11A (Q9H165), BCL11B (Q9C0K0), BCL7A (Q4VC05), BCL7B (Q9BQE9), BCL7C (Q8WUZ0). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355018","identifier":"O96019","identifierLink":"https://www.uniprot.org/uniprotkb/O96019/entry","name":"ACTL6A","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358441","identifier":"Q92925","identifierLink":"https://www.uniprot.org/uniprotkb/Q92925/entry","name":"SMARCD2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465496","identifier":"Q6STE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6STE5/entry","name":"SMARCD3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-637887","identifier":"O14497","identifierLink":"https://www.uniprot.org/uniprotkb/O14497/entry","name":"ARID1A","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679562","identifier":"P51531","identifierLink":"https://www.uniprot.org/uniprotkb/P51531/entry","name":"SMARCA2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1165","complexName":"CUL8-MMS1-MMS22-CTF4 E3 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Ubiquitin ligase complex required for the ubiquition of acetylated histone H3, thus facilitating nucleosome assembly during replication and promoting replication progression during S-phase. CTF4 is a component of the replisome, and may retain the CUL8 complex at a stalled replication fork.","predictedComplex":false,"interactors":[{"ac":"EBI-25861","identifier":"P47050","identifierLink":"https://www.uniprot.org/uniprotkb/P47050/entry","name":"RTT101","description":"Cullin-8","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31156","identifier":"Q06164","identifierLink":"https://www.uniprot.org/uniprotkb/Q06164/entry","name":"MMS22","description":"E3 ubiquitin-protein ligase substrate receptor MMS22","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28122","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31686","identifier":"Q08273","identifierLink":"https://www.uniprot.org/uniprotkb/Q08273/entry","name":"HRT1","description":"RING-box protein HRT1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-38894","identifier":"Q06211","identifierLink":"https://www.uniprot.org/uniprotkb/Q06211/entry","name":"MMS1","description":"E3 ubiquitin-protein ligase linker protein MMS1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-5209","identifier":"Q01454","identifierLink":"https://www.uniprot.org/uniprotkb/Q01454/entry","name":"CTF4","description":"DNA polymerase alpha-binding protein","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1166","complexName":"CUL8-MMS1-ESC2 E3 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Ubiquitin ligase complex that may play a role in transcriptional silencing at telomeric, rDNA and homothallic mating loci.","predictedComplex":false,"interactors":[{"ac":"EBI-25861","identifier":"P47050","identifierLink":"https://www.uniprot.org/uniprotkb/P47050/entry","name":"RTT101","description":"Cullin-8","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31686","identifier":"Q08273","identifierLink":"https://www.uniprot.org/uniprotkb/Q08273/entry","name":"HRT1","description":"RING-box protein HRT1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-33799","identifier":"Q06340","identifierLink":"https://www.uniprot.org/uniprotkb/Q06340/entry","name":"ESC2","description":"Protein ESC2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-38894","identifier":"Q06211","identifierLink":"https://www.uniprot.org/uniprotkb/Q06211/entry","name":"MMS1","description":"E3 ubiquitin-protein ligase linker protein MMS1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1167","complexName":"CUL8-MMS1-ORC5 E3 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A ubiquitin ligase complex that may be involved in regulation of DNA replication origins.","predictedComplex":false,"interactors":[{"ac":"EBI-12584","identifier":"P50874","identifierLink":"https://www.uniprot.org/uniprotkb/P50874/entry","name":"ORC5","description":"Origin recognition complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12705","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25861","identifier":"P47050","identifierLink":"https://www.uniprot.org/uniprotkb/P47050/entry","name":"RTT101","description":"Cullin-8","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31686","identifier":"Q08273","identifierLink":"https://www.uniprot.org/uniprotkb/Q08273/entry","name":"HRT1","description":"RING-box protein HRT1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-38894","identifier":"Q06211","identifierLink":"https://www.uniprot.org/uniprotkb/Q06211/entry","name":"MMS1","description":"E3 ubiquitin-protein ligase linker protein MMS1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1168","complexName":"WASH complex, variant WASH2P/WASHC2C","organismName":"Homo sapiens; 9606","description":"Acts as a nucleation-promoting factor to stimulate the Arp2/3 complex to mediate actin polymerisation and create patches of actin filaments on early endosomes that may be involved in the production and/or scission of endosomal tubules. The complex is required for the trafficking of specific  proteins as actin filaments also mediate myosin-driven short-range movement of proteins within endosomal compartments. The WASH complex is recruited to endosomes by the retromer complex. WASH genes duplicated to multiple chromosomal ends during evolution, and the WASH repertoire of humans, and therefore the number of complex variants, may vary among individuals.","predictedComplex":false,"interactors":[{"ac":"EBI-2563783","identifier":"Q2M389","identifierLink":"https://www.uniprot.org/uniprotkb/Q2M389/entry","name":"WASHC4","description":"WASH complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31409","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2563794","identifier":"Q12768","identifierLink":"https://www.uniprot.org/uniprotkb/Q12768/entry","name":"WASHC5","description":"WASH complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2870122","identifier":"Q6VEQ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6VEQ5/entry","name":"WASH2P","description":"WAS protein family homolog 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23331","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712969","identifier":"Q9Y3C0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3C0/entry","name":"WASHC3","description":"WASH complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13015","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-948957","identifier":"Q9Y4E1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4E1/entry","name":"WASHC2C","description":"WASH complex subunit 2C","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1169","complexName":"WASH complex, variant WASH3P/WASHC2C","organismName":"Homo sapiens; 9606","description":"Acts as a nucleation-promoting factor to stimulate the Arp2/3 complex to mediate actin polymerisation and create patches of actin filaments on early endosomes that may be involved in the production and/or scission of endosomal tubules. The complex is required for the trafficking of specific  proteins as actin filaments also mediate myosin-driven short-range movement of proteins within endosomal compartments. The WASH complex is recruited to endosomes by the retromer complex. WASH genes duplicated to multiple chromosomal ends during evolution, and the WASH repertoire of humans, and therefore the number of complex variants, may vary among individuals.","predictedComplex":false,"interactors":[{"ac":"EBI-11603347","identifier":"C4AMC7","identifierLink":"https://www.uniprot.org/uniprotkb/C4AMC7/entry","name":"WASH3P","description":"Putative WAS protein family homolog 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23331","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2563783","identifier":"Q2M389","identifierLink":"https://www.uniprot.org/uniprotkb/Q2M389/entry","name":"WASHC4","description":"WASH complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31409","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2563794","identifier":"Q12768","identifierLink":"https://www.uniprot.org/uniprotkb/Q12768/entry","name":"WASHC5","description":"WASH complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712969","identifier":"Q9Y3C0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3C0/entry","name":"WASHC3","description":"WASH complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13015","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-948957","identifier":"Q9Y4E1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4E1/entry","name":"WASHC2C","description":"WASH complex subunit 2C","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1170","complexName":"WASH complex, variant WASH4P/WASHC2C","organismName":"Homo sapiens; 9606","description":"Acts as a nucleation-promoting factor to stimulate the Arp2/3 complex to mediate actin polymerisation and create patches of actin filaments on early endosomes that may be involved in the production and/or scission of endosomal tubules. The complex is required for the trafficking of specific  proteins as actin filaments also mediate myosin-driven short-range movement of proteins within endosomal compartments. The WASH complex is recruited to endosomes by the retromer complex. WASH genes duplicated to multiple chromosomal ends during evolution, and the WASH repertoire of humans, and therefore the number of complex variants, may vary among individuals.","predictedComplex":false,"interactors":[{"ac":"EBI-15483511","identifier":"A8MWX3","identifierLink":"https://www.uniprot.org/uniprotkb/A8MWX3/entry","name":"WASH4P","description":"Putative WAS protein family homolog 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23331","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2563783","identifier":"Q2M389","identifierLink":"https://www.uniprot.org/uniprotkb/Q2M389/entry","name":"WASHC4","description":"WASH complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31409","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2563794","identifier":"Q12768","identifierLink":"https://www.uniprot.org/uniprotkb/Q12768/entry","name":"WASHC5","description":"WASH complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712969","identifier":"Q9Y3C0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3C0/entry","name":"WASHC3","description":"WASH complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13015","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-948957","identifier":"Q9Y4E1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4E1/entry","name":"WASHC2C","description":"WASH complex subunit 2C","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1171","complexName":"WASH complex, variant WASH6P/WASHC2C","organismName":"Homo sapiens; 9606","description":"Acts as a nucleation-promoting factor to stimulate the Arp2/3 complex to mediate actin polymerisation and create patches of actin filaments on early endosomes that may be involved in the production and/or scission of endosomal tubules. The complex is required for the trafficking of specific  proteins as actin filaments also mediate myosin-driven short-range movement of proteins within endosomal compartments. The WASH complex is recruited to endosomes by the retromer complex. WASH genes duplicated to multiple chromosomal ends during evolution, and the WASH repertoire of humans, and therefore the number of complex variants, may vary among individuals.","predictedComplex":false,"interactors":[{"ac":"EBI-2563783","identifier":"Q2M389","identifierLink":"https://www.uniprot.org/uniprotkb/Q2M389/entry","name":"WASHC4","description":"WASH complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31409","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2563794","identifier":"Q12768","identifierLink":"https://www.uniprot.org/uniprotkb/Q12768/entry","name":"WASHC5","description":"WASH complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712969","identifier":"Q9Y3C0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3C0/entry","name":"WASHC3","description":"WASH complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13015","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-948957","identifier":"Q9Y4E1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4E1/entry","name":"WASHC2C","description":"WASH complex subunit 2C","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9846564","identifier":"Q9NQA3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NQA3/entry","name":"WASH6P","description":"WAS protein family homolog 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23331","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1172","complexName":"WASH complex, variant WASHC1/WASHC2A","organismName":"Homo sapiens; 9606","description":"Acts as a nucleation-promoting factor to stimulate the Arp2/3 complex to mediate actin polymerisation and create patches of actin filaments on early endosomes that may be involved in the production and/or scission of endosomal tubules. The complex is required for the trafficking of specific  proteins as actin filaments also mediate myosin-driven short-range movement of proteins within endosomal compartments. The WASH complex is recruited to endosomes by the retromer complex. WASH genes duplicated to multiple chromosomal ends during evolution, and the WASH repertoire of humans, and therefore the number of complex variants, may vary among individuals.","predictedComplex":false,"interactors":[{"ac":"EBI-2563783","identifier":"Q2M389","identifierLink":"https://www.uniprot.org/uniprotkb/Q2M389/entry","name":"WASHC4","description":"WASH complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31409","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2563794","identifier":"Q12768","identifierLink":"https://www.uniprot.org/uniprotkb/Q12768/entry","name":"WASHC5","description":"WASH complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2870155","identifier":"Q641Q2","identifierLink":"https://www.uniprot.org/uniprotkb/Q641Q2/entry","name":"WASHC2A","description":"WASH complex subunit 2A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6160405","identifier":"A8K0Z3","identifierLink":"https://www.uniprot.org/uniprotkb/A8K0Z3/entry","name":"WASHC1","description":"WASH complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23331","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712969","identifier":"Q9Y3C0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3C0/entry","name":"WASHC3","description":"WASH complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13015","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1173","complexName":"WASH complex, variant WASH2P/WASHC2A","organismName":"Homo sapiens; 9606","description":"Acts as a nucleation-promoting factor to stimulate the Arp2/3 complex to mediate actin polymerisation and create patches of actin filaments on early endosomes that may be involved in the production and/or scission of endosomal tubules. The complex is required for the trafficking of specific  proteins as actin filaments also mediate myosin-driven short-range movement of proteins within endosomal compartments. The WASH complex is recruited to endosomes by the retromer complex. WASH genes duplicated to multiple chromosomal ends during evolution, and the WASH repertoire of humans, and therefore the number of complex variants, may vary among individuals.","predictedComplex":false,"interactors":[{"ac":"EBI-2563783","identifier":"Q2M389","identifierLink":"https://www.uniprot.org/uniprotkb/Q2M389/entry","name":"WASHC4","description":"WASH complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31409","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2563794","identifier":"Q12768","identifierLink":"https://www.uniprot.org/uniprotkb/Q12768/entry","name":"WASHC5","description":"WASH complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2870122","identifier":"Q6VEQ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6VEQ5/entry","name":"WASH2P","description":"WAS protein family homolog 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23331","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2870155","identifier":"Q641Q2","identifierLink":"https://www.uniprot.org/uniprotkb/Q641Q2/entry","name":"WASHC2A","description":"WASH complex subunit 2A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712969","identifier":"Q9Y3C0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3C0/entry","name":"WASHC3","description":"WASH complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13015","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1174","complexName":"WASH complex, variant WASH3P/WASHC2A","organismName":"Homo sapiens; 9606","description":"Acts as a nucleation-promoting factor to stimulate the Arp2/3 complex to mediate actin polymerisation and create patches of actin filaments on early endosomes that may be involved in the production and/or scission of endosomal tubules. The complex is required for the trafficking of specific  proteins as actin filaments also mediate myosin-driven short-range movement of proteins within endosomal compartments. The WASH complex is recruited to endosomes by the retromer complex. WASH genes duplicated to multiple chromosomal ends during evolution, and the WASH repertoire of humans, and therefore the number of complex variants, may vary among individuals.","predictedComplex":false,"interactors":[{"ac":"EBI-11603347","identifier":"C4AMC7","identifierLink":"https://www.uniprot.org/uniprotkb/C4AMC7/entry","name":"WASH3P","description":"Putative WAS protein family homolog 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23331","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2563783","identifier":"Q2M389","identifierLink":"https://www.uniprot.org/uniprotkb/Q2M389/entry","name":"WASHC4","description":"WASH complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31409","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2563794","identifier":"Q12768","identifierLink":"https://www.uniprot.org/uniprotkb/Q12768/entry","name":"WASHC5","description":"WASH complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2870155","identifier":"Q641Q2","identifierLink":"https://www.uniprot.org/uniprotkb/Q641Q2/entry","name":"WASHC2A","description":"WASH complex subunit 2A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712969","identifier":"Q9Y3C0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3C0/entry","name":"WASHC3","description":"WASH complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13015","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1175","complexName":"WASH complex, variant WASH4P/WASHC2A","organismName":"Homo sapiens; 9606","description":"Acts as a nucleation-promoting factor to stimulate the Arp2/3 complex to mediate actin polymerisation and create patches of actin filaments on early endosomes that may be involved in the production and/or scission of endosomal tubules. The complex is required for the trafficking of specific  proteins as actin filaments also mediate myosin-driven short-range movement of proteins within endosomal compartments. The WASH complex is recruited to endosomes by the retromer complex. WASH genes duplicated to multiple chromosomal ends during evolution, and the WASH repertoire of humans, and therefore the number of complex variants, may vary among individuals.","predictedComplex":false,"interactors":[{"ac":"EBI-15483511","identifier":"A8MWX3","identifierLink":"https://www.uniprot.org/uniprotkb/A8MWX3/entry","name":"WASH4P","description":"Putative WAS protein family homolog 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23331","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2563783","identifier":"Q2M389","identifierLink":"https://www.uniprot.org/uniprotkb/Q2M389/entry","name":"WASHC4","description":"WASH complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31409","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2563794","identifier":"Q12768","identifierLink":"https://www.uniprot.org/uniprotkb/Q12768/entry","name":"WASHC5","description":"WASH complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2870155","identifier":"Q641Q2","identifierLink":"https://www.uniprot.org/uniprotkb/Q641Q2/entry","name":"WASHC2A","description":"WASH complex subunit 2A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712969","identifier":"Q9Y3C0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3C0/entry","name":"WASHC3","description":"WASH complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13015","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1176","complexName":"WASH complex, variant WASH6P/WASHC2A","organismName":"Homo sapiens; 9606","description":"Acts as a nucleation-promoting factor to stimulate the Arp2/3 complex to mediate actin polymerisation and create patches of actin filaments on early endosomes that may be involved in the production and/or scission of endosomal tubules. The complex is required for the trafficking of specific  proteins as actin filaments also mediate myosin-driven short-range movement of proteins within endosomal compartments. The WASH complex is recruited to endosomes by the retromer complex. WASH genes duplicated to multiple chromosomal ends during evolution, and the WASH repertoire of humans, and therefore the number of complex variants, may vary among individuals.","predictedComplex":false,"interactors":[{"ac":"EBI-2563783","identifier":"Q2M389","identifierLink":"https://www.uniprot.org/uniprotkb/Q2M389/entry","name":"WASHC4","description":"WASH complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31409","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2563794","identifier":"Q12768","identifierLink":"https://www.uniprot.org/uniprotkb/Q12768/entry","name":"WASHC5","description":"WASH complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2870155","identifier":"Q641Q2","identifierLink":"https://www.uniprot.org/uniprotkb/Q641Q2/entry","name":"WASHC2A","description":"WASH complex subunit 2A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712969","identifier":"Q9Y3C0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3C0/entry","name":"WASHC3","description":"WASH complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13015","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9846564","identifier":"Q9NQA3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NQA3/entry","name":"WASH6P","description":"WAS protein family homolog 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23331","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1177","complexName":"WASH complex, variant WASHC1/WASHC2","organismName":"Mus musculus; 10090","description":"Acts as a nucleation-promoting factor to stimulate the Arp2/3 complex to mediate actin polymerisation and create patches of actin filaments on early endosomes that may be involved in the production and/or scission of endosomal tubules. The complex is required for the trafficking of specific  proteins as actin filaments also mediate myosin-driven short-range movement of proteins within endosomal compartments. The WASH complex is recruited to endosomes by the retromer complex.","predictedComplex":false,"interactors":[{"ac":"EBI-11566651","identifier":"Q9CR27","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CR27/entry","name":"Washc3","description":"WASH complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13015","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15483722","identifier":"Q3UMB9","identifierLink":"https://www.uniprot.org/uniprotkb/Q3UMB9/entry","name":"Washc4","description":"WASH complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR31409","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15483746","identifier":"Q8C2E7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C2E7/entry","name":"Washc5","description":"WASH complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5298041","identifier":"Q6PGL7","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PGL7/entry","name":"Washc2","description":"WASH complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9075564","identifier":"Q8VDD8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VDD8/entry","name":"Washc1","description":"WASH complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23331","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1178","complexName":"Cytoplasmic dynein complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A microtubule minus end-directed motor complex involved in positioning the mitotic spindle during cell division. Yeast undergoes a closed mitosis, and therefore the nucleus and its mitotic spindle must be positioned across the junction between the mother and bud, termed the bud neck, to provide a set of chromosomes to the daughter cell.  Dynein anchors to the bud end and becomes activated, allowing force generation between the microtubule and the cortex. The microtubule is pulled to slide along the cortex, causing the spindle to move into the mother-bud neck .Chemical transitions (ATP binding, ATP hydrolysis and the release of inorganic phosphate (Pi) and ADP) are coupled to structural changes in the motor, whilst conversely, mechanical events (such as microtubule binding) can influence the rate of chemical transitions.","predictedComplex":false,"interactors":[{"ac":"EBI-27644","identifier":"Q04949","identifierLink":"https://www.uniprot.org/uniprotkb/Q04949/entry","name":"DYN3","description":"Cytoplasmic dynein intermediate light chain DYN3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-30551","identifier":"P40960","identifierLink":"https://www.uniprot.org/uniprotkb/P40960/entry","name":"PAC11","description":"WD repeat-containing protein PAC11","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6230","identifier":"P36022","identifierLink":"https://www.uniprot.org/uniprotkb/P36022/entry","name":"DYN1","description":"Dynein heavy chain, cytoplasmic","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6240","identifier":"Q02647","identifierLink":"https://www.uniprot.org/uniprotkb/Q02647/entry","name":"DYN2","description":"Dynein light chain 1, cytoplasmic","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1179","complexName":"DCS1 decapping scavenger complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"m7G(5')pppN diphosphatase which degrades the 5-prime mRNA cap when the cap is no longer attached to the mRNA body but rather within short capped mRNA fragments that are generated from 3' to 5' mRNA decay. Releases m7GMP. Mononucleoside diphosphates (m7GDP and m3 2,2,7GDP) are not hydrolyzed by the complex, however mononucleoside triphosphates (m7GTP and m3 2,2,7GTP) are, demonstrating the importance of a triphosphate chain for DCS1 hydrolytic activity. Has a high binding affinity for m7GDP, which inhibits the complex, making this mononucleoside diphosphate a potential regulator of cap-dependent cellular processes.","predictedComplex":false,"interactors":[{"ac":"EBI-38973","identifier":"Q06151","identifierLink":"https://www.uniprot.org/uniprotkb/Q06151/entry","name":"DCS1","description":"m7GpppX diphosphatase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12978","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1180","complexName":"Amyloid-beta protein 40 oligomeric complex","organismName":"Homo sapiens; 9606","description":"Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. May have a role in depressing synaptic activity thus preventing excitotoxicity. Influences synaptic plasticity through various receptors, including NMDAR, mGluR and alpha7 nicotinic acetylcholine receptors (CPX-236). Mediates dendritic spine loss leading to decreased synapse density, inhibition of long-term potentiation (LTP), enhancement of long-term depression (LTD), excessive calcium influx, mitochondrial impairment, endoplasmic reticulum stress and activation of apoptotic processes. May bind plasma membrane lipids affecting their stability and leading to cytotoxicity. May affect metal ion homeostasis by chelating synaptic copper, zinc or iron ions. Mostly found in the extracellular space with a small proportion occurring as membrane-bound species. Dimers (CPX-1069) and oligomers of soluble amyloid-beta peptides are the main pathogenic species linked to Alzheimer's disease. Cellular prion protein (PrPC/PRNP, P04156) binds amyloid-beta oligomers mediating their synaptic dysfunction. Insoluble fibrils and plaques form during the latter stages of the disease. Chaperones, such as alphaB-crystallins or clusterin (P10909), bind to misfolded oligomeric species and form long-lived complexes, thereby preventing both their further growth into fibrils and their dissociation into synaptotoxic dimers. \r\n\r\nAmyloid-beta peptide may act as transcription factor for its own precursor protein APP and its cleavage enzyme BACE1 (P56817) initiating a positive feedback mechanism that ultimately leads to amyloidogenesis and Alzheimer's disease.","predictedComplex":false,"interactors":[{"ac":"EBI-2431589","identifier":"P05067-PRO_0000000093","identifierLink":"https://www.uniprot.org/uniprotkb/P05067-PRO_0000000093/entry","name":"APP","description":"Amyloid-beta protein 40","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-1181","complexName":"Amyloid-beta protein 40 oligomeric complex","organismName":"Mus musculus; 10090","description":"Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. May have a role in depressing synaptic activity thus preventing excitotoxicity. Influences synaptic plasticity through various receptors, including NMDAR, mGluR and alpha7 nicotinic acetylcholine receptors (CPX-234). Mediates dendritic spine loss leading to decreased synapse density, inhibition of long-term potentiation (LTP), enhancement of long-term depression (LTD), excessive calcium influx, mitochondrial impairment, endoplasmic reticulum stress and activation of apoptotic processes. May bind plasma membrane lipids affecting their stability and leading to cytotoxicity. May affect metal ion homeostasis by chelating synaptic copper, zinc or iron ions. Mostly found in the extracellular space with a small proportion occurring as membrane-bound species. Dimers (CPX-1106) and oligomers of soluble amyloid-beta peptides are the main pathogenic species linked to Alzheimer's disease. Cellular prion protein (PrPC/PRNP, P04925) binds amyloid-beta oligomers mediating their synaptic dysfunction. Insoluble fibrils and plaques form during the latter stages of the disease. Chaperones, such as alphaB-crystallins or clusterin (Q06890), bind to misfolded oligomeric species and form long-lived complexes, thereby preventing both their further growth into fibrils and their dissociation into synaptotoxic dimers. \r\n\r\nAmyloid-beta peptide may act as transcription factor for its own precursor protein APP and its cleavage enzyme BACE1 (P56818) initiating a positive feedback mechanism that ultimately leads to amyloidogenesis and Alzheimer's disease.","predictedComplex":false,"interactors":[{"ac":"EBI-14022236","identifier":"P12023-PRO_0000000119","identifierLink":"https://www.uniprot.org/uniprotkb/P12023-PRO_0000000119/entry","name":"App","description":"Amyloid-beta protein 40","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-1182","complexName":"Amyloid-beta protein 40 oligomeric complex","organismName":"Rattus norvegicus; 10116","description":"Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. May have a role in depressing synaptic activity thus preventing excitotoxicity. Influences synaptic plasticity through various receptors, including NMDAR, mGluR and alpha7 nicotinic acetylcholine receptors (CPX-233). Mediates dendritic spine loss leading to decreased synapse density, inhibition of long-term potentiation (LTP), enhancement of long-term depression (LTD), excessive calcium influx, mitochondrial impairment, endoplasmic reticulum stress and activation of apoptotic processes. May bind plasma membrane lipids affecting their stability and leading to cytotoxicity. May affect metal ion homeostasis by chelating synaptic copper, zinc or iron ions. Mostly found in the extracellular space with a small proportion occurring as membrane-bound species. Dimers (CPX-1109) and oligomers of soluble amyloid-beta peptides are the main pathogenic species linked to Alzheimer's disease. Cellular prion protein (PrPC/PRNP, P13852) binds amyloid-beta oligomers mediating their synaptic dysfunction. Insoluble fibrils and plaques form during the latter stages of the disease. Chaperones, such as alphaB-crystallins or clusterin (P05371), bind to misfolded oligomeric species and form long-lived complexes, thereby preventing both their further growth into fibrils and their dissociation into synaptotoxic dimers. \r\n\r\nAmyloid-beta peptide may act as transcription factor for its own precursor protein APP and its cleavage enzyme BACE1 (P56819) initiating a positive feedback mechanism that ultimately leads to amyloidogenesis and Alzheimer's disease.","predictedComplex":false,"interactors":[{"ac":"EBI-14022886","identifier":"P08592-PRO_0000000164","identifierLink":"https://www.uniprot.org/uniprotkb/P08592-PRO_0000000164/entry","name":"App","description":"Amyloid-beta protein 40","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-1183","complexName":"Amyloid-beta protein 42 oligomeric complex","organismName":"Rattus norvegicus; 10116","description":"Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. This oligomer of protein 42 only has positive neurogenetic effects by activating synaptic protein kinases. May have a role in depressing synaptic activity thus preventing excitotoxicity. Influences synaptic plasticity through various receptors, including NMDAR, mGluR and alpha7 nicotinic acetylcholine receptors (CPX-233). Mediates dendritic spine loss leading to decreased synapse density, inhibition of long-term potentiation (LTP), enhancement of long-term depression (LTD), excessive calcium influx, mitochondrial impairment, endoplasmic reticulum stress and activation of apoptotic processes. May bind plasma membrane lipids affecting their stability and leading to cytotoxicity. May affect metal ion homeostasis by chelating synaptic copper, zinc or iron ions. Mostly found in the extracellular space with a small proportion occurring as membrane-bound species. Dimers (CPX-1110) and oligomers of soluble amyloid-beta peptides are the main pathogenic species linked to Alzheimer's disease. Cellular prion protein (PrPC/PRNP, P13852) binds amyloid-beta oligomers mediating their synaptic dysfunction. Insoluble fibrils and plaques form during the latter stages of the disease. Chaperones, such as alphaB-crystallins or clusterin (P05371), bind to misfolded oligomeric species and form long-lived complexes, thereby preventing both their further growth into fibrils and their dissociation into synaptotoxic dimers. \r\n\r\nAmyloid-beta peptide may act as transcription factor for its own precursor protein APP and its cleavage enzyme BACE1 (P56819) initiating a positive feedback mechanism that ultimately leads to amyloidogenesis and Alzheimer's disease.","predictedComplex":false,"interactors":[{"ac":"EBI-14022881","identifier":"P08592-PRO_0000000163","identifierLink":"https://www.uniprot.org/uniprotkb/P08592-PRO_0000000163/entry","name":"App","description":"Amyloid-beta protein 42","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-1184","complexName":"Amyloid-beta protein 40/42 oligomeric complex","organismName":"Rattus norvegicus; 10116","description":"Protein complex involved in modulation of signaling and synaptic function in the brain, predominantly in the cerebral cortex and hippocampus. May have a role in depressing synaptic activity thus preventing excitotoxicity. Influences synaptic plasticity through various receptors, including NMDAR, mGluR and alpha7 nicotinic acetylcholine receptors (CPX-233). Mediates dendritic spine loss leading to decreased synapse density, inhibition of long-term potentiation (LTP), enhancement of long-term depression (LTD), excessive calcium influx, mitochondrial impairment, endoplasmic reticulum stress and activation of apoptotic processes. May bind plasma membrane lipids affecting their stability and leading to cytotoxicity. May affect metal ion homeostasis by chelating synaptic copper, zinc or iron ions. Oligomers of protein 42 only may have positive neurogenetic effects by activating synaptic protein kinases. Mostly found in the extracellular space with a small proportion occurring as membrane-bound species. Dimers (CPX-1108) and oligomers of soluble amyloid-beta peptides are the main pathogenic species linked to Alzheimer's disease. Cellular prion protein (PrPC/Prnp, P13852) binds amyloid-beta oligomers mediating their synaptic dysfunction. Insoluble fibrils and plaques form during the latter stages of the disease. Chaperones, such as alphaB-crystallins or clusterin (P05371), bind to misfolded oligomeric species and form long-lived complexes, thereby preventing both their further growth into fibrils and their dissociation into synaptotoxic dimers. \r\n\r\nAmyloid-beta peptide may act as transcription factor for its own precursor protein APP and its cleavage enzyme BACE1 (P56819) initiating a positive feedback mechanism that ultimately leads to amyloidogenesis and Alzheimer's disease.","predictedComplex":false,"interactors":[{"ac":"EBI-14022881","identifier":"P08592-PRO_0000000163","identifierLink":"https://www.uniprot.org/uniprotkb/P08592-PRO_0000000163/entry","name":"App","description":"Amyloid-beta protein 42","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-14022886","identifier":"P08592-PRO_0000000164","identifierLink":"https://www.uniprot.org/uniprotkb/P08592-PRO_0000000164/entry","name":"App","description":"Amyloid-beta protein 40","stochiometry":null,"interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]}]},{"complexAC":"CPX-1185","complexName":"DCS1-DCS2 regulator of decapping scavenger complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"m7G(5')pppN diphosphatase with a kcat/KM value that is significantly lower than that of the Decapping Scavenger complex, DCS1 (CPX-1179) and has almost lost the preference for m7GpppG as a substrate shown by the homodimer. Degrades the 5' mRNA cap, releasing m7GMP, when the cap is no longer attached to the mRNA body but rather within short capped mRNA fragments that are generated from 3' to 5' mRNA decay. DCS2 is only expressed by the cell under conditions of diauxic stress, and the formation of this complex may allow the cell to change the distribution and relative activities of the mRNA decay pathways in the stationary phase cell.","predictedComplex":false,"interactors":[{"ac":"EBI-38701","identifier":"Q12123","identifierLink":"https://www.uniprot.org/uniprotkb/Q12123/entry","name":"DCS2","description":"Inactive diphosphatase DCS2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12978","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-38973","identifier":"Q06151","identifierLink":"https://www.uniprot.org/uniprotkb/Q06151/entry","name":"DCS1","description":"m7GpppX diphosphatase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12978","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1188","complexName":"DPB11-SLD3-SLD2 DNA replication complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Associate with replication origins and promotes loading of DNA polymerases onto the origins to initiate chromosomal DNA replication when cyclin-dependent kinase activity increases at the G1/S cell cycle boundary. May play an active role in assembly or activation of the replication fork CMG helicase (CPX-297) thus playing a role in a critical S phase regulatory mechanism that restricts DNA replication to S phase. Interaction of the complex with with single-stranded DNA may be important for GINS attachment to MCM.","predictedComplex":false,"interactors":[{"ac":"EBI-23925","identifier":"P53135","identifierLink":"https://www.uniprot.org/uniprotkb/P53135/entry","name":"SLD3","description":"DNA replication regulator SLD3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25984","identifier":"P47027","identifierLink":"https://www.uniprot.org/uniprotkb/P47027/entry","name":"DPB11","description":"DNA replication regulator DPB11","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13561","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26824","identifier":"P34252","identifierLink":"https://www.uniprot.org/uniprotkb/P34252/entry","name":"SLD2","description":"DNA replication regulator SLD2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28124","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1189","complexName":"RAD26-DEF1 stalled RNAPII response complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Appears to form in response to DNA damage-stalled RNA polymerase II (RNAPII, CPX-2662), when the stall is persistent such as at DNA lesions. RAD26 appears to protect RNAPII from degradation to allow time for repair. When the lesion cannot be rapidly removed by RAD26-promoted DNA repair, DEF1 enables ubiquitination and proteolysis of RNAPII. The complex may therefore act to coordinate a stalling rescue mechanism driven by the two proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-14687","identifier":"P40352","identifierLink":"https://www.uniprot.org/uniprotkb/P40352/entry","name":"RAD26","description":"DNA repair and recombination protein RAD26","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45629","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26695","identifier":"P35732","identifierLink":"https://www.uniprot.org/uniprotkb/P35732/entry","name":"DEF1","description":"RNA polymerase II degradation factor 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1190","complexName":"TUL1 E3 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"E3 ubiquitin ligase complex required in cells lacking the multivesicular body pathway and under conditions of ubiquitin depletion. Functions in protein homeostasis under non-stress conditions and support a role in protein quality control.","predictedComplex":false,"interactors":[{"ac":"EBI-26635","identifier":"P36096","identifierLink":"https://www.uniprot.org/uniprotkb/P36096/entry","name":"TUL1","description":"Transmembrane E3 ubiquitin-protein ligase 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22763","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31423","identifier":"Q12015","identifierLink":"https://www.uniprot.org/uniprotkb/Q12015/entry","name":"DSC3","description":"DSC E3 ubiquitin ligase complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28049","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32978","identifier":"Q08232","identifierLink":"https://www.uniprot.org/uniprotkb/Q08232/entry","name":"DSC2","description":"DSC E3 ubiquitin ligase complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-35335","identifier":"Q12229","identifierLink":"https://www.uniprot.org/uniprotkb/Q12229/entry","name":"UBX3","description":"UBX domain-containing protein 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23322","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1191","complexName":"Global genome repair CUL3-RAD7-RAD16-ELC1 ubiquitin ligase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A ubiquitin ligase complex required for optimal nucleotide excision repair following UV-induced DNA damage. Ubiquinates the DNA repair protein RAD4 (P14736), targeting it for degradation by the 26S proteasome following UV radiation. de novo protein synthesis subsequently restores RAD4 to pre-irradiation levels.","predictedComplex":false,"interactors":[{"ac":"EBI-14645","identifier":"P31244","identifierLink":"https://www.uniprot.org/uniprotkb/P31244/entry","name":"RAD16","description":"DNA repair protein RAD16","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45626","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14780","identifier":"P06779","identifierLink":"https://www.uniprot.org/uniprotkb/P06779/entry","name":"RAD7","description":"DNA repair protein RAD7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13382","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-23065","identifier":"P53202","identifierLink":"https://www.uniprot.org/uniprotkb/P53202/entry","name":"CUL3","description":"Cullin-3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30154","identifier":"Q03071","identifierLink":"https://www.uniprot.org/uniprotkb/Q03071/entry","name":"ELC1","description":"Elongin-C","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR20648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1194","complexName":"Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to promoters and enhancers of target genes in muscle cells and alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nSWI/SNF complexes containing DPF3 are specific to muscle cells where they play an essential role in the development of heart and skeletal muscle cells. Also found in brown adipocytes where they regulate gene-expression of brown fat-selective genes. \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional repression is probably driven by the presence of the ARID1A subunit. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, SMARCA2/BRM (this complex) and SMARCA4/BRG1 (CPX-1222) do not co-occur in the same complex. SMARCD1 (BAF60A) and SMARCD2 (BAF60B) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: DPF2/BAF45D (Q92785), BRD9 (Q9H8M2), SS18 (Q15532), BCL11A (Q9H165), BCL11B (Q9C0K0), BCL7A (Q4VC05), BCL7B (Q9BQE9), BCL7C (Q8WUZ0). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-16355309","identifier":"Q92784","identifierLink":"https://www.uniprot.org/uniprotkb/Q92784/entry","name":"DPF3","description":"Zinc finger protein DPF3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355018","identifier":"O96019","identifierLink":"https://www.uniprot.org/uniprotkb/O96019/entry","name":"ACTL6A","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358441","identifier":"Q92925","identifierLink":"https://www.uniprot.org/uniprotkb/Q92925/entry","name":"SMARCD2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465496","identifier":"Q6STE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6STE5/entry","name":"SMARCD3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-637887","identifier":"O14497","identifierLink":"https://www.uniprot.org/uniprotkb/O14497/entry","name":"ARID1A","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679562","identifier":"P51531","identifierLink":"https://www.uniprot.org/uniprotkb/P51531/entry","name":"SMARCA2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1195","complexName":"Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nThe embryonic stem cell-specific SWI/SNF complex is critical for self-renewal, maintenance and pluripotency of embryonic stem cells. The lack of subunit ARID1B suggests it primarily acts as a transcriptional repressor but also has the ability to activate some genes. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. The embryonic stem cell-specific (esc-)SWI/SNF complex specifically lacks subunits ACTL6B (O94805), ARID1B (Q8NFD5), SMARCA2 (P51531), SMARCC2 (Q8TAQ2) and SMARCD3 (Q6STE5). SMARCD2 (Q92925) may be present in esc-SWI/SNF complexes in which case it probably forms a variant, replacing SMARCD1. BCL7A, BCL7B and BCL7C have been shown to be part of the esc-SWI/SNF complex but may be mutually exclusive and therefore probably forms further variants.\r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-2560588","identifier":"Q9BQE9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BQE9/entry","name":"BCL7B","description":"B-cell CLL/lymphoma 7 protein family member B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302489","identifier":"P51532","identifierLink":"https://www.uniprot.org/uniprotkb/P51532/entry","name":"SMARCA4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355018","identifier":"O96019","identifierLink":"https://www.uniprot.org/uniprotkb/O96019/entry","name":"ACTL6A","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359917","identifier":"Q4VC05","identifierLink":"https://www.uniprot.org/uniprotkb/Q4VC05/entry","name":"BCL7A","description":"B-cell CLL/lymphoma 7 protein family member A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359932","identifier":"Q92785","identifierLink":"https://www.uniprot.org/uniprotkb/Q92785/entry","name":"DPF2","description":"Zinc finger protein ubi-d4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-637887","identifier":"O14497","identifierLink":"https://www.uniprot.org/uniprotkb/O14497/entry","name":"ARID1A","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-716462","identifier":"Q8WUB8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WUB8/entry","name":"PHF10","description":"PHD finger protein 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7850114","identifier":"Q8WUZ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WUZ0/entry","name":"BCL7C","description":"B-cell CLL/lymphoma 7 protein family member C","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1196","complexName":"Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\npBAF complexes facilitate the ligand-dependant transcriptional activation of target genes by nuclear hormone receptors and regulates cell differentiation, esp. in cardiac development. \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. pBAF exists in two variants, containing either ACTL6A (this complex) or ACTL6B (CPX-1196) subunit. Subunit BRD7 may be restricted to pBAF complexes in embryonic stem cells and not present in differentiated cells. The alternative ATPase, SMARCA2/BRM (P51531), does not occur in the pBAF complexes. SMARCD1 (BAF60A) and SMARCD2 (BAF60B) may not co-occur. It is not clear if BCL7A (Q4VC05), BCL7B (Q9BQE9), BCL7C (Q8WUZ0) or SMARCD3 (Q6STE5) are part of any pBAF variants.\r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-302489","identifier":"P51532","identifierLink":"https://www.uniprot.org/uniprotkb/P51532/entry","name":"SMARCA4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358441","identifier":"Q92925","identifierLink":"https://www.uniprot.org/uniprotkb/Q92925/entry","name":"SMARCD2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-637807","identifier":"Q86U86","identifierLink":"https://www.uniprot.org/uniprotkb/Q86U86/entry","name":"PBRM1","description":"Protein polybromo-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16062","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-637818","identifier":"Q68CP9","identifierLink":"https://www.uniprot.org/uniprotkb/Q68CP9/entry","name":"ARID2","description":"AT-rich interactive domain-containing protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-711221","identifier":"Q9NPI1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPI1/entry","name":"BRD7","description":"Bromodomain-containing protein 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22881","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-716462","identifier":"Q8WUB8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WUB8/entry","name":"PHF10","description":"PHD finger protein 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724528","identifier":"O94805","identifierLink":"https://www.uniprot.org/uniprotkb/O94805/entry","name":"ACTL6B","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1198","complexName":"Gamma tubulin small complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Seeds microtubule nucleation at microtubule-organizing centres, controlling the location and timing of nucleation. Component of the spindle pole body, which is responsible for the nucleation and organisation of microtubules within the cell, thus playing a role in chromosome segregation in mitosis and meiosis and controlling cytoplasmic interphase microtubules. The complex is bound directly to the spindle pole body  by SPC110 (P32380) on the nuclear face and SPC72 (P39723) on the cytoplasmic face.","predictedComplex":false,"interactors":[{"ac":"EBI-17786","identifier":"P38863","identifierLink":"https://www.uniprot.org/uniprotkb/P38863/entry","name":"SPC97","description":"Spindle pole body component SPC97","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19302","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17794","identifier":"P53540","identifierLink":"https://www.uniprot.org/uniprotkb/P53540/entry","name":"SPC98","description":"Spindle pole body component SPC98","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19302","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19013","identifier":"P53378","identifierLink":"https://www.uniprot.org/uniprotkb/P53378/entry","name":"TUB4","description":"Tubulin gamma chain","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-989053","identifier":"CHEBI:15996","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15996","name":"gtp","description":"guanosine triphosphate - GTP","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1199","complexName":"Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\npBAF complexes facilitate the ligand-dependant transcriptional activation of target genes by nuclear hormone receptors and regulates cell differentiation, esp. in cardiac development. \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. pBAF exists in two variants, containing either ACTL6A (CPX-1199) or ACTL6B (CPX-1196) subunit. Subunit BRD7 may be restricted to pBAF complexes in embryonic stem cells and not present in differentiated cells. The alternative ATPase, SMARCA2/BRM (P51531), does not occur in the pBAF complexes. SMARCD1 (BAF60A) and SMARCD2 (BAF60B) may not co-occur. It is not clear if BCL7A (Q4VC05), BCL7B (Q9BQE9), BCL7C (Q8WUZ0) or SMARCD3 (Q6STE5) are part of any pBAF variants.\r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-302489","identifier":"P51532","identifierLink":"https://www.uniprot.org/uniprotkb/P51532/entry","name":"SMARCA4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355018","identifier":"O96019","identifierLink":"https://www.uniprot.org/uniprotkb/O96019/entry","name":"ACTL6A","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358441","identifier":"Q92925","identifierLink":"https://www.uniprot.org/uniprotkb/Q92925/entry","name":"SMARCD2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-637807","identifier":"Q86U86","identifierLink":"https://www.uniprot.org/uniprotkb/Q86U86/entry","name":"PBRM1","description":"Protein polybromo-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16062","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-637818","identifier":"Q68CP9","identifierLink":"https://www.uniprot.org/uniprotkb/Q68CP9/entry","name":"ARID2","description":"AT-rich interactive domain-containing protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-711221","identifier":"Q9NPI1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPI1/entry","name":"BRD7","description":"Bromodomain-containing protein 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22881","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-716462","identifier":"Q8WUB8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WUB8/entry","name":"PHF10","description":"PHD finger protein 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1200","complexName":"RAP1-GCR1 transcription activation complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Transcription factor required for the transcription of ribosomal protein and glycolytic genes. Appears to simultaneously bind to two adjacent DNA elements (UAS(RPG) and the CT box, bound specifically by RAP1 and GCR1, respectively). The complex can activate transcription through isolated UAS(RPG) (upstream activating sequence in (ribosomal protein genes)) but not CT elements.","predictedComplex":false,"interactors":[{"ac":"EBI-14821","identifier":"P11938","identifierLink":"https://www.uniprot.org/uniprotkb/P11938/entry","name":"RAP1","description":"DNA-binding protein RAP1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR16466","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7463","identifier":"P07261","identifierLink":"https://www.uniprot.org/uniprotkb/P07261/entry","name":"GCR1","description":"Glycolytic genes transcriptional activator GCR1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR37784","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1201","complexName":"Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nThe neural progenitor-specific SWI/SNF complex is critical for self-renewal, maintenance and pluripotency of neural progenitor stem cells by selectively activating or repressing its target genes. In this variant of the complex transcriptional repression is probably driven by the presence of the ARID1A subunit. \r\n\r\nDuring neural development a switch from a progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. This process requires a switch of two subunits: ACTL6A is replaced by ACTL6B (O94805) and PHF10 replaced by DPF1 (Q92782) or DPF3 (Q92784) in neuron-specific SWI/SNF complexes. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. Although similar in function to the embryonic stem cell-specific SWI/SNF complex the composition of the neural progenitor-specific SWI/SNF complexes is more similar to the standard SWI/SNF complexes. It is likely that the two ATPases, SMARCA2/BRM (this complex) and SMARCA4/BRG1 (CPX-1212) do not co-occur in the same complex. SMARCD1 (BAF60A) and SMARCD3 (BAF60C) also may not co-occur. It is not clear yet if DPF2/BAF45D (Q92785) is a member of the neural progenitor-specific SWI/SNF complex. \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355018","identifier":"O96019","identifierLink":"https://www.uniprot.org/uniprotkb/O96019/entry","name":"ACTL6A","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465496","identifier":"Q6STE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6STE5/entry","name":"SMARCD3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-637887","identifier":"O14497","identifierLink":"https://www.uniprot.org/uniprotkb/O14497/entry","name":"ARID1A","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679562","identifier":"P51531","identifierLink":"https://www.uniprot.org/uniprotkb/P51531/entry","name":"SMARCA2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-716462","identifier":"Q8WUB8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WUB8/entry","name":"PHF10","description":"PHD finger protein 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1202","complexName":"Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nThe neuron-specific SWI/SNF complex is critical for the proliferation of post-mitotic neurons and regulates genes specific for dendritic growth by binding tightly with CREST (O75177). In this variant of the complex transcriptional repression is probably driven by the presence of the ARID1A subunit. \r\n\r\nDuring neural development a switch from a progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. This process requires a switch of two subunits: ACTL6A (O96019) is replaced by ACTL6B and PHF10 (Q8WUB8) replaced by DPF1 or DPF3 in neuron-specific SWI/SNF complexes. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, SMARCA2/BRM (this complex) and SMARCA4/BRG1 (CPX-1216) do not co-occur in the same complex. SMARCD1 (BAF60A) and SMARCD3 (BAF60C) as well as DPF1 and DPF3 also may not co-occur.  \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-16355309","identifier":"Q92784","identifierLink":"https://www.uniprot.org/uniprotkb/Q92784/entry","name":"DPF3","description":"Zinc finger protein DPF3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465496","identifier":"Q6STE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6STE5/entry","name":"SMARCD3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-637887","identifier":"O14497","identifierLink":"https://www.uniprot.org/uniprotkb/O14497/entry","name":"ARID1A","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679562","identifier":"P51531","identifierLink":"https://www.uniprot.org/uniprotkb/P51531/entry","name":"SMARCA2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724528","identifier":"O94805","identifierLink":"https://www.uniprot.org/uniprotkb/O94805/entry","name":"ACTL6B","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-726953","identifier":"Q92782","identifierLink":"https://www.uniprot.org/uniprotkb/Q92782/entry","name":"DPF1","description":"Zinc finger protein neuro-d4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1203","complexName":"Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nRegulates cell differentiation specifically in post-mitotic brain tissue. In this variant of the complex transcriptional repression is probably driven by the presence of the ARID1A subunit. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, SMARCA2/BRM (this complex) and SMARCA4/BRG1 (CPX-1219) do not co-occur in the same complex. In contrast to the neuron-specific SWI/SNF complex the brain-specific SWI/SNF complex misses core subunit SMARCC1 (Q92922) and alternative subunits ACTL6A (O96019), SMARCD1 (Q96GM5) or SMARCD3 (Q6STE5). May contain pBAF-specific subunit PBRM1 (BAF180, Q86U86).  \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358441","identifier":"Q92925","identifierLink":"https://www.uniprot.org/uniprotkb/Q92925/entry","name":"SMARCD2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-637887","identifier":"O14497","identifierLink":"https://www.uniprot.org/uniprotkb/O14497/entry","name":"ARID1A","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679562","identifier":"P51531","identifierLink":"https://www.uniprot.org/uniprotkb/P51531/entry","name":"SMARCA2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724528","identifier":"O94805","identifierLink":"https://www.uniprot.org/uniprotkb/O94805/entry","name":"ACTL6B","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1204","complexName":"SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nRegulates cell differentiation in several lineages, such as T cells and myocytes, and specific variants exist in embryonic stem cells (esBAF) and neuronal progenitor cells (npBAF). \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional repression is probably driven by the presence of the ARID1A subunit. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, SMARCA2/BRM (CPX-1164) and SMARCA4/BRG1 (this complex) do not co-occur in the same complex. SMARCD1 (BAF60A) and SMARCD2 (BAF60B) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: DPF2/BAF45D (Q92785), BRD9 (Q9H8M2), SS18 (Q15532), BCL11A (Q9H165), BCL11B (Q9C0K0), BCL7A (Q4VC05), BCL7B (Q9BQE9), BCL7C (Q8WUZ0). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-302489","identifier":"P51532","identifierLink":"https://www.uniprot.org/uniprotkb/P51532/entry","name":"SMARCA4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355018","identifier":"O96019","identifierLink":"https://www.uniprot.org/uniprotkb/O96019/entry","name":"ACTL6A","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358441","identifier":"Q92925","identifierLink":"https://www.uniprot.org/uniprotkb/Q92925/entry","name":"SMARCD2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465496","identifier":"Q6STE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6STE5/entry","name":"SMARCD3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-637887","identifier":"O14497","identifierLink":"https://www.uniprot.org/uniprotkb/O14497/entry","name":"ARID1A","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1205","complexName":"SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nRegulates cell differentiation in several lineages, such as T cells and myocytes, and specific variants exist in embryonic stem cells (esBAF) and neuronal progenitor cells (npBAF). \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional activation is probably driven by the presence of the ARID1B subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 &  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, SMARCA2/BRM (this complex) and SMARCA4/BRG1 (P51532) do not co-occur in the same complex. SMARCD1 (BAF60A) and SMARCD2 (BAF60B) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: DPF2/BAF45D (Q92785), BRD9 (Q9H8M2), SS18 (Q15532), BCL11A (Q9H165), BCL11B (Q9C0K0), BCL7A (Q4VC05), BCL7B (Q9BQE9), BCL7C (Q8WUZ0). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355018","identifier":"O96019","identifierLink":"https://www.uniprot.org/uniprotkb/O96019/entry","name":"ACTL6A","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358441","identifier":"Q92925","identifierLink":"https://www.uniprot.org/uniprotkb/Q92925/entry","name":"SMARCD2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465496","identifier":"Q6STE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6STE5/entry","name":"SMARCD3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679562","identifier":"P51531","identifierLink":"https://www.uniprot.org/uniprotkb/P51531/entry","name":"SMARCA2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679921","identifier":"Q8NFD5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NFD5/entry","name":"ARID1B","description":"AT-rich interactive domain-containing protein 1B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1206","complexName":"SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nRegulates cell differentiation in several lineages, such as T cells and myocytes, and specific variants exist in embryonic stem cells (esBAF) and neuronal progenitor cells (npBAF). \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional activation is probably driven by the presence of the ARID1B subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 &  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, SMARCA2/BRM (CPX-1205) and SMARCA4/BRG1 (this complex) do not co-occur in the same complex. SMARCD1 (BAF60A) and SMARCD2 (BAF60B) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: DPF2/BAF45D (Q92785), BRD9 (Q9H8M2), SS18 (Q15532), BCL11A (Q9H165), BCL11B (Q9C0K0), BCL7A (Q4VC05), BCL7B (Q9BQE9), BCL7C (Q8WUZ0). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-302489","identifier":"P51532","identifierLink":"https://www.uniprot.org/uniprotkb/P51532/entry","name":"SMARCA4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355018","identifier":"O96019","identifierLink":"https://www.uniprot.org/uniprotkb/O96019/entry","name":"ACTL6A","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358441","identifier":"Q92925","identifierLink":"https://www.uniprot.org/uniprotkb/Q92925/entry","name":"SMARCD2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465496","identifier":"Q6STE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6STE5/entry","name":"SMARCD3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679921","identifier":"Q8NFD5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NFD5/entry","name":"ARID1B","description":"AT-rich interactive domain-containing protein 1B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1207","complexName":"SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nRegulates cell differentiation in several lineages, such as T cells and myocytes, and specific variants exist in embryonic stem cells (esBAF) and neuronal progenitor cells (npBAF). \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional repression is probably driven by the presence of the ARID1A subunit. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, SMARCA2/BRM (this complex) and SMARCA4/BRG1 (CPX-1209) do not co-occur in the same complex. SMARCD1 (BAF60A) and SMARCD2 (BAF60B) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: DPF2/BAF45D (Q92785), BRD9 (Q9H8M2), SS18 (Q15532), BCL11A (Q9H165), BCL11B (Q9C0K0), BCL7A (Q4VC05), BCL7B (Q9BQE9), BCL7C (Q8WUZ0). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358441","identifier":"Q92925","identifierLink":"https://www.uniprot.org/uniprotkb/Q92925/entry","name":"SMARCD2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465496","identifier":"Q6STE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6STE5/entry","name":"SMARCD3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-637887","identifier":"O14497","identifierLink":"https://www.uniprot.org/uniprotkb/O14497/entry","name":"ARID1A","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679562","identifier":"P51531","identifierLink":"https://www.uniprot.org/uniprotkb/P51531/entry","name":"SMARCA2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724528","identifier":"O94805","identifierLink":"https://www.uniprot.org/uniprotkb/O94805/entry","name":"ACTL6B","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1208","complexName":"Kinesin II motor complex","organismName":"Caenorhabditis elegans; 6239","description":"Motor complex required for intraflagellar transport (IFT) responsible for the formation and maintenance of the cilia. Together with the kinesin motor protein osm-3,  the complex moves along microtubules and is required for anterograde IFT along the middle segment of the sensory neuron cilia.","predictedComplex":false,"interactors":[{"ac":"EBI-16364299","identifier":"G5EEE6","identifierLink":"https://www.uniprot.org/uniprotkb/G5EEE6/entry","name":"kap-1","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR15605","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16364318","identifier":"Q965T6","identifierLink":"https://www.uniprot.org/uniprotkb/Q965T6/entry","name":"klp-20","description":"Kinesin-like protein klp-20","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-320052","identifier":"Q19633","identifierLink":"https://www.uniprot.org/uniprotkb/Q19633/entry","name":"klp-11","description":"Kinesin-like protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1209","complexName":"SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nRegulates cell differentiation in several lineages, such as T cells and myocytes, and specific variants exist in embryonic stem cells (esBAF) and neuronal progenitor cells (npBAF). \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional repression is probably driven by the presence of the ARID1A subunit. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, SMARCA2/BRM (CPX-1207) and SMARCA4/BRG1 (this complex) do not co-occur in the same complex. SMARCD1 (BAF60A) and SMARCD2 (BAF60B) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: DPF2/BAF45D (Q92785), BRD9 (Q9H8M2), SS18 (Q15532), BCL11A (Q9H165), BCL11B (Q9C0K0), BCL7A (Q4VC05), BCL7B (Q9BQE9), BCL7C (Q8WUZ0). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-302489","identifier":"P51532","identifierLink":"https://www.uniprot.org/uniprotkb/P51532/entry","name":"SMARCA4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358441","identifier":"Q92925","identifierLink":"https://www.uniprot.org/uniprotkb/Q92925/entry","name":"SMARCD2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465496","identifier":"Q6STE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6STE5/entry","name":"SMARCD3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-637887","identifier":"O14497","identifierLink":"https://www.uniprot.org/uniprotkb/O14497/entry","name":"ARID1A","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724528","identifier":"O94805","identifierLink":"https://www.uniprot.org/uniprotkb/O94805/entry","name":"ACTL6B","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1210","complexName":"SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nRegulates cell differentiation in several lineages, such as T cells and myocytes, and specific variants exist in embryonic stem cells (esBAF) and neuronal progenitor cells (npBAF). \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional activation is probably driven by the presence of the ARID1B subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 &  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, SMARCA2/BRM (this complex) and SMARCA4/BRG1 (CPX-1211) do not co-occur in the same complex. SMARCD1 (BAF60A) and SMARCD2 (BAF60B) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: DPF2/BAF45D (Q92785), BRD9 (Q9H8M2), SS18 (Q15532), BCL11A (Q9H165), BCL11B (Q9C0K0), BCL7A (Q4VC05), BCL7B (Q9BQE9), BCL7C (Q8WUZ0). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358441","identifier":"Q92925","identifierLink":"https://www.uniprot.org/uniprotkb/Q92925/entry","name":"SMARCD2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465496","identifier":"Q6STE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6STE5/entry","name":"SMARCD3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679562","identifier":"P51531","identifierLink":"https://www.uniprot.org/uniprotkb/P51531/entry","name":"SMARCA2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679921","identifier":"Q8NFD5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NFD5/entry","name":"ARID1B","description":"AT-rich interactive domain-containing protein 1B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724528","identifier":"O94805","identifierLink":"https://www.uniprot.org/uniprotkb/O94805/entry","name":"ACTL6B","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1211","complexName":"SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nRegulates cell differentiation in several lineages, such as T cells and myocytes, and specific variants exist in embryonic stem cells (esBAF) and neuronal progenitor cells (npBAF). \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional activation is probably driven by the presence of the ARID1B subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 &  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, SMARCA2/BRM (CPX-1210) and SMARCA4/BRG1 (this complex) do not co-occur in the same complex. SMARCD1 (BAF60A) and SMARCD2 (BAF60B) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: DPF2/BAF45D (Q92785), BRD9 (Q9H8M2), SS18 (Q15532), BCL11A (Q9H165), BCL11B (Q9C0K0), BCL7A (Q4VC05), BCL7B (Q9BQE9), BCL7C (Q8WUZ0). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-302489","identifier":"P51532","identifierLink":"https://www.uniprot.org/uniprotkb/P51532/entry","name":"SMARCA4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358441","identifier":"Q92925","identifierLink":"https://www.uniprot.org/uniprotkb/Q92925/entry","name":"SMARCD2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465496","identifier":"Q6STE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6STE5/entry","name":"SMARCD3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679921","identifier":"Q8NFD5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NFD5/entry","name":"ARID1B","description":"AT-rich interactive domain-containing protein 1B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724528","identifier":"O94805","identifierLink":"https://www.uniprot.org/uniprotkb/O94805/entry","name":"ACTL6B","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1212","complexName":"Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nThe neural progenitor-specific SWI/SNF complex is critical for self-renewal, maintenance and pluripotency of neural progenitor stem cells by selectively activating or repressing its target genes. In this variant of the complex transcriptional repression is probably driven by the presence of the ARID1A subunit. \r\n\r\nDuring neural development a switch from a progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. This process requires a switch of two subunits: ACTL6A is replaced by ACTL6B (O94805) and PHF10 replaced by DPF1 (Q92782) or DPF3 (Q92784) in neuron-specific SWI/SNF complexes. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. Although similar in function to the embryonic stem cell-specific SWI/SNF complex (CPX-1195) the composition of the neural progenitor-specific SWI/SNF complexes is more similar to the standard SWI/SNF complexes. It is likely that the two ATPases, SMARCA2/BRM (CPX-1201) and SMARCA4/BRG1 (this complex) do not co-occur in the same complex. SMARCD1 (BAF60A) and SMARCD3 (BAF60C) also may not co-occur. It is not clear yet if DPF2/BAF45D (Q92785) is a member of the neural progenitor-specific SWI/SNF complex. \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-302489","identifier":"P51532","identifierLink":"https://www.uniprot.org/uniprotkb/P51532/entry","name":"SMARCA4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355018","identifier":"O96019","identifierLink":"https://www.uniprot.org/uniprotkb/O96019/entry","name":"ACTL6A","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465496","identifier":"Q6STE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6STE5/entry","name":"SMARCD3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-637887","identifier":"O14497","identifierLink":"https://www.uniprot.org/uniprotkb/O14497/entry","name":"ARID1A","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-716462","identifier":"Q8WUB8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WUB8/entry","name":"PHF10","description":"PHD finger protein 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1213","complexName":"Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nThe neural progenitor-specific SWI/SNF complex is critical for self-renewal, maintenance and pluripotency of neural progenitor stem cells by selectively activating or repressing its target genes. In this variant of the complex transcriptional activation is probably driven by the presence of the ARID1B subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 &  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nDuring neural development a switch from a progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. This process requires a switch of two subunits: ACTL6A is replaced by ACTL6B (O94805) and PHF10 replaced by DPF1 (Q92782) or DPF3 (Q92784) in neuron-specific SWI/SNF complexes. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. Although similar in function to the embryonic stem cell-specific SWI/SNF complex the composition of the neural progenitor-specific SWI/SNF complexes is more similar to the standard SWI/SNF complexes. It is likely that the two ATPases, SMARCA2/BRM (this complex) and SMARCA4/BRG1 (CPX-1215) do not co-occur in the same complex. SMARCD1 (BAF60A) and SMARCD3 (BAF60C) also may not co-occur. It is not clear yet if DPF2/BAF45D (Q92785) is a member of the neural progenitor-specific SWI/SNF complex. \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355018","identifier":"O96019","identifierLink":"https://www.uniprot.org/uniprotkb/O96019/entry","name":"ACTL6A","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465496","identifier":"Q6STE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6STE5/entry","name":"SMARCD3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679562","identifier":"P51531","identifierLink":"https://www.uniprot.org/uniprotkb/P51531/entry","name":"SMARCA2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679921","identifier":"Q8NFD5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NFD5/entry","name":"ARID1B","description":"AT-rich interactive domain-containing protein 1B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-716462","identifier":"Q8WUB8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WUB8/entry","name":"PHF10","description":"PHD finger protein 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1214","complexName":"GLD-2-GLD-3 complex","organismName":"Caenorhabditis elegans; 6239","description":"Cytoplasmic poly(A) RNA polymerase complex that adds successive AMP monomers to the 3-prime-end of germ-line-specific RNAs, forming a poly(A) tail, thus switching RNA from a translationally dormant state into a translationally active state.\r\n\r\nActs as a regulator of mitosis/meiosis transition and is required to promote entry into meiosis from the mitotic cell cycle.","predictedComplex":false,"interactors":[{"ac":"EBI-2420017","identifier":"O17087","identifierLink":"https://www.uniprot.org/uniprotkb/O17087/entry","name":"gld-2","description":"Poly(A) RNA polymerase gld-2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12271","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-317828","identifier":"Q95ZK7","identifierLink":"https://www.uniprot.org/uniprotkb/Q95ZK7/entry","name":"gld-3","description":"Defective in germ line development protein 3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10627","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1215","complexName":"Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nThe neural progenitor-specific SWI/SNF complex is critical for self-renewal, maintenance and pluripotency of neural progenitor stem cells by selectively activating or repressing its target genes. In this variant of the complex transcriptional activation is probably driven by the presence of the ARID1B subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 &  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nDuring neural development a switch from a progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. This process requires a switch of two subunits: ACTL6A is replaced by ACTL6B (O94805) and PHF10 replaced by DPF1 (Q92782) or DPF3 (Q92784) in neuron-specific SWI/SNF complexes. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. Although similar in function to the embryonic stem cell-specific SWI/SNF complex the composition of the neural progenitor-specific SWI/SNF complexes is more similar to the standard SWI/SNF complexes. It is likely that the two ATPases, SMARCA2/BRM (CPX-1213) and SMARCA4/BRG1 (this complex) do not co-occur in the same complex. SMARCD1 (BAF60A) and SMARCD3 (BAF60C) also may not co-occur. It is not clear yet if DPF2/BAF45D (Q92785) is a member of the neural progenitor-specific SWI/SNF complex. \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-302489","identifier":"P51532","identifierLink":"https://www.uniprot.org/uniprotkb/P51532/entry","name":"SMARCA4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355018","identifier":"O96019","identifierLink":"https://www.uniprot.org/uniprotkb/O96019/entry","name":"ACTL6A","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465496","identifier":"Q6STE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6STE5/entry","name":"SMARCD3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679921","identifier":"Q8NFD5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NFD5/entry","name":"ARID1B","description":"AT-rich interactive domain-containing protein 1B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-716462","identifier":"Q8WUB8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WUB8/entry","name":"PHF10","description":"PHD finger protein 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1216","complexName":"Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nThe neuron-specific SWI/SNF complex is critical for the proliferation of post-mitotic neurons and regulates genes specific for dendritic growth by binding tightly with CREST (O75177). In this variant of the complex transcriptional repression is probably driven by the presence of the ARID1A subunit. \r\n\r\nDuring neural development a switch from a progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. This process requires a switch of two subunits: ACTL6A (O96019) is replaced by ACTL6B and PHF10 (Q8WUB8) replaced by DPF1 or DPF3 in neuron-specific SWI/SNF complexes. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, SMARCA2/BRM (CPX-1202) and SMARCA4/BRG1 (this complex) do not co-occur in the same complex. SMARCD1 (BAF60A) and SMARCD3 (BAF60C) as well as DPF1 and DPF3 also may not co-occur.  \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-16355309","identifier":"Q92784","identifierLink":"https://www.uniprot.org/uniprotkb/Q92784/entry","name":"DPF3","description":"Zinc finger protein DPF3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302489","identifier":"P51532","identifierLink":"https://www.uniprot.org/uniprotkb/P51532/entry","name":"SMARCA4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465496","identifier":"Q6STE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6STE5/entry","name":"SMARCD3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-637887","identifier":"O14497","identifierLink":"https://www.uniprot.org/uniprotkb/O14497/entry","name":"ARID1A","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724528","identifier":"O94805","identifierLink":"https://www.uniprot.org/uniprotkb/O94805/entry","name":"ACTL6B","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-726953","identifier":"Q92782","identifierLink":"https://www.uniprot.org/uniprotkb/Q92782/entry","name":"DPF1","description":"Zinc finger protein neuro-d4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1217","complexName":"Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nThe neuron-specific SWI/SNF complex is critical for the proliferation of post-mitotic neurons and regulates genes specific for dendritic growth by binding tightly with CREST (O75177). In this variant of the complex transcriptional activation is probably driven by the presence of the ARID1B subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 and  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nDuring neural development a switch from a progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. This process requires a switch of two subunits: ACTL6A (O96019) is replaced by ACTL6B and PHF10 (Q8WUB8) replaced by DPF1 or DPF3 in neuron-specific SWI/SNF complexes. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, SMARCA2/BRM (this complex) and SMARCA4/BRG1 (CPX-1218) do not co-occur in the same complex. SMARCD1 (BAF60A) and SMARCD3 (BAF60C) as well as DPF1 and DPF3 also may not co-occur.  \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-16355309","identifier":"Q92784","identifierLink":"https://www.uniprot.org/uniprotkb/Q92784/entry","name":"DPF3","description":"Zinc finger protein DPF3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465496","identifier":"Q6STE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6STE5/entry","name":"SMARCD3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679562","identifier":"P51531","identifierLink":"https://www.uniprot.org/uniprotkb/P51531/entry","name":"SMARCA2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679921","identifier":"Q8NFD5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NFD5/entry","name":"ARID1B","description":"AT-rich interactive domain-containing protein 1B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724528","identifier":"O94805","identifierLink":"https://www.uniprot.org/uniprotkb/O94805/entry","name":"ACTL6B","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-726953","identifier":"Q92782","identifierLink":"https://www.uniprot.org/uniprotkb/Q92782/entry","name":"DPF1","description":"Zinc finger protein neuro-d4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1218","complexName":"Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nThe neuron-specific SWI/SNF complex is critical for the proliferation of post-mitotic neurons and regulates genes specific for dendritic growth by binding tightly with CREST (O75177). In this variant of the complex transcriptional activation is probably driven by the presence of the ARID1B subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 and  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nDuring neural development a switch from a progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. This process requires a switch of two subunits: ACTL6A (O96019) is replaced by ACTL6B and PHF10 (Q8WUB8) replaced by DPF1 or DPF3 in neuron-specific SWI/SNF complexes. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, SMARCA2/BRM (CPX-1217) and SMARCA4/BRG1 (this complex) do not co-occur in the same complex. SMARCD1 (BAF60A) and SMARCD3 (BAF60C) as well as DPF1 and DPF3 also may not co-occur.  \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-16355309","identifier":"Q92784","identifierLink":"https://www.uniprot.org/uniprotkb/Q92784/entry","name":"DPF3","description":"Zinc finger protein DPF3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302489","identifier":"P51532","identifierLink":"https://www.uniprot.org/uniprotkb/P51532/entry","name":"SMARCA4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465496","identifier":"Q6STE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6STE5/entry","name":"SMARCD3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679921","identifier":"Q8NFD5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NFD5/entry","name":"ARID1B","description":"AT-rich interactive domain-containing protein 1B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724528","identifier":"O94805","identifierLink":"https://www.uniprot.org/uniprotkb/O94805/entry","name":"ACTL6B","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-726953","identifier":"Q92782","identifierLink":"https://www.uniprot.org/uniprotkb/Q92782/entry","name":"DPF1","description":"Zinc finger protein neuro-d4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9062","complexName":"Sodium leak channel complex","organismName":"Drosophila melanogaster; 7227","description":"Voltage-gated ion channel responsible for the depolarizing sodium (Na+) leak currents that determine resting Na(+) permeability and control neuronal excitability. Functions downstream of the molecular circadian clock in pacemaker neurons to promote behavioral rhythmicity.","predictedComplex":false,"interactors":[{"ac":"EBI-2507853","identifier":"Q9VB11","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VB11/entry","name":"unc80","description":"Protein unc-80 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR31781","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52361202","identifier":"A8JUW5","identifierLink":"https://www.uniprot.org/uniprotkb/A8JUW5/entry","name":"na","description":"Sodium leak channel NALCN","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46141","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9965060","identifier":"E1JIP9","identifierLink":"https://www.uniprot.org/uniprotkb/E1JIP9/entry","name":"unc79","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]}]},{"complexAC":"CPX-9063","complexName":"PA200-20S-PA200 double-capped proteasome complex","organismName":"Homo sapiens; 9606","description":"Multi-enzyme complex that functions as the primary degradation machinery for the selective turnover of surplus or damaged proteins within the cell. The core contains the protease active sites (chymotrypsin-like, trypsin-like and peptidylglutamyl-peptide hydrolyzing) that perform the proteolysis reactions in an internal chamber. Regulatory particles referred to as 'caps' act as a discriminating gateway for potential substrates.\r\n\r\nThis complex is formed upon a 200 kDa proteasome activator (PA200) binding either symmetrically or asymmetrically to the alpha-rings of the multicatalytic constitutive cylindrical 20S core complex (CPX-8806), composed of four heteroheptameric rings, of which the outer two are composed of alpha subunits (1-7) and the inner two of beta subunits (1-7). PA200 binds in an ubiquitin- and ATP-independent manner to either one (single-cap, CPX-8841) or both ends (double-capped, this complex) of the 20S Proteasome, but the efficiency of substrate processing by single and double-capped proteasomes in not known.\r\n\r\nA nuclear-localized proteasomal regulator, PA200 enhances the 20S proteasome's ability to degrade short peptides, disordered proteins, and PA200-bound inositol phosphates act on acetylated core (AC) histones during DNA repair and replication stress in an ubiquitin-independent manner. Also implicated in mitochondrial fission, turnover of ribosome-related transcription factor Sfp1 and maintaining intracellular glutamine levels. Thought not essential for DNA repair, the PA200 component is more sensitive to DNA damage and PA200-hybrid proteasomes are known to form in response to ionizing radiation. PA200 is also thought to work with PA28-gamma to regulate male fertility.\r\n\r\nExternal stimuli and diseases can change a proteasome's composition, thereby affecting the proteasome's substrate specificity and consequently protein homeostasis within a cell. Decreased proteasome activity is linked to neurodegerative disorders and cardiac dysfunction through the accumulation of proteins while, enhanced proteasome activity and induced-expression of certain proteasome components are implicated in muscle wasting conditions and several cancers.\r\n\r\nPA200 in association with PA28-gamma, plays a key role in male fertility by their ability to regulate sperm motility.","predictedComplex":false,"interactors":[{"ac":"EBI-1236916","identifier":"Q14997","identifierLink":"https://www.uniprot.org/uniprotkb/Q14997/entry","name":"PSME4","description":"Proteasome activator complex subunit 4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32170","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348380","identifier":"P25788","identifierLink":"https://www.uniprot.org/uniprotkb/P25788/entry","name":"PSMA3","description":"Proteasome subunit alpha type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355475","identifier":"P28066","identifierLink":"https://www.uniprot.org/uniprotkb/P28066/entry","name":"PSMA5","description":"Proteasome subunit alpha type-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357793","identifier":"P60900","identifierLink":"https://www.uniprot.org/uniprotkb/P60900/entry","name":"PSMA6","description":"Proteasome subunit alpha type-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357828","identifier":"P28074","identifierLink":"https://www.uniprot.org/uniprotkb/P28074/entry","name":"PSMB5","description":"Proteasome subunit beta type-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359288","identifier":"P28072","identifierLink":"https://www.uniprot.org/uniprotkb/P28072/entry","name":"PSMB6","description":"Proteasome subunit beta type-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359310","identifier":"P25789","identifierLink":"https://www.uniprot.org/uniprotkb/P25789/entry","name":"PSMA4","description":"Proteasome subunit alpha type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359335","identifier":"P49721","identifierLink":"https://www.uniprot.org/uniprotkb/P49721/entry","name":"PSMB2","description":"Proteasome subunit beta type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359352","identifier":"P25786","identifierLink":"https://www.uniprot.org/uniprotkb/P25786/entry","name":"PSMA1","description":"Proteasome subunit alpha type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372273","identifier":"P20618","identifierLink":"https://www.uniprot.org/uniprotkb/P20618/entry","name":"PSMB1","description":"Proteasome subunit beta type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32194","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603262","identifier":"P25787","identifierLink":"https://www.uniprot.org/uniprotkb/P25787/entry","name":"PSMA2","description":"Proteasome subunit alpha type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603272","identifier":"O14818","identifierLink":"https://www.uniprot.org/uniprotkb/O14818/entry","name":"PSMA7","description":"Proteasome subunit alpha type-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603319","identifier":"Q99436","identifierLink":"https://www.uniprot.org/uniprotkb/Q99436/entry","name":"PSMB7","description":"Proteasome subunit beta type-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603340","identifier":"P49720","identifierLink":"https://www.uniprot.org/uniprotkb/P49720/entry","name":"PSMB3","description":"Proteasome subunit beta type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603350","identifier":"P28070","identifierLink":"https://www.uniprot.org/uniprotkb/P28070/entry","name":"PSMB4","description":"Proteasome subunit beta type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9064","complexName":"LKB1-STRAD-MO25 serine/threonine protein kinase complex","organismName":"Drosophila melanogaster; 7227","description":"Directly phosphorylates adenosine monophosphate-activated protein kinase (AMPK) family members on the T-loop thereby activating them. May play a role in cell polarity.","predictedComplex":false,"interactors":[{"ac":"EBI-52361752","identifier":"P91891","identifierLink":"https://www.uniprot.org/uniprotkb/P91891/entry","name":"Mo25","description":"Protein Mo25","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10182","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52361770","identifier":"P83098","identifierLink":"https://www.uniprot.org/uniprotkb/P83098/entry","name":"Stlk","description":"STE20-related kinase adapter protein stlk","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR45832","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-92892","identifier":"Q8T9L5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8T9L5/entry","name":"Lkb1","description":"Serine/threonine-protein kinase STK11","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR24346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9065","complexName":"CoREST transcriptional corepressor complex, RCOR1-HDAC2 variant","organismName":"Homo sapiens; 9606","description":"Class I histone deacetylase complex unique in containing both histone demethylase and deacetylase enzymes, KDM1A and HDAC1/2 respectively. Acts as a transcriptional repressor, by acting as an epigenetic eraser removing methyl and acetyl groups from histone tails. This results in the loss of binding sites for regulatory reader proteins and causes chromatin compaction by restoring the positive charge on histone tails. Regulates neuronal differentiation gene expression and stem cell fate and development.","predictedComplex":false,"interactors":[{"ac":"EBI-301821","identifier":"Q92769","identifierLink":"https://www.uniprot.org/uniprotkb/Q92769/entry","name":"HDAC2","description":"Histone deacetylase 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-710124","identifier":"O60341","identifierLink":"https://www.uniprot.org/uniprotkb/O60341/entry","name":"KDM1A","description":"Lysine-specific histone demethylase 1A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-926563","identifier":"Q9UKL0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UKL0/entry","name":"RCOR1","description":"REST corepressor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16089","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-9066","complexName":"CoREST transcriptional corepressor complex, RCOR2-HDAC1 variant","organismName":"Homo sapiens; 9606","description":"Class I histone deacetylase complex unique in containing both histone demethylase and deacetylase enzymes, KDM1A and HDAC1/2 respectively. Acts as a transcriptional repressor, by acting as an epigenetic eraser removing methyl and acetyl groups from histone tails. This results in the loss of binding sites for regulatory reader proteins and causes chromatin compaction by restoring the positive charge on histone tails. Regulates neuronal differentiation gene expression and stem cell fate and development.","predictedComplex":false,"interactors":[{"ac":"EBI-301834","identifier":"Q13547","identifierLink":"https://www.uniprot.org/uniprotkb/Q13547/entry","name":"HDAC1","description":"Histone deacetylase 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-710124","identifier":"O60341","identifierLink":"https://www.uniprot.org/uniprotkb/O60341/entry","name":"KDM1A","description":"Lysine-specific histone demethylase 1A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-723853","identifier":"Q8IZ40","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IZ40/entry","name":"RCOR2","description":"REST corepressor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16089","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-9067","complexName":"CoREST transcriptional corepressor complex, RCOR2-HDAC2 variant","organismName":"Homo sapiens; 9606","description":"Class I histone deacetylase complex unique in containing both histone demethylase and deacetylase enzymes, KDM1A and HDAC1/2 respectively. Acts as a transcriptional repressor, by acting as an epigenetic eraser removing methyl and acetyl groups from histone tails. This results in the loss of binding sites for regulatory reader proteins and causes chromatin compaction by restoring the positive charge on histone tails. Regulates neuronal differentiation gene expression and stem cell fate and development.","predictedComplex":false,"interactors":[{"ac":"EBI-301821","identifier":"Q92769","identifierLink":"https://www.uniprot.org/uniprotkb/Q92769/entry","name":"HDAC2","description":"Histone deacetylase 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-710124","identifier":"O60341","identifierLink":"https://www.uniprot.org/uniprotkb/O60341/entry","name":"KDM1A","description":"Lysine-specific histone demethylase 1A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-723853","identifier":"Q8IZ40","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IZ40/entry","name":"RCOR2","description":"REST corepressor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16089","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-9068","complexName":"CoREST transcriptional corepressor complex, RCOR3-HDAC1 variant","organismName":"Homo sapiens; 9606","description":"Class I histone deacetylase complex unique in containing both histone demethylase and deacetylase enzymes, KDM1A and HDAC1/2 respectively. Acts as a transcriptional repressor, by acting as an epigenetic eraser removing methyl and acetyl groups from histone tails. This results in the loss of binding sites for regulatory reader proteins and causes chromatin compaction by restoring the positive charge on histone tails. Regulates neuronal differentiation gene expression and stem cell fate and development.","predictedComplex":false,"interactors":[{"ac":"EBI-301834","identifier":"Q13547","identifierLink":"https://www.uniprot.org/uniprotkb/Q13547/entry","name":"HDAC1","description":"Histone deacetylase 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-710124","identifier":"O60341","identifierLink":"https://www.uniprot.org/uniprotkb/O60341/entry","name":"KDM1A","description":"Lysine-specific histone demethylase 1A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743428","identifier":"Q9P2K3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P2K3/entry","name":"RCOR3","description":"REST corepressor 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16089","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-9069","complexName":"CoREST transcriptional corepressor complex, RCOR3-HDAC2 variant","organismName":"Homo sapiens; 9606","description":"Class I histone deacetylase complex unique in containing both histone demethylase and deacetylase enzymes, KDM1A and HDAC1/2 respectively. Acts as a transcriptional repressor, by acting as an epigenetic eraser removing methyl and acetyl groups from histone tails. This results in the loss of binding sites for regulatory reader proteins and causes chromatin compaction by restoring the positive charge on histone tails. 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284812","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52362607","identifier":"Q9USQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9USQ9/entry","name":"psb7","description":"Probable proteasome subunit beta type-7","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52362626","identifier":"Q10329","identifierLink":"https://www.uniprot.org/uniprotkb/Q10329/entry","name":"pre6","description":"Probable proteasome subunit alpha type-4","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52362647","identifier":"Q9UQY2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UQY2/entry","name":"pam1","description":"Probable proteasome subunit beta type-6","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR32194","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52362666","identifier":"O59770","identifierLink":"https://www.uniprot.org/uniprotkb/O59770/entry","name":"pre10","description":"Probable proteasome subunit alpha type-7","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52362691","identifier":"O43063","identifierLink":"https://www.uniprot.org/uniprotkb/O43063/entry","name":"pre3","description":"Probable proteasome subunit beta type-1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52362713","identifier":"O74445","identifierLink":"https://www.uniprot.org/uniprotkb/O74445/entry","name":"rpt4","description":"Probable 26S proteasome subunit rpt4","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52362742","identifier":"Q9Y7T8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y7T8/entry","name":"pup3","description":"Probable proteasome subunit beta type-3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52362762","identifier":"O94579","identifierLink":"https://www.uniprot.org/uniprotkb/O94579/entry","name":"pre8","description":"Probable proteasome subunit alpha type-2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52362788","identifier":"O14126","identifierLink":"https://www.uniprot.org/uniprotkb/O14126/entry","name":"tbp1","description":"26S proteasome regulatory subunit 6A","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52362820","identifier":"O74894","identifierLink":"https://www.uniprot.org/uniprotkb/O74894/entry","name":"rpt3","description":"26S proteasome regulatory subunit 6B homolog","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52362845","identifier":"Q10171","identifierLink":"https://www.uniprot.org/uniprotkb/Q10171/entry","name":"uch1","description":"Probable ubiquitin carboxyl-terminal hydrolase 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10589","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52362865","identifier":"Q09682","identifierLink":"https://www.uniprot.org/uniprotkb/Q09682/entry","name":"psa3","description":"Probable proteasome subunit alpha type-3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52362885","identifier":"Q10335","identifierLink":"https://www.uniprot.org/uniprotkb/Q10335/entry","name":"rpn7","description":"26S proteasome regulatory subunit rpn7","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR14145","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52362906","identifier":"Q9US13","identifierLink":"https://www.uniprot.org/uniprotkb/Q9US13/entry","name":"rpn9","description":"Probable 26S proteasome regulatory subunit rpn9","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10539","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7170665","identifier":"Q9UT97","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UT97/entry","name":"pup2","description":"Probable proteasome subunit alpha type-5","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9078","complexName":"CatSpermasome complex, gamma subunit variant 2","organismName":"Mus musculus; 10090","description":"Sperm-specific cation channel, CatSper mediated Ca2+ signalling initiates the tyrosine phosphorylation cascade thereby controlling sperm motility. Also plays a central role in sperm chemotaxis, and mediates the Ca2+ influx induced by the steroid sex hormone progesterone in human sperm. \r\n\r\nThis complex contains a variant gamma 2 subunit (CatSperg2, C6KI89), and though CatSperg1 exists, (E9Q355) the protein has not been identified in the mouse CatSper complex and its expression is not restricted to the testis.","predictedComplex":false,"interactors":[{"ac":"EBI-15619083","identifier":"Q91ZR5","identifierLink":"https://www.uniprot.org/uniprotkb/Q91ZR5/entry","name":"Catsper1","description":"Cation channel sperm-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR47193","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15619135","identifier":"Q80W99","identifierLink":"https://www.uniprot.org/uniprotkb/Q80W99/entry","name":"Catsper3","description":"Cation channel sperm-associated protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR47131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15619199","identifier":"Q8BVN3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BVN3/entry","name":"Catsper4","description":"Cation channel sperm-associated protein 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR47077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52363181","identifier":"A2RTF1","identifierLink":"https://www.uniprot.org/uniprotkb/A2RTF1/entry","name":"Catsperb","description":"Cation channel sperm-associated auxiliary subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14705","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52363202","identifier":"C6KI89","identifierLink":"https://www.uniprot.org/uniprotkb/C6KI89/entry","name":"Catsperg2","description":"Cation channel sperm-associated auxiliary subunit gamma 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14327","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52363223","identifier":"E9Q9F6","identifierLink":"https://www.uniprot.org/uniprotkb/E9Q9F6/entry","name":"Catsperd","description":"Cation channel sperm-associated auxiliary subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR33722","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52363246","identifier":"P0DP43","identifierLink":"https://www.uniprot.org/uniprotkb/P0DP43/entry","name":"Catspere","description":"Cation channel sperm-associated auxiliary subunit epsilon","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR33722","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52363259","identifier":"Q8C0X7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8C0X7/entry","name":"Slco6c1","description":"Solute carrier organic anion transporter family member 6C1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11388","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52363283","identifier":"A0A2R8VHF7","identifierLink":"https://www.uniprot.org/uniprotkb/A0A2R8VHF7/entry","name":"Tmem249","description":"Cation channel sperm-associated auxiliary subunit TMEM249","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR35442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52363294","identifier":"D3Z338","identifierLink":"https://www.uniprot.org/uniprotkb/D3Z338/entry","name":"Tmem262","description":"Cation channel sperm-associated auxiliary subunit TMEM262","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR37998","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52363307","identifier":"Q9DAM2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DAM2/entry","name":"Efcab9","description":"EF-hand calcium-binding domain-containing protein 9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR47065","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52363330","identifier":"Q9CQP8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CQP8/entry","name":"Catsperz","description":"Cation channel sperm-associated auxiliary subunit zeta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR42155","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8354050","identifier":"A2ARP9","identifierLink":"https://www.uniprot.org/uniprotkb/A2ARP9/entry","name":"Catsper2","description":"Cation channel sperm-associated protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46923","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9081","complexName":"CRL3 E3 ubiquitin ligase complex, KBTBD13 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.CRL3-KBTBD13 may play a role in skeletal and cardiac muscle function.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-44441108","identifier":"C9JR72","identifierLink":"https://www.uniprot.org/uniprotkb/C9JR72/entry","name":"KBTBD13","description":"Kelch repeat and BTB domain-containing protein 13","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9082","complexName":"19S-20S-PA28-alphabeta hybrid proteasome complex","organismName":"Homo sapiens; 9606","description":"Multi-enzyme complex that functions as the primary degradation machinery for the selective turnover of surplus or damaged proteins within the cell. Proteins targeted for degradation are covalently labelled with polyubiquitin chains which are recognized and removed by the proteasome. The core contains the protease active sites (chymotrypsin-like, trypsin-like and peptidylglutamyl-peptide hydrolysing) that perform the proteolysis reactions in an internal chamber. Regulatory particles referred to as 'caps' act as a discriminating gateway for potential substrates.\r\n\r\nFormed upon induction by IFN-gamma, this double-capped hybrid proteasome complex comprises the proteasome regulator PA28alpha-beta (PSME1-Q06323, PSME2-Q9UL46) at one end of the 20S catalytic core (CPX-8806), and the 19S regulatory particle (CPX-8964) at the other end. Protein degradation is directed in an ubiquitin and ATP-dependent manner by the 19S cap, while the PA28alpha-beta cap acts through an ATP and ubiquitin independent pathway.\r\n\r\nThe 19S cap is thought to determine the rate of protein hydrolysis, while the PA28alpha-beta cap is thought to allosterically modify the 20S core's active sites to increase production of suitable peptides for MHC class 1 presentation. In contrast to PA28alphabeta-20S proteasome, the 19S-20S-PA28alpha-beta hybrid proteasome generates an altered pattern of cleavage products, without altering the mean peptide length.","predictedComplex":false,"interactors":[{"ac":"EBI-348380","identifier":"P25788","identifierLink":"https://www.uniprot.org/uniprotkb/P25788/entry","name":"PSMA3","description":"Proteasome subunit alpha type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355475","identifier":"P28066","identifierLink":"https://www.uniprot.org/uniprotkb/P28066/entry","name":"PSMA5","description":"Proteasome subunit alpha type-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356070","identifier":"Q9UNM6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UNM6/entry","name":"PSMD13","description":"26S proteasome non-ATPase regulatory subunit 13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10539","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357598","identifier":"P62191","identifierLink":"https://www.uniprot.org/uniprotkb/P62191/entry","name":"PSMC1","description":"26S proteasome regulatory subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357622","identifier":"O43242","identifierLink":"https://www.uniprot.org/uniprotkb/O43242/entry","name":"PSMD3","description":"26S proteasome non-ATPase regulatory subunit 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10758","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357648","identifier":"Q13200","identifierLink":"https://www.uniprot.org/uniprotkb/Q13200/entry","name":"PSMD2","description":"26S proteasome non-ATPase regulatory subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10943","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357659","identifier":"P51665","identifierLink":"https://www.uniprot.org/uniprotkb/P51665/entry","name":"PSMD7","description":"26S proteasome non-ATPase regulatory subunit 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10540","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357669","identifier":"P62333","identifierLink":"https://www.uniprot.org/uniprotkb/P62333/entry","name":"PSMC6","description":"26S proteasome regulatory subunit 10B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357745","identifier":"P62195","identifierLink":"https://www.uniprot.org/uniprotkb/P62195/entry","name":"PSMC5","description":"26S proteasome regulatory subunit 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357793","identifier":"P60900","identifierLink":"https://www.uniprot.org/uniprotkb/P60900/entry","name":"PSMA6","description":"Proteasome subunit alpha type-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357816","identifier":"O00231","identifierLink":"https://www.uniprot.org/uniprotkb/O00231/entry","name":"PSMD11","description":"26S proteasome non-ATPase regulatory subunit 11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357828","identifier":"P28074","identifierLink":"https://www.uniprot.org/uniprotkb/P28074/entry","name":"PSMB5","description":"Proteasome subunit beta type-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357874","identifier":"Q99460","identifierLink":"https://www.uniprot.org/uniprotkb/Q99460/entry","name":"PSMD1","description":"26S proteasome non-ATPase regulatory subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10943","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359288","identifier":"P28072","identifierLink":"https://www.uniprot.org/uniprotkb/P28072/entry","name":"PSMB6","description":"Proteasome subunit beta type-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359304","identifier":"P48556","identifierLink":"https://www.uniprot.org/uniprotkb/P48556/entry","name":"PSMD8","description":"26S proteasome non-ATPase regulatory subunit 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12387","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359310","identifier":"P25789","identifierLink":"https://www.uniprot.org/uniprotkb/P25789/entry","name":"PSMA4","description":"Proteasome subunit alpha type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359318","identifier":"P55036","identifierLink":"https://www.uniprot.org/uniprotkb/P55036/entry","name":"PSMD4","description":"26S proteasome non-ATPase regulatory subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10223","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359335","identifier":"P49721","identifierLink":"https://www.uniprot.org/uniprotkb/P49721/entry","name":"PSMB2","description":"Proteasome subunit beta type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359352","identifier":"P25786","identifierLink":"https://www.uniprot.org/uniprotkb/P25786/entry","name":"PSMA1","description":"Proteasome subunit alpha type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359701","identifier":"Q15008","identifierLink":"https://www.uniprot.org/uniprotkb/Q15008/entry","name":"PSMD6","description":"26S proteasome non-ATPase regulatory subunit 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14145","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359710","identifier":"P35998","identifierLink":"https://www.uniprot.org/uniprotkb/P35998/entry","name":"PSMC2","description":"26S proteasome regulatory subunit 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359720","identifier":"P17980","identifierLink":"https://www.uniprot.org/uniprotkb/P17980/entry","name":"PSMC3","description":"26S proteasome regulatory subunit 6A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359733","identifier":"O00232","identifierLink":"https://www.uniprot.org/uniprotkb/O00232/entry","name":"PSMD12","description":"26S proteasome non-ATPase regulatory subunit 12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10855","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372273","identifier":"P20618","identifierLink":"https://www.uniprot.org/uniprotkb/P20618/entry","name":"PSMB1","description":"Proteasome subunit beta type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32194","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603262","identifier":"P25787","identifierLink":"https://www.uniprot.org/uniprotkb/P25787/entry","name":"PSMA2","description":"Proteasome subunit alpha type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603272","identifier":"O14818","identifierLink":"https://www.uniprot.org/uniprotkb/O14818/entry","name":"PSMA7","description":"Proteasome subunit alpha type-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603319","identifier":"Q99436","identifierLink":"https://www.uniprot.org/uniprotkb/Q99436/entry","name":"PSMB7","description":"Proteasome subunit beta type-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603340","identifier":"P49720","identifierLink":"https://www.uniprot.org/uniprotkb/P49720/entry","name":"PSMB3","description":"Proteasome subunit beta type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603350","identifier":"P28070","identifierLink":"https://www.uniprot.org/uniprotkb/P28070/entry","name":"PSMB4","description":"Proteasome subunit beta type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712149","identifier":"Q06323","identifierLink":"https://www.uniprot.org/uniprotkb/Q06323/entry","name":"PSME1","description":"Proteasome activator complex subunit 1","stochiometry":"minValue: 3, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10660","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-722193","identifier":"O00487","identifierLink":"https://www.uniprot.org/uniprotkb/O00487/entry","name":"PSMD14","description":"26S proteasome non-ATPase regulatory subunit 14","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10410","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-741630","identifier":"Q9UL46","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UL46/entry","name":"PSME2","description":"Proteasome activator complex subunit 2","stochiometry":"minValue: 3, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10660","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743997","identifier":"P43686","identifierLink":"https://www.uniprot.org/uniprotkb/P43686/entry","name":"PSMC4","description":"26S proteasome regulatory subunit 6B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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Proteins targeted for degradation are covalently labelled with polyubiquitin chains which are recognized and removed by the proteasome. The core contains the protease active sites (chymotrypsin-like, trypsin-like and peptidylglutamyl-peptide hydrolysing) that perform the proteolysis reactions in an internal chamber. Regulatory particles referred to as 'caps' act as a discriminating gateway for potential substrates.\r\n\r\nThis double-capped hybrid proteasome complex comprises the proteasome regulator PA28gamma (PSME3-P61289) at one end of the 20S catalytic core (CPX-8806), and the 19S regulatory particle (CPX-8964) at the other end. Protein degradation is directed in an ATP-dependent manner by the 19S cap, while the PA28gamma cap acts through an ATP and ubiquitin independent pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-348380","identifier":"P25788","identifierLink":"https://www.uniprot.org/uniprotkb/P25788/entry","name":"PSMA3","description":"Proteasome subunit alpha type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355475","identifier":"P28066","identifierLink":"https://www.uniprot.org/uniprotkb/P28066/entry","name":"PSMA5","description":"Proteasome subunit alpha type-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355546","identifier":"P61289","identifierLink":"https://www.uniprot.org/uniprotkb/P61289/entry","name":"PSME3","description":"Proteasome activator complex subunit 3","stochiometry":"minValue: 7, maxValue: 7","interactorType":"protein","organismName":"Homo sapiens; 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9606","xrefs":[{"identifier":"PTHR10758","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357648","identifier":"Q13200","identifierLink":"https://www.uniprot.org/uniprotkb/Q13200/entry","name":"PSMD2","description":"26S proteasome non-ATPase regulatory subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10943","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357659","identifier":"P51665","identifierLink":"https://www.uniprot.org/uniprotkb/P51665/entry","name":"PSMD7","description":"26S proteasome non-ATPase regulatory subunit 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10540","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357669","identifier":"P62333","identifierLink":"https://www.uniprot.org/uniprotkb/P62333/entry","name":"PSMC6","description":"26S proteasome regulatory subunit 10B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357745","identifier":"P62195","identifierLink":"https://www.uniprot.org/uniprotkb/P62195/entry","name":"PSMC5","description":"26S proteasome regulatory subunit 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357793","identifier":"P60900","identifierLink":"https://www.uniprot.org/uniprotkb/P60900/entry","name":"PSMA6","description":"Proteasome subunit alpha type-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357816","identifier":"O00231","identifierLink":"https://www.uniprot.org/uniprotkb/O00231/entry","name":"PSMD11","description":"26S proteasome non-ATPase regulatory subunit 11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357828","identifier":"P28074","identifierLink":"https://www.uniprot.org/uniprotkb/P28074/entry","name":"PSMB5","description":"Proteasome subunit beta type-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357874","identifier":"Q99460","identifierLink":"https://www.uniprot.org/uniprotkb/Q99460/entry","name":"PSMD1","description":"26S proteasome non-ATPase regulatory subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10943","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359288","identifier":"P28072","identifierLink":"https://www.uniprot.org/uniprotkb/P28072/entry","name":"PSMB6","description":"Proteasome subunit beta type-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359304","identifier":"P48556","identifierLink":"https://www.uniprot.org/uniprotkb/P48556/entry","name":"PSMD8","description":"26S proteasome non-ATPase regulatory subunit 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12387","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359310","identifier":"P25789","identifierLink":"https://www.uniprot.org/uniprotkb/P25789/entry","name":"PSMA4","description":"Proteasome subunit alpha type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359318","identifier":"P55036","identifierLink":"https://www.uniprot.org/uniprotkb/P55036/entry","name":"PSMD4","description":"26S proteasome non-ATPase regulatory subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10223","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359335","identifier":"P49721","identifierLink":"https://www.uniprot.org/uniprotkb/P49721/entry","name":"PSMB2","description":"Proteasome subunit beta type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359352","identifier":"P25786","identifierLink":"https://www.uniprot.org/uniprotkb/P25786/entry","name":"PSMA1","description":"Proteasome subunit alpha type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359701","identifier":"Q15008","identifierLink":"https://www.uniprot.org/uniprotkb/Q15008/entry","name":"PSMD6","description":"26S proteasome non-ATPase regulatory subunit 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14145","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359710","identifier":"P35998","identifierLink":"https://www.uniprot.org/uniprotkb/P35998/entry","name":"PSMC2","description":"26S proteasome regulatory subunit 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359720","identifier":"P17980","identifierLink":"https://www.uniprot.org/uniprotkb/P17980/entry","name":"PSMC3","description":"26S proteasome regulatory subunit 6A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359733","identifier":"O00232","identifierLink":"https://www.uniprot.org/uniprotkb/O00232/entry","name":"PSMD12","description":"26S proteasome non-ATPase regulatory subunit 12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10855","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372273","identifier":"P20618","identifierLink":"https://www.uniprot.org/uniprotkb/P20618/entry","name":"PSMB1","description":"Proteasome subunit beta type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32194","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603262","identifier":"P25787","identifierLink":"https://www.uniprot.org/uniprotkb/P25787/entry","name":"PSMA2","description":"Proteasome subunit alpha type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603272","identifier":"O14818","identifierLink":"https://www.uniprot.org/uniprotkb/O14818/entry","name":"PSMA7","description":"Proteasome subunit alpha type-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603319","identifier":"Q99436","identifierLink":"https://www.uniprot.org/uniprotkb/Q99436/entry","name":"PSMB7","description":"Proteasome subunit beta type-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603340","identifier":"P49720","identifierLink":"https://www.uniprot.org/uniprotkb/P49720/entry","name":"PSMB3","description":"Proteasome subunit beta type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603350","identifier":"P28070","identifierLink":"https://www.uniprot.org/uniprotkb/P28070/entry","name":"PSMB4","description":"Proteasome subunit beta type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-722193","identifier":"O00487","identifierLink":"https://www.uniprot.org/uniprotkb/O00487/entry","name":"PSMD14","description":"26S proteasome non-ATPase regulatory subunit 14","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10410","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743997","identifier":"P43686","identifierLink":"https://www.uniprot.org/uniprotkb/P43686/entry","name":"PSMC4","description":"26S proteasome regulatory subunit 6B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-79819","identifier":"P60896","identifierLink":"https://www.uniprot.org/uniprotkb/P60896/entry","name":"SEM1","description":"26S proteasome complex subunit SEM1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-954387","identifier":"Q16186","identifierLink":"https://www.uniprot.org/uniprotkb/Q16186/entry","name":"ADRM1","description":"Proteasomal ubiquitin receptor ADRM1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12225","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9086","complexName":"30S proteasome complex","organismName":"Homo sapiens; 9606","description":"Multi-enzyme complex that functions as the primary degradation machinery for the selective turnover of surplus or damaged proteins within the cell. Proteins targeted for degradation are covalently labelled with polyubiquitin chains which are recognized and removed by the proteasome. The core contains the protease active sites (chymotrypsin-like, trypsin-like and peptidylglutamyl-peptide hydrolysing) that perform the proteolysis reactions in an internal chamber. The regulatory particles act as a discriminating gateway for potential substrates.\r\n\r\nThis complex is composed of the 20S Proteasome (CPX-8806) and two 19S regulatory particles. The 19S regulatory particle (CPX-8964) is the major activator that allows the 20S Proteasome to degrade almost any protein tagged with the small protein modifier ubiquitin. The 19S recognises and deubiquitinates substrates as they enter the 20S catalytic core, thereby enabling protein degradation and maintaining cellular protein homeostasis. Attachment of the 19S to one end of the 20S forms the 26S proteasome (single-capped, CPX-5993), and two ends, the 30S Proteasome (double-capped, this complex).\r\n\r\nWhile both 19S regulatory particles can engage with a protein substrate and be functional, it is thought that the proteasome function is more efficient if the opposite side to substrate entry side serves for peptide exit. Thus, concurrent functionality of both 19S particles may be mutually exclusive and the 30S Proteasome may function most efficiently as a single capped 26S Proteasome.\r\n\r\nDysregulated proteasome function has been implicated, as a primary cause or a secondary consequence, in the pathogenesis of a broad array of neurodegenerative diseases, including Alzheimer’s, Parkinson’s, and Huntington’s diseases.","predictedComplex":false,"interactors":[{"ac":"EBI-348380","identifier":"P25788","identifierLink":"https://www.uniprot.org/uniprotkb/P25788/entry","name":"PSMA3","description":"Proteasome subunit alpha type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355475","identifier":"P28066","identifierLink":"https://www.uniprot.org/uniprotkb/P28066/entry","name":"PSMA5","description":"Proteasome subunit alpha type-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 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7227","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3416638","identifier":"Q9XZJ4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XZJ4/entry","name":"Prosalpha1","description":"Proteasome subunit alpha type-6","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52367760","identifier":"Q9VA12","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VA12/entry","name":"Prosalpha3T","description":"Proteasome subunit alpha type-4-like","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52367779","identifier":"Q27575","identifierLink":"https://www.uniprot.org/uniprotkb/Q27575/entry","name":"Prosalpha4T2","description":"Proteasome subunit alpha type-7-1B","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-86891","identifier":"Q9VQE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VQE5/entry","name":"Prosbeta4R2","description":"Probable proteasome subunit beta type-2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-91327","identifier":"Q9VYQ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VYQ3/entry","name":"Uch-L5R","description":"Ubiquitin carboxyl-terminal hydrolase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10589","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-98473","identifier":"Q9VNA5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VNA5/entry","name":"Prosbeta7","description":"Proteasome subunit beta type-4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-98978","identifier":"P40301","identifierLink":"https://www.uniprot.org/uniprotkb/P40301/entry","name":"Prosalpha2","description":"Proteasome subunit alpha type-2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9124","complexName":"RPD3S histone deacetylase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Histone deacetylase which functions by deacetylating chromatin, thereby limiting accessibility of the transcriptional machinery to the underlying DNA. May recognize the H3K36me3 marker and function in the suppression of antisense transcription and protection from genotoxic agents","predictedComplex":false,"interactors":[{"ac":"EBI-15632828","identifier":"Q09819","identifierLink":"https://www.uniprot.org/uniprotkb/Q09819/entry","name":"yac5","description":"Uncharacterized protein C16C9.05","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR47636","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15632917","identifier":"Q09698","identifierLink":"https://www.uniprot.org/uniprotkb/Q09698/entry","name":"ya27","description":"Uncharacterized protein C2F7.07c","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR47636","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-904651","identifier":"O59702","identifierLink":"https://www.uniprot.org/uniprotkb/O59702/entry","name":"clr6","description":"Histone deacetylase clr6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-904686","identifier":"O13919","identifierLink":"https://www.uniprot.org/uniprotkb/O13919/entry","name":"pst2","description":"Paired amphipathic helix protein pst2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-904698","identifier":"O14021","identifierLink":"https://www.uniprot.org/uniprotkb/O14021/entry","name":"prw1","description":"RbAp48-related WD40 repeat-containing protein prw1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-904711","identifier":"O13953","identifierLink":"https://www.uniprot.org/uniprotkb/O13953/entry","name":"alp13","description":"Chromatin modification-related protein eaf3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10880","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9126","complexName":"Interleukin-1 antagonist complex","organismName":"Homo sapiens; 9606","description":"Complex formed on the binding of the interleukin-1 receptor (IL1R1) to the interleukin-1 receptor agonist (IL1RA). IL1RA competitively binds to the IL1R1 with a high affinity thereby preventing it binding to IL1A (P01583) and IL1B (P01584), resulting in the non-recruitment of the accessory protein subunit responsible for signalling, IL1RAP (Q9NPH3) and abrogation of signal transduction.\r\n\r\nOverproduction of IL1B and IL1A and the consequent up-regulation of IL1R1 are responsible for driving various chronic inflammatory and auto-immune disorders. Therapeutic approaches have targeted IL1 neutralization through antagonists or by inhibiting IL1 signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-1026330","identifier":"P18510","identifierLink":"https://www.uniprot.org/uniprotkb/P18510/entry","name":"IL1RN","description":"Interleukin-1 receptor antagonist protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10078","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-525905","identifier":"P14778","identifierLink":"https://www.uniprot.org/uniprotkb/P14778/entry","name":"IL1R1","description":"Interleukin-1 receptor type 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9128","complexName":"Interleukin-1 beta ligand-soluble receptor type 1 complex","organismName":"Homo sapiens; 9606","description":"Complex formed on the binding of a pre-bound extracellular interleukin-1 beta (IL1B) and a soluble form of its receptor, interleukin-1R1 (IL1R1) to its coreceptor, interleukin-1 receptor accessory protein (IL1RAP). Recruitment of IL1RAP completes complex assembly and initiates activation of the NFKB signalling pathway. \r\n\r\nA member of the IL1 family of cytokines, IL1B is closely related to interleukin-1 alpha (IL1A, P01583) carrying out similar biological functions by binding to their shared receptor complex. Although both IL1A and IL1B function via the same IL1R1 to drive an inflammatory response, IL1A is thought to act as an alarmin which regulates local inflammation while IL1B acts as a master regulator of systemic inflammation.  IL1B is an inducible cytokine produced mainly by blood myeloid cells, pathogenic lymphocytes and the central nervous system's (CNS) microglia and astroyctes during autoimmune, metabolic and neurodegenerative disorders.\r\n\r\nIL1 activity is regulated by two forms of the IL1R1: a membrane-bound form (mIL1R1, CPX-527) and a soluble form (sIL1R1, this complex) created through proteolytic release of the ectodomain (ECD) of mIL1R1 by matrix metalloproteases. The ECD in both forms is vital for ligand recognition and binding. Both forms of IL1R1 are biologically active, mediating an inflammatory response through agonistic and antagonistic regulation of cytokine activity.","predictedComplex":false,"interactors":[{"ac":"EBI-52378185","identifier":"P01584-PRO_0000015302","identifierLink":"https://www.uniprot.org/uniprotkb/P01584-PRO_0000015302/entry","name":"IL1B","description":"Interleukin-1 beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-52378192","identifier":"P14778-PRO_0000415344","identifierLink":"https://www.uniprot.org/uniprotkb/P14778-PRO_0000415344/entry","name":"IL1R1","description":"Interleukin-1 receptor type 1, soluble form","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-525939","identifier":"Q9NPH3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPH3/entry","name":"IL1RAP","description":"Interleukin-1 receptor accessory protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9129","complexName":"RPD3L histone deacetylase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Histone deacetylase recruited to promoters in association with specific transcription factors where it acts as a promoter targeted regulator of transcription by deacetylating lysine residues on the N-terminal region of the core histones (H2A, H2B, H3 and H4). Potential additional components include  laf1 (O13719) and laf2 (O74443).","predictedComplex":false,"interactors":[{"ac":"EBI-15632777","identifier":"O74736","identifierLink":"https://www.uniprot.org/uniprotkb/O74736/entry","name":"png2","description":"Chromatin modification-related protein png2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15632806","identifier":"Q9UTB6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UTB6/entry","name":"sds3","description":"Transcriptional regulatory protein sds3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR21964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52378533","identifier":"O74755","identifierLink":"https://www.uniprot.org/uniprotkb/O74755/entry","name":"pst3","description":"Paired amphipathic helix protein pst3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52378558","identifier":"O94707","identifierLink":"https://www.uniprot.org/uniprotkb/O94707/entry","name":"rxt3","description":"Transcriptional regulatory protein rxt3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-52378571","identifier":"O94355","identifierLink":"https://www.uniprot.org/uniprotkb/O94355/entry","name":"rtx2","description":"Transcriptional regulatory protein rxt2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52378588","identifier":"Q9P7M1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P7M1/entry","name":"dep1","description":"Transcriptional regulatory protein dep1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR21964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52378697","identifier":"Q1MTR4","identifierLink":"https://www.uniprot.org/uniprotkb/Q1MTR4/entry","name":"cti6","description":"Putative histone deacetylase complex subunit cti6","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR47793","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-904651","identifier":"O59702","identifierLink":"https://www.uniprot.org/uniprotkb/O59702/entry","name":"clr6","description":"Histone deacetylase clr6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-904671","identifier":"Q09750","identifierLink":"https://www.uniprot.org/uniprotkb/Q09750/entry","name":"pst1","description":"Paired amphipathic helix protein pst1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-904698","identifier":"O14021","identifierLink":"https://www.uniprot.org/uniprotkb/O14021/entry","name":"prw1","description":"RbAp48-related WD40 repeat-containing protein prw1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9141","complexName":"Silencing factor of the integrated stress response complex","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase complex which silences the cellular response to mitochondrial protein import stress. The complex turns off a general stress response after a specific stress event has been resolved by recognizing bifunctional substrate motifs that equally encode protein localization and degradation. Ubiquitinylates DELE1 (Q14154) a sensor of mitochondrial import stress, and EIF2AK1 (Q9BQI3), a kinase involved in the integrated stress response promoting the degradation of these proteins that actively mediate the cellular response to mitochondrial import stress.","predictedComplex":false,"interactors":[{"ac":"EBI-1995940","identifier":"Q5T4S7","identifierLink":"https://www.uniprot.org/uniprotkb/Q5T4S7/entry","name":"UBR4","description":"E3 ubiquitin-protein ligase UBR4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21725","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397435","identifier":"P62158","identifierLink":"https://www.uniprot.org/uniprotkb/P62158/entry","name":"calm_human","description":"Calmodulin","stochiometry":"minValue: 2, maxValue: 2","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-6870925","identifier":"Q9P0J7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P0J7/entry","name":"KCMF1","description":"E3 ubiquitin-protein ligase KCMF1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12268","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9162","complexName":"MIER1 histone deacetylase complex, HDAC2 variant","organismName":"Homo sapiens; 9606","description":"Class I histone deacetylase complex with a role in transcriptional repression, by acting as an epigenetic eraser removing acetyl groups from histone tails. This results in the loss of binding sites for regulatory reader proteins and causes chromatin compaction by restoring the positive charge on histone tails. May act downstream of the Polycomb repressive 2 family of complexes to expand regions of repressed chromatin and may bind and deposit histone octamers onto nucleosome-depleted regions of DNA.","predictedComplex":false,"interactors":[{"ac":"EBI-301821","identifier":"Q92769","identifierLink":"https://www.uniprot.org/uniprotkb/Q92769/entry","name":"HDAC2","description":"Histone deacetylase 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3504940","identifier":"Q8N108","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N108/entry","name":"MIER1","description":"Mesoderm induction early response protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10865","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9163","complexName":"MIER2 histone deacetylase complex, HDAC1 variant","organismName":"Homo sapiens; 9606","description":"Class I histone deacetylase complex with a role in transcriptional repression, by acting as an epigenetic eraser removing acetyl groups from histone tails. This results in the loss of binding sites for regulatory reader proteins and causes chromatin compaction by restoring the positive charge on histone tails. May act downstream of the Polycomb repressive 2 family of complexes to expand regions of repressed chromatin and may bind and deposit histone octamers onto nucleosome-depleted regions of DNA.","predictedComplex":false,"interactors":[{"ac":"EBI-301834","identifier":"Q13547","identifierLink":"https://www.uniprot.org/uniprotkb/Q13547/entry","name":"HDAC1","description":"Histone deacetylase 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3504938","identifier":"Q8N344","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N344/entry","name":"MIER2","description":"Mesoderm induction early response protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10865","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9165","complexName":"CatSpermasome complex","organismName":"Homo sapiens; 9606","description":"Sperm-specific cation channel, CatSper mediated Ca2+ signalling initiates the tyrosine phosphorylation cascade thereby controlling sperm motility. Also plays a central role in sperm chemotaxis, and mediates the Ca2+ influx induced by the steroid sex hormone progesterone in human sperm. \r\n\r\nDefective CatSper function affects migration, possibly preventing sperm reaching the site of fertilization, thereby displaying an infertility phenotype in mice and humans. Deletions of CatSper2 and CatSper epsilon variants c.2394_2399del are associated with CatSper-related male infertility.","predictedComplex":false,"interactors":[{"ac":"EBI-10260328","identifier":"Q86XM0","identifierLink":"https://www.uniprot.org/uniprotkb/Q86XM0/entry","name":"CATSPERD","description":"Cation channel sperm-associated auxiliary subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR33722","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17180389","identifier":"E9PQX1","identifierLink":"https://www.uniprot.org/uniprotkb/E9PQX1/entry","name":"TMEM262","description":"Cation channel sperm-associated auxiliary subunit TMEM262","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR37998","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21541251","identifier":"Q7RTX7","identifierLink":"https://www.uniprot.org/uniprotkb/Q7RTX7/entry","name":"CATSPER4","description":"Cation channel sperm-associated protein 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2215024","identifier":"Q96P56","identifierLink":"https://www.uniprot.org/uniprotkb/Q96P56/entry","name":"CATSPER2","description":"Cation channel sperm-associated protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46923","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2874593","identifier":"Q5SY80","identifierLink":"https://www.uniprot.org/uniprotkb/Q5SY80/entry","name":"CATSPERE","description":"Cation channel sperm-associated auxiliary subunit epsilon","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR33722","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52385699","identifier":"Q6ZRH7","identifierLink":"https://www.uniprot.org/uniprotkb/Q6ZRH7/entry","name":"CATSPERG","description":"Cation channel sperm-associated auxiliary subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14327","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52385724","identifier":"Q86XQ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q86XQ3/entry","name":"CATSPER3","description":"Cation channel sperm-associated protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52385746","identifier":"Q9H7T0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H7T0/entry","name":"CATSPERB","description":"Cation channel sperm-associated auxiliary subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14705","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52385772","identifier":"Q9NTU4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NTU4/entry","name":"CATSPERZ","description":"Cation channel sperm-associated auxiliary subunit zeta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR42155","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52385790","identifier":"A8MZ26","identifierLink":"https://www.uniprot.org/uniprotkb/A8MZ26/entry","name":"EFCAB9","description":"EF-hand calcium-binding domain-containing protein 9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47065","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52385809","identifier":"Q2WGJ8","identifierLink":"https://www.uniprot.org/uniprotkb/Q2WGJ8/entry","name":"TMEM249","description":"Cation channel sperm-associated auxiliary subunit TMEM249","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR35442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744545","identifier":"Q8NEC5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NEC5/entry","name":"CATSPER1","description":"Cation channel sperm-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47193","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9166","complexName":"Precursor interleukin-1 alpha-soluble receptor type 1 complex","organismName":"Homo sapiens; 9606","description":"Complex formed on the binding of a pre-bound precursor form of interleukin-1 alpha (IL1A) and a soluble form of its receptor, interleukin-1R1 (IL1R1) to its coreceptor, interleukin-1 receptor accessory protein (IL1RAP). \r\nA member of the IL1 family of cytokines, IL1A is closely related to interleukin-1 beta (IL1B, P01584) carrying out similar biological functions by binding to their shared receptor complex. Although both IL1A and IL1B function via the same IL1R1 to drive an inflammatory response, IL1A acts as an alarmin and is thought to focus its efforts on local inflammation while IL1B acts as a master regulator of systemic inflammation.  \r\n\r\n\r\nIL1A precursor protein (ProIL1A) is constitutively expressed by many cell types and is released upon necrotic cell death as a bioactive mediator, making it central to the pathogenesis of all conditions characterized by organ or tissue inflammation where the epitheilal barrier is disrupted.\r\n\r\nProIL1A (this complex) is processed by calpain II (P17655) to produce the more biologically active, secreted form. IL1A activity is regulated by two forms of the IL1R1: a membrane-bound form (mIL1R1, CPX-9169) and a soluble form (sIL1R1, this complex) created through proteolytic release of the ectodomain (ECD) of mIL1R1 by matrix metalloproteases. Both forms of IL1R1 are biologically active and the ECD in both forms is vital for ligand recognition and binding.","predictedComplex":false,"interactors":[{"ac":"EBI-1749782","identifier":"P01583","identifierLink":"https://www.uniprot.org/uniprotkb/P01583/entry","name":"IL1A","description":"Interleukin-1 alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10078","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52378192","identifier":"P14778-PRO_0000415344","identifierLink":"https://www.uniprot.org/uniprotkb/P14778-PRO_0000415344/entry","name":"IL1R1","description":"Interleukin-1 receptor type 1, soluble form","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-525939","identifier":"Q9NPH3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPH3/entry","name":"IL1RAP","description":"Interleukin-1 receptor accessory protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9167","complexName":"MIER2 histone deacetylase complex, HDAC2 variant","organismName":"Homo sapiens; 9606","description":"Class I histone deacetylase complex with a role in transcriptional repression, by acting as an epigenetic eraser removing acetyl groups from histone tails. This results in the loss of binding sites for regulatory reader proteins and causes chromatin compaction by restoring the positive charge on histone tails. May act downstream of the Polycomb repressive 2 family of complexes to expand regions of repressed chromatin and may bind and deposit histone octamers onto nucleosome-depleted regions of DNA.","predictedComplex":false,"interactors":[{"ac":"EBI-301821","identifier":"Q92769","identifierLink":"https://www.uniprot.org/uniprotkb/Q92769/entry","name":"HDAC2","description":"Histone deacetylase 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3504938","identifier":"Q8N344","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N344/entry","name":"MIER2","description":"Mesoderm induction early response protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10865","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9168","complexName":"Interleukin-1 alpha decoy receptor-ligand type 2 complex","organismName":"Homo sapiens; 9606","description":"A decoy receptor complex which acts by competitively binding both IL1A and  IL1RAP with high affinity, preventing their binding to IL1R1 thus inhibiting IL1 induced inflammation  IL1R2 binding to precursor IL1A prevents calpain cleavage. \r\n\r\nNon-signaling IL1R2 is the predominant IL1 binding receptor expressed by monocytes, neutrophils and B cells. Regulatory T-cells also express membrane-bound and soluble IL1R2 (sIL1R2) but pro-inflammatory molecules are thought to inhibit IL1R2 expression. \r\n\r\nPlasma of healthy individuals are thought to contain high levels of sIL1R2, while defective or increased expression sIL1R2 in tissue or bodily fluids are ascribed to a range of pathological conditions, including critical autoimmune diseases, tumours and neuroinflammatory diseases.","predictedComplex":false,"interactors":[{"ac":"EBI-1749782","identifier":"P01583","identifierLink":"https://www.uniprot.org/uniprotkb/P01583/entry","name":"IL1A","description":"Interleukin-1 alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10078","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2831568","identifier":"P27930","identifierLink":"https://www.uniprot.org/uniprotkb/P27930/entry","name":"IL1R2","description":"Interleukin-1 receptor type 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-525939","identifier":"Q9NPH3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPH3/entry","name":"IL1RAP","description":"Interleukin-1 receptor accessory protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9169","complexName":"Precursor interleukin-1 alpha-membrane-bound receptor type 1 complex","organismName":"Homo sapiens; 9606","description":"Complex formed on the binding of a pre-bound precursor form of interleukin-1 alpha (IL1A) and the membrane-bound form of its receptor, interleukin-1R1 (IL1R1) to its coreceptor, interleukin-1 receptor accessory protein (IL1RAP).  \r\n\r\nA member of the IL1 family of cytokines, IL1A is closely related to interleukin-1 beta (IL1B, P01584) carrying out similar biological functions by binding to their shared receptor complex. Although both IL1A and IL1B function via the same IL1R1 to drive an inflammatory response, IL1A acts as an alarmin and is thought to focus its efforts on local inflammation while IL1B acts as a master regulator of systemic inflammation.","predictedComplex":false,"interactors":[{"ac":"EBI-1749782","identifier":"P01583","identifierLink":"https://www.uniprot.org/uniprotkb/P01583/entry","name":"IL1A","description":"Interleukin-1 alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10078","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52378176","identifier":"P14778-PRO_0000015435","identifierLink":"https://www.uniprot.org/uniprotkb/P14778-PRO_0000015435/entry","name":"IL1R1","description":"Interleukin-1 receptor type 1, membrane form","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-525939","identifier":"Q9NPH3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPH3/entry","name":"IL1RAP","description":"Interleukin-1 receptor accessory protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9173","complexName":"Interleukin-1 alpha-membrane-bound receptor type 1 complex","organismName":"Homo sapiens; 9606","description":"Complex formed on the binding of a pre-bound mature form of interleukin-1 alpha (IL1A) and a membrane-bound form of its receptor, interleukin-1R1 (IL1R1) to its coreceptor, interleukin-1 receptor accessory protein (IL1RAP). Recruitment of IL1RAP completes complex assembly and initiates activation of the NFKB signalling pathway.\r\n\r\nA member of the IL1 family of cytokines, IL1A is closely related to interleukin-1 beta (IL1B, P01584) carrying out similar biological functions by binding to their shared receptor complex. Although both IL1A and IL1B function via the same IL1R1 to drive an inflammatory response, IL1A acts as an alarmin which regulates local inflammation while IL1B acts as a master regulator of systemic inflammation.\r\n\r\nIL1A is synthesized as a precursor protein which is processed by calpain II (P17655) to produce a more active, mature form. IL1A activity is regulated by two forms of the IL1R1: a membrane-bound form (mIL1R1, this complex) and a soluble form (sIL1R1) created through proteolytic release of the ectodomain (ECD) of mIL1R1 via matrix metalloproteases. The ECD in both forms is vital for ligand recognition and binding. Both forms of IL1A and IL1R1 are biologically active, mediating an inflammatory response through agonistic and antagonistic regulation of cytokine activity.","predictedComplex":false,"interactors":[{"ac":"EBI-52378176","identifier":"P14778-PRO_0000015435","identifierLink":"https://www.uniprot.org/uniprotkb/P14778-PRO_0000015435/entry","name":"IL1R1","description":"Interleukin-1 receptor type 1, membrane form","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-52386506","identifier":"P01583-PRO_0000015266","identifierLink":"https://www.uniprot.org/uniprotkb/P01583-PRO_0000015266/entry","name":"IL1A","description":"Interleukin-1 alpha","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-525939","identifier":"Q9NPH3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPH3/entry","name":"IL1RAP","description":"Interleukin-1 receptor accessory protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9181","complexName":"SESAME metabolic enzyme complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Multi-enzyme complex which regulates the crosstalk between Histone H3 (HHt1/HHT2, P61830) methylation and phosphorylation by sensing glycolysis and glucose-derived serine metabolism. This leads to auto-regulation of the expression of the PYK1 pyruvate kinase. Complex activity is stimulated by glycolysis and serine metabolism to repress gene expression and confer cell resistance to oxidative stress.\r\nIn the presence of sufficient glucose, PYK1 is activated, and SET1 (P38827) is recruited at the promoter of PYK1 by active RNA polymerase II. PYK1 phosphorylates Thr-12 of histone H3 using phosphoenolpyruvate as a substrate, while serine biosynthetic enzymes in SESAME generate serine from 3-phosphoglyceric acid to stimulate this phosphorylation. The COMPASS complex (CPX-1039) then recruits SESAME to the PYK1 coding region, allowing COMPASS to utilize SAM synthesized by SESAME to methylate H3 Lys-5. This interaction with COMPASS promotes SESAME recruitment, which phosphorylates H3 Thr-12 at the gene body and suppresses PYK1 transcription. The acetyl-coenzyme A synthetase ACS2 is required for the regulation of telomere silencing and cellular senescence. SESAME interacts with the  SAS histone acetyltransferase complex (CPX-777) to promote histone H4 (HHF1/ HHF2) Lys-17 acetylation and the occupancy of the transcription factor , BDF1 (P35817), at subtelomeric regions. This interaction maintains telomere silencing by antagonizing the spreading of SIR2 (P06700) histone deacetylase along the telomeres, which is enhanced by acetate.","predictedComplex":false,"interactors":[{"ac":"EBI-10789","identifier":"P10659","identifierLink":"https://www.uniprot.org/uniprotkb/P10659/entry","name":"SAM1","description":"S-adenosylmethionine synthase 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10795","identifier":"P19358","identifierLink":"https://www.uniprot.org/uniprotkb/P19358/entry","name":"SAM2","description":"S-adenosylmethionine synthase 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11964","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16821","identifier":"P40510","identifierLink":"https://www.uniprot.org/uniprotkb/P40510/entry","name":"SER33","description":"D-3-phosphoglycerate dehydrogenase 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10996","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16961","identifier":"P40054","identifierLink":"https://www.uniprot.org/uniprotkb/P40054/entry","name":"SER3","description":"D-3-phosphoglycerate dehydrogenase 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10996","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2136","identifier":"P52910","identifierLink":"https://www.uniprot.org/uniprotkb/P52910/entry","name":"ACS2","description":"Acetyl-coenzyme A synthetase 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24095","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32717409","identifier":"CHEBI:57540","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57540","name":"nad(1-)","description":"NAD(1-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-7744","identifier":"P37291","identifierLink":"https://www.uniprot.org/uniprotkb/P37291/entry","name":"SHM2","description":"Serine hydroxymethyltransferase, cytosolic","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11680","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8852014","identifier":"CHEBI:597326","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:597326","name":"pyridoxal 5'-phosphate(2-)","description":"pyridoxal 5'-phosphate(2-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9890","identifier":"P00549","identifierLink":"https://www.uniprot.org/uniprotkb/P00549/entry","name":"CDC19","description":"Pyruvate kinase 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11817","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9182","complexName":"SPATA5-SPATA5L1 ATPase complex","organismName":"Homo sapiens; 9606","description":"Acts as an ubiquitin-independent unfoldase, remodeling protein complexes and facilitating their subsequent cleavage by cysteine proteases and their subsequent removal from the chromatin. Processes replisome substrates in response to replication fork damage.\r\n\r\nDeficiency of the complex induces ubiquitin-independent proteotoxicity, replication stress and acute chromosome instability. Neurodevelopmental syndromes including epilepsy, hearing loss, mental retardation syndrome (EHLMRS) and neurodevelopmental disorder with hearing loss and spasticity (NEDHLS) are associated with SPATA5 and SPATA5L1 mutations.","predictedComplex":false,"interactors":[{"ac":"EBI-3184062","identifier":"Q8NB90","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NB90/entry","name":"AFG2A","description":"ATPase family gene 2 protein homolog A","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-739784","identifier":"Q9BW66","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BW66/entry","name":"CINP","description":"Cyclin-dependent kinase 2-interacting protein","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15827","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7950854","identifier":"Q9BVQ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BVQ7/entry","name":"AFG2B","description":"ATPase family gene 2 protein homolog B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8643161","identifier":"Q9NX04","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NX04/entry","name":"AIRIM","description":"AFG2-interacting ribosome maturation factor","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16234","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9184","complexName":"Chitinase 3-like-1-tmem219-interleukin-13 receptor-ligand alpha-2 signalling complex","organismName":"Homo sapiens; 9606","description":"Complex formed upon Chitinase-3-like protein 1 (CHI3L1) binding to interleukin-13 receptor alpha-2 (IL13RA2) by associating with TMEM219 which is a cell-death receptor for IGFBP-3 (P17936). CHI3L1 interaction with IL13RA2 through a TMEM219-dependent pathway prevents cell death by activating the MAP kinases, ERK1/2 and AKT pathways, while direct interaction with IL13RA2 results in apoptosis through activation of Wnt/beta-catenin (P35222). Functional effects of this complex is also moderated by LGALS3 (P17931), which physically interacts with IL13RA2 and CHI3L1 to compete with TMEM219 for IL13RA2 binding, thereby diminishing the anti-apoptotic role of CHI3L1.\r\n\r\nIL13RA2 also forms a complex with IL13 and TMEM219 (CPX847) which largely acts as a decoy to diminish IL13 activity. IL13RA2 N-glycosylation is a critical determinant of whether it binds CHI3L1 or IL13; CHI3L1 binding to IL13RA2 and signalling is increased if IL13RA2 N-glycosylation is diminished.\r\n\r\nCHI3L1 is a carbohydrate-binding lectin with a preference for chitin, produced by immune cells, osteoclasts, chondrocytes, smooth muscle cells, astrocytes and cancer cells upon stimulation from several interleukins including IL13, IL6, IL1B and TNF. CHI3L1 expression is inhibited by miR-24, miR-342-3p, miR-449a, miR125a-3p and miR-96-5p.\r\n\r\nCHI3L1 binding to IL13RA2 leads to inflammasome activation, melanoma metastasis, apoptosis, oxidative damage, allergic inflammation, wound healing, fibrosis, and TGFB1 production. CH3L1 also plays a key role in antipathogenic responses and is involved in stimulating disease tolerance by controlling cell death, inflammation and remodelling.","predictedComplex":false,"interactors":[{"ac":"EBI-1647828","identifier":"P35225","identifierLink":"https://www.uniprot.org/uniprotkb/P35225/entry","name":"IL13","description":"Interleukin-13","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48486","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20264080","identifier":"Q86XT9","identifierLink":"https://www.uniprot.org/uniprotkb/Q86XT9/entry","name":"TMEM219","description":"Insulin-like growth factor-binding protein 3 receptor","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16002","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4320063","identifier":"Q14627","identifierLink":"https://www.uniprot.org/uniprotkb/Q14627/entry","name":"IL13RA2","description":"Interleukin-13 receptor subunit alpha-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6917454","identifier":"P36222","identifierLink":"https://www.uniprot.org/uniprotkb/P36222/entry","name":"CHI3L1","description":"Chitinase-3-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11177","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9201","complexName":"Interleukin-17A receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Pro-inflammatory cytokine receptor which plays a key role in both adaptive and innate immunity. TRAF3IP2 polyubiquitinates TRAF6 (Q9Y4K3) leading to the recruitment of downstream molecules and the activation of NF-KB and the mitogen-activated protein kinase (MAPK) pathways.\r\n\r\nExpressed by CD4+ type 17 helper cells and Tc17 cells, IL17 is also produced by several innate immune cells. IL17RA is the common subunit for all of the IL17 receptors and IL17A signalling is moderated by the restricted expression of IL17RC to non-hematopoietic epithelial and mesenchymal cells.\r\n\r\nUnrestrained IL17 signalling is associated with autoimmune diseases and cancer progression, but it is also crucial for protection from fungal and bacterial infections, including the commensal Candida albicans and Klebsiella pneumoniae. IL17 is also thought to play a dominant protective role in maintaining intestinal barrier integrity. Among the IL17 family of cytokines, IL17A is the main cytokine associated with the pathogenesis of autoimmune diseases including psoriasis, systemic lupus erythematosus and multiple sclerosis.","predictedComplex":false,"interactors":[{"ac":"EBI-10237926","identifier":"Q16552","identifierLink":"https://www.uniprot.org/uniprotkb/Q16552/entry","name":"IL17A","description":"Interleukin-17A","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-53978998","identifier":"Q8NAC3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NAC3/entry","name":"IL17RC","description":"Interleukin-17 receptor C","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15583","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5591258","identifier":"Q96F46","identifierLink":"https://www.uniprot.org/uniprotkb/Q96F46/entry","name":"IL17RA","description":"Interleukin-17 receptor A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15583","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744798","identifier":"O43734","identifierLink":"https://www.uniprot.org/uniprotkb/O43734/entry","name":"TRAF3IP2","description":"E3 ubiquitin ligase TRAF3IP2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR34257","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9202","complexName":"Interleukin-17F receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Pro-inflammatory cytokine receptor which plays a key role in both adaptive and innate immunity. TRAF3IP2 polyubiquitinates TRAF6 (Q9Y4K3) leading to the recruitment of downstream molecules and the activation of NF-KB and the mitogen-activated protein kinase (MAPK) pathways.\r\n\r\nExpressed by CD4+ type 17 helper cells and Tc17 cells, IL17 is also produced by several innate immune cells. IL17RA is the common subunit for all of the IL17 receptors and IL17F signalling is moderated by the restricted expression of IL17RC to non-hematopoietic epithelial and mesenchymal cells.\r\n\r\nUnrestrained IL17 signalling is associated with autoimmune diseases and cancer progression, but it is also crucial for protection from fungal and bacterial infections, including the commensal Candida albicans and Klebsiella pneumoniae. IL17 is also thought to play a dominant protective role in maintaining intestinal barrier integrity.","predictedComplex":false,"interactors":[{"ac":"EBI-10292310","identifier":"Q96PD4","identifierLink":"https://www.uniprot.org/uniprotkb/Q96PD4/entry","name":"IL17F","description":"Interleukin-17F","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-53978998","identifier":"Q8NAC3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NAC3/entry","name":"IL17RC","description":"Interleukin-17 receptor C","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15583","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5591258","identifier":"Q96F46","identifierLink":"https://www.uniprot.org/uniprotkb/Q96F46/entry","name":"IL17RA","description":"Interleukin-17 receptor A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15583","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744798","identifier":"O43734","identifierLink":"https://www.uniprot.org/uniprotkb/O43734/entry","name":"TRAF3IP2","description":"E3 ubiquitin ligase TRAF3IP2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR34257","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9204","complexName":"Interleukin-25 receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Pro-inflammatory cytokine receptor which plays a key role in both adaptive and innate immunity. TRAF3IP2 polyubiquitinates TRAF6 (Q9Y4K3) leading to the recruitment of downstream molecules and the activation of NF-KB and the mitogen-activated protein kinase (MAPK) pathways.\r\n\r\nExpressed by CD4+ type 17 helper cells and Tc17 cells, IL17 is also produced by several innate immune cells. IL25 binds only to IL17RB but requires the IL17RA:IL17RB receptor complex to mediate its effects. \r\n\r\nUnrestrained IL17 signalling is associated with autoimmune diseases and cancer progression, but it is also crucial for protection from fungal and bacterial infections, including the commensal Candida albicans and Klebsiella pneumoniae. Both IL25 and IL17B promote IL33-driven (O95760) type 2 immune responses, but perform contradictory roles in colitis; IL25 is pathogenic and IL17B is protective. IL17B is thought to inhibit IL25 binding to IL17RA:IL17RB expressed on epithelial cells thereby limiting IL25 induced IL6 (P05231) production by colonic epithelial cells.","predictedComplex":false,"interactors":[{"ac":"EBI-2867349","identifier":"Q9NRM6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NRM6/entry","name":"IL17RB","description":"Interleukin-17 receptor B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15583","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2880054","identifier":"Q9H293","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H293/entry","name":"IL25","description":"Interleukin-25","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-5591258","identifier":"Q96F46","identifierLink":"https://www.uniprot.org/uniprotkb/Q96F46/entry","name":"IL17RA","description":"Interleukin-17 receptor A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15583","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744798","identifier":"O43734","identifierLink":"https://www.uniprot.org/uniprotkb/O43734/entry","name":"TRAF3IP2","description":"E3 ubiquitin ligase TRAF3IP2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR34257","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9206","complexName":"Interleukin-17B receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Pro-inflammatory cytokine receptor which plays a key role in both adaptive and innate immunity. TRAF3IP2 polyubiquitinates TRAF6 (Q9Y4K3) leading to the recruitment of downstream molecules and the activation of NF-KB and the mitogen-activated protein kinase (MAPK) pathways.\r\n\r\nExpressed by CD4+ type 17 helper cells and Tc17 cells, IL17 is also produced by several innate immune cells. IL17RA is the common subunit for all of the IL17 receptors and IL17B signalling is moderated by the restricted expression of IL17RB to various endocrine and mucosal tissues and epithelial cells. \r\n\r\nUnrestrained IL17 signalling is associated with autoimmune diseases and cancer progression, but it is also crucial for protection from fungal and bacterial infections, including the commensal Candida albicans and Klebsiella pneumoniae. Both IL17B and IL25 promote IL33-driven (O95760) type 2 immune responses, but perform contradictory roles in colitis; IL-25 is pathogenic and IL17B is protective. IL17B is thought to inhibit IL25 binding to IL17RA:IL17RB expressed on epithelial cells thereby limiting IL25 induced IL6 production by colonic epithelial cells. Heightened IL17B and IL17RB expression are associated with poor prognosis for several cancers including breast and pancreatic cancers.","predictedComplex":false,"interactors":[{"ac":"EBI-2867349","identifier":"Q9NRM6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NRM6/entry","name":"IL17RB","description":"Interleukin-17 receptor B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15583","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5591258","identifier":"Q96F46","identifierLink":"https://www.uniprot.org/uniprotkb/Q96F46/entry","name":"IL17RA","description":"Interleukin-17 receptor A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15583","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-719639","identifier":"Q9UHF5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UHF5/entry","name":"IL17B","description":"Interleukin-17B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-744798","identifier":"O43734","identifierLink":"https://www.uniprot.org/uniprotkb/O43734/entry","name":"TRAF3IP2","description":"E3 ubiquitin ligase TRAF3IP2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR34257","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9207","complexName":"Interleukin-17C receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Pro-inflammatory cytokine receptor which plays a key role in both adaptive and innate immunity. TRAF3IP2 polyubiquitinates TRAF6 (Q9Y4K3) leading to the recruitment of downstream molecules and the activation of NF-KB and the mitogen-activated protein kinase (MAPK) pathways. IL17C-IL17RE signalling also activates anti-apoptotic pathways via BCL2(P10415) and BCL2L1 (Q07817).\r\n\r\nWhile the prototypic IL17A is preferentially produced by immune cells, IL17C is predominantly produced by non-immune cells and its production is up-regulated in epethelial cells at an early stage in several diseases. IL17C mediates its effects through the IL17RA:IL17RE expressed by both epithelial and CD4+ type 17 helper cells.\r\n\r\nUnrestrained IL17C signalling is associated with autoimmune diseases and cancer progression, but it is also crucial for protection from fungal and bacterial infections such as Pseudomonas aeruginosa. IL17C is induced under hypoxic and hyperglycemic conditions and is thought to drive a pathogenic inflammatory response in kidney disease. IL17C may also be involved in the development of atherosclerosis, COPD and cystic fibrosis.","predictedComplex":false,"interactors":[{"ac":"EBI-54439466","identifier":"Q9P0M4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P0M4/entry","name":"IL17C","description":"Interleukin-17C","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-5591258","identifier":"Q96F46","identifierLink":"https://www.uniprot.org/uniprotkb/Q96F46/entry","name":"IL17RA","description":"Interleukin-17 receptor A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15583","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5591275","identifier":"Q8NFR9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NFR9/entry","name":"IL17RE","description":"Interleukin-17 receptor E","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15583","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744798","identifier":"O43734","identifierLink":"https://www.uniprot.org/uniprotkb/O43734/entry","name":"TRAF3IP2","description":"E3 ubiquitin ligase TRAF3IP2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR34257","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9221","complexName":"Lymphotoxin-alpha-TNFRSF1B receptor complex","organismName":"Homo sapiens; 9606","description":"Receptor complex whose primary role is in lymphoid organ development, organization and the maintenance of lymphoid microenvironments to promote host defense, and inflammation. LTA mediates its effects through one of three receptors: TNFRSF1A (CPX-8945), TNFRSF1B (this complex) or TNFRSF14 (CPX-9222). TNFRSF1B lacks the death domain and is a prototypical TNFRSF receptor with a TRAF2 (Q12933) binding site at its C-terminal. Signalling can lead to apoptosis but preferentially results in cell proliferation and survival via NF-KB-NIK activation. \r\n\r\nLTA is produced by activated innate and adaptive immune cells and its effects are mediated through TNFRSF1B which is expressed on almost most cells, including tumour cell types.","predictedComplex":false,"interactors":[{"ac":"EBI-358983","identifier":"P20333","identifierLink":"https://www.uniprot.org/uniprotkb/P20333/entry","name":"TNFRSF1B","description":"Tumor necrosis factor receptor superfamily member 1B","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47386","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-524105","identifier":"P01374","identifierLink":"https://www.uniprot.org/uniprotkb/P01374/entry","name":"LTA","description":"Lymphotoxin-alpha","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11471","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9222","complexName":"Lymphotoxin-alpha-TNFRSF14 receptor complex","organismName":"Homo sapiens; 9606","description":"Receptor complex which may play a role in lymphoid organ development and cytotoxic responses in the immune system. Little is known about LTA's effects through TNFRSF14 as their interaction is thought to be weak. LTA also mediates its effects through two other receptors: TNFRSF1A (CPX-8945) and TNFRSF1B (CPX-9221).","predictedComplex":false,"interactors":[{"ac":"EBI-1056653","identifier":"Q92956","identifierLink":"https://www.uniprot.org/uniprotkb/Q92956/entry","name":"TNFRSF14","description":"Tumor necrosis factor receptor superfamily member 14","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46838","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-524105","identifier":"P01374","identifierLink":"https://www.uniprot.org/uniprotkb/P01374/entry","name":"LTA","description":"Lymphotoxin-alpha","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11471","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9223","complexName":"TNFSF14-TNFRSF14 receptor complex","organismName":"Homo sapiens; 9606","description":"Receptor complex which coordinates innate and adaptive immune responses. TNFSF14 mediated signalling through TNFRSF14 provides a costimulatory signal for T and B cell activation, and in particular signalling through the TRAF2-cIAP complex (Q12933,Q13489) which initiates the NF-KB-RelA (Q04206) led transcription of genes important for inflammatory, proliferative, and survival functions. TNFSF14 also mediates its effects through LTBR (CPX-9310), and the decoy receptor TNFRSF6B (CPX-9309).\r\n\r\nPotent modulator of T-cell driven inflammatory responses but its effects are negatively modulated by herpes simplex virus (HSV) 1 virion glycoprotein D (gD); HSV1 gD inhibits the interaction of TNFRSF14 with TNFSF14, and TNFSF14 and HSV1 gD interfere with TNFRSF14-dependent cell entry by HSV1.\r\n\r\nElevated levels of TNFSF14 is associated with the pathogenesis of inflammatory and autoimmune disorders such as asthma and IBD. TNFSF14 expression is a prognostic biomarker for COVID-19 through its ability to instigate ARDS.","predictedComplex":false,"interactors":[{"ac":"EBI-1056653","identifier":"Q92956","identifierLink":"https://www.uniprot.org/uniprotkb/Q92956/entry","name":"TNFRSF14","description":"Tumor necrosis factor receptor superfamily member 14","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46838","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-524131","identifier":"O43557","identifierLink":"https://www.uniprot.org/uniprotkb/O43557/entry","name":"TNFSF14","description":"Tumor necrosis factor ligand superfamily member 14","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11471","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9241","complexName":"CLR4 E3 ubiquitin ligase/methyltransferase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Multi-enzyme complex required  for heterochromatin assembly by RNAi. rik1, pcu4, pip1, and raf1 form an active E3 ubiquitin ligase. The pip1 pprotein referentially ubiquitylates H3K14. This H3 ubiquitination promotes clr4 methylation of H3K9. Methylated H3K9 acts as a specific tag for epigenetic transcriptional repression by recruiting swi6 (P40381), leading to transcriptional silencing within centromeric heterochromatin, telomeres, ribosomal DNA repeats, and the silent mating-type region","predictedComplex":false,"interactors":[{"ac":"EBI-1111936","identifier":"Q10426","identifierLink":"https://www.uniprot.org/uniprotkb/Q10426/entry","name":"rik1","description":"Chromatin modification-related protein rik1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1112060","identifier":"O13959","identifierLink":"https://www.uniprot.org/uniprotkb/O13959/entry","name":"pip1","description":"RING-box protein pip1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30813205","identifier":"CHEBI:59789","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:59789","name":"s-adenosyl-l-methionine zwitterion","description":"S-adenosyl-L-methionine zwitterion","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-354657","identifier":"O60016","identifierLink":"https://www.uniprot.org/uniprotkb/O60016/entry","name":"clr4","description":"Histone-lysine N-methyltransferase, H3 lysine-9 specific","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR45660","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-904886","identifier":"O74560","identifierLink":"https://www.uniprot.org/uniprotkb/O74560/entry","name":"raf2","description":"Rik1-associated factor 2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-904890","identifier":"O14122","identifierLink":"https://www.uniprot.org/uniprotkb/O14122/entry","name":"pcu4","description":"Cullin-4","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-904913","identifier":"O74910","identifierLink":"https://www.uniprot.org/uniprotkb/O74910/entry","name":"raf1","description":"Rik1-associated factor 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-9261","complexName":"Snf2/HDAC repressor complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Corepressor complex that couples histone deacetylase and ATP-dependent chromatin remodeling activities. It regulates the higher-order structure of chromatin, making chromatin more compact by removing acetyl groups from nucleosomes, and has important roles in the regulation of gene expression and DNA damage repair. The complex is recruited to heterochromatin by chp2 (O42934).","predictedComplex":false,"interactors":[{"ac":"EBI-15953973","identifier":"P56523","identifierLink":"https://www.uniprot.org/uniprotkb/P56523/entry","name":"clr3","description":"Histone deacetylase clr3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-54454406","identifier":"O74808","identifierLink":"https://www.uniprot.org/uniprotkb/O74808/entry","name":"clr1","description":"Cryptic loci regulator protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-54454426","identifier":"O13881","identifierLink":"https://www.uniprot.org/uniprotkb/O13881/entry","name":"clr2","description":"Cryptic loci regulator 2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR38046","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-54454445","identifier":"Q9P793","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P793/entry","name":"mit1","description":"Chromatin remodeling factor mit1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR45623","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9262","complexName":"USP46 deubiquitinase complex","organismName":"Drosophila melanogaster; 7227","description":"Deubiquitinase complex responsible for the removal of ubiquitin chains from proteins. The complex appears to play a role in increasing the low-density lipoprotein receptor-related protein arr/LRP6 (Q95V09) stability and therefore protein levels at the cell surface, enhancing the sensitivity of cells to Wingless (P09615) stimulation.","predictedComplex":false,"interactors":[{"ac":"EBI-54454594","identifier":"Q1LZ08","identifierLink":"https://www.uniprot.org/uniprotkb/Q1LZ08/entry","name":"Uaf1","description":"WD repeat-containing protein 48 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19862","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-54454616","identifier":"Q9VCT9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VCT9/entry","name":"Usp12-46","description":"Ubiquitin carboxyl-terminal hydrolase 12/46 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR24006","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-54454643","identifier":"Q9VBC4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VBC4/entry","name":"Wdr20","description":"WD repeat-containing protein 20 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14107","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9281","complexName":"USP46 deubiquitinase complex","organismName":"Homo sapiens; 9606","description":"Deubiquitinase complex responsible for the removal of ubiquitin chains from proteins. The complex appears to be required for the deubiquitination of proteins involved in cell development and cellular signaling. May act as a positive regulator of Wnt signaling by deubiquitylating the cell surface LRP6 (O75581), inhibiting its turnover.","predictedComplex":false,"interactors":[{"ac":"EBI-1045469","identifier":"Q8TAF3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAF3/entry","name":"WDR48","description":"WD repeat-containing protein 48","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19862","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2511486","identifier":"Q8TBZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TBZ3/entry","name":"WDR20","description":"WD repeat-containing protein 20","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14107","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2512753","identifier":"P62068","identifierLink":"https://www.uniprot.org/uniprotkb/P62068/entry","name":"USP46","description":"Ubiquitin carboxyl-terminal hydrolase 46","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24006","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9301","complexName":"Interleukin-17A complex","organismName":"Homo sapiens; 9606","description":"A proinflmmatory cytokine. Member of the interleukin-17 (IL17) family which consists of six structurally related cytokines: IL17A (CPX-9301), IL17B (CPX-9302), IL17C (CPX-9305), IL17D, IL25 (CPX-9306) and IL17F (CPX-9303).\r\n\r\nExpressed by CD4+ type 17 helper cells and Tc17 cells, IL17 is also produced by several innate immune cells. \r\n\r\nUnrestrained IL17 mediated signalling, and in particular IL17A is associated with autoimmune diseases and cancer progression. However, IL17 is also crucial for protection from fungal and bacterial infections, including the commensal Candida albicans and Klebsiella pneumoniae. IL17 is also thought to play a dominant protective role in maintaining intestinal barrier integrity.","predictedComplex":false,"interactors":[{"ac":"EBI-10237926","identifier":"Q16552","identifierLink":"https://www.uniprot.org/uniprotkb/Q16552/entry","name":"IL17A","description":"Interleukin-17A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-9302","complexName":"Interleukin-17B complex","organismName":"Homo sapiens; 9606","description":"A proinflammatory cytokine. Member of the IL17 family which consists of six structurally related cytokines: IL17A (CPX-9301), IL17B (this complex), IL17C (CPX-9305), IL17D, IL25 (CPX-9306) and IL17F (CPX-9303).\r\n\r\nExpressed by CD4+ type 17 helper cells and Tc17 cells, IL17 is also produced by several innate immune cells. \r\n\r\nUnrestrained IL17 signalling is associated with autoimmune diseases and cancer progression, but it is also crucial for protection from fungal and bacterial infections, including the commensal Candida albicans and Klebsiella pneumoniae. Both IL17B and IL25 promote IL33-driven (O95760) type 2 immune responses, but perform contradictory roles in colitis; IL-25 is pathogenic and IL17B is protective. IL17B is thought to inhibit IL25 binding to IL17RA:IL17RB expressed on epithelial cells thereby limiting IL25 induced IL6 production by colonic epithelial cells.","predictedComplex":false,"interactors":[{"ac":"EBI-719639","identifier":"Q9UHF5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UHF5/entry","name":"IL17B","description":"Interleukin-17B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-9303","complexName":"Interleukin-17F complex","organismName":"Homo sapiens; 9606","description":"A proinflammatory cytokine, interleukin-17F (IL17F) is a member of the  IL17 family which consists of six structurally related cytokines: IL17A, (CPX-9301) IL17B (CPX-9302), IL17C (CPX-9305), IL17D, IL25 (CPX-9306) and IL17F (CPX-9303).\r\n\r\nExpressed by CD4+ type 17 helper cells and Tc17 cells, IL17 is also produced by several innate immune cells. \r\n\r\nUnrestrained IL17 signalling is associated with autoimmune diseases and cancer progression, but it is also crucial for protection from fungal and bacterial infections, including the commensal Candida albicans and Klebsiella pneumoniae. IL17 is also thought to play a dominant protective role in maintaining intestinal barrier integrity.","predictedComplex":false,"interactors":[{"ac":"EBI-10292310","identifier":"Q96PD4","identifierLink":"https://www.uniprot.org/uniprotkb/Q96PD4/entry","name":"IL17F","description":"Interleukin-17F","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-9305","complexName":"Interleukin-17C complex","organismName":"Homo sapiens; 9606","description":"Member of the interleukin-17 (IL17) family which consists of six structurally related cytokines: IL17A (CPX-9301), IL17B (CPX-9302), IL17C (this complex), IL17D, IL25 (CPX-9306) and IL17F (CPX-9303)\r\n\r\nIL17C is predominantly produced by non-immune cells such as colonic and lung epithelial cells, keratinocytes and smooth muscle cells. IL17C production is up-regulated in pethelial cells at an early stage in several diseases. \r\n\r\nUnrestrained IL17C signalling is associated with autoimmune diseases and cancer progression, but it is also crucial for protection from fungal and bacterial infections such as Pseudomonas aeruginosa. IL17C is induced under hypoxic and hyperglycemic conditions and is thought to drive a pathogenic inflammatory response in kidney disease. IL17C may also be involved in the development of atherosclerosis, COPD and cystic fibrosis.","predictedComplex":false,"interactors":[{"ac":"EBI-54439466","identifier":"Q9P0M4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P0M4/entry","name":"IL17C","description":"Interleukin-17C","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-9306","complexName":"Interleukin-25 complex","organismName":"Homo sapiens; 9606","description":"A member of the IL17 family which consists of six structurally related cytokines: IL17A (CPX-9301), IL17B (CPX-9302), IL17C (CPX-9305), IL17D, IL25 (this complex) and IL17F (CPX-9303).\r\n\r\nIL17 is expressed by CD4+ type 17 helper cells, the Tc17 subset of CD8+ cells, as well as innate-acting gamma-delta T cells, natural killer T cells and TCR-beta+ natural Th17 cells.  \r\n\r\nUnrestrained IL17 signalling is associated with autoimmune diseases and cancer progression, but it is also crucial for protection from fungal and bacterial infections, including the commensal Candida albicans and Klebsiella pneumoniae. Both IL25 and IL17B promote IL33-driven (O95760) type 2 immune responses, but perform contradictory roles in colitis; IL25 is pathogenic and IL17B is protective. IL17B is thought to inhibit IL25 binding to IL17RA:IL17RB expressed on epithelial cells thereby limiting IL25 induced IL6 production by colonic epithelial cells.\r\n\r\nIL25 expression is up-regulated in skin inflammatory diseases such as psoriasis and atopic and contact dermatitis.","predictedComplex":false,"interactors":[{"ac":"EBI-2880054","identifier":"Q9H293","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H293/entry","name":"IL25","description":"Interleukin-25","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-9307","complexName":"Interleukin-17A-F complex","organismName":"Homo sapiens; 9606","description":"Proinflammatory modulator constituted of IL17A , the prototypic member of the IL17 family and IL17F, it's most closely related subunit. \r\n\r\nIL17 is expressed by CD4+ type 17 helper cells, the Tc17 subset of CD8+ cells, as well as innate-acting gamma-delta T cells, natural killer T cells and TCR-beta+ natural Th17 cells.\r\n\r\nUnrestrained IL17 signalling is associated with autoimmune diseases and cancer progression, but it is also crucial for protection from fungal and bacterial infections, including the commensal Candida albicans and Klebsiella pneumoniae. IL17 is also thought to play a dominant protective role in maintaining intestinal barrier integrity.","predictedComplex":false,"interactors":[{"ac":"EBI-10237926","identifier":"Q16552","identifierLink":"https://www.uniprot.org/uniprotkb/Q16552/entry","name":"IL17A","description":"Interleukin-17A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-10292310","identifier":"Q96PD4","identifierLink":"https://www.uniprot.org/uniprotkb/Q96PD4/entry","name":"IL17F","description":"Interleukin-17F","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-9308","complexName":"Mitochondrial respiratory chain complex III","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Key role in aerobic respiration, in which mitochondrial enzymes accept electrons from electron carriers reduced in glycolysis and the tricarboxylic acid cycle.  Ubiquinol-cytochrome c reductase pumps protons into the intermembrane space, creating an electrochemical gradient. This is achieved by oxidizing ubiquinol (ubihydroquinone) which reacts from the membrane phase, reducing cytochrome c in the intermembrane space, and using the free energy change to transport  H+ ions across the membrane from the matrix to the inter membrane space. Quinol oxidation occurs in a bifurcated reaction, in which one electron is transferred to a high potential chain and the other to a low potential chain. The high potential chain, consisting of the iron sulfur protein, cyt c1 and cyt c2, transfers the first electron from quinol to an acceptor (cytochrome oxidase). The low potential chain consists of two cyt b hemes, which serve as a pathway through which electrons are transferred across the coupling membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-55020583","identifier":"Q09154","identifierLink":"https://www.uniprot.org/uniprotkb/Q09154/entry","name":"rip1","description":"Cytochrome b-c1 complex subunit Rieske, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10134","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55020607","identifier":"O59680","identifierLink":"https://www.uniprot.org/uniprotkb/O59680/entry","name":"cyt1","description":"Cytochrome c1, heme protein, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55020625","identifier":"P50523","identifierLink":"https://www.uniprot.org/uniprotkb/P50523/entry","name":"qcr8","description":"Cytochrome b-c1 complex subunit 8","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12119","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55020638","identifier":"P05501","identifierLink":"https://www.uniprot.org/uniprotkb/P05501/entry","name":"cob","description":"Cytochrome b","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR19271","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55020658","identifier":"O74433","identifierLink":"https://www.uniprot.org/uniprotkb/O74433/entry","name":"qcr9","description":"Cytochrome b-c1 complex subunit 9","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12980","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55020677","identifier":"O74533","identifierLink":"https://www.uniprot.org/uniprotkb/O74533/entry","name":"qcr7","description":"Cytochrome b-c1 complex subunit 7","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12022","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55020691","identifier":"Q9P7E0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P7E0/entry","name":"qcr10","description":"Cytochrome b-c1 complex subunit 10","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28254","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55020703","identifier":"O42932","identifierLink":"https://www.uniprot.org/uniprotkb/O42932/entry","name":"qcr6","description":"Cytochrome b-c1 complex subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15336","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55020717","identifier":"P78761","identifierLink":"https://www.uniprot.org/uniprotkb/P78761/entry","name":"qcr2","description":"Cytochrome b-c1 complex subunit 2, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11851","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55020740","identifier":"CHEBI:61717","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:61717","name":"ferroheme c(2-)","description":"ferroheme c(2-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-55030778","identifier":"CHEBI:60344","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60344","name":"ferroheme b(2-)","description":"ferroheme b(2-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-9309","complexName":"TNFSF14-TNFRSF6B receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Decoy receptor complex known to promote anti-apoptotic pathways. Binding to TNFRSF6B (this complex) competitively inhibits TNFSF14's interaction with LTBR (CPX-9310) and TNFRSF14 (CPX-9223). \r\n\r\nTNFRSF6B circulating in plasma and found anchored in tissues regulates TNFSF14 bioavailability in tissue microenvironments, and TNFRSF6B binds and sequesters TNFSF14 with an affinity equal to that of TNFRSF14 and LTBR. \r\n\r\nInflammatory signals during sepsis by elipthelial and innate immune T-cells induces TNFRSF6B secretion and decoy receptor complex formation.","predictedComplex":false,"interactors":[{"ac":"EBI-524131","identifier":"O43557","identifierLink":"https://www.uniprot.org/uniprotkb/O43557/entry","name":"TNFSF14","description":"Tumor necrosis factor ligand superfamily member 14","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11471","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-524171","identifier":"O95407","identifierLink":"https://www.uniprot.org/uniprotkb/O95407/entry","name":"TNFRSF6B","description":"Tumor necrosis factor receptor superfamily member 6B","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9310","complexName":"TNFSF14-LTBR receptor complex","organismName":"Homo sapiens; 9606","description":"Receptor complex which coordinates innate and adaptive immune responses. Contributes directly and indirectly to myeloid cell activation, enhanced antigen presentation, and the induction of both adaptive and innate immune cytokines and chemokines. LTBR-mediated signalling through NF-KB and RelB (Q01201) induces transcription of CXCL13 (O43927), CCL19 (Q99731) and CCL21 (O00585) involved in positioning T and B cells in germinal centers and the creation of new tertiary lymphoid structures and extra-lymphatic immune environments. TNFSF14 also mediates its effects through TNFRSF14 (CPX-9223), and the decoy receptor TNFRSF6B (CPX-9309).\r\n\r\nExpressed on myeloid cells, various tumour cell types and stromal cells in the tumour microenvrionment, TNFSF14 mediated activity has been linked with the negative selection of potentially autoreactive T cells to act as a safeguard against automimmune disease.","predictedComplex":false,"interactors":[{"ac":"EBI-3509981","identifier":"P36941","identifierLink":"https://www.uniprot.org/uniprotkb/P36941/entry","name":"LTBR","description":"Tumor necrosis factor receptor superfamily member 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-524131","identifier":"O43557","identifierLink":"https://www.uniprot.org/uniprotkb/O43557/entry","name":"TNFSF14","description":"Tumor necrosis factor ligand superfamily member 14","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11471","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9322","complexName":"B-T lymphocyte attenuator, BTLA-TNFRSF14 complex","organismName":"Homo sapiens; 9606","description":"Receptor complex that acts as a potent inhibitor of T-cell and cytokine activation, it triggers an inhibitory signalling pathway to negatively regulate lymphocyte proliferation. TNFRSF14 binding to BTLA results in a molecular switch to a co-inhibitory form from a co-stimulatory role when bound to TNFSF14 (CPX-9309).\r\n\r\nBTLA-TNFRSF14 mediates immune tolerance by inhibiting B-cell receptor (BCR) signalling molecules. BTLA's trans-engagement with HVEM on effector T cells results in the recruitment of PTPN6/SHP-1 (P29350) and PTPN11/SHP-2 (Q06124), two potent tyrosine phosphatases, to disable early T cell activation.","predictedComplex":false,"interactors":[{"ac":"EBI-1056653","identifier":"Q92956","identifierLink":"https://www.uniprot.org/uniprotkb/Q92956/entry","name":"TNFRSF14","description":"Tumor necrosis factor receptor superfamily member 14","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46838","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4314354","identifier":"Q7Z6A9","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z6A9/entry","name":"BTLA","description":"B- and T-lymphocyte attenuator","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR37996","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9341","complexName":"BRISC-SHMT2 complex","organismName":"Homo sapiens; 9606","description":"Endogenous deubiquitinase (DUB) inhibitor that specifically recognizes Lys63-linked ubiquitinated chains during cellular stress responses and immune signalling functions. Required for viral protein degradation, as well as IFNAR1 (P17181)/ IFNAR2 (P48551) deubiquitylation and receptor stabilization on the cell membrane. Deubiquitination of Lys63 chains on IFNAR1/IFNAR2 limits their endocytosis and lysosomal degradation, thereby increasing their cell surface expression and stability to promote type 1 interferon activity. \r\n\r\nSHMT2 performs counterintuitive functions, acting as both an inhibitor of BRISC activity as well as a key mediator of BRISC association at sites of DUB action, in its role as a reversible endogenous BRISC inhibitor that prevents non-specific DUB activity.\r\n\r\nPyridoxal-5'-phosphate (Viatmin B6-PLP, CHEBI:18405) is key for the transition of SHMT2 from dimeric to a tetrameric state. Only the inactive, dimeric SHMT2 can interact with BRISC. An increase in intracellular PLP is associated with a reduction in BRISC-SHMT2 interaction and inflammatory signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-1056583","identifier":"Q15018","identifierLink":"https://www.uniprot.org/uniprotkb/Q15018/entry","name":"ABRAXAS2","description":"BRISC complex subunit Abraxas 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31728","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10987854","identifier":"P34897-3","identifierLink":"https://www.uniprot.org/uniprotkb/P34897-3/entry","name":"SHMT2","description":"Serine hydroxymethyltransferase, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-745725","identifier":"Q9NWV8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NWV8/entry","name":"BABAM1","description":"BRISC and BRCA1-A complex member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15660","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-750352","identifier":"P46736","identifierLink":"https://www.uniprot.org/uniprotkb/P46736/entry","name":"BRCC3","description":"Lys-63-specific deubiquitinase BRCC36","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10410","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-949389","identifier":"Q9NXR7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NXR7/entry","name":"BABAM2","description":"BRISC and BRCA1-A complex member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15189","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-9361","complexName":"USP12-WDR20 deubiquitinase complex","organismName":"Homo sapiens; 9606","description":"Deubiquitinase complex responsible for the removal of ubiquitin chains from proteins.The complex shuttles between the plasma membrane, cytoplasm and nucleus in a XPO1 (O14980)-dependent manner.","predictedComplex":false,"interactors":[{"ac":"EBI-1045469","identifier":"Q8TAF3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAF3/entry","name":"WDR48","description":"WD repeat-containing protein 48","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19862","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2511486","identifier":"Q8TBZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TBZ3/entry","name":"WDR20","description":"WD repeat-containing protein 20","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14107","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2511507","identifier":"O75317","identifierLink":"https://www.uniprot.org/uniprotkb/O75317/entry","name":"USP12","description":"Ubiquitin carboxyl-terminal hydrolase 12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24006","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-9381","complexName":"USP12-DMWD deubiquitinase complex","organismName":"Homo sapiens; 9606","description":"Deubiquitinase complex responsible for the removal of ubiquitin chains from proteins. DMWD competes with WDR20 (Q8TBZ3) to occupy a binding site in USP12 and thus regulate USP12 subcellular location with the USP12-DMWD deubiquitinase complex being mainly located in the cytoplasm.","predictedComplex":false,"interactors":[{"ac":"EBI-1045469","identifier":"Q8TAF3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAF3/entry","name":"WDR48","description":"WD repeat-containing protein 48","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19862","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2511507","identifier":"O75317","identifierLink":"https://www.uniprot.org/uniprotkb/O75317/entry","name":"USP12","description":"Ubiquitin carboxyl-terminal hydrolase 12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24006","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724564","identifier":"Q09019","identifierLink":"https://www.uniprot.org/uniprotkb/Q09019/entry","name":"DMWD","description":"Dystrophia myotonica WD repeat-containing protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14107","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-9421","complexName":"BRISC complex","organismName":"Homo sapiens; 9606","description":"Modular deubiquitinase (DUB) complex that specifically recognizes Lys63-linked ubiquitinated chains through the BRCC3 datalytic subunit during cellular stress responses and immune signalling functions mediated by activated cytokine receptors.\r\n\r\nDeubiquitinates AURKB (Q96GD4); BRISC deficiency leads to AURKB hyperactivity during mitosis thereby disrupting kinetochore-microtubule attachment which results in defects in the separation of paired kinetochores and the formation of kinetochore aggregates or rod-shaped/misshapen/distorted kinetochores. Also required for functional bipolar spindle assembly through deubiquitination of NuMA (Q14980), at the spindle pole.","predictedComplex":false,"interactors":[{"ac":"EBI-1056583","identifier":"Q15018","identifierLink":"https://www.uniprot.org/uniprotkb/Q15018/entry","name":"ABRAXAS2","description":"BRISC complex subunit Abraxas 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31728","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-745725","identifier":"Q9NWV8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NWV8/entry","name":"BABAM1","description":"BRISC and BRCA1-A complex member 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15660","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-750352","identifier":"P46736","identifierLink":"https://www.uniprot.org/uniprotkb/P46736/entry","name":"BRCC3","description":"Lys-63-specific deubiquitinase BRCC36","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10410","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-949389","identifier":"Q9NXR7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NXR7/entry","name":"BABAM2","description":"BRISC and BRCA1-A complex member 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15189","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-9442","complexName":"USP1-UAF1 deubiquitinase complex","organismName":"Homo sapiens; 9606","description":"Deubiquitinase complex responsible for the removal of ubiquitin chains from proteins. Acts during DNA repair processes to remove monoubiquitin signals from PCNA (CPX-538), and FANCI and FANCD2 of the Fanconi anemia ID complex (CPX-6264), each of which is monoubiquitinated at a specific lysine residue during repair of DNA damage. Both complexes form DNA clamps.","predictedComplex":false,"interactors":[{"ac":"EBI-1045469","identifier":"Q8TAF3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAF3/entry","name":"WDR48","description":"WD repeat-containing protein 48","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19862","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2513396","identifier":"O94782","identifierLink":"https://www.uniprot.org/uniprotkb/O94782/entry","name":"USP1","description":"Ubiquitin carboxyl-terminal hydrolase 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24006","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9461","complexName":"USP7-TRIM27 ubiquitinase/deubiquitinase complex","organismName":"Homo sapiens; 9606","description":"Deubiquitinase complex responsible for the removal of ubiquitin chains from proteins. Plays a role in the regulation of TNFA-induced apoptosis by deubiquinating the serine-threonine kinase RIPK1 (Q13546). The E3 ligase TRIM27 activates USP7 through ubiquitination at Lys-869. TRIM27 itself undergoes Lys-48 ubiquitination which can be removed by USP7, enabling  inhibition of the an antiviral signaling pathway by promoting kinase TBK1 (Q9UHD2) ubiquitination and degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-302474","identifier":"Q93009","identifierLink":"https://www.uniprot.org/uniprotkb/Q93009/entry","name":"USP7","description":"Ubiquitin carboxyl-terminal hydrolase 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24006","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-719493","identifier":"P14373","identifierLink":"https://www.uniprot.org/uniprotkb/P14373/entry","name":"TRIM27","description":"Zinc finger protein RFP","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24103","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9481","complexName":"ALYREF-binding exon junction complex","organismName":"Homo sapiens; 9606","description":"Exon junction complexes (EJCs) are multi-protein complexes (CPX-680,CPX-682, CPX-1941, CPX-1942) that help regulate mRNA metabolism. There are on average eight EJC binding sites per human mRNA, making them a major component of mature ribonucleoprotein complexes (mRNPs). EJCs selectively bind mRNPs through close association with the transcription-export complex (TREX) complex (CPX-2488, CPX-7261). TREX selectively recognizes mRNPs through its subunits ALYREF (this complex) and DDX39B. ALYREF is initially recruited by the Nuclear cap binding complex (CPX-1427) but its binding to the mRNA relies on the splicing and deposition of EJCs. EJC's and their auxiliary factors have considerable influence over the nonsense mediated mRNA decay pathway and their dysfunction is thought to be implicated in developmental and neurological diseases.","predictedComplex":false,"interactors":[{"ac":"EBI-14022093","identifier":"CHEBI:33699","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:33699","name":"messenger rna","description":"messenger RNA","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-299104","identifier":"P38919","identifierLink":"https://www.uniprot.org/uniprotkb/P38919/entry","name":"EIF4A3","description":"Eukaryotic initiation factor 4A-III","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47958","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-299134","identifier":"P61326","identifierLink":"https://www.uniprot.org/uniprotkb/P61326/entry","name":"MAGOH","description":"Protein mago nashi homolog","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12638","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347640","identifier":"Q86V81","identifierLink":"https://www.uniprot.org/uniprotkb/Q86V81/entry","name":"ALYREF","description":"THO complex subunit 4","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19965","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-447231","identifier":"Q9Y5S9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5S9/entry","name":"RBM8A","description":"RNA-binding protein 8A","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9521","complexName":"LINC complex, SUN1-KASH6 complex","organismName":"Homo sapiens; 9606","description":"Forms immediately below the outer nuclear membrane and traverses the nuclear envelope to mechanically couple cytoskeletal and nuclear components across the nuclear envelope, allowing the transmission of force.","predictedComplex":false,"interactors":[{"ac":"EBI-2796904","identifier":"O94901","identifierLink":"https://www.uniprot.org/uniprotkb/O94901/entry","name":"SUN1","description":"SUN domain-containing protein 1","stochiometry":"minValue: 9, maxValue: 9","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12911","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2839307","identifier":"Q12912","identifierLink":"https://www.uniprot.org/uniprotkb/Q12912/entry","name":"IRAG2","description":"Inositol 1,4,5-triphosphate receptor associated 2","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15352","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9541","complexName":"LINC complex, SUN2-KASH6 complex","organismName":"Homo sapiens; 9606","description":"Forms immediately below the outer nuclear membrane and traverses the nuclear envelope to mechanically couple cytoskeletal and nuclear components across the nuclear envelope, allowing the transmission of force.","predictedComplex":false,"interactors":[{"ac":"EBI-1044964","identifier":"Q9UH99","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UH99/entry","name":"SUN2","description":"SUN domain-containing protein 2","stochiometry":"minValue: 9, maxValue: 9","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12911","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2839307","identifier":"Q12912","identifierLink":"https://www.uniprot.org/uniprotkb/Q12912/entry","name":"IRAG2","description":"Inositol 1,4,5-triphosphate receptor associated 2","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15352","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9561","complexName":"FLIP-FIGNL1 DNA interstrand crosslink repair complex","organismName":"Homo sapiens; 9606","description":"Regulates RAD51 (Q06609) chromatin association and persistence on nucleofilaments following exogenous DNA damage. Required for both interstrand crosslinking and homologous repair.","predictedComplex":false,"interactors":[{"ac":"EBI-11128910","identifier":"Q9NSG2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NSG2/entry","name":"FIRRM","description":"FIGNL1-interacting regulator of recombination and mitosis","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16071","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8468390","identifier":"Q6PIW4","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PIW4/entry","name":"FIGNL1","description":"Fidgetin-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23074","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9581","complexName":"Phosphorylase kinase, liver variant","organismName":"Homo sapiens; 9606","description":"Serine/threonine-specific protein kinase which phosphorylates glycogen phosphorylase and transforms it from the inactive b form to the active a form to initiate glycogenolysis, the breaking down of glycogen into glucose.","predictedComplex":false,"interactors":[{"ac":"EBI-1383819","identifier":"P15735","identifierLink":"https://www.uniprot.org/uniprotkb/P15735/entry","name":"PHKG2","description":"Phosphorylase b kinase gamma catalytic chain, liver/testis isoform","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24347","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1642846","identifier":"P46019","identifierLink":"https://www.uniprot.org/uniprotkb/P46019/entry","name":"PHKA2","description":"Phosphorylase b kinase regulatory subunit alpha, liver isoform","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10749","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-397435","identifier":"P62158","identifierLink":"https://www.uniprot.org/uniprotkb/P62158/entry","name":"calm_human","description":"Calmodulin","stochiometry":"minValue: 4, maxValue: 4","interactorType":"molecule set","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-740559","identifier":"Q93100","identifierLink":"https://www.uniprot.org/uniprotkb/Q93100/entry","name":"PHKB","description":"Phosphorylase b kinase regulatory subunit beta","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10749","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9621","complexName":"TRAF6-TIFA E3 ubiquitin ligase complex","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase complex which polyubiquitinaties TRAF6, a required step in NF-kappa-B (P19838) activation.","predictedComplex":false,"interactors":[{"ac":"EBI-359276","identifier":"Q9Y4K3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4K3/entry","name":"TRAF6","description":"TNF receptor-associated factor 6","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-740711","identifier":"Q96CG3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96CG3/entry","name":"TIFA","description":"TRAF-interacting protein with FHA domain-containing protein A","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9661","complexName":"TIFA-TIFAB signalling regulator complex","organismName":"Homo sapiens; 9606","description":"Formation of the TIFA-TIFAB heterodimer prevents TIFA dimerization, thus blocking the formation of the TRAF6-TIFA E3 ubiquitin ligase complex which is required for NF-kappa-B (P19838) activation.","predictedComplex":false,"interactors":[{"ac":"EBI-26453465","identifier":"Q6ZNK6","identifierLink":"https://www.uniprot.org/uniprotkb/Q6ZNK6/entry","name":"TIFAB","description":"TRAF-interacting protein with FHA domain-containing protein B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-740711","identifier":"Q96CG3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96CG3/entry","name":"TIFA","description":"TRAF-interacting protein with FHA domain-containing protein A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9741","complexName":"TRAF2-TIFA E3 ubiquitin ligase complex","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase complex which polyubiquitinaties TRAF6, a required step in NF-kappa-B (P19838) activation. DNA damage-inducesd TIFA phosphorylation at Thr-9 resulting in its enrichment on damaged chromatin. Complex formation then stimulattes ubiquitination of IKBKG (Q9Y6K9), a subunit of the IkappaB kinase complex (CPX-3269).","predictedComplex":false,"interactors":[{"ac":"EBI-355744","identifier":"Q12933","identifierLink":"https://www.uniprot.org/uniprotkb/Q12933/entry","name":"TRAF2","description":"TNF receptor-associated factor 2","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-740711","identifier":"Q96CG3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96CG3/entry","name":"TIFA","description":"TRAF-interacting protein with FHA domain-containing protein A","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31266","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9801","complexName":"IL11-sIL11RA-sIL-6ST receptor-ligand buffering complex","organismName":"Homo sapiens; 9606","description":"Antagonist cytokine-receptor complex that acts as a buffer to IL11 activity. IL11 binds to a soluble form of its specific receptor component, sIL11RA, and recruits a soluble form of IL6ST (sIL6ST) to form a complex which abrogates IL11-mediated trans-signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-52333529","identifier":"P40189-2","identifierLink":"https://www.uniprot.org/uniprotkb/P40189-2/entry","name":"IL6ST","description":"Interleukin-6 receptor subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-55034297","identifier":"Q14626-PRO_0000450688","identifierLink":"https://www.uniprot.org/uniprotkb/Q14626-PRO_0000450688/entry","name":"IL11RA","description":"Soluble interleukin-11 receptor subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-751694","identifier":"P20809","identifierLink":"https://www.uniprot.org/uniprotkb/P20809/entry","name":"IL11","description":"Interleukin-11","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16922","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9841","complexName":"CXCL8-ACKR1, atypical receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Atypical chemokine-receptor complex that controls the bioavailability of CXCL8 and its localization. Produced mainly by non-leukocytes, ACKR1 primarily acts as a scavenging receptor to dampen CXCL8 mediated immune responses by binding, internalizing, and degrading it. However, ACKR1 can promote CXCL8 transcytosis promoting inflammation.\r\n\r\nACKR1 is used by Plasmodium vivax and Plasmodium knowlesi as an entry receptor for erythrocyte invasion and a silencing mutation in ACKR1's promoter region is associated with a resistance to malaria found in the majority of Sub-saharan Afrian populations","predictedComplex":false,"interactors":[{"ac":"EBI-16355853","identifier":"Q16570","identifierLink":"https://www.uniprot.org/uniprotkb/Q16570/entry","name":"ACKR1","description":"Atypical chemokine receptor 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14181","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3917999","identifier":"P10145","identifierLink":"https://www.uniprot.org/uniprotkb/P10145/entry","name":"CXCL8","description":"Interleukin-8","stochiometry":"minValue: 1, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12015","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9861","complexName":"Augmin complex","organismName":"Drosophila melanogaster; 7227","description":"Regulates mitotic spindle assembly and centrosome integrity and is required for completion of cytokinesis. The complex interacts with the gamma-tubulin ring complex (CPX-2801) and this interaction is required for spindle assembly.","predictedComplex":false,"interactors":[{"ac":"EBI-125735","identifier":"Q9W4M8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W4M8/entry","name":"dgt4","description":"Augmin complex subunit dgt4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-15769774","identifier":"Q9W0G7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W0G7/entry","name":"msd1","description":"Augmin complex subunit msd1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-1628748","identifier":"Q9W2P0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W2P0/entry","name":"dgt3","description":"Augmin complex subunit dgt3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-180262","identifier":"Q9W0S8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W0S8/entry","name":"wac","description":"Augmin complex subunit wac","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-186540","identifier":"Q9VAP2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VAP2/entry","name":"dgt6","description":"Augmin complex subunit dgt6","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR16151","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-191477","identifier":"Q9W0G6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W0G6/entry","name":"msd5","description":"Augmin complex subunit msd5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-3407113","identifier":"Q7K4B4","identifierLink":"https://www.uniprot.org/uniprotkb/Q7K4B4/entry","name":"dgt5","description":"Augmin complex subunit dgt5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR34491","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-84322","identifier":"Q9VKD6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VKD6/entry","name":"dgt2","description":"Augmin complex subunit dgt2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]}]},{"complexAC":"CPX-9881","complexName":"MutSgamma meiotic recombination complex","organismName":"Homo sapiens; 9606","description":"Binds to double Holliday Junctions and other DNA repair intermediates. Binding physically entraps at least one, and possibly two, duplexes of double-stranded DNA, thereby stabilising the recombination intermediate.","predictedComplex":false,"interactors":[{"ac":"EBI-6092730","identifier":"O43196","identifierLink":"https://www.uniprot.org/uniprotkb/O43196/entry","name":"MSH5","description":"MutS protein homolog 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11361","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6092777","identifier":"O15457","identifierLink":"https://www.uniprot.org/uniprotkb/O15457/entry","name":"MSH4","description":"MutS protein homolog 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11361","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9901","complexName":"MutLalpha endonuclease complex","organismName":"Homo sapiens; 9606","description":"Endonuclease complex which nicks a DNA strand containing a pre-existing nick, presumably to provide an entry site for a mispair excision reaction. Required for DNA mismatch repair (MMR), correcting base-base mismatches and insertion-deletion loops resulting from DNA replication, DNA damage or from recombination events between non-identical sequences during meiosis. ATP binding  induces a conformational change in the MutSalpha/MSH2-MSH6 (CPX-80) and MutSbeta/MSH2-MSH3 (CPX-77) complexes which converts these to a clamp form that slides along the DNA and leads to recruitment of MutLalpha/MLH1-PMS2, MutLbeta/MLH1-PMS1 (CPX-9941) and MLH1-MLH3 (CPX-9961).","predictedComplex":false,"interactors":[{"ac":"EBI-1162561","identifier":"P54278","identifierLink":"https://www.uniprot.org/uniprotkb/P54278/entry","name":"PMS2","description":"Mismatch repair endonuclease PMS2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744248","identifier":"P40692","identifierLink":"https://www.uniprot.org/uniprotkb/P40692/entry","name":"MLH1","description":"DNA mismatch repair protein Mlh1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9941","complexName":"MutLabeta endonuclease complex","organismName":"Homo sapiens; 9606","description":"Endonuclease complex which nicks a DNA strand containing a pre-existing nick, presumably to provide an entry site for a mispair excision reaction. Required for DNA mismatch repair (MMR), correcting base-base mismatches and insertion-deletion loops resulting from DNA replication, DNA damage or from recombination events between non-identical sequences during meiosis. ATP binding  induces a conformational change in the MutSalpha/MSH2-MSH6 (CPX-80) and  MutSbeta/MSH2-MSH3 (CPX-77) complexes which converts these to a clamp form that slides along the DNA and leads to recruitment of MutLalpha/MLH1-PMS2 (CPX-9901), MutLbeta/MLH1-PMS1 and MutLgamma/MLH1-MLH3 (CPX-9961). MutLbeta appears to function in repair of single base pair mismatches and small insertion/deletion mispairs.","predictedComplex":false,"interactors":[{"ac":"EBI-2893308","identifier":"P54277","identifierLink":"https://www.uniprot.org/uniprotkb/P54277/entry","name":"PMS1","description":"PMS1 protein homolog 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744248","identifier":"P40692","identifierLink":"https://www.uniprot.org/uniprotkb/P40692/entry","name":"MLH1","description":"DNA mismatch repair protein Mlh1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9961","complexName":"MutLgamma endonuclease complex","organismName":"Homo sapiens; 9606","description":"Mn2+-dependent endonuclease which nicks a DNA strand containing a pre-existing nick, presumably to provide an entry site for a mispair excision reaction. Required for DNA mismatch repair (MMR), correcting base-base mismatches and insertion-deletion loops resulting from DNA replication, DNA damage or from recombination events between non-identical sequences during meiosis. ATP binding  induces a conformational change in the MutSalpha/MSH2-MSH6 (CPX-80) and  MutSbeta/MSH2-MSH3 (CPX-77) complexes which converts these to a clamp form that slides along the DNA and leads to recruitment of MutLalpha/MLH1-PMS2 (CPX-9901), MutLbeta/MLH1-PMS1 (CPX-9941) and MutLgamma/MLH1-MLH3. May play a role inthe  repair of specific insertions/deletions.","predictedComplex":false,"interactors":[{"ac":"EBI-3893094","identifier":"Q9UHC1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UHC1/entry","name":"MLH3","description":"DNA mismatch repair protein Mlh3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744248","identifier":"P40692","identifierLink":"https://www.uniprot.org/uniprotkb/P40692/entry","name":"MLH1","description":"DNA mismatch repair protein Mlh1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9981","complexName":"Peroxisomal receptor export module complex","organismName":"Drosophila melanogaster; 7227","description":"Processive protein translocase that mediates the ATP-dependent relocation and recycling of the peroxisomal targeting signal import receptor PEX5 (P35056) from the peroxisomal membrane to the cytosol, where it is then available for another round of protein import. The PEX1-PEX6 complex acts as an ATPase that threads monoubiquitinated PEX5 through its central pore.","predictedComplex":false,"interactors":[{"ac":"EBI-177260","identifier":"Q9VUC7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VUC7/entry","name":"Pex1","description":"Peroxisomal ATPase PEX1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55036476","identifier":"A1Z8D1","identifierLink":"https://www.uniprot.org/uniprotkb/A1Z8D1/entry","name":"Pex6","description":"Peroxisomal ATPase PEX6","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10001","complexName":"Peroxisomal PEX13-PEX14 docking complex","organismName":"Drosophila melanogaster; 7227","description":"Facilitates the peroxoisomal-membrane docking of cargo-loaded, peroxisomal targeting signal type 1 (PTS1) and PTS2 proteins. Proteins designated for peroxisomes are synthezised on cytosolic ribosomes and are recognised  by the receptor PEX5 (O46085)  via their PTS1 or PEX7 (Q9VSN7) via their PTS2  The receptor-cargo-complex bind to the docking-complex at the peroxisomal membrane. It is assumed that the binding between the docking complex and cargo-loaded receptors leads to the formation of a transient pore.","predictedComplex":false,"interactors":[{"ac":"EBI-113203","identifier":"Q9VPB8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VPB8/entry","name":"Pex14","description":"Peroxisomal membrane protein PEX14","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23058","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-186471","identifier":"Q7JRD4","identifierLink":"https://www.uniprot.org/uniprotkb/Q7JRD4/entry","name":"Pex13","description":"Peroxisomal membrane protein PEX13","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR19332","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10021","complexName":"Peroxisomal PEX13-PEX14 docking complex","organismName":"Homo sapiens; 9606","description":"Facilitates the peroxoisomal-membrane docking of cargo-loaded, peroxisomal targeting signal type 1 (PTS1) and PTS2 proteins. Proteins designated for peroxisomes are synthezised on cytosolic ribosomes and are recognised by the receptor PEX5 (P50542) via their PTS1 or PTS2 region. The receptor-cargo-complexes bind to the docking-complex at the peroxisomal membrane. It is assumed that the binding between the docking complex and cargo-loaded receptors leads to the formation of a transient pore.","predictedComplex":false,"interactors":[{"ac":"EBI-594849","identifier":"Q92968","identifierLink":"https://www.uniprot.org/uniprotkb/Q92968/entry","name":"PEX13","description":"Peroxisomal membrane protein PEX13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19332","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-594898","identifier":"O75381","identifierLink":"https://www.uniprot.org/uniprotkb/O75381/entry","name":"PEX14","description":"Peroxisomal membrane protein PEX14","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23058","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10041","complexName":"Interleukin-18 receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Proinflammatory cytokine-receptor complex which strongly augments IFNG production (P01579) in synergy with IL12 (CPX-381) from T helper-1 and natural killer cells.\r\n\r\nSynthesised as a biological inactive precursor upon exposure to intracellular pathogens, proIL18 is stored in the cytoplasm until cleavage by inflammasome-mediated CASP1 (P29466), CASP4 (P49662) or CASP5 (P51878), when it is secreted extracellularly. Mature IL18 initiates signalling by binding IL18R1 and IL18RAP in a step-wise fashion at the immunocyte plasma membrane. Complex formation and heterodimerization of the receptors' Toll/IL-1 receptor domains triggers recruitment of MyD88(Q99836), which initiates downstream signalling through phosphorylation of IRAKs,TRAF6 (Q9Y4K3), and NFKB (P19838) activation.\r\n\r\nIL18 is tightly regulated at the gene level by CASP1 and at the protein level by IL18BP (O95998), and over-expression of IL18 is associated with several autoimmune diseases including, rheumatoid arthritis, Crohn's diseases and systemic lupus erythematosus.","predictedComplex":false,"interactors":[{"ac":"EBI-21018056","identifier":"O95256","identifierLink":"https://www.uniprot.org/uniprotkb/O95256/entry","name":"IL18RAP","description":"Interleukin-18 receptor accessory protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3910835","identifier":"Q14116","identifierLink":"https://www.uniprot.org/uniprotkb/Q14116/entry","name":"IL18","description":"Interleukin-18","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10078","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9817499","identifier":"Q13478","identifierLink":"https://www.uniprot.org/uniprotkb/Q13478/entry","name":"IL18R1","description":"Interleukin-18 receptor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10061","complexName":"Oligosaccharyltransferase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Transfers the dolicholphosphate-linked core oligosaccharide to selected Asn-X-Ser/Thr sequences of the nascent polypeptide chain, a key step in N-glycosylation of secretory and membrane-bound proteins in the lumen of the endoplasmic reticulum.","predictedComplex":false,"interactors":[{"ac":"EBI-55039236","identifier":"O94335","identifierLink":"https://www.uniprot.org/uniprotkb/O94335/entry","name":"stt3","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13872","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55039253","identifier":"O59866","identifierLink":"https://www.uniprot.org/uniprotkb/O59866/entry","name":"wbp1","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit wbp1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10830","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55039266","identifier":"O14238","identifierLink":"https://www.uniprot.org/uniprotkb/O14238/entry","name":"ost2","description":"Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit ost2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10705","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55039277","identifier":"Q8TFH3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TFH3/entry","name":"ost3","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12692","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55039290","identifier":"Q10176","identifierLink":"https://www.uniprot.org/uniprotkb/Q10176/entry","name":"ost1","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR21049","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55039302","identifier":"Q96VG2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96VG2/entry","name":"ost4","description":"Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase 4 kDa subunit","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-55039313","identifier":"G2TRU0","identifierLink":"https://www.uniprot.org/uniprotkb/G2TRU0/entry","name":"ost5","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit ost5","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-55039329","identifier":"O74943","identifierLink":"https://www.uniprot.org/uniprotkb/O74943/entry","name":"yjb6","description":"Uncharacterized protein C553.06","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]}]},{"complexAC":"CPX-10081","complexName":"DASH complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Heterodecameric component of the kinetochore necessary for accurate chromosome segregation, supporting the dynamic attachment of mitotic chromosomes to the ends of shortening spindle microtubules. DASH forms closed rings around microtubules with a large gap between the DASH ring and the microtubule cylinder. A DASH-microtubule interface is believed to form, in which extensions from DASH rings reach across a gap between the ring and the microtubule and dock on the microtubule wall. DASH rings spontaneously oligomerize in the presence of microtubules of the mitotic spindle. DASH rings are processivity factors that allow kinetochores to translate along a single microtubule without dissociating. Each DASH ring may contain from 16-30 heterodecamers. The NDC80 complex (CPX-549) can simultaneously bind and bridge across two DASH complex rings through a tripartite interaction. This ensures a consistent spacing between rings. The complex may also may serve as a link between the kinetochore and the mitotic spindle. DASH is assembled and localized onto kinetochores specifically in mitosis.","predictedComplex":false,"interactors":[{"ac":"EBI-21242644","identifier":"Q9HDZ6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HDZ6/entry","name":"dam1","description":"DASH complex subunit dam1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28113","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21242666","identifier":"P87297","identifierLink":"https://www.uniprot.org/uniprotkb/P87297/entry","name":"dad1","description":"DASH complex subunit dad1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28025","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21244132","identifier":"O74372","identifierLink":"https://www.uniprot.org/uniprotkb/O74372/entry","name":"duo1","description":"DASH complex subunit duo1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28216","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21244680","identifier":"O14285","identifierLink":"https://www.uniprot.org/uniprotkb/O14285/entry","name":"spc34","description":"DASH complex subunit spc34","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-55039384","identifier":"Q9UTG8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UTG8/entry","name":"dad2","description":"DASH complex subunit dad2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55039405","identifier":"Q9P6S5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P6S5/entry","name":"ask1","description":"DASH complex subunit ask1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28200","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55039427","identifier":"P62505","identifierLink":"https://www.uniprot.org/uniprotkb/P62505/entry","name":"dad3","description":"DASH complex subunit dad3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28017","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55039445","identifier":"O94483","identifierLink":"https://www.uniprot.org/uniprotkb/O94483/entry","name":"dad5","description":"DASH complex subunit DAD5","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28289","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55039465","identifier":"Q50HP4","identifierLink":"https://www.uniprot.org/uniprotkb/Q50HP4/entry","name":"dad4","description":"DASH complex subunit dad4","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55039481","identifier":"Q50HP3","identifierLink":"https://www.uniprot.org/uniprotkb/Q50HP3/entry","name":"spc19","description":"DASH complex subunit spc19","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28262","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10101","complexName":"Interleukin-18 decoy complex","organismName":"Homo sapiens; 9606","description":"Decoy cytokine-receptor complex which acts as an antagonist to moderate the potent proinflammatory activities of IL18 (CPX-10041). \r\n\r\nIL18 plays key roles in driving autoimmune and inflammatory diseases and its sequestration by its soluble decoy receptor IL18BP is critical to the regulation of IL18 activity. Therefore, IL18BP is present in human serum at a 20-fold molar excess and binds IL18 with a several-fold higher affinity than it's receptor, IL18R1 (Q13478).","predictedComplex":false,"interactors":[{"ac":"EBI-2831962","identifier":"O95998","identifierLink":"https://www.uniprot.org/uniprotkb/O95998/entry","name":"IL18BP","description":"Interleukin-18-binding protein","stochiometry":"minValue: 1, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14292","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3910835","identifier":"Q14116","identifierLink":"https://www.uniprot.org/uniprotkb/Q14116/entry","name":"IL18","description":"Interleukin-18","stochiometry":"minValue: 1, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10078","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10121","complexName":"Glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Monoglycosyltransferase complex that catalyses the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to the 6-position of phosphatidylinositol, the first, and committed, step of glycosylphosphatidylinositol (GPI) biosynthesis. GPI is a complex glycolipid with a core structure, phosphoethanolamine-6-mannose-alpha1,2-mannose-alpha1,6-mannose-alpha1,4-glucosamine-alpha1,6-inositol-phospholipid that functions as a membrane anchor for many cell surface proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-55040165","identifier":"O13904","identifierLink":"https://www.uniprot.org/uniprotkb/O13904/entry","name":"mug84","description":"Meiotically up-regulated gene 84 protein","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR46346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55040216","identifier":"C6Y4B7","identifierLink":"https://www.uniprot.org/uniprotkb/C6Y4B7/entry","name":"yids","description":"Uncharacterized protein C227.19c","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-55040226","identifier":"O14357","identifierLink":"https://www.uniprot.org/uniprotkb/O14357/entry","name":"gpi1","description":"N-acetylglucosaminyl-phosphatidylinositol biosynthetic protein gpi1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR21329","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55040238","identifier":"Q9Y7L7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y7L7/entry","name":"gpi15","description":"Phosphatidylinositol N-acetylglucosaminyltransferase subunit gpi15","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15231","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55040250","identifier":"O59802","identifierLink":"https://www.uniprot.org/uniprotkb/O59802/entry","name":"gpi2","description":"Phosphatidylinositol N-acetylglucosaminyltransferase GPI2 subunit","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12982","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55040261","identifier":"P87172","identifierLink":"https://www.uniprot.org/uniprotkb/P87172/entry","name":"gpi3","description":"Phosphatidylinositol N-acetylglucosaminyltransferase gpi3 subunit","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR45871","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10141","complexName":"GPI-anchor transamidase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Transamidase enzyme complex that transfers the glycosylphosphatidylinositol (GPI) lipid to the newly made GPI protein in the endoplasmic reticulum, replacing the C-terminal GPI attachment signal peptide of a protein with the lipid. GPI is a complex glycolipid with a core structure, phosphoethanolamine-6-mannose-alpha1,2-mannose-alpha1,6-mannose-alpha1,4-glucosamine-alpha1,6-inositol-phospholipid that functions as a membrane anchor for many cell surface proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-55040425","identifier":"O94380","identifierLink":"https://www.uniprot.org/uniprotkb/O94380/entry","name":"gpi16","description":"GPI transamidase component PIG-T homolog","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12959","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55040435","identifier":"Q10351","identifierLink":"https://www.uniprot.org/uniprotkb/Q10351/entry","name":"gpi17","description":"GPI transamidase component PIG-S homolog","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR21072","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55040445","identifier":"Q9USP5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9USP5/entry","name":"gpi8","description":"GPI-anchor transamidase","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR48067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55040458","identifier":"O13883","identifierLink":"https://www.uniprot.org/uniprotkb/O13883/entry","name":"pigu","description":"GPI transamidase component GAB1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13121","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55040469","identifier":"Q9US48","identifierLink":"https://www.uniprot.org/uniprotkb/Q9US48/entry","name":"gaa1","description":"GPI transamidase component gaa1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10161","complexName":"Interleukin-16 receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Chemoattractant cytokine-receptor complex. Processing of precursor IL16 by CASP3 (P42574) cleavage is required to produce bioactive IL16 capable of chemoattractant functions. IL16 activity is dependent on the cell surface expression of CD4, the target signal transducing receptor for IL16.","predictedComplex":false,"interactors":[{"ac":"EBI-353826","identifier":"P01730","identifierLink":"https://www.uniprot.org/uniprotkb/P01730/entry","name":"CD4","description":"T-cell surface glycoprotein CD4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11422","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56888005","identifier":"Q14005-PRO_0000015412","identifierLink":"https://www.uniprot.org/uniprotkb/Q14005-PRO_0000015412/entry","name":"IL16","description":"Interleukin-16","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-10181","complexName":"Vault ribonucleoprotein complex","organismName":"Homo sapiens; 9606","description":"May act to facilitate protein exchange between the cytoplasm and nucleus. Rapidly redistributed in response to external stimuli or stress. The VTRNA-1 locus contains the genetic information for three vault RNAs (vtRNA1-1, vtRNA1-2, and vtRNA1-3). vtRNA1-1 is involved in the regulation of apoptosis and autophagy and associated with homeostasis. vtRNA1-2 is localized predominantly in the nucleus and may regulate expression of cell membrane proteins. vtRNA1-3 has been linked to multi-drug resistance.","predictedComplex":false,"interactors":[{"ac":"EBI-2623021","identifier":"Q9UKK3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UKK3/entry","name":"PARP4","description":"Protein mono-ADP-ribosyltransferase PARP4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46530","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2816254","identifier":"Q14764","identifierLink":"https://www.uniprot.org/uniprotkb/Q14764/entry","name":"MVP","description":"Major vault protein","stochiometry":"minValue: 78, maxValue: 78","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55043056","identifier":"URS00005CCF67_9606","identifierLink":"http://rnacentral.org/rna/URS00005CCF67_9606","name":"vault rna 1-1 (vtrna1-1)","description":"Homo sapiens (human) vault RNA 1-1 (VTRNA1-1)","stochiometry":null,"interactorType":"ribonucleic acid","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-55043064","identifier":"URS0000000A8C_9606","identifierLink":"http://rnacentral.org/rna/URS0000000A8C_9606","name":"vault rna 1-2 (vtrna1-2)","description":"Homo sapiens (human) vault RNA 1-2 (VTRNA1-2)","stochiometry":null,"interactorType":"ribonucleic acid","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-55043072","identifier":"URS000058CD99_9606","identifierLink":"http://rnacentral.org/rna/URS000058CD99_9606","name":"vault rna 1-3 (vtrna1-3)","description":"Homo sapiens (human) vault RNA 1-3 (VTRNA1-3)","stochiometry":null,"interactorType":"ribonucleic acid","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-55043080","identifier":"URS0000A76E3A_9606","identifierLink":"http://rnacentral.org/rna/URS0000A76E3A_9606","name":"vault rna 2-1 (vtrna2-1)","description":"Homo sapiens (human) vault RNA 2-1 (VTRNA2-1)","stochiometry":null,"interactorType":"ribonucleic acid","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-947859","identifier":"Q99973","identifierLink":"https://www.uniprot.org/uniprotkb/Q99973/entry","name":"TEP1","description":"Telomerase protein component 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44791","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10201","complexName":"MRN double-strand break repair complex","organismName":"Drosophila melanogaster; 7227","description":"Endo- and exonuclease complex that plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. It possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11. MRE11 and Rad50 form an ATP-regulated nuclease that senses DSBs and tethers DNA ends in close proximity via long Rad50 coiled-coil domains.","predictedComplex":false,"interactors":[{"ac":"EBI-110666","identifier":"Q9XYZ4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XYZ4/entry","name":"mre11","description":"Double-strand break repair protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-145564","identifier":"Q9W252","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W252/entry","name":"rad50","description":"DNA repair protein RAD50","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR18867","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-190718","identifier":"Q9VT40","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VT40/entry","name":"nbs","description":"Nibrin","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12162","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-10281","complexName":"Myddosome core complex","organismName":"Homo sapiens; 9606","description":"Innate immune signalling platform which transmits inflammatory signals as a result of TLR/IL1R (P14778) activation to promote proinflammatory responses. Myddosome assembly occurs in a stepwise manner in which MyD88 recruits IRAK4, and the intermediary MyD88:IRAK4 complex recruits and binds IRAK1/IRAK2 drawing IRAKs' kinase domains closer, allowing for phosphorylation and activation. IRAK1/IRAK2 subsequently enables binding to TRAF6 (Q9Y4K3), which is vital for recruiting transcription factors in the NFKB and MAPK pathways to elicit expression of proinflammatory cytokines. Myddosome assembly is tightly-regulated by IRAK4 and occurs in a context-specific manner with all components playing substantial roles in scaffolding. Myddosome size, number and assembly speed governs the intensity of the inflammatory response.\r\n\r\nMyddosome-mediated proinflammatory responses are determined by IRAK4 activity but IRAK4 is also capable of indirectly inhibiting myddosome signalling thereby forming a negative feedback loop. Uncontrolled myddosome activation is linked to cancers caused by gain-of-function mutations.","predictedComplex":false,"interactors":[{"ac":"EBI-358664","identifier":"P51617","identifierLink":"https://www.uniprot.org/uniprotkb/P51617/entry","name":"IRAK1","description":"Interleukin-1 receptor-associated kinase 1","stochiometry":"minValue: 1, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24419","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-447677","identifier":"Q99836","identifierLink":"https://www.uniprot.org/uniprotkb/Q99836/entry","name":"MYD88","description":"Myeloid differentiation primary response protein MyD88","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15079","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-447733","identifier":"O43187","identifierLink":"https://www.uniprot.org/uniprotkb/O43187/entry","name":"IRAK2","description":"Interleukin-1 receptor-associated kinase-like 2","stochiometry":"minValue: 1, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24419","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-448378","identifier":"Q9NWZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NWZ3/entry","name":"IRAK4","description":"Interleukin-1 receptor-associated kinase 4","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24419","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10301","complexName":"RAVE complex, DMXL1 variant","organismName":"Homo sapiens; 9606","description":"Regulates the acidification of organelles such as lysosomes and endosomes by catalyzing the assembly of the proton-pumping V-ATPase complex (CPX-2470/CPX-6904/CPX-6905/CPX-6912).","predictedComplex":false,"interactors":[{"ac":"EBI-11115143","identifier":"Q9Y485","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y485/entry","name":"DMXL1","description":"DmX-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13950","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16783626","identifier":"Q9Y4E6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4E6/entry","name":"WDR7","description":"WD repeat-containing protein 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44099","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-713255","identifier":"Q9GZN7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9GZN7/entry","name":"ROGDI","description":"Protein rogdi homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13618","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10302","complexName":"MRN double-strand break repair complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Endo- and exonuclease complex that plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis  via non-homologous end joining and homologous recombination.. The complex possesses both single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11. Mre11 and Rad50 form an ATP-regulated nuclease that senses DSBs and tethers DNA ends in close proximity via long Rad50 coiled-coil domains.","predictedComplex":false,"interactors":[{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2124866","identifier":"Q09683","identifierLink":"https://www.uniprot.org/uniprotkb/Q09683/entry","name":"rad32","description":"Double-strand break repair protein rad32","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2125045","identifier":"O43070","identifierLink":"https://www.uniprot.org/uniprotkb/O43070/entry","name":"nbs1","description":"DNA repair and telomere maintenance protein nbs1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12162","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2125086","identifier":"Q9UTJ8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UTJ8/entry","name":"rad50","description":"DNA repair protein rad50","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR18867","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-10303","complexName":"RAVE complex, DMXL2 variant","organismName":"Homo sapiens; 9606","description":"Regulates the acidification of organelles such as lysosomes and endosomes by catalyzing the assembly of the proton-pumping V-ATPase complex (CPX-2470/CPX-6904/CPX-6905/CPX-6912).","predictedComplex":false,"interactors":[{"ac":"EBI-16783626","identifier":"Q9Y4E6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4E6/entry","name":"WDR7","description":"WD repeat-containing protein 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44099","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5653014","identifier":"Q8TDJ6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TDJ6/entry","name":"DMXL2","description":"DmX-like protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13950","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-713255","identifier":"Q9GZN7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9GZN7/entry","name":"ROGDI","description":"Protein rogdi homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13618","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10304","complexName":"ILK-PINCH-Parvin complex, LIMS1-PARVA variant","organismName":"Homo sapiens; 9606","description":"Assembles at sites of focal adhesion where it controls bidirectional signaling between the extracellular matrix and intracellular compartment. The complex triggers F-actin filament bundling thus generating force/mechanical signals which promote cytoskeleton reassembly and cell adhesion.","predictedComplex":false,"interactors":[{"ac":"EBI-306928","identifier":"P48059","identifierLink":"https://www.uniprot.org/uniprotkb/P48059/entry","name":"LIMS1","description":"LIM and senescent cell antigen-like-containing domain protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-747644","identifier":"Q13418","identifierLink":"https://www.uniprot.org/uniprotkb/Q13418/entry","name":"ILK","description":"Scaffold protein ILK","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44329","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-747655","identifier":"Q9NVD7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NVD7/entry","name":"PARVA","description":"Alpha-parvin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12114","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10309","complexName":"Interleukin-22 decoy receptor complex","organismName":"Homo sapiens; 9606","description":"Inhibitory cytokine-receptor complex. IL22RA2 competitively binds IL22 with over 1000-fold affinity than its specific membrane-bound receptor IL22RA1 (Q8N6P7). There are three functionally different isoforms of IL22RA2 in humans, the non-functional isoform 1, isoform 2 which has a strong inhibitory effect on IL22 activity and isoform 3, which is abundantly distributed but binds IL22 with an affinity that is 27-fold lower than that of isoform 2.\r\n\r\nThough constitutively expressed by a range of epithelial cells, IL22RA2 expression is rarely detected during acute inflammatory responses.","predictedComplex":false,"interactors":[{"ac":"EBI-8040250","identifier":"Q9GZX6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9GZX6/entry","name":"IL22","description":"Interleukin-22","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48488","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8591719","identifier":"Q969J5","identifierLink":"https://www.uniprot.org/uniprotkb/Q969J5/entry","name":"IL22RA2","description":"Interleukin-22 receptor subunit alpha-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10312","complexName":"ILK-PINCH-Parvin complex, LIMS1-PARVB variant","organismName":"Homo sapiens; 9606","description":"Assembles at sites of focal adhesion where it controls bidirectional signaling between the extracellular matrix and intracellular compartment. The complex triggers F-actin filament bundling thus generating force/mechanical signals which promote cytoskeleton reassembly and cell adhesion.","predictedComplex":false,"interactors":[{"ac":"EBI-1047679","identifier":"Q9HBI1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HBI1/entry","name":"PARVB","description":"Beta-parvin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12114","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-306928","identifier":"P48059","identifierLink":"https://www.uniprot.org/uniprotkb/P48059/entry","name":"LIMS1","description":"LIM and senescent cell antigen-like-containing domain protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-747644","identifier":"Q13418","identifierLink":"https://www.uniprot.org/uniprotkb/Q13418/entry","name":"ILK","description":"Scaffold protein ILK","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44329","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10313","complexName":"ILK-PINCH-Parvin complex, LIMS2-PARVA variant","organismName":"Homo sapiens; 9606","description":"Assembles at sites of focal adhesion where it controls bidirectional signaling between the extracellular matrix and intracellular compartment. The complex triggers F-actin filament bundling thus generating force/mechanical signals which promote cytoskeleton reassembly and cell adhesion.","predictedComplex":false,"interactors":[{"ac":"EBI-6256404","identifier":"Q7Z4I7","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z4I7/entry","name":"LIMS2","description":"LIM and senescent cell antigen-like-containing domain protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-747644","identifier":"Q13418","identifierLink":"https://www.uniprot.org/uniprotkb/Q13418/entry","name":"ILK","description":"Scaffold protein ILK","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44329","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-747655","identifier":"Q9NVD7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NVD7/entry","name":"PARVA","description":"Alpha-parvin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12114","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10314","complexName":"ILK-PINCH-Parvin complex, LIMS2-PARVB variant","organismName":"Homo sapiens; 9606","description":"Assembles at sites of focal adhesion where it controls bidirectional signaling between the extracellular matrix and intracellular compartment. The complex triggers F-actin filament bundling thus generating force/mechanical signals which promote cytoskeleton reassembly and cell adhesion.","predictedComplex":false,"interactors":[{"ac":"EBI-1047679","identifier":"Q9HBI1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HBI1/entry","name":"PARVB","description":"Beta-parvin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12114","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6256404","identifier":"Q7Z4I7","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z4I7/entry","name":"LIMS2","description":"LIM and senescent cell antigen-like-containing domain protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-747644","identifier":"Q13418","identifierLink":"https://www.uniprot.org/uniprotkb/Q13418/entry","name":"ILK","description":"Scaffold protein ILK","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44329","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10315","complexName":"37S mitochondrial small ribosomal subunit","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Component of the ribsome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). Acts as the decoding centre of the ribosome which brings mRNA and aminoacylated transfer (t)RNAs. The mitochondrial ribosome (mitoribosome) is responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are tethered to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-16823313","identifier":"O74802","identifierLink":"https://www.uniprot.org/uniprotkb/O74802/entry","name":"snr1","description":"Small ribosomal subunit protein mS47","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR43176","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56885902","identifier":"O60063","identifierLink":"https://www.uniprot.org/uniprotkb/O60063/entry","name":"nam9","description":"Small ribosomal subunit protein uS4m","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11831","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56885919","identifier":"O60096","identifierLink":"https://www.uniprot.org/uniprotkb/O60096/entry","name":"bot1","description":"Small ribosomal subunit protein mS45","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28158","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56885929","identifier":"Q10234","identifierLink":"https://www.uniprot.org/uniprotkb/Q10234/entry","name":"mrp5","description":"Small ribosomal subunit protein uS5m","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13718","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56885948","identifier":"O14006","identifierLink":"https://www.uniprot.org/uniprotkb/O14006/entry","name":"mrps9","description":"Small ribosomal subunit protein uS9m","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR21569","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56885963","identifier":"O13602","identifierLink":"https://www.uniprot.org/uniprotkb/O13602/entry","name":"mrps28","description":"Small ribosomal subunit protein uS15m","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56885979","identifier":"O13970","identifierLink":"https://www.uniprot.org/uniprotkb/O13970/entry","name":"mrp4","description":"Small ribosomal subunit protein uS2m","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12534","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56886001","identifier":"Q9USL7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9USL7/entry","name":"rsm18","description":"Small ribosomal subunit protein bS18m","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13479","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56886015","identifier":"O59677","identifierLink":"https://www.uniprot.org/uniprotkb/O59677/entry","name":"rsm23","description":"Small ribosomal subunit protein mS29","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12810","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56886028","identifier":"O13744","identifierLink":"https://www.uniprot.org/uniprotkb/O13744/entry","name":"rsm7","description":"Small ribosomal subunit protein uS7m","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11205","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56886049","identifier":"O74379","identifierLink":"https://www.uniprot.org/uniprotkb/O74379/entry","name":"rt26","description":"Small ribosomal subunit protein mS42","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR43595","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56886070","identifier":"O42855","identifierLink":"https://www.uniprot.org/uniprotkb/O42855/entry","name":"mrp51","description":"Small ribosomal subunit protein bS1m","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28058","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56886081","identifier":"P21547","identifierLink":"https://www.uniprot.org/uniprotkb/P21547/entry","name":"var1","description":"Small ribosomal subunit protein uS3m","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-56886092","identifier":"O43020","identifierLink":"https://www.uniprot.org/uniprotkb/O43020/entry","name":"mrps16","description":"Small ribosomal subunit protein bS16m","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12919","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56886103","identifier":"O43006","identifierLink":"https://www.uniprot.org/uniprotkb/O43006/entry","name":"mug178","description":"Small ribosomal subunit protein L51-b","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28058","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56886118","identifier":"O74972","identifierLink":"https://www.uniprot.org/uniprotkb/O74972/entry","name":"fyv4","description":"Small ribosomal subunit protein mS41","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28235","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56886129","identifier":"O74956","identifierLink":"https://www.uniprot.org/uniprotkb/O74956/entry","name":"mrps8","description":"Small ribosomal subunit protein uS8m","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11758","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56886142","identifier":"O42911","identifierLink":"https://www.uniprot.org/uniprotkb/O42911/entry","name":"rsm25","description":"Small ribosomal subunit protein mS23","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15925","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56886153","identifier":"O60186","identifierLink":"https://www.uniprot.org/uniprotkb/O60186/entry","name":"rsm10","description":"Small ribosomal subunit protein uS10m","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11700","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56886172","identifier":"Q8WZK1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WZK1/entry","name":"mrp21","description":"Small ribosomal subunit protein bS21m","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR41237","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56886185","identifier":"Q9UUB0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UUB0/entry","name":"mrps17","description":"Small ribosomal subunit protein uS17m","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10744","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56886199","identifier":"O42859","identifierLink":"https://www.uniprot.org/uniprotkb/O42859/entry","name":"mrp2","description":"Small ribosomal subunit protein uS14m","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR19836","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56886211","identifier":"O42919","identifierLink":"https://www.uniprot.org/uniprotkb/O42919/entry","name":"rt01","description":"Small ribosomal subunit protein mS43","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR43595","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56886229","identifier":"O59772","identifierLink":"https://www.uniprot.org/uniprotkb/O59772/entry","name":"sws2","description":"Small ribosomal subunit protein uS13m","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10871","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56886246","identifier":"Q9UT82","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UT82/entry","name":"mrp17","description":"Small ribosomal subunit protein bS6m","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR21011","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56886262","identifier":"Q09705","identifierLink":"https://www.uniprot.org/uniprotkb/Q09705/entry","name":"rsm24","description":"Small ribosomal subunit protein mS35","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13490","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56886275","identifier":"O14358","identifierLink":"https://www.uniprot.org/uniprotkb/O14358/entry","name":"rsm27","description":"Small ribosomal subunit protein mS33","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13362","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56886290","identifier":"O13882","identifierLink":"https://www.uniprot.org/uniprotkb/O13882/entry","name":"mrps18","description":"Small ribosomal subunit protein uS11m","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11759","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56886304","identifier":"O13973","identifierLink":"https://www.uniprot.org/uniprotkb/O13973/entry","name":"mrp10","description":"Small ribosomal subunit protein mS37","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28066","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56886315","identifier":"Q9US30","identifierLink":"https://www.uniprot.org/uniprotkb/Q9US30/entry","name":"rsm19","description":"Small ribosomal subunit protein uS19m","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11880","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56887030","identifier":"O60169","identifierLink":"https://www.uniprot.org/uniprotkb/O60169/entry","name":"rtpt","description":"Small ribosomal subunit protein mS26","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-9494077","identifier":"CHEBI:18111","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18111","name":"ribosomal rna","description":"ribosomal RNA","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-10317","complexName":"Interleukin-26 complex","organismName":"Homo sapiens; 9606","description":"Cationic homodimeric cytokine that binds to extracellular DNA released from damaged cells. Acts as a carrier molecule for translocation of IL26-DNA complexes into the cytoplasm triggering proinflammatory effects through the activation of inflammasomes and interferon genes via the STING pathway.  May activate innate and adaptive lymphoid cells, myeloid cells and plasmacytoid dendritic cells (pDC) by allowing DNA to be internalized by pDC, leading to its activation via TLR9 (Q9NR96) or TLR3 (O15455). IL26 binds as a monomer to a conventional heterodimeric receptor (CPX-10316) to exert some potentially pathological effects in inflammatory disorders. \r\n\r\nIL26 is primarily secreted by pathogenic T helper 1 (Th1), Th17 and CD4+ cells.\r\n\r\nIL26 is considered to be a master regulator of inflammation but is also a catalyst for driving chronic inflammatory disorders. In addition to the proinflammatory effects it mediates, IL26 functions as a kinocidin or antimicrobial protein (AMP) with strong antimicrobial and bactericidal effects, particularly on Gram-positive bacteria through its capacity to form pores in bacterial membranes.","predictedComplex":false,"interactors":[{"ac":"EBI-54772883","identifier":"Q9NPH9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPH9/entry","name":"IL26","description":"Interleukin-26","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48482","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10318","complexName":"m-AAA protease complex, AFG3L2 variant","organismName":"Homo sapiens; 9606","description":"ATP-dependent protease embedded in the inner mitochondrial membrane, essential for mitochondrial ribosome assembly, the expression, maturation, and degradation of electron transport chain complexes, and the regulation of calcium homeostasis.","predictedComplex":false,"interactors":[{"ac":"EBI-358755","identifier":"Q9Y4W6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4W6/entry","name":"AFG3L2","description":"Mitochondrial inner membrane m-AAA protease component AFG3L2","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43655","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 6, maxValue: 6","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-10319","complexName":"m-AAA protease complex, AFG3L2-SPG7 variant","organismName":"Homo sapiens; 9606","description":"ATP-dependent protease embedded in the inner mitochondrial membrane, essential for mitochondrial ribosome assembly, the expression, maturation, and degradation of electron transport chain complexes, and the regulation of calcium homeostasis.","predictedComplex":false,"interactors":[{"ac":"EBI-358755","identifier":"Q9Y4W6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4W6/entry","name":"AFG3L2","description":"Mitochondrial inner membrane m-AAA protease component AFG3L2","stochiometry":"minValue: 1, maxValue: 5","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43655","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-717201","identifier":"Q9UQ90","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UQ90/entry","name":"SPG7","description":"Mitochondrial inner membrane m-AAA protease component paraplegin","stochiometry":"minValue: 1, maxValue: 5","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43655","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-7982","complexName":"SCF E3 ubiquitin ligase complex, FBXO41 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXO41 target proteins include the S-phase kinase-associated protein 2 SKP2 (Q13309) thus playing a role in the regulation of autophagy.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-914807","identifier":"Q8TF61","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TF61/entry","name":"FBXO41","description":"F-box only protein 41","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15739","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-7983","complexName":"SCF E3 ubiquitin ligase complex, FBXO42 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXO42 target proteins include the Notch signaling pathway transcriptional regulator RBPJ (Q06330).","predictedComplex":false,"interactors":[{"ac":"EBI-2506081","identifier":"Q6P3S6","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P3S6/entry","name":"FBXO42","description":"F-box only protein 42","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46432","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8001","complexName":"LMAN1-MCFD2 cargo receptor complex","organismName":"Homo sapiens; 9606","description":"Cargo receptor which cycles between the endoplasmin reticulum and the cis-Golgi, binding and ensuring the transportation of glycoproteins such as coagulation factors FV (P12259) and FVIII (P00451).","predictedComplex":false,"interactors":[{"ac":"EBI-1057738","identifier":"P49257","identifierLink":"https://www.uniprot.org/uniprotkb/P49257/entry","name":"LMAN1","description":"Protein ERGIC-53","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12223","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2689785","identifier":"Q8NI22","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NI22/entry","name":"MCFD2","description":"Multiple coagulation factor deficiency protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23104","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8002","complexName":"SCF E3 ubiquitin ligase complex, FBXO43 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXO43 target proteins include the cyclin CCND1 (P24385), promoting its stability by polyubiquitination.","predictedComplex":false,"interactors":[{"ac":"EBI-12053217","identifier":"Q4G163","identifierLink":"https://www.uniprot.org/uniprotkb/Q4G163/entry","name":"FBXO43","description":"F-box only protein 43","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15493","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8003","complexName":"SCF E3 ubiquitin ligase complex, FBXO44 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXO44 target proteins include the negative regulator of G-protein signaling RGS2 (P41220).","predictedComplex":false,"interactors":[{"ac":"EBI-2322644","identifier":"Q9H4M3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H4M3/entry","name":"FBXO44","description":"F-box only protein 44","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12125","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8004","complexName":"Non-canonical FBXO45-MYCBP2-SKP1 E3 ubiquitin ligase complex","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. FBXO45-MYCBP2-SKP1 target proteins include the Nicotinamide/nicotinate-nucleotide adenylyltransferase NMNAT2 (Q9BZQ4) that acts as an axon maintenance factor thus playing a role in neuromuscular synaptogenesis, axon pathfinding and neuronal migration.","predictedComplex":false,"interactors":[{"ac":"EBI-1043774","identifier":"O75592","identifierLink":"https://www.uniprot.org/uniprotkb/O75592/entry","name":"MYCBP2","description":"E3 ubiquitin-protein ligase MYCBP2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45943","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2511355","identifier":"P0C2W1","identifierLink":"https://www.uniprot.org/uniprotkb/P0C2W1/entry","name":"FBXO45","description":"F-box/SPRY domain-containing protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12245","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8005","complexName":"SCF E3 ubiquitin ligase complex, FBXO46 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXO46 target proteins include the F-box protein FBXO31 (Q5XUX0). The SCF-FBXO31 complex (CPX-7971) regulates levels of FBXO31 and thereby prevents senescence in normal growth conditions. Following genotoxic stress, complex activity is abrogated thus increasing FBXO31 levels and enabling maintenance of genomic stability.","predictedComplex":false,"interactors":[{"ac":"EBI-2322982","identifier":"Q6PJ61","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PJ61/entry","name":"FBXO46","description":"F-box only protein 46","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16271","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8006","complexName":"SCF E3 ubiquitin ligase complex, FBXO47 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SCF-FBXO47 target proteins include HOMAD1 (Q86X24) which plays a key role in meiotic progression.","predictedComplex":false,"interactors":[{"ac":"EBI-307486","identifier":"P63208","identifierLink":"https://www.uniprot.org/uniprotkb/P63208/entry","name":"SKP1","description":"S-phase kinase-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359390","identifier":"Q13616","identifierLink":"https://www.uniprot.org/uniprotkb/Q13616/entry","name":"CUL1","description":"Cullin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-44453014","identifier":"Q5MNV8","identifierLink":"https://www.uniprot.org/uniprotkb/Q5MNV8/entry","name":"FBXO47","description":"F-box only protein 47","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR34098","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8007","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL1 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. KLHL1 may play a role in organizing the actin cytoskeleton of brain cells.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6426228","identifier":"Q9NR64","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NR64/entry","name":"KLHL1","description":"Kelch-like protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8008","complexName":"Survival motor neuron complex, Gem4A variant","organismName":"Drosophila melanogaster; 7227","description":"Molecular chaperone that plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, thus playing an important role in the splicing of cellular pre-mRNAs.","predictedComplex":false,"interactors":[{"ac":"EBI-108834","identifier":"Q9VVX0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVX0/entry","name":"Gem2","description":"Gem-associated protein 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12794","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-111600","identifier":"Q9W4N9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W4N9/entry","name":"Glos","description":"Gem-associated protein 4a","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-126900","identifier":"Q9V3C4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V3C4/entry","name":"Gem3","description":"RNA helicase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR47958","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-185315","identifier":"Q9VV74","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VV74/entry","name":"Smn","description":"Survival motor neuron protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR39267","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-422757","identifier":"Q86BY9","identifierLink":"https://www.uniprot.org/uniprotkb/Q86BY9/entry","name":"rig","description":"Gem-associated protein 5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46362","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8009","complexName":"Sodium:potassium-exchanging ATPase complex, FXYD1 variant","organismName":"Homo sapiens; 9606","description":"An ATPase-dependent transmembrane transport complex capable of generating electrochemical gradients by exchanging three intracellular sodium ions for two extracellular potassium ions during each cycle of ATP hydrolysis. Na+/K+ pumps can also generate an inward current of protons.  \r\n\r\nEach transport cycle comprises a sequence of conformational transitions that permit extracellular K+ ions to access the binding sites in phosphorylated pumps and cytoplasmic Na+ ions to access the sites after dephosphorylation . Binding of the third Na+ ion triggers autophosphorylation, and binding of the second K+ ion prompts auto-dephosphorylation. This coupling of alternating ion access to ATP hydrolysis ensures forward, energetically uphill, progress of the Na+/K+ transport cycle. The larger pumped Na+ efflux than K+ influx constitutes outward current, a direction tending to make the membrane potential more negative. However, because each step in the cycle is reversible , if the normally transported intracellular Na+ and extracellular K+ are both scarce, the cycle can run backward, thus synthesizing ATP and generating inward, depolarizing current. Variants containing ATP1A1-ATP1B1 appear to be most widely expressed.","predictedComplex":false,"interactors":[{"ac":"EBI-21862610","identifier":"O00168","identifierLink":"https://www.uniprot.org/uniprotkb/O00168/entry","name":"FXYD1","description":"Phospholemman","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14132","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358778","identifier":"P05023","identifierLink":"https://www.uniprot.org/uniprotkb/P05023/entry","name":"ATP1A1","description":"Sodium/potassium-transporting ATPase subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714630","identifier":"P05026","identifierLink":"https://www.uniprot.org/uniprotkb/P05026/entry","name":"ATP1B1","description":"Sodium/potassium-transporting ATPase subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11523","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8021","complexName":"BOS complex, NOMO1 variant","organismName":"Homo sapiens; 9606","description":"Mediates insertion of transmembrane regions of multi-spanning membrane proteins into the endoplasmic reticulum (ER) membrane. Acts as part of an ER translocon that functions co-translationally with the SEC61 channel-forming translocon complex (CPX-8073) during biogenesis of multi-pass membrane proteins, along with the PAT intramembrane chaperone complex (CPX-7020) and the GEL multi-spanning membrane protein insertion complex (CPX-5606). The multipass translocon co-assembles on ribosomes containing the SEC61 and TRAP (CPX-8024) complexes, when  two transmembrane domains of a multi-pass protein have been membrane inserted and the third is inside the ribosome exit tunnel which displaces the OST oligosaccharyl transferase complex (CPX-5621/CPX-5622)","predictedComplex":false,"interactors":[{"ac":"EBI-1056979","identifier":"Q969V3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969V3/entry","name":"NCLN","description":"BOS complex subunit NCLN","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31826","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348587","identifier":"Q9BVK8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BVK8/entry","name":"TMEM147","description":"BOS complex subunit TMEM147","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12869","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373107","identifier":"Q15155","identifierLink":"https://www.uniprot.org/uniprotkb/Q15155/entry","name":"NOMO1","description":"BOS complex subunit NOMO1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23303","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8022","complexName":"BOS complex, NOMO2 variant","organismName":"Homo sapiens; 9606","description":"Mediates insertion of transmembrane regions of multi-spanning membrane proteins into the endoplasmic reticulum (ER) membrane. Acts as part of an ER translocon that functions co-translationally with the SEC61 channel-forming translocon complex during biogenesis of multi-pass membrane proteins, along with the PAT intramembrane chaperone complex (CPX-7020) and the GEL multi-spanning membrane protein insertion complex (CPX-5606). The multipass translocon co-assembles on ribosomes containing the SEC61 and TRAP complexes, when  two transmembrane domains of a multi-pass protein have been membrane inserted and the third is inside the ribosome exit tunnel which displaces the OST oligosaccharyl transferase complex (CPX-5621/CPX-5622)","predictedComplex":false,"interactors":[{"ac":"EBI-1056979","identifier":"Q969V3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969V3/entry","name":"NCLN","description":"BOS complex subunit NCLN","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31826","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2680477","identifier":"Q5JPE7","identifierLink":"https://www.uniprot.org/uniprotkb/Q5JPE7/entry","name":"NOMO2","description":"BOS complex subunit NOMO2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23303","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348587","identifier":"Q9BVK8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BVK8/entry","name":"TMEM147","description":"BOS complex subunit TMEM147","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12869","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8023","complexName":"BOS complex, NOMO3 variant","organismName":"Homo sapiens; 9606","description":"Mediates insertion of transmembrane regions of multi-spanning membrane proteins into the endoplasmic reticulum (ER) membrane. Acts as part of an ER translocon that functions co-translationally with the SEC61 channel-forming translocon complex during biogenesis of multi-pass membrane proteins, along with the PAT intramembrane chaperone complex (CPX-7020) and the GEL multi-spanning membrane protein insertion complex (CPX-5606). The multipass translocon co-assembles on ribosomes containing the SEC61 and TRAP complexes, when  two transmembrane domains of a multi-pass protein have been membrane inserted and the third is inside the ribosome exit tunnel which displaces the OST oligosaccharyl transferase complex (CPX-5621/CPX-5622)","predictedComplex":false,"interactors":[{"ac":"EBI-1056979","identifier":"Q969V3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969V3/entry","name":"NCLN","description":"BOS complex subunit NCLN","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31826","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348587","identifier":"Q9BVK8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BVK8/entry","name":"TMEM147","description":"BOS complex subunit TMEM147","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12869","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-947048","identifier":"P69849","identifierLink":"https://www.uniprot.org/uniprotkb/P69849/entry","name":"NOMO3","description":"BOS complex subunit NOMO3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23303","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8024","complexName":"Translocon-associated protein complex","organismName":"Homo sapiens; 9606","description":"Stimulates translocation of proteins depending on the efficiency of their signal sequence in transport initiation and may affect the topology of transmembrane helices containing topogenic determinants that do not promote one specific orientation in the membrane. May also play a role in the biogenesis of N-glycosylated proteins.Acts as part of the endoplasmic reticulum translocon protein translocon in association with the SEC61 complex (CPX-8073).","predictedComplex":false,"interactors":[{"ac":"EBI-1043938","identifier":"Q9UNL2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UNL2/entry","name":"SSR3","description":"Translocon-associated protein subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13399","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1054539","identifier":"P51571","identifierLink":"https://www.uniprot.org/uniprotkb/P51571/entry","name":"SSR4","description":"Translocon-associated protein subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12731","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2822012","identifier":"P43308","identifierLink":"https://www.uniprot.org/uniprotkb/P43308/entry","name":"SSR2","description":"Translocon-associated protein subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12861","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714168","identifier":"P43307","identifierLink":"https://www.uniprot.org/uniprotkb/P43307/entry","name":"SSR1","description":"Translocon-associated protein subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12924","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8025","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL2 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. CRL3-KLHL2 target proteins include the WNK kinases which play roles in the regulation of electrolyte homeostasis and Rho guanine nucleotide exchange factor ARHGEF7 (Q14155).","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-746999","identifier":"O95198","identifierLink":"https://www.uniprot.org/uniprotkb/O95198/entry","name":"KLHL2","description":"Kelch-like protein 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8041","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL3 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. CRL3-KLHL3 target proteins include the WNK kinases which play roles in the regulation of electrolyte homeostasis.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8524663","identifier":"Q9UH77","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UH77/entry","name":"KLHL3","description":"Kelch-like protein 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8061","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL4 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9478822","identifier":"Q9C0H6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9C0H6/entry","name":"KLHL4","description":"Kelch-like protein 4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8062","complexName":"Mitochondrial pyruvate carrier complex, testis variant","organismName":"Homo sapiens; 9606","description":"Regulates the uptake of pyruvate from the mitochondrial intermembrane space into the mitochondrial matrix. This variant forms in the testis, specifically in post meiotic germ cells.","predictedComplex":false,"interactors":[{"ac":"EBI-44454819","identifier":"P0DKB6","identifierLink":"https://www.uniprot.org/uniprotkb/P0DKB6/entry","name":"MPC1L","description":"Mitochondrial pyruvate carrier 1-like protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14154","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-719403","identifier":"O95563","identifierLink":"https://www.uniprot.org/uniprotkb/O95563/entry","name":"MPC2","description":"Mitochondrial pyruvate carrier 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14154","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8063","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL5 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. CRL3-KLHL5 target proteins include the sphingosine kinase SK1 (Q9NYA1) which phosphorylates sphingosine to generate sphingosine 1-phosphate, a bioactive lipid that acts as both an intracellular second messenger, and as a ligand for a family of five S1P-specific G protein-coupled receptors","predictedComplex":false,"interactors":[{"ac":"EBI-2692595","identifier":"Q96PQ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q96PQ7/entry","name":"KLHL5","description":"Kelch-like protein 5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8064","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL6 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. CRL3-KLHL6 may play a role in BCR signal transduction and formation of the full germinal center response.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6426464","identifier":"Q8WZ60","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WZ60/entry","name":"KLHL6","description":"Kelch-like protein 6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8065","complexName":"Intron-binding complex","organismName":"Homo sapiens; 9606","description":"Spliceosomal complex with an important role in guiding the multifunctional RNA helicase AQR, to bind precursor-mRNA introns at a defined position on the intron. AQR is required for efficient pre-mRNA splicing, connecting, and potentially fixing, intron nucleotides that lie upstream of the extended U2/branch site helix and downstream from the extended U6/intron helix This allows the intron located between these regions to loop out, and thus prevents the intron from interfering with the spliceosome’s core machinery. The introns potentially contain intronic small nucleolar RNAs (snoRNAs) that are processed during spliceosome assembly,","predictedComplex":false,"interactors":[{"ac":"EBI-2512328","identifier":"O60306","identifierLink":"https://www.uniprot.org/uniprotkb/O60306/entry","name":"AQR","description":"RNA helicase aquarius","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10887","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2557660","identifier":"Q9ULR0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ULR0/entry","name":"ISY1","description":"Pre-mRNA-splicing factor ISY1 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-295232","identifier":"Q9HCS7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HCS7/entry","name":"XAB2","description":"Pre-mRNA-splicing factor SYF1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11246","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3920997","identifier":"Q96NB3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96NB3/entry","name":"ZNF830","description":"Zinc finger protein 830","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13278","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-591818","identifier":"Q9UNP9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UNP9/entry","name":"PPIE","description":"Peptidyl-prolyl cis-trans isomerase E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11071","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8066","complexName":"Survival motor neuron complex, Gem4B variant","organismName":"Drosophila melanogaster; 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7227","xrefs":[{"identifier":"PTHR12794","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-126900","identifier":"Q9V3C4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V3C4/entry","name":"Gem3","description":"RNA helicase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR47958","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-185315","identifier":"Q9VV74","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VV74/entry","name":"Smn","description":"Survival motor neuron protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR39267","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3412151","identifier":"Q8IRS9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IRS9/entry","name":"Gem4c","description":"Gem-associated protein 4c","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-422757","identifier":"Q86BY9","identifierLink":"https://www.uniprot.org/uniprotkb/Q86BY9/entry","name":"rig","description":"Gem-associated protein 5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46362","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8068","complexName":"Mitochondrial pyruvate carrier complex","organismName":"Drosophila melanogaster; 7227","description":"Regulates the uptake of pyruvate from the mitochondrial intermembrane space into the mitochondrial matrix.","predictedComplex":false,"interactors":[{"ac":"EBI-188770","identifier":"Q9VHB2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VHB2/entry","name":"Dmel\\CG9396","description":"Mitochondrial pyruvate carrier","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14154","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-195938","identifier":"Q7KSC4","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KSC4/entry","name":"Mpc1","description":"Mitochondrial pyruvate carrier 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 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It destabilizes monopolar attachments by phosphorylating key proteins at the kinetophore. The chromosomal passenger complex (CPC) regulates chromosome segregation and cytokinesis.","predictedComplex":false,"interactors":[{"ac":"EBI-118412","identifier":"Q9VKN7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VKN7/entry","name":"aurB","description":"Aurora kinase B","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR24350","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-137031","identifier":"Q9VEM2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VEM2/entry","name":"Det","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46771","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-147863","identifier":"Q9VLD6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VLD6/entry","name":"borr","description":"Borealin","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR16040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-193598","identifier":"Q7JRJ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q7JRJ9/entry","name":"Incenp","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13142","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8070","complexName":"SCC2-SCC4 cohesin loader complex","organismName":"Homo sapiens; 9606","description":"Required for the stable association of the cohesin complex (CPX-5989/CPX-5991) with DNA. Dynamically loads cohesin to chromatin accessible sites and guides the bidirectional loop extrusion mechanism of genomic DNA. May act to convert cohesin into an active loop-extruding holoenzyme.","predictedComplex":false,"interactors":[{"ac":"EBI-4395624","identifier":"Q9Y6X3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6X3/entry","name":"MAU2","description":"MAU2 chromatid cohesion factor homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21394","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-722767","identifier":"Q6KC79","identifierLink":"https://www.uniprot.org/uniprotkb/Q6KC79/entry","name":"NIPBL","description":"Nipped-B-like protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21704","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8071","complexName":"Chromosomal passenger complex, meiotic variant","organismName":"Drosophila melanogaster; 7227","description":"Serine/threonine kinase complex which ensures chromosome bi-orientation on the male meiotic spindle during metaphase by phosphorylating multiple kinetochore components. It destabilizes monopolar attachments by phosphorylating key proteins at the kinetophore. The chromosomal passenger complex (CPC) regulates chromosome segregation and cytokinesis.","predictedComplex":false,"interactors":[{"ac":"EBI-118412","identifier":"Q9VKN7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VKN7/entry","name":"aurB","description":"Aurora kinase B","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR24350","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-118637","identifier":"Q9VLD7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VLD7/entry","name":"aust","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR16040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-137031","identifier":"Q9VEM2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VEM2/entry","name":"Det","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46771","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-193598","identifier":"Q7JRJ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q7JRJ9/entry","name":"Incenp","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13142","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8073","complexName":"SEC61 protein-conducting channel complex, SEC1A1 variant","organismName":"Homo sapiens; 9606","description":"Translocates hydrophilic polypeptide segments of newly synthesized proteins across the endoplasmic reticulum membrane and integrates hydrophobic transmembrane segments into the membrane for subsequent transport to other subcellular locations via vesicular trafficking. The complex associates with several other molecular machines and enzymes, such as the ribosome, the SEC62-SEC63 complex, and oligosaccharyltransferase complex (CPX-5621/CPX-5622).","predictedComplex":false,"interactors":[{"ac":"EBI-1788819","identifier":"P60468","identifierLink":"https://www.uniprot.org/uniprotkb/P60468/entry","name":"SEC61B","description":"Protein transport protein Sec61 subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13509","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358919","identifier":"P61619","identifierLink":"https://www.uniprot.org/uniprotkb/P61619/entry","name":"SEC61A1","description":"Protein transport protein Sec61 subunit alpha isoform 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10906","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4402709","identifier":"P60059","identifierLink":"https://www.uniprot.org/uniprotkb/P60059/entry","name":"SEC61G","description":"Protein transport protein Sec61 subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12309","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8081","complexName":"Rixosome RNA degradation complex","organismName":"Homo sapiens; 9606","description":"Role in ribosomal RNA (rRNA) processing and ribosome biogenesis. The LAS1L endonuclease subunit cleaves within the rRNA internal transcribed spacer 2 and generates a precursor with a 5'-OH group. The NOL9 polynucleotide kinase subunit then phosphorylates the precursor, leading to XRN2 (Q9H0D6)-mediated trimming and the generation of mature 26S rRNA.  Associates with Polycomb repressive complexes 1 and 2 and is recruited to Polycomb target genes, where it promotes degradation of nascent RNA and release of DNA-directed RNA polymerase II complex (CPX-2387/CPX-7481). Recruited by CHTOP (Q9Y3Y2) when this chromatin-bound protein  is arginine-methylated by PRMT1 (Q99873).","predictedComplex":false,"interactors":[{"ac":"EBI-1050480","identifier":"Q9NU22","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NU22/entry","name":"MDN1","description":"Midasin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48103","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1051591","identifier":"Q9Y4W2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4W2/entry","name":"LAS1L","description":"Ribosomal biogenesis protein LAS1L","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15002","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1055462","identifier":"Q5SY16","identifierLink":"https://www.uniprot.org/uniprotkb/Q5SY16/entry","name":"NOL9","description":"Polynucleotide 5'-hydroxyl-kinase NOL9","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12755","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2371062","identifier":"Q9NXF1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NXF1/entry","name":"TEX10","description":"Testis-expressed protein 10","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2880236","identifier":"Q9H4L4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H4L4/entry","name":"SENP3","description":"Sentrin-specific protease 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12606","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-716449","identifier":"Q8IZL8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IZL8/entry","name":"PELP1","description":"Proline-, glutamic acid- and leucine-rich protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR34105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727429","identifier":"Q9BV38","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BV38/entry","name":"WDR18","description":"WD repeat-containing protein 18","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18763","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8083","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL9 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.  CRL3-KLHL9 target proteins include the serine/threonine-protein kinase Aurora B (Q96GD4), which as a component of the Chromosomal Passenger complex (CPX-116) ensures chromosome bi-orientation on the mitotic spindle during metaphase by phosphorylating multiple kinetochore components. AURKB also acts as a critical regulator of the assembly and disassembly of type III intermediate filaments, including vimentin and desmin suggesting a role for this complex in skeletal muscle function.","predictedComplex":false,"interactors":[{"ac":"EBI-2510152","identifier":"Q9P2J3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P2J3/entry","name":"KLHL9","description":"Kelch-like protein 9","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45632","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8084","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL7 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. RL3-KLHL7 target proteins include the Ras GTPase-activating protein RASA2 (Q15283) which acts as an inhibitory regulator of the Ras-cyclic AMP pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6153160","identifier":"Q8IXQ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IXQ5/entry","name":"KLHL7","description":"Kelch-like protein 7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8085","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL8 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. RL3-KLHL8 target proteins include the postsynaptic protein RAPSN (Q13702) required for clustering of nicotinic acetylcholine receptors (nAChRs) at the neuromuscular junction.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-949008","identifier":"Q9P2G9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P2G9/entry","name":"KLHL8","description":"Kelch-like protein 8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8086","complexName":"Nexin-dynein regulatory complex","organismName":"Homo sapiens; 9606","description":"Present in the axonemes of cilia where it plays a critical role in ciliary motility, by linking adjacent outer microtubule duplexes. Maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes","predictedComplex":false,"interactors":[{"ac":"EBI-10262896","identifier":"Q8IY82","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IY82/entry","name":"DRC7","description":"Dynein regulatory complex subunit 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR35249","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1052570","identifier":"O95995","identifierLink":"https://www.uniprot.org/uniprotkb/O95995/entry","name":"GAS8","description":"Dynein regulatory complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31543","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10963444","identifier":"Q96MC2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96MC2/entry","name":"DRC1","description":"Dynein regulatory complex protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11335160","identifier":"Q5JU00","identifierLink":"https://www.uniprot.org/uniprotkb/Q5JU00/entry","name":"TCTE1","description":"Dynein regulatory complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24107","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13070008","identifier":"Q9H069","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H069/entry","name":"DRC3","description":"Dynein regulatory complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45973","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13628179","identifier":"Q5VUJ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q5VUJ9/entry","name":"EFCAB2","description":"Dynein regulatory complex protein 8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46763","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20836323","identifier":"Q8IXS2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IXS2/entry","name":"CCDC65","description":"Dynein regulatory complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20854387","identifier":"Q96DY2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96DY2/entry","name":"IQCD","description":"Dynein regulatory complex protein 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31598","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-44458341","identifier":"Q86XH1","identifierLink":"https://www.uniprot.org/uniprotkb/Q86XH1/entry","name":"IQCA1","description":"Dynein regulatory complex protein 11","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23074","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6425502","identifier":"Q8NEE6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NEE6/entry","name":"FBXL13","description":"F-box and leucine-rich repeat protein 13","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13318","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-719386","identifier":"Q9H095","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H095/entry","name":"IQCG","description":"Dynein regulatory complex protein 9","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14871","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8087","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL10 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. The complex appears to function specifically in the testis to mediate protein ubiquitination during spermiogenesis.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6426253","identifier":"Q6JEL2","identifierLink":"https://www.uniprot.org/uniprotkb/Q6JEL2/entry","name":"KLHL10","description":"Kelch-like protein 10","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8088","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL11 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.","predictedComplex":false,"interactors":[{"ac":"EBI-2691832","identifier":"Q9NVR0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NVR0/entry","name":"KLHL11","description":"Kelch-like protein 11","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8089","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL12 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. RL3-KLHL12 target proteins include the  transport protein  SEC31 (O94979/Q9NQW1) resulting in enlarged COPII (CPX-2360) vesicles which can accommodate procollagen molecules and thus enabling collagen secretion.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-740929","identifier":"Q53G59","identifierLink":"https://www.uniprot.org/uniprotkb/Q53G59/entry","name":"KLHL12","description":"Kelch-like protein 12","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8090","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL13 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. RL3-KLHL13 target proteins include the serine/threonine-protein kinase Aurora B (Q96GD4), which as a component of the Chromosomal Passenger complex (CPX-116) ensures chromosome bi-orientation on the mitotic spindle during metaphase by phosphorylating multiple kinetochore components. AURKB also acts as a critical regulator of the assembly and disassembly of type III intermediate filaments, including vimentin and desmin suggesting a role for this complex in skeletal muscle function.","predictedComplex":false,"interactors":[{"ac":"EBI-1996321","identifier":"Q9P2N7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P2N7/entry","name":"KLHL13","description":"Kelch-like protein 13","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45632","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8091","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL14 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6426284","identifier":"Q9P2G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P2G3/entry","name":"KLHL14","description":"Kelch-like protein 14","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45632","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8093","complexName":"SWI5-SFR1 recombination accessory factor complex","organismName":"Homo sapiens; 9606","description":"Regulates homologous recombination repair by binding to, and stimulating, the homologous DNA strand exchange activity of RAD51 (Q06609) and meiosis-specific DMC1 (Q14565). Enhances ATP hydrolysis-dependent transitioning of the first three-strand intermediate (a paranemic joint) of RAD51-driven DNA strand exchange into the second three-strand intermediate (a plectonemic joint), and then into reaction products, thus potentiating RAD51 activity in both the presynaptic and synaptic phases of DNA strand exchange.","predictedComplex":false,"interactors":[{"ac":"EBI-1104535","identifier":"Q86XK3","identifierLink":"https://www.uniprot.org/uniprotkb/Q86XK3/entry","name":"SFR1","description":"Swi5-dependent recombination DNA repair protein 1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28643","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20832852","identifier":"Q1ZZU3","identifierLink":"https://www.uniprot.org/uniprotkb/Q1ZZU3/entry","name":"SWI5","description":"DNA repair protein SWI5 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28529","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8094","complexName":"SWI5-SFR1 recombination accessory factor complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Regulates homologous recombination repair by binding to, and stimulating, the homologous DNA strand exchange activity of RAD51 (P36601) and meiosis-specific DMC1 (O42634). Enhances ATP hydrolysis-dependent transitioning of the first three-strand intermediate (a paranemic joint) of RAD51-driven DNA strand exchange into the second three-strand intermediate (a plectonemic joint), and then into reaction products, thus potentiating RAD51 activity in both the presynaptic and synaptic phases of DNA strand exchange.","predictedComplex":false,"interactors":[{"ac":"EBI-926902","identifier":"Q9UUB7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UUB7/entry","name":"swi5","description":"Mating-type switching protein swi5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-927233","identifier":"Q9USV1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9USV1/entry","name":"sfr1","description":"Swi5-dependent recombination DNA repair protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8095","complexName":"VCP-FAF1 AAA ATPase complex","organismName":"Homo sapiens; 9606","description":"A type II AAA ATPase that is involved in the dislocation/extraction step of retrotranslocation of misfolded proteins from the endoplasmic reticulum (ER) into the cytosol where they are degraded by the proteasome as part of the ER-associated protein degradation (ERAD) pathway. Targets proteins ubiquinated on Lys-48 for degradation, including the DNA replication licensing factor CDT1 (Q9H211) thus enabling DNA replication fork progression.","predictedComplex":false,"interactors":[{"ac":"EBI-355164","identifier":"P55072","identifierLink":"https://www.uniprot.org/uniprotkb/P55072/entry","name":"VCP","description":"Transitional endoplasmic reticulum ATPase","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-718246","identifier":"Q9UNN5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UNN5/entry","name":"FAF1","description":"FAS-associated factor 1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23322","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8096","complexName":"VCP-NPL4-UFD1-FAF1 AAA ATPase complex","organismName":"Homo sapiens; 9606","description":"A type II AAA ATPase that is involved in the dislocation/extraction step of its substrate proteins from cellular structures or multiprotein complexes into the cytosol where they are largely degraded by the proteasome. The complex targets proteins ubiquinylated on Lys-48 for degradation, including the DNA replication licensing factor CDT1 (Q9H211) thus enabling DNA replication fork progression and extracts topologically trapped DNA repair factor KU70/80 complex (CPX-1993) from DNA, specifically targeting XRCC5/KU80 (P13010).","predictedComplex":false,"interactors":[{"ac":"EBI-1994090","identifier":"Q92890","identifierLink":"https://www.uniprot.org/uniprotkb/Q92890/entry","name":"UFD1","description":"Ubiquitin recognition factor in ER-associated degradation protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12555","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1994109","identifier":"Q8TAT6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAT6/entry","name":"NPLOC4","description":"Nuclear protein localization protein 4 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12710","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355164","identifier":"P55072","identifierLink":"https://www.uniprot.org/uniprotkb/P55072/entry","name":"VCP","description":"Transitional endoplasmic reticulum ATPase","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-718246","identifier":"Q9UNN5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UNN5/entry","name":"FAF1","description":"FAS-associated factor 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23322","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8097","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL15 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. RL3-KLHL15 target proteins include the neuronal microtubule-associated proteins doublecortin (O43602), DCLK1 (O15075) and DCLK2 (Q8N568)suggesting a role for this complex in the development of the nervous system.","predictedComplex":false,"interactors":[{"ac":"EBI-2510129","identifier":"Q96M94","identifierLink":"https://www.uniprot.org/uniprotkb/Q96M94/entry","name":"KLHL15","description":"Kelch-like protein 15","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45632","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8101","complexName":"VCP-NPL4-UFD1-UBXN7 AAA ATPase complex","organismName":"Homo sapiens; 9606","description":"A type II AAA ATPase that is involved in the dislocation/extraction step of its substrate proteins from cellular structures or multiprotein complexes into the cytosol where they are largely degraded by the proteasome. Substrates include the CRL3-KEAP1 and CRL2-VHL (CPX-2250) ubiquitin ligase complexes which are involved in the regulation of the NFE2L2 (Q16236) and HIF1A (Q16665) protein levels respectively. Binds to polyubiquitylated CMG helicase (CPX-4526) and unloads this complex from a stalled DNA replication fork.","predictedComplex":false,"interactors":[{"ac":"EBI-1993627","identifier":"O94888","identifierLink":"https://www.uniprot.org/uniprotkb/O94888/entry","name":"UBXN7","description":"UBX domain-containing protein 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23322","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1994090","identifier":"Q92890","identifierLink":"https://www.uniprot.org/uniprotkb/Q92890/entry","name":"UFD1","description":"Ubiquitin recognition factor in ER-associated degradation protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12555","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1994109","identifier":"Q8TAT6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAT6/entry","name":"NPLOC4","description":"Nuclear protein localization protein 4 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12710","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355164","identifier":"P55072","identifierLink":"https://www.uniprot.org/uniprotkb/P55072/entry","name":"VCP","description":"Transitional endoplasmic reticulum ATPase","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8102","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL16 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. 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Dissociates the PPP1R7-PP1-PPP1R11 intermediate complex which keeps the PP1 catalytic subunit (P62136/P62140/P36873) in an inactive state enabling assembly of PP1 holoenzymes with its activating subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-1993668","identifier":"P68543","identifierLink":"https://www.uniprot.org/uniprotkb/P68543/entry","name":"UBXN2A","description":"UBX domain-containing protein 2A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355164","identifier":"P55072","identifierLink":"https://www.uniprot.org/uniprotkb/P55072/entry","name":"VCP","description":"Transitional endoplasmic reticulum ATPase","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8125","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL24 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. CRL3-KLHL24 target proteins include the keratin KRT15 (P19012), an intermediate filament which is part of the hair follicle stem cell cytoskeleton network.","predictedComplex":false,"interactors":[{"ac":"EBI-2510117","identifier":"Q6TFL4","identifierLink":"https://www.uniprot.org/uniprotkb/Q6TFL4/entry","name":"KLHL24","description":"Kelch-like protein 24","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8126","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL25 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. CRL3-KLHL25 target proteins include the ATP-citrate lyase (P53396) which converts mitochondrial-derived citrate into acetyl-CoA and oxaloacetic acid, and provides the main acetyl-CoA source for de novo fatty acid synthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6426337","identifier":"Q9H0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H0H3/entry","name":"KLHL25","description":"Kelch-like protein 25","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24410","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8127","complexName":"CDC48-SHP1 AAA ATPase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"A type II AAA ATPase that is involved in the dislocation/extraction step of its substrate proteins from cellular structures or multiprotein complexes into the cytosol where they are largely degraded by the proteasome. Acts to separate the substrate receptor MET30 (P39014) from the SCF-Met30 (CPX-3249) ubiquitin ligase complex when methionine limitation blocks the interaction between SCF-MET30 and its substrates MET4 (P32389) and MET32 (Q12041).","predictedComplex":false,"interactors":[{"ac":"EBI-17093","identifier":"P34223","identifierLink":"https://www.uniprot.org/uniprotkb/P34223/entry","name":"SHP1","description":"UBX domain-containing protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23333","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4308","identifier":"P25694","identifierLink":"https://www.uniprot.org/uniprotkb/P25694/entry","name":"CDC48","description":"Cell division control protein 48","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8128","complexName":"VCP-YOD1 AAA ATPase complex","organismName":"Homo sapiens; 9606","description":"A type II AAA ATPase that is involved in the dislocation/extraction step of its substrate proteins from cellular structures or multiprotein complexes into the cytosol where they are largely degraded by the proteasome. Binds Lys-11-, Lys-27-, Lys-29- and Lys-33-linked polyubiquitin chains and may play a role in autohagy and endoplasmic reticulum-associated protein degradation (ERAD).","predictedComplex":false,"interactors":[{"ac":"EBI-355164","identifier":"P55072","identifierLink":"https://www.uniprot.org/uniprotkb/P55072/entry","name":"VCP","description":"Transitional endoplasmic reticulum ATPase","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-488878","identifier":"P15172","identifierLink":"https://www.uniprot.org/uniprotkb/P15172/entry","name":"MYOD1","description":"Myoblast determination protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11534","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8129","complexName":"VCP-PLAA AAA ATPase complex","organismName":"Homo sapiens; 9606","description":"A type II AAA ATPase that is involved in the dislocation/extraction step of its substrate proteins from cellular structures or multiprotein complexes into the cytosol where they are largely degraded by the proteasome. Binds Lys-11-, Lys-27-, Lys-29- and Lys-33-linked polyubiquitin chains and may play a role in autohagy and endoplasmic reticulum-associated protein degradation (ERAD).","predictedComplex":false,"interactors":[{"ac":"EBI-1994037","identifier":"Q9Y263","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y263/entry","name":"PLAA","description":"Phospholipase A-2-activating protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19849","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355164","identifier":"P55072","identifierLink":"https://www.uniprot.org/uniprotkb/P55072/entry","name":"VCP","description":"Transitional endoplasmic reticulum ATPase","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8130","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL26 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724915","identifier":"Q53HC5","identifierLink":"https://www.uniprot.org/uniprotkb/Q53HC5/entry","name":"KLHL26","description":"Kelch-like protein 26","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45632","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8131","complexName":"CRL3 E3 ubiquitin ligase complex, IPP variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.","predictedComplex":false,"interactors":[{"ac":"EBI-11278395","identifier":"Q9Y573","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y573/entry","name":"IPP","description":"Actin-binding protein IPP","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8132","complexName":"VCP-VCPIP1 AAA ATPase complex","organismName":"Homo sapiens; 9606","description":"A type II AAA ATPase that is involved in the dislocation/extraction step of its substrate proteins from cellular structures or multiprotein complexes into the cytosol where they are largely degraded by the proteasome. Appears to play a role in the reassembly of Golgi stacks after mitosis and the formation of the transitional endoplasmic reticulum.The VCP-NSFL1C AAA ATPase complex (CPX-262) requires the deubiquitylase activity of CCPIP1 for postmitotic Golgi cisternae regrowth and Golgi structure maintenance in interphase. Formation of this complex appears to cause the dissociation of the VCP-NSFL complex.","predictedComplex":false,"interactors":[{"ac":"EBI-1995920","identifier":"Q96JH7","identifierLink":"https://www.uniprot.org/uniprotkb/Q96JH7/entry","name":"VCPIP1","description":"Deubiquitinating protein VCPIP1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14843","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355164","identifier":"P55072","identifierLink":"https://www.uniprot.org/uniprotkb/P55072/entry","name":"VCP","description":"Transitional endoplasmic reticulum ATPase","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8133","complexName":"VCP-UBXN6 AAA ATPase complex","organismName":"Homo sapiens; 9606","description":"A type II AAA ATPase that is involved in the dislocation/extraction step of its substrate proteins from cellular structures or multiprotein complexes into the cytosol where they are largely degraded by the proteasome. Promotes PRKN (O60260)-dependent mitophagy by specifically recognizing damaged mitochondria undergoing autophagic clearance.","predictedComplex":false,"interactors":[{"ac":"EBI-1993899","identifier":"Q9BZV1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BZV1/entry","name":"UBXN6","description":"UBX domain-containing protein 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23153","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355164","identifier":"P55072","identifierLink":"https://www.uniprot.org/uniprotkb/P55072/entry","name":"VCP","description":"Transitional endoplasmic reticulum ATPase","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8134","complexName":"VCP-AMFR AAA ATPase complex","organismName":"Homo sapiens; 9606","description":"A type II AAA ATPase that is involved in the dislocation/extraction step of its substrate proteins from cellular structures or multiprotein complexes into the cytosol where they are largely degraded by the proteasome. Plays a role in  endoplasmic reticulum-associated degradation (ERAD). AMFR is an endoplasmic reticulum membrane-anchored ubiquitin ligase that mediates the ubiquitylation of a key enzyme  in the synthesis of cholesterol and other isoprenoids, HMGCR (P04035) when cholesterol is abundant. The ubiquitinated protein is then extracted from the membrane by VCP.","predictedComplex":false,"interactors":[{"ac":"EBI-1046367","identifier":"Q9UKV5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UKV5/entry","name":"AMFR","description":"E3 ubiquitin-protein ligase AMFR","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355164","identifier":"P55072","identifierLink":"https://www.uniprot.org/uniprotkb/P55072/entry","name":"VCP","description":"Transitional endoplasmic reticulum ATPase","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8135","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL28 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.","predictedComplex":false,"interactors":[{"ac":"EBI-21328957","identifier":"Q9NXS3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NXS3/entry","name":"KLHL28","description":"Kelch-like protein 28","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8141","complexName":"Sodium:potassium-exchanging ATPase complex, FXYD3 variant","organismName":"Homo sapiens; 9606","description":"An ATPase-dependent transmembrane transport complex capable of generating electrochemical gradients by exchanging three intracellular sodium ions for two extracellular potassium ions during each cycle of ATP hydrolysis. Na+/K+ pumps can also generate an inward current of protons.  \r\n\r\nEach transport cycle comprises a sequence of conformational transitions that permit extracellular K+ ions to access the binding sites in phosphorylated pumps and cytoplasmic Na+ ions to access the sites after dephosphorylation . Binding of the third Na+ ion triggers autophosphorylation, and binding of the second K+ ion prompts auto-dephosphorylation. This coupling of alternating ion access to ATP hydrolysis ensures forward, energetically uphill, progress of the Na+/K+ transport cycle. The larger pumped Na+ efflux than K+ influx constitutes outward current, a direction tending to make the membrane potential more negative. However, because each step in the cycle is reversible , if the normally transported intracellular Na+ and extracellular K+ are both scarce, the cycle can run backward, thus synthesizing ATP and generating inward, depolarizing current.","predictedComplex":false,"interactors":[{"ac":"EBI-358778","identifier":"P05023","identifierLink":"https://www.uniprot.org/uniprotkb/P05023/entry","name":"ATP1A1","description":"Sodium/potassium-transporting ATPase subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714630","identifier":"P05026","identifierLink":"https://www.uniprot.org/uniprotkb/P05026/entry","name":"ATP1B1","description":"Sodium/potassium-transporting ATPase subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11523","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-719805","identifier":"Q14802","identifierLink":"https://www.uniprot.org/uniprotkb/Q14802/entry","name":"FXYD3","description":"FXYD domain-containing ion transport regulator 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14132","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8142","complexName":"Sodium:potassium-exchanging ATPase complex, FXYD4 variant","organismName":"Homo sapiens; 9606","description":"An ATPase-dependent transmembrane transport complex capable of generating electrochemical gradients by exchanging three intracellular sodium ions for two extracellular potassium ions during each cycle of ATP hydrolysis. Na+/K+ pumps can also generate an inward current of protons.  \r\n\r\nEach transport cycle comprises a sequence of conformational transitions that permit extracellular K+ ions to access the binding sites in phosphorylated pumps and cytoplasmic Na+ ions to access the sites after dephosphorylation . Binding of the third Na+ ion triggers autophosphorylation, and binding of the second K+ ion prompts auto-dephosphorylation. This coupling of alternating ion access to ATP hydrolysis ensures forward, energetically uphill, progress of the Na+/K+ transport cycle. The larger pumped Na+ efflux than K+ influx constitutes outward current, a direction tending to make the membrane potential more negative. However, because each step in the cycle is reversible , if the normally transported intracellular Na+ and extracellular K+ are both scarce, the cycle can run backward, thus synthesizing ATP and generating inward, depolarizing current. Variants containing ATP1A1-ATP1B1 appear to be most widely expressed.","predictedComplex":false,"interactors":[{"ac":"EBI-358778","identifier":"P05023","identifierLink":"https://www.uniprot.org/uniprotkb/P05023/entry","name":"ATP1A1","description":"Sodium/potassium-transporting ATPase subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46435011","identifier":"P59646","identifierLink":"https://www.uniprot.org/uniprotkb/P59646/entry","name":"FXYD4","description":"FXYD domain-containing ion transport regulator 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14132","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714630","identifier":"P05026","identifierLink":"https://www.uniprot.org/uniprotkb/P05026/entry","name":"ATP1B1","description":"Sodium/potassium-transporting ATPase subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11523","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8143","complexName":"Sodium:potassium-exchanging ATPase complex, FXYD5 variant","organismName":"Homo sapiens; 9606","description":"An ATPase-dependent transmembrane transport complex capable of generating electrochemical gradients by exchanging three intracellular sodium ions for two extracellular potassium ions during each cycle of ATP hydrolysis. Na+/K+ pumps can also generate an inward current of protons.  \r\n\r\nEach transport cycle comprises a sequence of conformational transitions that permit extracellular K+ ions to access the binding sites in phosphorylated pumps and cytoplasmic Na+ ions to access the sites after dephosphorylation . Binding of the third Na+ ion triggers autophosphorylation, and binding of the second K+ ion prompts auto-dephosphorylation. This coupling of alternating ion access to ATP hydrolysis ensures forward, energetically uphill, progress of the Na+/K+ transport cycle. The larger pumped Na+ efflux than K+ influx constitutes outward current, a direction tending to make the membrane potential more negative. However, because each step in the cycle is reversible , if the normally transported intracellular Na+ and extracellular K+ are both scarce, the cycle can run backward, thus synthesizing ATP and generating inward, depolarizing current. Variants containing ATP1A1-ATP1B1 appear to be most widely expressed.","predictedComplex":false,"interactors":[{"ac":"EBI-14022463","identifier":"Q96DB9","identifierLink":"https://www.uniprot.org/uniprotkb/Q96DB9/entry","name":"FXYD5","description":"FXYD domain-containing ion transport regulator 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14132","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358778","identifier":"P05023","identifierLink":"https://www.uniprot.org/uniprotkb/P05023/entry","name":"ATP1A1","description":"Sodium/potassium-transporting ATPase subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714630","identifier":"P05026","identifierLink":"https://www.uniprot.org/uniprotkb/P05026/entry","name":"ATP1B1","description":"Sodium/potassium-transporting ATPase subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11523","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8144","complexName":"Sodium:potassium-exchanging ATPase complex, FXYD6 variant","organismName":"Homo sapiens; 9606","description":"An ATPase-dependent transmembrane transport complex capable of generating electrochemical gradients by exchanging three intracellular sodium ions for two extracellular potassium ions during each cycle of ATP hydrolysis. Na+/K+ pumps can also generate an inward current of protons.  \r\n\r\nEach transport cycle comprises a sequence of conformational transitions that permit extracellular K+ ions to access the binding sites in phosphorylated pumps and cytoplasmic Na+ ions to access the sites after dephosphorylation . Binding of the third Na+ ion triggers autophosphorylation, and binding of the second K+ ion prompts auto-dephosphorylation. This coupling of alternating ion access to ATP hydrolysis ensures forward, energetically uphill, progress of the Na+/K+ transport cycle. The larger pumped Na+ efflux than K+ influx constitutes outward current, a direction tending to make the membrane potential more negative. However, because each step in the cycle is reversible , if the normally transported intracellular Na+ and extracellular K+ are both scarce, the cycle can run backward, thus synthesizing ATP and generating inward, depolarizing current. Variants containing ATP1A1-ATP1B1 appear to be most widely expressed.","predictedComplex":false,"interactors":[{"ac":"EBI-358778","identifier":"P05023","identifierLink":"https://www.uniprot.org/uniprotkb/P05023/entry","name":"ATP1A1","description":"Sodium/potassium-transporting ATPase subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-713304","identifier":"Q9H0Q3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H0Q3/entry","name":"FXYD6","description":"FXYD domain-containing ion transport regulator 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14132","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714630","identifier":"P05026","identifierLink":"https://www.uniprot.org/uniprotkb/P05026/entry","name":"ATP1B1","description":"Sodium/potassium-transporting ATPase subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11523","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8146","complexName":"Sodium:potassium-exchanging ATPase complex, FXYD7 variant","organismName":"Homo sapiens; 9606","description":"An ATPase-dependent transmembrane transport complex capable of generating electrochemical gradients by exchanging three intracellular sodium ions for two extracellular potassium ions during each cycle of ATP hydrolysis. Na+/K+ pumps can also generate an inward current of protons.  \r\n\r\nEach transport cycle comprises a sequence of conformational transitions that permit extracellular K+ ions to access the binding sites in phosphorylated pumps and cytoplasmic Na+ ions to access the sites after dephosphorylation . Binding of the third Na+ ion triggers autophosphorylation, and binding of the second K+ ion prompts auto-dephosphorylation. This coupling of alternating ion access to ATP hydrolysis ensures forward, energetically uphill, progress of the Na+/K+ transport cycle. The larger pumped Na+ efflux than K+ influx constitutes outward current, a direction tending to make the membrane potential more negative. However, because each step in the cycle is reversible , if the normally transported intracellular Na+ and extracellular K+ are both scarce, the cycle can run backward, thus synthesizing ATP and generating inward, depolarizing current. Variants containing ATP1A1-ATP1B1 appear to be most widely expressed.","predictedComplex":false,"interactors":[{"ac":"EBI-10216171","identifier":"P58549","identifierLink":"https://www.uniprot.org/uniprotkb/P58549/entry","name":"FXYD7","description":"FXYD domain-containing ion transport regulator 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14132","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358778","identifier":"P05023","identifierLink":"https://www.uniprot.org/uniprotkb/P05023/entry","name":"ATP1A1","description":"Sodium/potassium-transporting ATPase subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43294","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714630","identifier":"P05026","identifierLink":"https://www.uniprot.org/uniprotkb/P05026/entry","name":"ATP1B1","description":"Sodium/potassium-transporting ATPase subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11523","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8147","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL29 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6426370","identifier":"Q96CT2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96CT2/entry","name":"KLHL29","description":"Kelch-like protein 29","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8148","complexName":"PRMT5 methylosome complex, RIOK1 variant","organismName":"Homo sapiens; 9606","description":"Type II arginine methyltransferase which dimethylates substrate proteins by catalyzing a 2-step transfer of 2 methyl groups from 2 S-adenosyl methionine (SAM) cofactor molecules to substrate arginine residues. RIOK1 recruits nucleolin (P19338) and ribosomal subunit RPS10 (P46783) to the complex for methylation thus regulating ribosome biogenesis.","predictedComplex":false,"interactors":[{"ac":"EBI-1237307","identifier":"Q9BQA1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BQA1/entry","name":"WDR77","description":"Methylosome protein WDR77","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46853","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-351098","identifier":"O14744","identifierLink":"https://www.uniprot.org/uniprotkb/O14744/entry","name":"PRMT5","description":"Protein arginine N-methyltransferase 5","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10738","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7307838","identifier":"Q9BRS2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BRS2/entry","name":"RIOK1","description":"Serine/threonine-protein kinase RIO1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45723","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8149","complexName":"PRMT5 methylosome complex, COPR5 variant","organismName":"Homo sapiens; 9606","description":"Type II arginine methyltransferase which dimethylates substrate proteins by catalyzing a 2-step transfer of 2 methyl groups from 2 S-adenosyl methionine (SAM) cofactor molecules to substrate arginine residues. COPRS recruits PRMT5 to nucleosomes and promotes methylation of arginine residues including H3R8 and H4R3 thus regulating  chromatin remodelling.","predictedComplex":false,"interactors":[{"ac":"EBI-1237307","identifier":"Q9BQA1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BQA1/entry","name":"WDR77","description":"Methylosome protein WDR77","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46853","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1642558","identifier":"Q9NQ92","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NQ92/entry","name":"COPRS","description":"Coordinator of PRMT5 and differentiation stimulator","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR36461","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-351098","identifier":"O14744","identifierLink":"https://www.uniprot.org/uniprotkb/O14744/entry","name":"PRMT5","description":"Protein arginine N-methyltransferase 5","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10738","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8150","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL30 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46435896","identifier":"Q0D2K2","identifierLink":"https://www.uniprot.org/uniprotkb/Q0D2K2/entry","name":"KLHL30","description":"Kelch-like protein 30","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8151","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL31 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. CRL3-KLHL31 target proteins include the muscle-specific FLNC (Q14315), which plays a central role in sarcomere assembly and organization, the complex may therefore play a role in myogenesis.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9478985","identifier":"Q9H511","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H511/entry","name":"KLHL31","description":"Kelch-like protein 31","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45632","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8152","complexName":"MON1-CCZ1 guanyl-nucleotide exchange factor complex, MON1B variant","organismName":"Homo sapiens; 9606","description":"Guanyl-nucleotide exchange factor complex required to activate the endosomal GTPase RAB7A/B (P51149/Q96AH8). The complex is recruited to endosomal membranes by phosphatidylinositol 3-phosphate and its activation of RAB7 drives RAB5 (P20339/P61020)-to-RAB7 conversion, endosome maturation and fusion with the vacuolar/lysosomal compartment. RAB7 activation additionally causes NPC1 (O15118)-dependent lysosomal cholesterol export.","predictedComplex":false,"interactors":[{"ac":"EBI-2655311","identifier":"Q7L1V2","identifierLink":"https://www.uniprot.org/uniprotkb/Q7L1V2/entry","name":"MON1B","description":"Vacuolar fusion protein MON1 homolog B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13027","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2804848","identifier":"Q96DM3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96DM3/entry","name":"RMC1","description":"Regulator of MON1-CCZ1 complex","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12897","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46436054","identifier":"P86791","identifierLink":"https://www.uniprot.org/uniprotkb/P86791/entry","name":"CCZ1","description":"Vacuolar fusion protein CCZ1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8153","complexName":"MON1-CCZ1 guanyl-nucleotide exchange factor complex, MON1A variant","organismName":"Homo sapiens; 9606","description":"Guanyl-nucleotide exchange factor complex required to activate the endosomal GTPase RAB7A/B (P51149/Q96AH8). The complex is recruited to endosomal membranes by phosphatidylinositol 3-phosphate and its activation of RAB7 drives RAB5 (P20339/P61020)-to-RAB7 conversion, endosome maturation and fusion with the vacuolar/lysosomal compartment. RAB7 activation additionally causes NPC1 (O15118)-dependent lysosomal cholesterol export","predictedComplex":false,"interactors":[{"ac":"EBI-2804848","identifier":"Q96DM3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96DM3/entry","name":"RMC1","description":"Regulator of MON1-CCZ1 complex","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12897","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46436054","identifier":"P86791","identifierLink":"https://www.uniprot.org/uniprotkb/P86791/entry","name":"CCZ1","description":"Vacuolar fusion protein CCZ1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-949638","identifier":"Q86VX9","identifierLink":"https://www.uniprot.org/uniprotkb/Q86VX9/entry","name":"MON1A","description":"Vacuolar fusion protein MON1 homolog A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13027","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8161","complexName":"Radial spoke complex, ciliiar variant","organismName":"Mus musculus; 10090","description":"Mechanochemical signal transducer acting between the central pair of microtubules and dyneins in motile cilia and flagella to modulates the beat frequency, amplitude, and waveform of their movement. The majority of motile cilia and flagella are composed of an array of microtubules, typically arranged in in nine doublet pairs around the central pair (the 9+2 axoneme). Each 96-nm-long axonemal unit contains three radical spokes, RS1, RS2, and RS3 which each maintain a T-shaped morphology","predictedComplex":false,"interactors":[{"ac":"EBI-46437008","identifier":"Q8VIG3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VIG3/entry","name":"Rsph1","description":"Radial spoke head 1 homolog","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR43215","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46437031","identifier":"Q9DA80","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DA80/entry","name":"Rsph3b","description":"Radial spoke head protein 3 homolog B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46437046","identifier":"Q8BYM7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BYM7/entry","name":"Rsph4a","description":"Radial spoke head protein 4 homolog A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13159","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46437067","identifier":"Q9D9V4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D9V4/entry","name":"Rsph9","description":"Radial spoke head protein 9 homolog","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22069","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46437144","identifier":"Q9D9T0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D9T0/entry","name":"Dydc1","description":"DPY30 domain-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23356","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46437162","identifier":"Q99MH5","identifierLink":"https://www.uniprot.org/uniprotkb/Q99MH5/entry","name":"Nme5","description":"Nucleoside diphosphate kinase homolog 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46161","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46437202","identifier":"Q9EQ00","identifierLink":"https://www.uniprot.org/uniprotkb/Q9EQ00/entry","name":"Ropn1l","description":"Ropporin-1-like protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14952","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46437220","identifier":"Q9D3W1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D3W1/entry","name":"Rsph14","description":"Radial spoke head 14 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46437256","identifier":"Q80Y75","identifierLink":"https://www.uniprot.org/uniprotkb/Q80Y75/entry","name":"Dnajb13","description":"DnaJ homolog subfamily B member 13","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24078","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46437298","identifier":"Q5NCY3","identifierLink":"https://www.uniprot.org/uniprotkb/Q5NCY3/entry","name":"Cyb5d1","description":"Cytochrome b5 domain-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21281","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46437320","identifier":"Q6PE87","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PE87/entry","name":"Cfap206","description":"Cilia- and flagella-associated protein 206","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46437349","identifier":"Q3UFY4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3UFY4/entry","name":"Rsph3a","description":"Radial spoke head protein 3 homolog A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-767129","identifier":"Q9D0M5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D0M5/entry","name":"Dynll2","description":"Dynein light chain 2, cytoplasmic","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8162","complexName":"Radial spoke complex, flagellar variant","organismName":"Mus musculus; 10090","description":"Mechanochemical signal transducer acting between the central pair of microtubules and dyneins in motile cilia and flagella to modulates the beat frequency, amplitude, and waveform of their movement. The majority of motile cilia and flagella are composed of an array of microtubules, typically arranged in in nine doublet pairs around the central pair (the 9+2 axoneme). Each 96-nm-long axonemal unit contains three radical spokes, RS1, RS2, and RS3 which each maintain a T-shaped morphology","predictedComplex":false,"interactors":[{"ac":"EBI-46437008","identifier":"Q8VIG3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VIG3/entry","name":"Rsph1","description":"Radial spoke head 1 homolog","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR43215","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46437031","identifier":"Q9DA80","identifierLink":"https://www.uniprot.org/uniprotkb/Q9DA80/entry","name":"Rsph3b","description":"Radial spoke head protein 3 homolog B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46437067","identifier":"Q9D9V4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D9V4/entry","name":"Rsph9","description":"Radial spoke head protein 9 homolog","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22069","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46437144","identifier":"Q9D9T0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D9T0/entry","name":"Dydc1","description":"DPY30 domain-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23356","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46437162","identifier":"Q99MH5","identifierLink":"https://www.uniprot.org/uniprotkb/Q99MH5/entry","name":"Nme5","description":"Nucleoside diphosphate kinase homolog 5","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46161","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46437202","identifier":"Q9EQ00","identifierLink":"https://www.uniprot.org/uniprotkb/Q9EQ00/entry","name":"Ropn1l","description":"Ropporin-1-like protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR14952","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46437220","identifier":"Q9D3W1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D3W1/entry","name":"Rsph14","description":"Radial spoke head 14 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46437256","identifier":"Q80Y75","identifierLink":"https://www.uniprot.org/uniprotkb/Q80Y75/entry","name":"Dnajb13","description":"DnaJ homolog subfamily B member 13","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24078","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46437298","identifier":"Q5NCY3","identifierLink":"https://www.uniprot.org/uniprotkb/Q5NCY3/entry","name":"Cyb5d1","description":"Cytochrome b5 domain-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21281","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46437320","identifier":"Q6PE87","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PE87/entry","name":"Cfap206","description":"Cilia- and flagella-associated protein 206","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46437349","identifier":"Q3UFY4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3UFY4/entry","name":"Rsph3a","description":"Radial spoke head protein 3 homolog A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR21648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46437371","identifier":"Q8CDR2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8CDR2/entry","name":"Rsph6a","description":"Radial spoke head protein 6 homolog A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Mus musculus; 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The majority of motile cilia and flagella are composed of an array of microtubules, typically arranged in in nine doublet pairs around the central pair (the 9+2 axoneme). 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9606","xrefs":[{"identifier":"PTHR14952","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8164","complexName":"Radial spoke complex, flagellar variant","organismName":"Homo sapiens; 9606","description":"Mechanochemical signal transducer acting between the central pair of microtubules and dyneins in motile cilia and flagella to modulates the beat frequency, amplitude, and waveform of their movement. The majority of motile cilia and flagella are composed of an array of microtubules, typically arranged in in nine doublet pairs around the central pair (the 9+2 axoneme). Each 96-nm-long axonemal unit contains three radical spokes, RS1, RS2, and RS3 which each maintain a T-shaped morphology","predictedComplex":false,"interactors":[{"ac":"EBI-10220600","identifier":"Q8NA54","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NA54/entry","name":"IQUB","description":"IQ motif and ubiquitin-like domain-containing protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21074","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10253582","identifier":"Q8WYR4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WYR4/entry","name":"RSPH1","description":"Radial spoke head 1 homolog","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43215","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10305303","identifier":"Q9H1X1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H1X1/entry","name":"RSPH9","description":"Radial spoke head protein 9 homolog","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22069","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11514233","identifier":"P59910","identifierLink":"https://www.uniprot.org/uniprotkb/P59910/entry","name":"DNAJB13","description":"DnaJ homolog subfamily B member 13","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24078","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12169267","identifier":"Q9H0K4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H0K4/entry","name":"RSPH6A","description":"Radial spoke head protein 6 homolog A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13159","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21325161","identifier":"Q6P9G0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P9G0/entry","name":"CYB5D1","description":"Cytochrome b5 domain-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21281","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6873025","identifier":"Q86UC2","identifierLink":"https://www.uniprot.org/uniprotkb/Q86UC2/entry","name":"RSPH3","description":"Radial spoke head protein 3 homolog","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-740667","identifier":"P56597","identifierLink":"https://www.uniprot.org/uniprotkb/P56597/entry","name":"NME5","description":"Nucleoside diphosphate kinase homolog 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46161","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-740680","identifier":"Q8WWB3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WWB3/entry","name":"DYDC1","description":"DPY30 domain-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23356","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742371","identifier":"Q96FJ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96FJ2/entry","name":"DYNLL2","description":"Dynein light chain 2, cytoplasmic","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-748350","identifier":"Q9UHP6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UHP6/entry","name":"RSPH14","description":"Radial spoke head 14 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749051","identifier":"Q8IYR0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IYR0/entry","name":"CFAP206","description":"Cilia- and flagella-associated protein 206","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9033237","identifier":"Q96C74","identifierLink":"https://www.uniprot.org/uniprotkb/Q96C74/entry","name":"ROPN1L","description":"Ropporin-1-like protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14952","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8165","complexName":"MON1-CCZ1B guanyl-nucleotide exchange factor complex, MON1A variant","organismName":"Homo sapiens; 9606","description":"Guanyl-nucleotide exchange factor complex required to activate the endosomal GTPase RAB7A/B (P51149/Q96AH8). The complex is recruited to endosomal membranes by phosphatidylinositol 3-phosphate and its activation of RAB7 drives RAB5 (P20339/P61020)-to-RAB7 conversion, endosome maturation and fusion with the vacuolar/lysosomal compartment. RAB7 activation additionally causes NPC1 (O15118)-dependent lysosomal cholesterol export.","predictedComplex":false,"interactors":[{"ac":"EBI-11353190","identifier":"P86790","identifierLink":"https://www.uniprot.org/uniprotkb/P86790/entry","name":"CCZ1B","description":"Vacuolar fusion protein CCZ1 homolog B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2804848","identifier":"Q96DM3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96DM3/entry","name":"RMC1","description":"Regulator of MON1-CCZ1 complex","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12897","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-949638","identifier":"Q86VX9","identifierLink":"https://www.uniprot.org/uniprotkb/Q86VX9/entry","name":"MON1A","description":"Vacuolar fusion protein MON1 homolog A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13027","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8166","complexName":"MON1-CCZ1B guanyl-nucleotide exchange factor complex, MON1B variant","organismName":"Homo sapiens; 9606","description":"Guanyl-nucleotide exchange factor complex required to activate the endosomal GTPase RAB7A/B (P51149/Q96AH8). The complex is recruited to endosomal membranes by phosphatidylinositol 3-phosphate and its activation of RAB7 drives RAB5 (P20339/P61020)-to-RAB7 conversion, endosome maturation and fusion with the vacuolar/lysosomal compartment. RAB7 activation additionally causes NPC1 (O15118)-dependent lysosomal cholesterol export.","predictedComplex":false,"interactors":[{"ac":"EBI-11353190","identifier":"P86790","identifierLink":"https://www.uniprot.org/uniprotkb/P86790/entry","name":"CCZ1B","description":"Vacuolar fusion protein CCZ1 homolog B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2655311","identifier":"Q7L1V2","identifierLink":"https://www.uniprot.org/uniprotkb/Q7L1V2/entry","name":"MON1B","description":"Vacuolar fusion protein MON1 homolog B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13027","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2804848","identifier":"Q96DM3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96DM3/entry","name":"RMC1","description":"Regulator of MON1-CCZ1 complex","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12897","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8167","complexName":"OSBPL9-OSBPL10 oxysterol-binding protein-related complex","organismName":"Homo sapiens; 9606","description":"Lipid binding complex which plays a critical role in regulating phosphatidylinositol 4-phosphate in the trans-Golgi network, maintaining maintain lipid homeostasis between the endoplasmic reticulum and  trans-Golgi network and regulating vesicle trafficking..Recruited by phosphatidylinositol-4 kinase type 2-alpha PI4K2A (Q9BTU6) following lysosomal membrane permeabilization to create new membrane contact sites between damaged lysosomes and the endoplasmic reticulum and transfer phosphatidylserine and cholesterol to support rapid lysosomal repair.","predictedComplex":false,"interactors":[{"ac":"EBI-2511286","identifier":"Q9BXB5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BXB5/entry","name":"OSBPL10","description":"Oxysterol-binding protein-related protein 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10972","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2511368","identifier":"Q96SU4","identifierLink":"https://www.uniprot.org/uniprotkb/Q96SU4/entry","name":"OSBPL9","description":"Oxysterol-binding protein-related protein 9","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10972","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8168","complexName":"OSBPL9-OSBPL11 oxysterol-binding protein-related complex","organismName":"Homo sapiens; 9606","description":"Lipid binding complex which plays a critical role in regulating phosphatidylinositol 4-phosphate in the trans-Golgi network, maintaining maintain lipid homeostasis between the endoplasmic reticulum and  trans-Golgi network and regulating vesicle trafficking..Recruited by phosphatidylinositol-4 kinase type 2-alpha PI4K2A (Q9BTU6) following lysosomal membrane permeabilization to create new membrane contact sites between damaged lysosomes and the endoplasmic reticulum and transfer phosphatidylserine and cholesterol to support rapid lysosomal repair.","predictedComplex":false,"interactors":[{"ac":"EBI-2511368","identifier":"Q96SU4","identifierLink":"https://www.uniprot.org/uniprotkb/Q96SU4/entry","name":"OSBPL9","description":"Oxysterol-binding protein-related protein 9","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10972","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2514786","identifier":"Q9BXB4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BXB4/entry","name":"OSBPL11","description":"Oxysterol-binding protein-related protein 11","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10972","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8169","complexName":"SEC61 protein-conducting channel complex, SEC1A2 variant","organismName":"Homo sapiens; 9606","description":"Translocates hydrophilic polypeptide segments of newly synthesized proteins across the endoplasmic reticulum membrane and integrates hydrophobic transmembrane segments into the membrane for subsequent transport to other subcellular locations via vesicular trafficking. The complex associates with several other molecular machines and enzymes, such as the ribosome, the SEC62-SEC63 complex, and oligosaccharyltransferase complex (CPX-5621/CPX-5622).","predictedComplex":false,"interactors":[{"ac":"EBI-1172006","identifier":"Q9H9S3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H9S3/entry","name":"SEC61A2","description":"Protein transport protein Sec61 subunit alpha isoform 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10906","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1788819","identifier":"P60468","identifierLink":"https://www.uniprot.org/uniprotkb/P60468/entry","name":"SEC61B","description":"Protein transport protein Sec61 subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13509","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4402709","identifier":"P60059","identifierLink":"https://www.uniprot.org/uniprotkb/P60059/entry","name":"SEC61G","description":"Protein transport protein Sec61 subunit gamma","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12309","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8171","complexName":"PBA1-PBA2 proteasomal chaperone complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Chaperone complex with a role in the early stage assembly of the 26S proteasome (CPX-2262). Binds to the top of the alpha ring as it assembles, on the opposite side to the PBA3-PBA4 complex (CPX-8172) and is assumed to enforce the proper configuration of the ring and prevent the premature binding of other complexes which interact with the core barrel-shaped chamber. Release of the PBA1-PBA2 complex is one of the final stages of proteasome assembly.","predictedComplex":false,"interactors":[{"ac":"EBI-27001","identifier":"P36040","identifierLink":"https://www.uniprot.org/uniprotkb/P36040/entry","name":"ADD66","description":"Proteasome assembly chaperone 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12970","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-33792","identifier":"Q05778","identifierLink":"https://www.uniprot.org/uniprotkb/Q05778/entry","name":"PBA1","description":"Proteasome chaperone 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-8172","complexName":"PBA3-PBA4 proteasomal chaperone complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Chaperone complex with a role in the early stage assembly of the 26S proteasome (CPX-2262). Binds to the bottom of the alpha ring as it assembles, on the opposite side to the PBA1-PBA2 complex (CPX-8171) and is assumed to enforce the proper configuration of the ring and prevent the premature binding of other complexes which interact with the core barrel-shaped chamber. PBA3-PBA4 appears to disengage shortly after completion of the alpha-ring.","predictedComplex":false,"interactors":[{"ac":"EBI-2343020","identifier":"Q12245","identifierLink":"https://www.uniprot.org/uniprotkb/Q12245/entry","name":"POC4","description":"Proteasome chaperone 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-31959","identifier":"Q07951","identifierLink":"https://www.uniprot.org/uniprotkb/Q07951/entry","name":"IRC25","description":"Proteasome chaperone 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-8173","complexName":"PSMG1-PSMG2 proteasomal chaperone complex","organismName":"Homo sapiens; 9606","description":"Chaperone complex with a role in the early stage assembly of the 26S proteasome (CPX-2262). Binds to the alpha-subunits before alpha-rings are complete, functioning as a scaffold for alpha-ring assembly and preventing unregulated aggregation of alpha-ring intermediates. The complex binds to the top-side of the alpha-ring, the opposite surface to which the PSMG3-PSMG4 (CPX-8174) complex binds.","predictedComplex":false,"interactors":[{"ac":"EBI-6286129","identifier":"O95456","identifierLink":"https://www.uniprot.org/uniprotkb/O95456/entry","name":"PSMG1","description":"Proteasome assembly chaperone 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15069","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-723276","identifier":"Q969U7","identifierLink":"https://www.uniprot.org/uniprotkb/Q969U7/entry","name":"PSMG2","description":"Proteasome assembly chaperone 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12970","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8174","complexName":"PSMG3-PSMG4 proteasomal chaperone complex","organismName":"Homo sapiens; 9606","description":"Chaperone complex with a role in the early stage assembly of the 26S proteasome (CPX-2262). Binds to the alpha-subunits before alpha-rings are complete, functioning as a scaffold for alpha-ring assembly and preventing unregulated aggregation of alpha-ring intermediates. The complex binds to the underside of the alpha-ring where the beta-subunits will later assemble.","predictedComplex":false,"interactors":[{"ac":"EBI-16780812","identifier":"Q5JS54","identifierLink":"https://www.uniprot.org/uniprotkb/Q5JS54/entry","name":"PSMG4","description":"Proteasome assembly chaperone 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR33559","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3921395","identifier":"Q9BT73","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BT73/entry","name":"PSMG3","description":"Proteasome assembly chaperone 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31051","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8175","complexName":"SLX1-SLX4 structure-specific endonuclease complex","organismName":"Homo sapiens; 9606","description":"A structure-specific DNA endonuclease that cleaves the phosphodiester backbone on the 3'-side of the DNA branchpoint of branched DNA substrates including stem-loops and Y-structures, replication forks, 5'- and 3'-flaps, and nicked or intact Holliday junctions and is therefore involved in DNA recombination and repair.","predictedComplex":false,"interactors":[{"ac":"EBI-2370740","identifier":"Q8IY92","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IY92/entry","name":"SLX4","description":"Structure-specific endonuclease subunit SLX4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21541","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2370858","identifier":"Q9BQ83","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BQ83/entry","name":"SLX1A","description":"Structure-specific endonuclease subunit SLX1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20208","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-8182","complexName":"DUOX2-DUOXA2 dual oxidase complex","organismName":"Homo sapiens; 9606","description":"Calcium-dependent NADPH oxidase which catalyzes cross-membrane electron transfer resulting in the production of hydrogen peroxide (H2O2).  Electrons are transferred from NADPH to FAD, to a heme molecule on the cytoplasmic side of the membrane, to Phe-1097 of DUOX2, and finally to the heme group on the extracellular side of the membrane where they react with oxygen. Required for the H2O2-dependent activity of thyroperoxidase (P07202) which catalyzes the three steps of thyroid hormone biosynthesis. May also have an antimicrobial role at mucosal surfases such as salivary glands in the trachea and play a role in wound response at the airway epithelium.","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-12740885","identifier":"Q9NRD8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NRD8/entry","name":"DUOX2","description":"Dual oxidase 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11972","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25589731","identifier":"Q1HG44","identifierLink":"https://www.uniprot.org/uniprotkb/Q1HG44/entry","name":"DUOXA2","description":"Dual oxidase maturation factor 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31158","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-8183","complexName":"DUOX1-DUOXA1 dual oxidase complex","organismName":"Homo sapiens; 9606","description":"Calcium-dependent NADPH oxidase which catalyzes cross-membrane electron transfer resulting in the production of hydrogen peroxide (H2O2).  Electrons are transferred from NADPH to FAD, then to a heme molecule on the cytoplasmic side of the membrane to Phe-1097 of DUOX1, and finally to the heme group on the extracellular side of the membrane where they react with oxygen. Required for the H2O2-dependent activity of thyroperoxidase (P07202) which catalyzes the three steps of thyroid hormone biosynthesis. May also have an antimicrobial role at mucosal surfases such as salivary glands in the trachea and play a role in wound response at the airway epithelium.","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-46442099","identifier":"Q1HG43","identifierLink":"https://www.uniprot.org/uniprotkb/Q1HG43/entry","name":"DUOXA1","description":"Dual oxidase maturation factor 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31158","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6677285","identifier":"Q9NRD9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NRD9/entry","name":"DUOX1","description":"Dual oxidase 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11972","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6880399","identifier":"CHEBI:30413","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30413","name":"heme","description":"heme","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-8184","complexName":"B(0,+)AT1-rBAT heteromeric amino acid transporter complex","organismName":"Homo sapiens; 9606","description":"L-type amino acid transporter which catalyses the transmembrane electroneutral reabsoption and exchange of extracellular cationic dibasic amino acids and cystine with intracellular neutral amino acids across the apical membrane of epithelial cells of the renal proximal tubule and small intestine in a sodium-independent manner.","predictedComplex":false,"interactors":[{"ac":"EBI-3936589","identifier":"P82251","identifierLink":"https://www.uniprot.org/uniprotkb/P82251/entry","name":"SLC7A9","description":"b(0,+)-type amino acid transporter 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11785","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46442178","identifier":"Q07837","identifierLink":"https://www.uniprot.org/uniprotkb/Q07837/entry","name":"SLC3A1","description":"Amino acid transporter heavy chain SLC3A1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10357","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8185","complexName":"LAT1-4F2 heteromeric amino acid transporter complex","organismName":"Homo sapiens; 9606","description":"L-type amino acid transporter which catalyses the transmembrane electroneutral antiport  of large neutral amino acids, such as phenylalanine, tyrosine, leucine, histidine, methionine, tryptophan, valine, isoleucine and alanine, and also cysteine in a sodium- and pH-independent manner across the blood-brain barrier and placenta.","predictedComplex":false,"interactors":[{"ac":"EBI-6138761","identifier":"Q01650","identifierLink":"https://www.uniprot.org/uniprotkb/Q01650/entry","name":"SLC7A5","description":"Large neutral amino acids transporter small subunit 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11785","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-702356","identifier":"P08195","identifierLink":"https://www.uniprot.org/uniprotkb/P08195/entry","name":"SLC3A2","description":"Amino acid transporter heavy chain SLC3A2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8186","complexName":"LAT2-4F2 heteromeric amino acid transporter complex","organismName":"Homo sapiens; 9606","description":"L-type amino acid transporter which catalyses the transmembrane electroneutral antiport  of large neutral amino acids, such as phenylalanine, tyrosine, leucine, histidine, methionine, tryptophan, valine, isoleucine and alanine, and also cysteine in a sodium- and pH-independent manner. Also transports  thyroid hormones T3 and T4.","predictedComplex":false,"interactors":[{"ac":"EBI-13292283","identifier":"Q9UHI5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UHI5/entry","name":"SLC7A8","description":"Large neutral amino acids transporter small subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11785","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-702356","identifier":"P08195","identifierLink":"https://www.uniprot.org/uniprotkb/P08195/entry","name":"SLC3A2","description":"Amino acid transporter heavy chain SLC3A2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8762","complexName":"Cav1.1 voltage-gated calcium channel complex, CACNA2D3-CACNB1-CACNG1 variant","organismName":"Homo sapiens; 9606","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.1 channel is responsible for the excitation-contraction coupling that causes contraction of skeletal muscles in response to changes in membrane potential, relaying an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmic membrane. The action potential-induced conformational changes of the complex activates the type 1 ryanodine receptor ( [RyR1: CPX-3135, RyR3: CPX-3162]), which releases Ca2+ from the sarcoplasmic reticulum, triggering muscle contraction.","predictedComplex":false,"interactors":[{"ac":"EBI-50433533","identifier":"Q8IZS8-PRO_0000304647","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IZS8-PRO_0000304647/entry","name":"CACNA2D3","description":"Voltage-dependent calcium channel subunit alpha-2-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-50433550","identifier":"Q8IZS8-PRO_0000304648","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IZS8-PRO_0000304648/entry","name":"CACNA2D3","description":"Voltage-dependent calcium channel subunit delta-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-5329490","identifier":"Q13698","identifierLink":"https://www.uniprot.org/uniprotkb/Q13698/entry","name":"CACNA1S","description":"Voltage-dependent L-type calcium channel subunit alpha-1S","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-947514","identifier":"Q02641","identifierLink":"https://www.uniprot.org/uniprotkb/Q02641/entry","name":"CACNB1","description":"Voltage-dependent L-type calcium channel subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9686780","identifier":"Q06432","identifierLink":"https://www.uniprot.org/uniprotkb/Q06432/entry","name":"CACNG1","description":"Voltage-dependent calcium channel gamma-1 subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15025","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8763","complexName":"Cav1.1 voltage-gated calcium channel complex, CACNA2D3-CACNB2-CACNG1 variant","organismName":"Homo sapiens; 9606","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.1 channel is responsible for the excitation-contraction coupling that causes contraction of skeletal muscles in response to changes in membrane potential, relaying an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmic membrane. The action potential-induced conformational changes of the complex activates the type 1 ryanodine receptor ( [RyR1: CPX-3135, RyR3: CPX-3162]), which releases Ca2+ from the sarcoplasmic reticulum, triggering muscle contraction.","predictedComplex":false,"interactors":[{"ac":"EBI-2874501","identifier":"Q08289","identifierLink":"https://www.uniprot.org/uniprotkb/Q08289/entry","name":"CACNB2","description":"Voltage-dependent L-type calcium channel subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50433533","identifier":"Q8IZS8-PRO_0000304647","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IZS8-PRO_0000304647/entry","name":"CACNA2D3","description":"Voltage-dependent calcium channel subunit alpha-2-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-50433550","identifier":"Q8IZS8-PRO_0000304648","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IZS8-PRO_0000304648/entry","name":"CACNA2D3","description":"Voltage-dependent calcium channel subunit delta-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-5329490","identifier":"Q13698","identifierLink":"https://www.uniprot.org/uniprotkb/Q13698/entry","name":"CACNA1S","description":"Voltage-dependent L-type calcium channel subunit alpha-1S","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9686780","identifier":"Q06432","identifierLink":"https://www.uniprot.org/uniprotkb/Q06432/entry","name":"CACNG1","description":"Voltage-dependent calcium channel gamma-1 subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15025","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8764","complexName":"Cav1.1 voltage-gated calcium channel complex, CACNA2D3-CACNB3-CACNG1 variant","organismName":"Homo sapiens; 9606","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.1 channel is responsible for the excitation-contraction coupling that causes contraction of skeletal muscles in response to changes in membrane potential, relaying an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmic membrane. The action potential-induced conformational changes of the complex activates the type 1 ryanodine receptor ( [RyR1: CPX-3135, RyR3: CPX-3162]), which releases Ca2+ from the sarcoplasmic reticulum, triggering muscle contraction.","predictedComplex":false,"interactors":[{"ac":"EBI-1184651","identifier":"P54284","identifierLink":"https://www.uniprot.org/uniprotkb/P54284/entry","name":"CACNB3","description":"Voltage-dependent L-type calcium channel subunit beta-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50433533","identifier":"Q8IZS8-PRO_0000304647","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IZS8-PRO_0000304647/entry","name":"CACNA2D3","description":"Voltage-dependent calcium channel subunit alpha-2-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-50433550","identifier":"Q8IZS8-PRO_0000304648","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IZS8-PRO_0000304648/entry","name":"CACNA2D3","description":"Voltage-dependent calcium channel subunit delta-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-5329490","identifier":"Q13698","identifierLink":"https://www.uniprot.org/uniprotkb/Q13698/entry","name":"CACNA1S","description":"Voltage-dependent L-type calcium channel subunit alpha-1S","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9686780","identifier":"Q06432","identifierLink":"https://www.uniprot.org/uniprotkb/Q06432/entry","name":"CACNG1","description":"Voltage-dependent calcium channel gamma-1 subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15025","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8766","complexName":"GluA1-GluA2 AMPA receptor complex","organismName":"Rattus norvegicus; 10116","description":"Ligand-gated ion channel implicated in nearly all aspects of development and function of the central nervous system (CNS). Post-synaptic ionotropic transmembrane receptor which increases membrane permeability for sodium, calcium, and potassium. \r\n\r\nMediates the majority of excitatory synaptic transmissions upon binding to the excitatory neurotransmitter L-glutamate released from the presynapse of an adjacent cell. \r\n\r\nActivation of AMPARs induces depolarization of the postsynaptic membrane to mediate rapid synaptic signaling and precise information transfer at synapses. \r\n\r\nAssemble into tetramers in various combinations from four key subunits, GluA1 to GluA4. The GluA1/A2 heterodimer, dominant throughout the forebrain, is selectively recruited during long-term potentiation (LTP) at the key hippocampal synapse, CA3-CA1.\r\n\r\nThe hippocampus is particularly vulnerable to AMPAR-mediated delayed neuronal death (DND) following ischemic stroke.","predictedComplex":false,"interactors":[{"ac":"EBI-371642","identifier":"P19490","identifierLink":"https://www.uniprot.org/uniprotkb/P19490/entry","name":"Gria1","description":"Glutamate receptor 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-77718","identifier":"P19491","identifierLink":"https://www.uniprot.org/uniprotkb/P19491/entry","name":"Gria2","description":"Glutamate receptor 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8767","complexName":"GluA1-GluA2 AMPA receptor complex","organismName":"Homo sapiens; 9606","description":"Ligand-gated ion channel implicated in nearly all aspects of development and function of the central nervous system (CNS). Post-synaptic ionotropic transmembrane receptor which increases membrane permeability for sodium, calcium, and potassium. \r\n\r\nMediates the majority of excitatory synaptic transmissions upon binding to the excitatory neurotransmitter L-glutamate released from the presynapse of an adjacent cell. \r\n\r\nActivation of AMPARs induces depolarization of the postsynaptic membrane to mediate rapid synaptic signaling and precise information transfer at synapses. \r\n\r\nAssemble into tetramers in various combinations from four key subunits, GluA1 to GluA4. The GluA1/A2 heterodimer, dominant throughout the forebrain, is selectively recruited during long-term potentiation (LTP) at the key hippocampal synapse, CA3-CA1.\r\n\r\nThe hippocampus is particularly vulnerable to AMPAR-mediated delayed neuronal death (DND) following ischemic stroke.","predictedComplex":false,"interactors":[{"ac":"EBI-3909876","identifier":"P42262","identifierLink":"https://www.uniprot.org/uniprotkb/P42262/entry","name":"GRIA2","description":"Glutamate receptor 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6980805","identifier":"P42261","identifierLink":"https://www.uniprot.org/uniprotkb/P42261/entry","name":"GRIA1","description":"Glutamate receptor 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8768","complexName":"Cav1.1 voltage-gated calcium channel complex, CACNA2D3-CACNB4-CACNG1 variant","organismName":"Homo sapiens; 9606","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.1 channel is responsible for the excitation-contraction coupling that causes contraction of skeletal muscles in response to changes in membrane potential, relaying an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmic membrane. 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The action potential-induced conformational changes of the complex activates the type 1 ryanodine receptor ( [RyR1: CPX-3135, RyR3: CPX-3162]), which releases Ca2+ from the sarcoplasmic reticulum, triggering muscle contraction.","predictedComplex":false,"interactors":[{"ac":"EBI-1184651","identifier":"P54284","identifierLink":"https://www.uniprot.org/uniprotkb/P54284/entry","name":"CACNB3","description":"Voltage-dependent L-type calcium channel subunit beta-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-49274646","identifier":"Q7Z3S7-PRO_0000304656","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z3S7-PRO_0000304656/entry","name":"CACNA2D4","description":"Voltage-dependent calcium channel subunit alpha-2-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-49275536","identifier":"Q7Z3S7-PRO_0000304657","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z3S7-PRO_0000304657/entry","name":"CACNA2D4","description":"Voltage-dependent calcium channel subunit delta-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-5329490","identifier":"Q13698","identifierLink":"https://www.uniprot.org/uniprotkb/Q13698/entry","name":"CACNA1S","description":"Voltage-dependent L-type calcium channel subunit alpha-1S","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9686780","identifier":"Q06432","identifierLink":"https://www.uniprot.org/uniprotkb/Q06432/entry","name":"CACNG1","description":"Voltage-dependent calcium channel gamma-1 subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15025","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8773","complexName":"Cav1.1 voltage-gated calcium channel complex, CACNA2D4-CACNB4-CACNG1 variant","organismName":"Homo sapiens; 9606","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. 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7227","xrefs":[{"identifier":"PTHR13636","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2109067","identifier":"Q8SY53","identifierLink":"https://www.uniprot.org/uniprotkb/Q8SY53/entry","name":"Ostgamma","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12692","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26767216","identifier":"Q9VLM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VLM5/entry","name":"Dad1","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10705","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48447068","identifier":"Q76NQ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q76NQ0/entry","name":"CG5364","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21049","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48447083","identifier":"A1Z7U3","identifierLink":"https://www.uniprot.org/uniprotkb/A1Z7U3/entry","name":"ost4","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-48447094","identifier":"Q9VQP9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VQP9/entry","name":"ostc","description":"Putative oligosaccharyltransferase complex subunit CG9662","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13160","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48447106","identifier":"Q7K110","identifierLink":"https://www.uniprot.org/uniprotkb/Q7K110/entry","name":"OstDelta","description":"Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12640","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8804","complexName":"FOXP1-FOXP4 transcription factor complex","organismName":"Homo sapiens; 9606","description":"Transcriptional regulator with a role in the development of the central nervous system, regulating transcription of  genes involved in early neuronal development mainly through transcriptional repression.","predictedComplex":false,"interactors":[{"ac":"EBI-1054619","identifier":"Q8IVH2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IVH2/entry","name":"FOXP4","description":"Forkhead box protein P4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45796","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-983809","identifier":"Q9H334","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H334/entry","name":"FOXP1","description":"Forkhead box protein P1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45796","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8805","complexName":"FOXP2-FOXP4 transcription factor complex","organismName":"Homo sapiens; 9606","description":"Transcriptional regulator with a role in the development of the central nervous system, regulating transcription of  genes involved in early neuronal development mainly through transcriptional repression.","predictedComplex":false,"interactors":[{"ac":"EBI-1054619","identifier":"Q8IVH2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IVH2/entry","name":"FOXP4","description":"Forkhead box protein P4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45796","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-983612","identifier":"O15409","identifierLink":"https://www.uniprot.org/uniprotkb/O15409/entry","name":"FOXP2","description":"Forkhead box protein P2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45796","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8806","complexName":"20S proteasome complex","organismName":"Homo sapiens; 9606","description":"Primordial protein-degrading machine essential for maintaining cellular homeostasis, possibly aided by loosely associated ATPase activators. An integral part of the 26S proteasome, but also exists as a free complex in many cell types. Once considered as either a proteasome assembly intermediate, 26S breakdown product from disassembly or stand-alone proteolytic enzyme complex, there is evidence for the independent direct action of the 20S proteasome on disordered, oxidized and damaged proteins.\r\n\r\nPlays an important role in adaptation to oxidative stress and the adaptive immune response. Mediates ubiquitin-independent protein degradation through association with PA200 and PA28. Required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex).\r\n\r\nCirculating 20S proteasomes present in human plasma are known to increase significantly under various pathological conditions including acute respiratory disease, autoimmune disorders and cancerous tumours. The correlation with disease progression suggests a potential role as a biomarker for disease state and treatment efficacy.\r\n\r\nDysregulated proteasome function has been implicated, as a primary cause or a secondary consequence, in the pathogenesis of a broad array of neurodegenerative diseases, including Alzheimer’s, Parkinson’s, and Huntington’s diseases.","predictedComplex":false,"interactors":[{"ac":"EBI-348380","identifier":"P25788","identifierLink":"https://www.uniprot.org/uniprotkb/P25788/entry","name":"PSMA3","description":"Proteasome subunit alpha type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355475","identifier":"P28066","identifierLink":"https://www.uniprot.org/uniprotkb/P28066/entry","name":"PSMA5","description":"Proteasome subunit alpha type-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357793","identifier":"P60900","identifierLink":"https://www.uniprot.org/uniprotkb/P60900/entry","name":"PSMA6","description":"Proteasome subunit alpha type-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357828","identifier":"P28074","identifierLink":"https://www.uniprot.org/uniprotkb/P28074/entry","name":"PSMB5","description":"Proteasome subunit beta type-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359288","identifier":"P28072","identifierLink":"https://www.uniprot.org/uniprotkb/P28072/entry","name":"PSMB6","description":"Proteasome subunit beta type-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359310","identifier":"P25789","identifierLink":"https://www.uniprot.org/uniprotkb/P25789/entry","name":"PSMA4","description":"Proteasome subunit alpha type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359335","identifier":"P49721","identifierLink":"https://www.uniprot.org/uniprotkb/P49721/entry","name":"PSMB2","description":"Proteasome subunit beta type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359352","identifier":"P25786","identifierLink":"https://www.uniprot.org/uniprotkb/P25786/entry","name":"PSMA1","description":"Proteasome subunit alpha type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372273","identifier":"P20618","identifierLink":"https://www.uniprot.org/uniprotkb/P20618/entry","name":"PSMB1","description":"Proteasome subunit beta type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32194","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603262","identifier":"P25787","identifierLink":"https://www.uniprot.org/uniprotkb/P25787/entry","name":"PSMA2","description":"Proteasome subunit alpha type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603272","identifier":"O14818","identifierLink":"https://www.uniprot.org/uniprotkb/O14818/entry","name":"PSMA7","description":"Proteasome subunit alpha type-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603319","identifier":"Q99436","identifierLink":"https://www.uniprot.org/uniprotkb/Q99436/entry","name":"PSMB7","description":"Proteasome subunit beta type-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603340","identifier":"P49720","identifierLink":"https://www.uniprot.org/uniprotkb/P49720/entry","name":"PSMB3","description":"Proteasome subunit beta type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603350","identifier":"P28070","identifierLink":"https://www.uniprot.org/uniprotkb/P28070/entry","name":"PSMB4","description":"Proteasome subunit beta type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8807","complexName":"FOXP4 transcription factor homodimer","organismName":"Homo sapiens; 9606","description":"Transcriptional regulator with a role in the development of the central nervous system, regulating transcription of  genes involved in early neuronal development mainly through transcriptional repression.","predictedComplex":false,"interactors":[{"ac":"EBI-1054619","identifier":"Q8IVH2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IVH2/entry","name":"FOXP4","description":"Forkhead box protein P4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45796","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8808","complexName":"Peroxisomal receptor export module complex","organismName":"Homo sapiens; 9606","description":"Processive protein translocase that mediates the ATP-dependent relocation and recycling of the peroxisomal targeting signal import receptor PEX5 (P50542) from the peroxisomal membrane to the cytosol, where it is then available for another round of protein import. The PEX1-PEX6 heterohexamer acts as an AAA-ATPase that threads monoubiquitinated PEX5 through its central pore.","predictedComplex":false,"interactors":[{"ac":"EBI-752057","identifier":"Q7Z412","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z412/entry","name":"PEX26","description":"Peroxisome assembly protein 26","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16262","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-988581","identifier":"Q13608","identifierLink":"https://www.uniprot.org/uniprotkb/Q13608/entry","name":"PEX6","description":"Peroxisomal ATPase PEX6","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-988601","identifier":"O43933","identifierLink":"https://www.uniprot.org/uniprotkb/O43933/entry","name":"PEX1","description":"Peroxisomal ATPase PEX1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8822","complexName":"Interleukin-27 complex","organismName":"Homo sapiens; 9606","description":"A member of the IL12/IL6 family of cytokines, IL27 is a heterodimer comprised of a p28 four-alpha helical cytokine subunit non-covalently linked to a compact soluble receptor subunit, which serve as the alpha- and beta-subunits of the cytokine, respectively. Binds to a heterodimeric receptor to form the Interleukin27 ligand-receptor complex (CPX-8836) to activate either the JAK/STAT or the p38 MAPK/ERK signaling cascade.\r\n\r\nA pleiotropic cytokine with both anti- and pro-inflammatory activity, it is capable of exerting both innate and adaptive immune responses. Functions to restrain T cell-mediated inflammation and plays an important role in immune homeostasis through its ability to: modify CD4+ and CD8+ T cell effector functions, promote T regulatory (Treg) responses, mobilize a suppressive transcriptional network through activation of SOCS (suppressors of cytokine signalling), downregulate proinflammatory cytokines IFNG (P01579), TNF (P01375) and IL17, and induce the production of anti-inflammatory cytokine IL10 by T cells. Interestingly, IL27 suppresses IL10 production by human monocytes.\r\n\r\nIL27A is secreted bound to IL27B mainly by antigen presenting cells (APCs) such as monocytes, macrophages and dendritic cells (DCs). Varying levels of IL-27 is also secreted by other cells such as myeloid-derived supressor cells, CD4+, CD8+ T cells, osteoclasts and activated B cells. Specific signaling stimulation, including Toll-like receptor (TLR9) and lipopolysaccharides (LPS) also regulates IL-27 expression.\r\n\r\nIL27 possesses both pro-tumourigenic and anti-tumourigenic functions. IL27 induction of IL10 in T cells, leads to IL-10 inhibiting antitumor immunity. It is considered therapeutically important due to its ability to induce inhibitory receptors.","predictedComplex":false,"interactors":[{"ac":"EBI-15887997","identifier":"Q8NEV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NEV9/entry","name":"IL27","description":"Interleukin-27 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20879","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742959","identifier":"Q14213","identifierLink":"https://www.uniprot.org/uniprotkb/Q14213/entry","name":"EBI3","description":"Interleukin-27 subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48483","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8823","complexName":"SNX1-SNX5 sorting nexin complex","organismName":"Homo sapiens; 9606","description":"Coat complex which is essential for shaping and maintaining endosomal membranes and regulating intracellular trafficking of cargo proteins by  self-assembling into helical arrays on the membrane to stabilize and expand the local membrane curvature underlying endosomal tubule formation. Interacts with the Retromer complex (CPX-7842/CPX-7843), promoting tubulation from phosphatidylinositol 3-phosphate (PI3P)-positive endosomes which facilitates the specific transport of retromer-associated cargoes.","predictedComplex":false,"interactors":[{"ac":"EBI-2822329","identifier":"Q13596","identifierLink":"https://www.uniprot.org/uniprotkb/Q13596/entry","name":"SNX1","description":"Sorting nexin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10555","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-715760","identifier":"Q9Y5X3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5X3/entry","name":"SNX5","description":"Sorting nexin-5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8826","complexName":"Soluble tumor necrosis factor complex","organismName":"Homo sapiens; 9606","description":"Potent pro-inflammatory cytokine capable of exerting pleiotropic effects on a variety of cell types. Belongs to the tumour necrosis factor (TNF) superfamily of type II transmembrane proteins. \r\n\r\nMainly secreted by macrophages, T helper 1 and natural killer cells, TNF is expressed on activated macrophages and lymphocytes. Generated as a precursor form known as transmembrane TNF (mTNF, CPX-8931), TACE (ADAM17) cleavage of mTNF results in the release of a soluble form (sTNF, this complex) with the residual cytoplasmic domain of mTNF migrating back into the nucleus of mTNF producing cells. sTNF exerts its functions through either type-1 (TNR1A, P19438) or type-2 (TNR1B, P20333)  TNF receptors and while mTNF can act through either receptor type, its activities are mainly mediated through TNR1B, its primary biological target.\r\n\r\nBoth the soluble and the transmembrane forms play a role in inflammatory responses and whilst mTNF exerts its biological function through cell-to-cell contact to moderate inflammation, sTNF, acts at sites remote from the TNF-producing cells to drive inflammation.\r\n\r\nBoth protective and pathogenic, it induces cell death in response to microbial infection but behaves aberrantly when induced as a result of environmental or genetic factors, thereby driving the pathogenesis of inflammatory disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-2905409","identifier":"P01375-PRO_0000034424","identifierLink":"https://www.uniprot.org/uniprotkb/P01375-PRO_0000034424/entry","name":"TNF","description":"Tumor necrosis factor, soluble form","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-8830","complexName":"Interleukin-1 alpha-soluble receptor type 1 complex","organismName":"Homo sapiens; 9606","description":"Complex formed on the binding of a pre-bound mature form of interleukin-1 alpha (IL1A) and a soluble form of its receptor, interleukin-1R1 (sIL1R1) to its coreceptor, interleukin-1 receptor accessory protein (IL1RAP). Recruitment of IL1RAP completes complex assembly and initiates activation of the NFKB signalling pathway.\r\n\r\nA member of the IL1 family of cytokines, IL1A is closely related to interleukin-1 beta (IL1B, P01584) carrying out similar biological functions by binding to their shared receptor complex. Although both IL1A and IL1B function via the same IL1R1 to drive an inflammatory response, IL1A acts as an alarmin which regulates local inflammation while IL1B acts as a master regulator of systemic inflammation.\r\n\r\nIL1A is synthesized as a precursor protein and is processed by calpain II (P17655) to produce a more active, mature form. IL1A activity is regulated by two forms of the IL1R1: a membrane-bound form (mIL1R1) and a soluble form (sIL1R1, this complex) created through proteolytic release of the ectodomain (ECD) of mIL1R1 via matrix metalloproteases. Both forms of IL1R1 are biologically active and the ECD in both forms is vital for ligand recognition and binding.","predictedComplex":false,"interactors":[{"ac":"EBI-52378192","identifier":"P14778-PRO_0000415344","identifierLink":"https://www.uniprot.org/uniprotkb/P14778-PRO_0000415344/entry","name":"IL1R1","description":"Interleukin-1 receptor type 1, soluble form","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-52386506","identifier":"P01583-PRO_0000015266","identifierLink":"https://www.uniprot.org/uniprotkb/P01583-PRO_0000015266/entry","name":"IL1A","description":"Interleukin-1 alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-525939","identifier":"Q9NPH3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPH3/entry","name":"IL1RAP","description":"Interleukin-1 receptor accessory protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8835","complexName":"SNX1-SNX6 sorting nexin complex","organismName":"Homo sapiens; 9606","description":"Coat complex which is essential for shaping and maintaining endosomal membranes and regulating intracellular trafficking of cargo proteins by  self-assembling into helical arrays on the membrane to stabilize and expand the local membrane curvature underlying endosomal tubule formation. Interacts with the Retromer complex (CPX-7842/CPX-7843), promoting tubulation from phosphatidylinositol 3-phosphate (PI3P)-positive endosomes which facilitates the specific transport of retromer-associated cargoes.","predictedComplex":false,"interactors":[{"ac":"EBI-2822329","identifier":"Q13596","identifierLink":"https://www.uniprot.org/uniprotkb/Q13596/entry","name":"SNX1","description":"Sorting nexin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10555","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-949294","identifier":"Q9UNH7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UNH7/entry","name":"SNX6","description":"Sorting nexin-6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8837","complexName":"SNX1-SNX32 sorting nexin complex","organismName":"Homo sapiens; 9606","description":"Coat complex which is essential for shaping and maintaining endosomal membranes and regulating intracellular trafficking of cargo proteins by  self-assembling into helical arrays on the membrane to stabilize and expand the local membrane curvature underlying endosomal tubule formation. Interacts with the Retromer complex (CPX-7842/CPX-7843), promoting tubulation from phosphatidylinositol 3-phosphate (PI3P)-positive endosomes which facilitates the specific transport of retromer-associated cargoes. SNX32 may contribute to maintaining neuroglial coordination via its role in Basigin (P35613) trafficking and the associated monocarboxylate transporter activity.","predictedComplex":false,"interactors":[{"ac":"EBI-2822329","identifier":"Q13596","identifierLink":"https://www.uniprot.org/uniprotkb/Q13596/entry","name":"SNX1","description":"Sorting nexin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10555","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8099743","identifier":"Q86XE0","identifierLink":"https://www.uniprot.org/uniprotkb/Q86XE0/entry","name":"SNX32","description":"Sorting nexin-32","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8838","complexName":"SNX2-SNX5 sorting nexin complex","organismName":"Homo sapiens; 9606","description":"Coat complex which is essential for shaping and maintaining endosomal membranes and regulating intracellular trafficking of cargo proteins by  self-assembling into helical arrays on the membrane to stabilize and expand the local membrane curvature underlying endosomal tubule formation. Interacts with the Retromer complex (CPX-7842/CPX-7843), promoting tubulation from phosphatidylinositol 3-phosphate (PI3P)-positive endosomes which facilitates the specific transport of retromer-associated cargoes.","predictedComplex":false,"interactors":[{"ac":"EBI-1046690","identifier":"O60749","identifierLink":"https://www.uniprot.org/uniprotkb/O60749/entry","name":"SNX2","description":"Sorting nexin-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10555","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-715760","identifier":"Q9Y5X3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5X3/entry","name":"SNX5","description":"Sorting nexin-5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8839","complexName":"SNX2-SNX6 sorting nexin complex","organismName":"Homo sapiens; 9606","description":"Coat complex which is essential for shaping and maintaining endosomal membranes and regulating intracellular trafficking of cargo proteins by  self-assembling into helical arrays on the membrane to stabilize and expand the local membrane curvature underlying endosomal tubule formation. Interacts with the Retromer complex (CPX-7842/CPX-7843), promoting tubulation from phosphatidylinositol 3-phosphate (PI3P)-positive endosomes which facilitates the specific transport of retromer-associated cargoes.","predictedComplex":false,"interactors":[{"ac":"EBI-1046690","identifier":"O60749","identifierLink":"https://www.uniprot.org/uniprotkb/O60749/entry","name":"SNX2","description":"Sorting nexin-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10555","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-949294","identifier":"Q9UNH7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UNH7/entry","name":"SNX6","description":"Sorting nexin-6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8840","complexName":"SNX2-SNX32 sorting nexin complex","organismName":"Homo sapiens; 9606","description":"Coat complex which is essential for shaping and maintaining endosomal membranes and regulating intracellular trafficking of cargo proteins by  self-assembling into helical arrays on the membrane to stabilize and expand the local membrane curvature underlying endosomal tubule formation. Interacts with the Retromer complex (CPX-7842/CPX-7843), promoting tubulation from phosphatidylinositol 3-phosphate (PI3P)-positive endosomes.which facilitates the specific transport of retromer-associated cargoes. SNX32 may contribute to maintaining neuroglial coordination via its role in Basigin (P35613) trafficking and the associated monocarboxylate transporter activity.","predictedComplex":false,"interactors":[{"ac":"EBI-1046690","identifier":"O60749","identifierLink":"https://www.uniprot.org/uniprotkb/O60749/entry","name":"SNX2","description":"Sorting nexin-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10555","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8099743","identifier":"Q86XE0","identifierLink":"https://www.uniprot.org/uniprotkb/Q86XE0/entry","name":"SNX32","description":"Sorting nexin-32","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8841","complexName":"PA200-20S single-capped proteasome","organismName":"Homo sapiens; 9606","description":"Complex formed upon a 200 kDa proteasome activator (PA200) binding either symmetrically or asymmetrically to the alpha-rings of the multicatalytic constitutive cylindrical 20S core complex (CPX-8806), composed of four heteroheptameric rings, of which the outer two are composed of alpha subunits (1-7) and the inner two of beta subunits (1-7). PA200 binds in an ubiquitin- and ATP-independent manner to either one (single-cap, this complex) or both ends (double-capped, CPX-9063) of the 20S Proteasome, but the efficiency of substrate processing by single and double-capped proteasomes in not known.\r\n\r\nA nuclear-localized proteasomal regulator, PA200 enhances the 20S proteasome's ability to degrade short peptides, disordered proteins, and PA200-bound inositol phosphates act on acetylated core (AC) histones during DNA repair and replication stress in an ubiquitin-independent manner. Also implicated in mitochondrial fission, turnover of ribosome-related transcription factor Sfp1 and maintaining intracellular glutamine levels. Thought not essential for DNA repair, the PA200 component is more sensitive to DNA damage and PA200-hybrid proteasomes are known to form in response to ionizing radiation. \r\n\r\nExternal stimuli and diseases can change a proteasome's composition, thereby affecting the proteasome's substrate specificity and consequently protein homeostasis within a cell. Decreased proteasome activity is linked to neurodegerative disorders and cardiac dysfunction through the accumulation of proteins while, enhanced proteasome activity and induced-expression of certain proteasome components are implicated in muscle wasting conditions and several cancers.","predictedComplex":false,"interactors":[{"ac":"EBI-1236916","identifier":"Q14997","identifierLink":"https://www.uniprot.org/uniprotkb/Q14997/entry","name":"PSME4","description":"Proteasome activator complex subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32170","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348380","identifier":"P25788","identifierLink":"https://www.uniprot.org/uniprotkb/P25788/entry","name":"PSMA3","description":"Proteasome subunit alpha type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355475","identifier":"P28066","identifierLink":"https://www.uniprot.org/uniprotkb/P28066/entry","name":"PSMA5","description":"Proteasome subunit alpha type-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357793","identifier":"P60900","identifierLink":"https://www.uniprot.org/uniprotkb/P60900/entry","name":"PSMA6","description":"Proteasome subunit alpha type-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357828","identifier":"P28074","identifierLink":"https://www.uniprot.org/uniprotkb/P28074/entry","name":"PSMB5","description":"Proteasome subunit beta type-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359288","identifier":"P28072","identifierLink":"https://www.uniprot.org/uniprotkb/P28072/entry","name":"PSMB6","description":"Proteasome subunit beta type-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359310","identifier":"P25789","identifierLink":"https://www.uniprot.org/uniprotkb/P25789/entry","name":"PSMA4","description":"Proteasome subunit alpha type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359335","identifier":"P49721","identifierLink":"https://www.uniprot.org/uniprotkb/P49721/entry","name":"PSMB2","description":"Proteasome subunit beta type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359352","identifier":"P25786","identifierLink":"https://www.uniprot.org/uniprotkb/P25786/entry","name":"PSMA1","description":"Proteasome subunit alpha type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372273","identifier":"P20618","identifierLink":"https://www.uniprot.org/uniprotkb/P20618/entry","name":"PSMB1","description":"Proteasome subunit beta type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32194","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603262","identifier":"P25787","identifierLink":"https://www.uniprot.org/uniprotkb/P25787/entry","name":"PSMA2","description":"Proteasome subunit alpha type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603272","identifier":"O14818","identifierLink":"https://www.uniprot.org/uniprotkb/O14818/entry","name":"PSMA7","description":"Proteasome subunit alpha type-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603319","identifier":"Q99436","identifierLink":"https://www.uniprot.org/uniprotkb/Q99436/entry","name":"PSMB7","description":"Proteasome subunit beta type-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603340","identifier":"P49720","identifierLink":"https://www.uniprot.org/uniprotkb/P49720/entry","name":"PSMB3","description":"Proteasome subunit beta type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603350","identifier":"P28070","identifierLink":"https://www.uniprot.org/uniprotkb/P28070/entry","name":"PSMB4","description":"Proteasome subunit beta type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8842","complexName":"PA28-alphabeta double-capped 20S proteasome complex","organismName":"Homo sapiens; 9606","description":"Multi-enzyme complex that functions as the primary degradation machinery for the selective turnover of surplus or damaged proteins within the cell. The core contains the protease active sites (chymotrypsin-like, trypsin-like and peptidylglutamyl-peptide hydrolyzing) that perform the proteolysis reactions in an internal chamber. Regulatory particles referred to as 'caps' act as a discriminating gateway for potential substrates.\r\n\r\nThis complex is formed upon the endogenous proteasomal activator, PA28, a 28 kDa protein binding to the 20S proteasome (CPX-8806). PA28 exists as three highly homologous isoforms, alpha, beta and gamma (Q06323, Q9UL46 and P61289 respectively). The three subunits differ significantly in their biochemical and biological properties. PA28-alpha and PA28-beta favour the release of peptide products by the proteasome and are specifically involved in optimizing MHC class 1 antigen presentation. PA28-alpha and PA28-beta bind in an ATP-independent manner to either one (single-cap, CPX-9002) or both ends (double-capped, this complex) of the of the 20S proteasome, but the efficiency of substrate processing by single and double-capped proteasomes in not known. Binding of the activator modifies the 20S peptidase and opens its outer alpha-ring gates allowing substrate entry to the antechamber through an internal activation loop. \r\n\r\nRegulates protein degradation either in a regulated manner upon specific molecular cues or acts on damaged and disordered proteins. Plays a key role under oxidative stress conditions to degrade damaged and unfolded proteins and is up-regulated by interferon-gamma during antigen presentation.\r\n\r\nTumorigenesis of PA28-alpha is unclear but up-regulation of the subunit is associated with several cancers, including ovarian, prostate and oral squamous cell carcinoma (OSCC), and interestingly, silencing it suppressed OSCC cell growth and metastasis.","predictedComplex":false,"interactors":[{"ac":"EBI-348380","identifier":"P25788","identifierLink":"https://www.uniprot.org/uniprotkb/P25788/entry","name":"PSMA3","description":"Proteasome subunit alpha type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355475","identifier":"P28066","identifierLink":"https://www.uniprot.org/uniprotkb/P28066/entry","name":"PSMA5","description":"Proteasome subunit alpha type-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357793","identifier":"P60900","identifierLink":"https://www.uniprot.org/uniprotkb/P60900/entry","name":"PSMA6","description":"Proteasome subunit alpha type-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357828","identifier":"P28074","identifierLink":"https://www.uniprot.org/uniprotkb/P28074/entry","name":"PSMB5","description":"Proteasome subunit beta type-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359288","identifier":"P28072","identifierLink":"https://www.uniprot.org/uniprotkb/P28072/entry","name":"PSMB6","description":"Proteasome subunit beta type-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359310","identifier":"P25789","identifierLink":"https://www.uniprot.org/uniprotkb/P25789/entry","name":"PSMA4","description":"Proteasome subunit alpha type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359335","identifier":"P49721","identifierLink":"https://www.uniprot.org/uniprotkb/P49721/entry","name":"PSMB2","description":"Proteasome subunit beta type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359352","identifier":"P25786","identifierLink":"https://www.uniprot.org/uniprotkb/P25786/entry","name":"PSMA1","description":"Proteasome subunit alpha type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372273","identifier":"P20618","identifierLink":"https://www.uniprot.org/uniprotkb/P20618/entry","name":"PSMB1","description":"Proteasome subunit beta type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32194","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603262","identifier":"P25787","identifierLink":"https://www.uniprot.org/uniprotkb/P25787/entry","name":"PSMA2","description":"Proteasome subunit alpha type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603272","identifier":"O14818","identifierLink":"https://www.uniprot.org/uniprotkb/O14818/entry","name":"PSMA7","description":"Proteasome subunit alpha type-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603319","identifier":"Q99436","identifierLink":"https://www.uniprot.org/uniprotkb/Q99436/entry","name":"PSMB7","description":"Proteasome subunit beta type-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603340","identifier":"P49720","identifierLink":"https://www.uniprot.org/uniprotkb/P49720/entry","name":"PSMB3","description":"Proteasome subunit beta type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603350","identifier":"P28070","identifierLink":"https://www.uniprot.org/uniprotkb/P28070/entry","name":"PSMB4","description":"Proteasome subunit beta type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712149","identifier":"Q06323","identifierLink":"https://www.uniprot.org/uniprotkb/Q06323/entry","name":"PSME1","description":"Proteasome activator complex subunit 1","stochiometry":"minValue: 6, maxValue: 8","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10660","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-741630","identifier":"Q9UL46","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UL46/entry","name":"PSME2","description":"Proteasome activator complex subunit 2","stochiometry":"minValue: 6, maxValue: 8","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10660","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8861","complexName":"Cav1.2 voltage-gated calcium channel complex, CACNA2D1-CACNB3 variant","organismName":"Homo sapiens; 9606","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.2 channel is responsible for excitation-contraction (E-C) coupling of cardiac and, to some extent, smooth muscle. It relays an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmatic membrane. More specifically, rapid depolarization-induced conformational changes of the complex stimulates calcium efflux from the sarcoplasmatic reticulum through the Ryanodine 2 complex  (CPX-3156) calcium release channel, which subsequently triggers the contractile apparatus until the calcium concentration is reduced again due to re-uptake into the sarcoplasmic reticulum by the Ca2+-ATPase, ATP2A1 (O14983).","predictedComplex":false,"interactors":[{"ac":"EBI-1038838","identifier":"Q13936","identifierLink":"https://www.uniprot.org/uniprotkb/Q13936/entry","name":"CACNA1C","description":"Voltage-dependent L-type calcium channel subunit alpha-1C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1184651","identifier":"P54284","identifierLink":"https://www.uniprot.org/uniprotkb/P54284/entry","name":"CACNB3","description":"Voltage-dependent L-type calcium channel subunit beta-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9686800","identifier":"P54289-PRO_0000005001","identifierLink":"https://www.uniprot.org/uniprotkb/P54289-PRO_0000005001/entry","name":"CACNA2D1","description":"Voltage-dependent calcium channel subunit alpha-2-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-9686811","identifier":"P54289-PRO_0000005002","identifierLink":"https://www.uniprot.org/uniprotkb/P54289-PRO_0000005002/entry","name":"CACNA2D1","description":"Voltage-dependent calcium channel subunit delta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-8862","complexName":"Cav1.2 voltage-gated calcium channel complex, CACNA2D1-CACNB1 variant","organismName":"Homo sapiens; 9606","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.2 channel is responsible for excitation-contraction (E-C) coupling of cardiac and, to some extent, smooth muscle. It relays an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmatic membrane. More specifically, rapid depolarization-induced conformational changes of the complex stimulates calcium efflux from the sarcoplasmatic reticulum through the Ryanodine 2 complex  (CPX-3156) calcium release channel, which subsequently triggers the contractile apparatus until the calcium concentration is reduced again due to re-uptake into the sarcoplasmic reticulum by the Ca2+-ATPase, ATP2A1 (O14983).","predictedComplex":false,"interactors":[{"ac":"EBI-1038838","identifier":"Q13936","identifierLink":"https://www.uniprot.org/uniprotkb/Q13936/entry","name":"CACNA1C","description":"Voltage-dependent L-type calcium channel subunit alpha-1C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-947514","identifier":"Q02641","identifierLink":"https://www.uniprot.org/uniprotkb/Q02641/entry","name":"CACNB1","description":"Voltage-dependent L-type calcium channel subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9686800","identifier":"P54289-PRO_0000005001","identifierLink":"https://www.uniprot.org/uniprotkb/P54289-PRO_0000005001/entry","name":"CACNA2D1","description":"Voltage-dependent calcium channel subunit alpha-2-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-9686811","identifier":"P54289-PRO_0000005002","identifierLink":"https://www.uniprot.org/uniprotkb/P54289-PRO_0000005002/entry","name":"CACNA2D1","description":"Voltage-dependent calcium channel subunit delta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-8863","complexName":"Cav1.2 voltage-gated calcium channel complex, CACNA2D1-CACNB4 variant","organismName":"Homo sapiens; 9606","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.2 channel is responsible for excitation-contraction (E-C) coupling of cardiac and, to some extent, smooth muscle. It relays an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmatic membrane. More specifically, rapid depolarization-induced conformational changes of the complex stimulates calcium efflux from the sarcoplasmatic reticulum through the Ryanodine 2 complex  (CPX-3156) calcium release channel, which subsequently triggers the contractile apparatus until the calcium concentration is reduced again due to re-uptake into the sarcoplasmic reticulum by the Ca2+-ATPase, ATP2A1 (O14983).","predictedComplex":false,"interactors":[{"ac":"EBI-1038838","identifier":"Q13936","identifierLink":"https://www.uniprot.org/uniprotkb/Q13936/entry","name":"CACNA1C","description":"Voltage-dependent L-type calcium channel subunit alpha-1C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-714838","identifier":"O00305","identifierLink":"https://www.uniprot.org/uniprotkb/O00305/entry","name":"CACNB4","description":"Voltage-dependent L-type calcium channel subunit beta-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9686800","identifier":"P54289-PRO_0000005001","identifierLink":"https://www.uniprot.org/uniprotkb/P54289-PRO_0000005001/entry","name":"CACNA2D1","description":"Voltage-dependent calcium channel subunit alpha-2-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-9686811","identifier":"P54289-PRO_0000005002","identifierLink":"https://www.uniprot.org/uniprotkb/P54289-PRO_0000005002/entry","name":"CACNA2D1","description":"Voltage-dependent calcium channel subunit delta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-8864","complexName":"Cav1.2 voltage-gated calcium channel complex, CACNA2D2-CACNB2 variant","organismName":"Homo sapiens; 9606","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.2 channel is responsible for excitation-contraction (E-C) coupling of cardiac and, to some extent, smooth muscle. It relays an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmatic membrane. More specifically, rapid depolarization-induced conformational changes of  the complex stimulates calcium efflux from the sarcoplasmatic reticulum through the Ryanodine 2 complex  (CPX-3156) calcium release channel, which subsequently triggers the contractile apparatus until the calcium concentration is reduced again due to re-uptake into the sarcoplasmic reticulum by the Ca2+-ATPase, ATP2A1 (O14983).","predictedComplex":false,"interactors":[{"ac":"EBI-1038838","identifier":"Q13936","identifierLink":"https://www.uniprot.org/uniprotkb/Q13936/entry","name":"CACNA1C","description":"Voltage-dependent L-type calcium channel subunit alpha-1C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2874501","identifier":"Q08289","identifierLink":"https://www.uniprot.org/uniprotkb/Q08289/entry","name":"CACNB2","description":"Voltage-dependent L-type calcium channel subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48446589","identifier":"Q9NY47-PRO_0000304637","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NY47-PRO_0000304637/entry","name":"CACNA2D2","description":"Voltage-dependent calcium channel subunit alpha-2/delta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-48446668","identifier":"Q9NY47-PRO_0000304639","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NY47-PRO_0000304639/entry","name":"CACNA2D2","description":"Voltage-dependent calcium channel subunit delta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-8865","complexName":"Cav1.2 voltage-gated calcium channel complex, CACNA2D2-CACNB1 variant","organismName":"Homo sapiens; 9606","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.2 channel is responsible for excitation-contraction (E-C) coupling of cardiac and, to some extent, smooth muscle. It relays an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmatic membrane. More specifically, rapid depolarization-induced conformational changes of  the complex stimulates calcium efflux from the sarcoplasmatic reticulum through the Ryanodine 2 complex  (CPX-3156) calcium release channel, which subsequently triggers the contractile apparatus until the calcium concentration is reduced again due to re-uptake into the sarcoplasmic reticulum by the Ca2+-ATPase, ATP2A1 (O14983).","predictedComplex":false,"interactors":[{"ac":"EBI-1038838","identifier":"Q13936","identifierLink":"https://www.uniprot.org/uniprotkb/Q13936/entry","name":"CACNA1C","description":"Voltage-dependent L-type calcium channel subunit alpha-1C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48446589","identifier":"Q9NY47-PRO_0000304637","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NY47-PRO_0000304637/entry","name":"CACNA2D2","description":"Voltage-dependent calcium channel subunit alpha-2/delta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-48446668","identifier":"Q9NY47-PRO_0000304639","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NY47-PRO_0000304639/entry","name":"CACNA2D2","description":"Voltage-dependent calcium channel subunit delta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-947514","identifier":"Q02641","identifierLink":"https://www.uniprot.org/uniprotkb/Q02641/entry","name":"CACNB1","description":"Voltage-dependent L-type calcium channel subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8866","complexName":"Cav1.2 voltage-gated calcium channel complex, CACNA2D2-CACNB3 variant","organismName":"Homo sapiens; 9606","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.2 channel is responsible for excitation-contraction (E-C) coupling of cardiac and, to some extent, smooth muscle. It relays an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmatic membrane. More specifically, rapid depolarization-induced conformational changes of  the complex stimulates calcium efflux from the sarcoplasmatic reticulum through the Ryanodine 2 complex  (CPX-3156) calcium release channel, which subsequently triggers the contractile apparatus until the calcium concentration is reduced again due to re-uptake into the sarcoplasmic reticulum by the Ca2+-ATPase, ATP2A1 (O14983).","predictedComplex":false,"interactors":[{"ac":"EBI-1038838","identifier":"Q13936","identifierLink":"https://www.uniprot.org/uniprotkb/Q13936/entry","name":"CACNA1C","description":"Voltage-dependent L-type calcium channel subunit alpha-1C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1184651","identifier":"P54284","identifierLink":"https://www.uniprot.org/uniprotkb/P54284/entry","name":"CACNB3","description":"Voltage-dependent L-type calcium channel subunit beta-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48446589","identifier":"Q9NY47-PRO_0000304637","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NY47-PRO_0000304637/entry","name":"CACNA2D2","description":"Voltage-dependent calcium channel subunit alpha-2/delta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-48446668","identifier":"Q9NY47-PRO_0000304639","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NY47-PRO_0000304639/entry","name":"CACNA2D2","description":"Voltage-dependent calcium channel subunit delta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-8867","complexName":"Cav1.2 voltage-gated calcium channel complex, CACNA2D2-CACNB4 variant","organismName":"Homo sapiens; 9606","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.2 channel is responsible for excitation-contraction (E-C) coupling of cardiac and, to some extent, smooth muscle. It relays an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmatic membrane. More specifically, rapid depolarization-induced conformational changes of  the complex stimulates calcium efflux from the sarcoplasmatic reticulum through the Ryanodine 2 complex  (CPX-3156) calcium release channel, which subsequently triggers the contractile apparatus until the calcium concentration is reduced again due to re-uptake into the sarcoplasmic reticulum by the Ca2+-ATPase, ATP2A1 (O14983).","predictedComplex":false,"interactors":[{"ac":"EBI-1038838","identifier":"Q13936","identifierLink":"https://www.uniprot.org/uniprotkb/Q13936/entry","name":"CACNA1C","description":"Voltage-dependent L-type calcium channel subunit alpha-1C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48446589","identifier":"Q9NY47-PRO_0000304637","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NY47-PRO_0000304637/entry","name":"CACNA2D2","description":"Voltage-dependent calcium channel subunit alpha-2/delta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-48446668","identifier":"Q9NY47-PRO_0000304639","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NY47-PRO_0000304639/entry","name":"CACNA2D2","description":"Voltage-dependent calcium channel subunit delta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-714838","identifier":"O00305","identifierLink":"https://www.uniprot.org/uniprotkb/O00305/entry","name":"CACNB4","description":"Voltage-dependent L-type calcium channel subunit beta-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8868","complexName":"Cav1.2 voltage-gated calcium channel complex, CACNA2D3-CACNB1 variant","organismName":"Homo sapiens; 9606","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.2 channel is responsible for excitation-contraction (E-C) coupling of cardiac and, to some extent, smooth muscle. It relays an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmatic membrane. More specifically, rapid depolarization-induced conformational changes of  the complex stimulates calcium efflux from the sarcoplasmatic reticulum through the Ryanodine 2 complex  (CPX-3156) calcium release channel, which subsequently triggers the contractile apparatus until the calcium concentration is reduced again due to re-uptake into the sarcoplasmic reticulum by the Ca2+-ATPase, ATP2A1 (O14983).","predictedComplex":false,"interactors":[{"ac":"EBI-1038838","identifier":"Q13936","identifierLink":"https://www.uniprot.org/uniprotkb/Q13936/entry","name":"CACNA1C","description":"Voltage-dependent L-type calcium channel subunit alpha-1C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50433533","identifier":"Q8IZS8-PRO_0000304647","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IZS8-PRO_0000304647/entry","name":"CACNA2D3","description":"Voltage-dependent calcium channel subunit alpha-2-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-50433550","identifier":"Q8IZS8-PRO_0000304648","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IZS8-PRO_0000304648/entry","name":"CACNA2D3","description":"Voltage-dependent calcium channel subunit delta-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-947514","identifier":"Q02641","identifierLink":"https://www.uniprot.org/uniprotkb/Q02641/entry","name":"CACNB1","description":"Voltage-dependent L-type calcium channel subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8869","complexName":"Cav1.2 voltage-gated calcium channel complex, CACNA2D3-CACNB2 variant","organismName":"Homo sapiens; 9606","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.2 channel is responsible for excitation-contraction (E-C) coupling of cardiac and, to some extent, smooth muscle. It relays an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmatic membrane. More specifically, rapid depolarization-induced conformational changes of  the complex stimulates calcium efflux from the sarcoplasmatic reticulum through the Ryanodine 2 complex  (CPX-3156) calcium release channel, which subsequently triggers the contractile apparatus until the calcium concentration is reduced again due to re-uptake into the sarcoplasmic reticulum by the Ca2+-ATPase, ATP2A1 (O14983).","predictedComplex":false,"interactors":[{"ac":"EBI-1038838","identifier":"Q13936","identifierLink":"https://www.uniprot.org/uniprotkb/Q13936/entry","name":"CACNA1C","description":"Voltage-dependent L-type calcium channel subunit alpha-1C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2874501","identifier":"Q08289","identifierLink":"https://www.uniprot.org/uniprotkb/Q08289/entry","name":"CACNB2","description":"Voltage-dependent L-type calcium channel subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50433533","identifier":"Q8IZS8-PRO_0000304647","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IZS8-PRO_0000304647/entry","name":"CACNA2D3","description":"Voltage-dependent calcium channel subunit alpha-2-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-50433550","identifier":"Q8IZS8-PRO_0000304648","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IZS8-PRO_0000304648/entry","name":"CACNA2D3","description":"Voltage-dependent calcium channel subunit delta-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-8870","complexName":"Cav1.2 voltage-gated calcium channel complex, CACNA2D3-CACNB3 variant","organismName":"Homo sapiens; 9606","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.2 channel is responsible for excitation-contraction (E-C) coupling of cardiac and, to some extent, smooth muscle. It relays an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmatic membrane. More specifically, rapid depolarization-induced conformational changes of  the complex stimulates calcium efflux from the sarcoplasmatic reticulum through the Ryanodine 2 complex  (CPX-3156) calcium release channel, which subsequently triggers the contractile apparatus until the calcium concentration is reduced again due to re-uptake into the sarcoplasmic reticulum by the Ca2+-ATPase, ATP2A1 (O14983).","predictedComplex":false,"interactors":[{"ac":"EBI-1038838","identifier":"Q13936","identifierLink":"https://www.uniprot.org/uniprotkb/Q13936/entry","name":"CACNA1C","description":"Voltage-dependent L-type calcium channel subunit alpha-1C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1184651","identifier":"P54284","identifierLink":"https://www.uniprot.org/uniprotkb/P54284/entry","name":"CACNB3","description":"Voltage-dependent L-type calcium channel subunit beta-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50433533","identifier":"Q8IZS8-PRO_0000304647","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IZS8-PRO_0000304647/entry","name":"CACNA2D3","description":"Voltage-dependent calcium channel subunit alpha-2-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-50433550","identifier":"Q8IZS8-PRO_0000304648","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IZS8-PRO_0000304648/entry","name":"CACNA2D3","description":"Voltage-dependent calcium channel subunit delta-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-8871","complexName":"Cav1.2 voltage-gated calcium channel complex, CACNA2D3-CACNB4 variant","organismName":"Homo sapiens; 9606","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.2 channel is responsible for excitation-contraction (E-C) coupling of cardiac and, to some extent, smooth muscle. It relays an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmatic membrane. More specifically, rapid depolarization-induced conformational changes of  the complex stimulates calcium efflux from the sarcoplasmatic reticulum through the Ryanodine 2 complex  (CPX-3156) calcium release channel, which subsequently triggers the contractile apparatus until the calcium concentration is reduced again due to re-uptake into the sarcoplasmic reticulum by the Ca2+-ATPase, ATP2A1 (O14983).","predictedComplex":false,"interactors":[{"ac":"EBI-1038838","identifier":"Q13936","identifierLink":"https://www.uniprot.org/uniprotkb/Q13936/entry","name":"CACNA1C","description":"Voltage-dependent L-type calcium channel subunit alpha-1C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50433533","identifier":"Q8IZS8-PRO_0000304647","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IZS8-PRO_0000304647/entry","name":"CACNA2D3","description":"Voltage-dependent calcium channel subunit alpha-2-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-50433550","identifier":"Q8IZS8-PRO_0000304648","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IZS8-PRO_0000304648/entry","name":"CACNA2D3","description":"Voltage-dependent calcium channel subunit delta-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-714838","identifier":"O00305","identifierLink":"https://www.uniprot.org/uniprotkb/O00305/entry","name":"CACNB4","description":"Voltage-dependent L-type calcium channel subunit beta-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8872","complexName":"Cav1.2 voltage-gated calcium channel complex, CACNA2D4-CACNB1 variant","organismName":"Homo sapiens; 9606","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. 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More specifically, rapid depolarization-induced conformational changes of  the complex stimulates calcium efflux from the sarcoplasmatic reticulum through the Ryanodine 2 complex  (CPX-3156) calcium release channel, which subsequently triggers the contractile apparatus until the calcium concentration is reduced again due to re-uptake into the sarcoplasmic reticulum by the Ca2+-ATPase, ATP2A1 (O14983).","predictedComplex":false,"interactors":[{"ac":"EBI-1038838","identifier":"Q13936","identifierLink":"https://www.uniprot.org/uniprotkb/Q13936/entry","name":"CACNA1C","description":"Voltage-dependent L-type calcium channel subunit alpha-1C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-49274646","identifier":"Q7Z3S7-PRO_0000304656","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z3S7-PRO_0000304656/entry","name":"CACNA2D4","description":"Voltage-dependent calcium channel subunit alpha-2-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-49275536","identifier":"Q7Z3S7-PRO_0000304657","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z3S7-PRO_0000304657/entry","name":"CACNA2D4","description":"Voltage-dependent calcium channel subunit delta-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-947514","identifier":"Q02641","identifierLink":"https://www.uniprot.org/uniprotkb/Q02641/entry","name":"CACNB1","description":"Voltage-dependent L-type calcium channel subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8873","complexName":"Cav1.2 voltage-gated calcium channel complex, CACNA2D4-CACNB2 variant","organismName":"Homo sapiens; 9606","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.2 channel is responsible for excitation-contraction (E-C) coupling of cardiac and, to some extent, smooth muscle. It relays an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmatic membrane. More specifically, rapid depolarization-induced conformational changes of  the complex stimulates calcium efflux from the sarcoplasmatic reticulum through the Ryanodine 2 complex  (CPX-3156) calcium release channel, which subsequently triggers the contractile apparatus until the calcium concentration is reduced again due to re-uptake into the sarcoplasmic reticulum by the Ca2+-ATPase, ATP2A1 (O14983).","predictedComplex":false,"interactors":[{"ac":"EBI-1038838","identifier":"Q13936","identifierLink":"https://www.uniprot.org/uniprotkb/Q13936/entry","name":"CACNA1C","description":"Voltage-dependent L-type calcium channel subunit alpha-1C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2874501","identifier":"Q08289","identifierLink":"https://www.uniprot.org/uniprotkb/Q08289/entry","name":"CACNB2","description":"Voltage-dependent L-type calcium channel subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-49274646","identifier":"Q7Z3S7-PRO_0000304656","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z3S7-PRO_0000304656/entry","name":"CACNA2D4","description":"Voltage-dependent calcium channel subunit alpha-2-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-49275536","identifier":"Q7Z3S7-PRO_0000304657","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z3S7-PRO_0000304657/entry","name":"CACNA2D4","description":"Voltage-dependent calcium channel subunit delta-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-8875","complexName":"Cav1.2 voltage-gated calcium channel complex, CACNA2D4-CACNB3 variant","organismName":"Homo sapiens; 9606","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.2 channel is responsible for excitation-contraction (E-C) coupling of cardiac and, to some extent, smooth muscle. It relays an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmatic membrane. More specifically, rapid depolarization-induced conformational changes of  the complex stimulates calcium efflux from the sarcoplasmatic reticulum through the Ryanodine 2 complex  (CPX-3156) calcium release channel, which subsequently triggers the contractile apparatus until the calcium concentration is reduced again due to re-uptake into the sarcoplasmic reticulum by the Ca2+-ATPase, ATP2A1 (O14983).","predictedComplex":false,"interactors":[{"ac":"EBI-1038838","identifier":"Q13936","identifierLink":"https://www.uniprot.org/uniprotkb/Q13936/entry","name":"CACNA1C","description":"Voltage-dependent L-type calcium channel subunit alpha-1C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1184651","identifier":"P54284","identifierLink":"https://www.uniprot.org/uniprotkb/P54284/entry","name":"CACNB3","description":"Voltage-dependent L-type calcium channel subunit beta-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-49274646","identifier":"Q7Z3S7-PRO_0000304656","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z3S7-PRO_0000304656/entry","name":"CACNA2D4","description":"Voltage-dependent calcium channel subunit alpha-2-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-49275536","identifier":"Q7Z3S7-PRO_0000304657","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z3S7-PRO_0000304657/entry","name":"CACNA2D4","description":"Voltage-dependent calcium channel subunit delta-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-8876","complexName":"Cav1.2 voltage-gated calcium channel complex, CACNA2D4-CACNB4 variant","organismName":"Homo sapiens; 9606","description":"Voltage‐gated calcium channel which reacts to membrane depolarization by opening to allow Ca2+ to move down an electrochemical gradient. The L-type, high voltage-activated Cav1.2 channel is responsible for excitation-contraction (E-C) coupling of cardiac and, to some extent, smooth muscle. It relays an excitatory depolarization in the T-tubular membrane to the calcium release channel in the sarcoplasmatic membrane. More specifically, rapid depolarization-induced conformational changes of  the complex stimulates calcium efflux from the sarcoplasmatic reticulum through the Ryanodine 2 complex  (CPX-3156) calcium release channel, which subsequently triggers the contractile apparatus until the calcium concentration is reduced again due to re-uptake into the sarcoplasmic reticulum by the Ca2+-ATPase, ATP2A1 (O14983).","predictedComplex":false,"interactors":[{"ac":"EBI-1038838","identifier":"Q13936","identifierLink":"https://www.uniprot.org/uniprotkb/Q13936/entry","name":"CACNA1C","description":"Voltage-dependent L-type calcium channel subunit alpha-1C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-49274646","identifier":"Q7Z3S7-PRO_0000304656","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z3S7-PRO_0000304656/entry","name":"CACNA2D4","description":"Voltage-dependent calcium channel subunit alpha-2-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-49275536","identifier":"Q7Z3S7-PRO_0000304657","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z3S7-PRO_0000304657/entry","name":"CACNA2D4","description":"Voltage-dependent calcium channel subunit delta-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-714838","identifier":"O00305","identifierLink":"https://www.uniprot.org/uniprotkb/O00305/entry","name":"CACNB4","description":"Voltage-dependent L-type calcium channel subunit beta-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8877","complexName":"CORVET tethering complex","organismName":"Drosophila melanogaster; 7227","description":"Multisubunit tethering complex involved in early endosomal fusions by cross-linking two membranes, and facilitating the formation of a SNARE complex during fusion. Interacts with Rab GTPase RAB5 (Q9V3I2).","predictedComplex":false,"interactors":[{"ac":"EBI-187940","identifier":"Q9VHG1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VHG1/entry","name":"Vps16A","description":"Vacuolar protein sorting-associated protein 16 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12811","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-192483","identifier":"Q9VRX2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VRX2/entry","name":"Vps8","description":"Vacuolar protein sorting-associated protein 8 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12616","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-421908","identifier":"Q24314","identifierLink":"https://www.uniprot.org/uniprotkb/Q24314/entry","name":"dor","description":"Vacuolar protein sorting-associated protein 18 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23323","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9924110","identifier":"Q9Y1I2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y1I2/entry","name":"car","description":"Vacuolar protein sorting-associated protein 33A","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11679","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8879","complexName":"SGLT2-MAP17 glucose cotransporter complex","organismName":"Homo sapiens; 9606","description":"Na+-coupled sugar simporter that actively transports D-glucose at the plasma membrane and is responsible for reabsorption of glucose in the kidney proximal tubules after filtration through the glomerulus. SGLT2/SLC5A2 binds a single Na2+ ion and undergoes a resulting conformational change which enablies the protein to bind one sugar molecule.","predictedComplex":false,"interactors":[{"ac":"EBI-21022766","identifier":"P31639","identifierLink":"https://www.uniprot.org/uniprotkb/P31639/entry","name":"SLC5A2","description":"Sodium/glucose cotransporter 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11819","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-716063","identifier":"Q13113","identifierLink":"https://www.uniprot.org/uniprotkb/Q13113/entry","name":"PDZK1IP1","description":"PDZK1-interacting protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15296","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8881","complexName":"CARD-BCL10-MALT1 complex, CARD9 variant","organismName":"Homo sapiens; 9606","description":"Scaffolding platform that bridges T- and B-cell receptor proximal signaling to the canonical I-kappa-B kinase, NF-kappa-B and JNK pathway in lymphocytes thus triggering the adaptive immune response in lymphocytes and lymphoma cells. Activation of the CARD protein results in its interaction with BCL10 and facilitates its forming of large macromolecular filaments, providing a large scaffold for binding and activation of MALT1, which is the enzymatic caspase-like subunit of the complex. This results in the further downstream activation of a variety of effector molecules. CARD9 expression is restricted to myeloid cells.","predictedComplex":false,"interactors":[{"ac":"EBI-1047372","identifier":"Q9UDY8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UDY8/entry","name":"MALT1","description":"Mucosa-associated lymphoid tissue lymphoma translocation protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22576","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-751319","identifier":"Q9H257","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H257/entry","name":"CARD9","description":"Caspase recruitment domain-containing protein 9","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14559","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-958922","identifier":"O95999","identifierLink":"https://www.uniprot.org/uniprotkb/O95999/entry","name":"BCL10","description":"B-cell lymphoma/leukemia 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR34920","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8901","complexName":"CARD-BCL10-MALT1 complex, CARD11 variant","organismName":"Homo sapiens; 9606","description":"Scaffolding platform that bridges T- and B-cell receptor proximal signaling to the canonical I-kappa-B kinase, NF-kappa-B and JNK pathway in lymphocytes thus triggering the adaptive immune response in lymphocytes and lymphoma cells. Activation of the CARD protein results in its interaction with BCL10 and facilitates its forming of large macromolecular filaments, providing a large scaffold for binding and activation of MALT1, which is the enzymatic caspase-like subunit of the complex. This results in the further downstream activation of a variety of effector molecules. CARD11 is expressed in haematopoietic cells.","predictedComplex":false,"interactors":[{"ac":"EBI-1047372","identifier":"Q9UDY8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UDY8/entry","name":"MALT1","description":"Mucosa-associated lymphoid tissue lymphoma translocation protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22576","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7006141","identifier":"Q9BXL7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BXL7/entry","name":"CARD11","description":"Caspase recruitment domain-containing protein 11","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14559","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-958922","identifier":"O95999","identifierLink":"https://www.uniprot.org/uniprotkb/O95999/entry","name":"BCL10","description":"B-cell lymphoma/leukemia 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR34920","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8902","complexName":"CARD-BCL10-MALT1 complex, CARD10 variant","organismName":"Homo sapiens; 9606","description":"Scaffolding platform that bridges T- and B-cell receptor proximal signaling to the canonical I-kappa-B kinase, NF-kappa-B and JNK pathway in lymphocytes thus triggering the adaptive immune response in lymphocytes and lymphoma cells. Activation of the CARD protein results in its interaction with BCL10 and facilitates its forming of large macromolecular filaments, providing a large scaffold for binding and activation of MALT1, which is the enzymatic caspase-like subunit of the complex. This results in the further downstream activation of a variety of effector molecules. CARD10 is expressed in non-haematopoietic cells and is activated by G protein-coupled receptors  such as the receptors for angiotensin II or lysophosphatidic acid, and by growth factor receptor tyrosine kinases of the epidermal growth factor receptor family.","predictedComplex":false,"interactors":[{"ac":"EBI-1047372","identifier":"Q9UDY8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UDY8/entry","name":"MALT1","description":"Mucosa-associated lymphoid tissue lymphoma translocation protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22576","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3866279","identifier":"Q9BWT7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BWT7/entry","name":"CARD10","description":"Caspase recruitment domain-containing protein 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14559","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-958922","identifier":"O95999","identifierLink":"https://www.uniprot.org/uniprotkb/O95999/entry","name":"BCL10","description":"B-cell lymphoma/leukemia 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR34920","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8903","complexName":"General transcription factor TFIIIC complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Transcription factor required for Pol III transcription complex assembly. Mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Assembles the initiation complex TFIIIB-TFIIIC-tDNA upstream of the transcription start site, which is sufficient for RNA polymerase III recruitment and function.","predictedComplex":false,"interactors":[{"ac":"EBI-1564368","identifier":"Q9UST7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UST7/entry","name":"sfc3","description":"Transcription factor tau subunit sfc3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15180","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1564387","identifier":"O14229","identifierLink":"https://www.uniprot.org/uniprotkb/O14229/entry","name":"sfc1","description":"Transcription factor tau subunit sfc1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13230","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1564416","identifier":"O74458","identifierLink":"https://www.uniprot.org/uniprotkb/O74458/entry","name":"sfc4","description":"Transcription factor tau subunit sfc4","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1564437","identifier":"O60174","identifierLink":"https://www.uniprot.org/uniprotkb/O60174/entry","name":"sfc6","description":"Transcription factor tau subunit sfc6","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15052","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50435562","identifier":"A6X980","identifierLink":"https://www.uniprot.org/uniprotkb/A6X980/entry","name":"sfc7","description":"Transcription factor tau subunit sfc7","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR21860","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50435638","identifier":"O13650","identifierLink":"https://www.uniprot.org/uniprotkb/O13650/entry","name":"sfc9","description":"Putative transcription factor tau subunit sfc9","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15496","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8904","complexName":"General transcription factor TFIIIB complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Transcription factor complex required for Pol III transcription complex  assembly which transcribes short noncoding RNA genes. Cooperates with TFIIIC (CPX-8903) to recruit Pol III to different types of gene promoters and form the preinitiation complex (PIC). Once assembled upstream of the start site, TFIIIB generates a significant DNA distortion of the class III gene promoter through the SPT15 and BDP1 subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-1152238","identifier":"P17871","identifierLink":"https://www.uniprot.org/uniprotkb/P17871/entry","name":"tbp1","description":"TATA-box-binding protein","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10126","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50435746","identifier":"Q9P6R0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P6R0/entry","name":"brf1","description":"Transcription factor IIIB 60 kDa subunit","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11618","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50435773","identifier":"O94481","identifierLink":"https://www.uniprot.org/uniprotkb/O94481/entry","name":"bdp1","description":"Transcription factor TFIIIB component B''","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR22929","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8905","complexName":"DNA-directed RNA polymerase III complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Catalyzes the transcription of RNA from an DNA template by acting as a nucleotidyl transferase that polymerizes ribonucleotides at the 3-prime end of an RNA transcript. Responsible for the transcription of genes encoding small structured RNAs such as tRNAs, the 7 SL lncRNA, spliceosomal U6 snRNA and ribosomal 5S RNA. Pol III machinery recognizes conserved promoter elements located within the transcribed region, generally the box A and box B sequences, which contribute to the D- and T-loops in the tRNA structure. rpc6, rpc31 and rpc82 play a role in transcription initiation whereas the rpc37-rpc53 heterodimer is crucial for the correct recognition of the termination signals of class III genes. rpc11 is required for RNA cleavage. Pol III is capable of reinitiating transcription more rapidly on the same gene after the first transcription cycle without being released (facilitated reinitiation), resulting in a higher initiation efficiency; this appears to require an rpc11-dependent conformational change of Pol III. The core complex is believed to assemble in the cytoplasm before being transported to the nucleus.","predictedComplex":false,"interactors":[{"ac":"EBI-1533422","identifier":"Q09191","identifierLink":"https://www.uniprot.org/uniprotkb/Q09191/entry","name":"rpb5","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10535","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1533481","identifier":"Q92399","identifierLink":"https://www.uniprot.org/uniprotkb/Q92399/entry","name":"rpb8","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10917","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1533514","identifier":"P48011","identifierLink":"https://www.uniprot.org/uniprotkb/P48011/entry","name":"rpc10","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC4","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1533685","identifier":"P36595","identifierLink":"https://www.uniprot.org/uniprotkb/P36595/entry","name":"rpb6","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR47227","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1534105","identifier":"O13877","identifierLink":"https://www.uniprot.org/uniprotkb/O13877/entry","name":"rpb10","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC5","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23431","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15672685","identifier":"Q10233","identifierLink":"https://www.uniprot.org/uniprotkb/Q10233/entry","name":"rpc2","description":"DNA-directed RNA polymerase III subunit RPC2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 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Functions at the interface between transcription and mRNA export via its interaction with SUB2 in the TREX complex (CPX-1793). Recruited to transcribed genes and moves along the gene with the elongating polymerase during transcription. THO is important for stabilizing nascent RNA in the RNA polymerase II elongation complex by preventing formation of DNA:RNA hybrids behind the elongating polymerase. The inclusion o Tex1 in this complex is debated in the literature.","predictedComplex":false,"interactors":[{"ac":"EBI-10841","identifier":"P33441","identifierLink":"https://www.uniprot.org/uniprotkb/P33441/entry","name":"MFT1","description":"THO complex subunit MFT1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-15475","identifier":"P53552","identifierLink":"https://www.uniprot.org/uniprotkb/P53552/entry","name":"THO2","description":"THO complex subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21597","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-29234","identifier":"P53851","identifierLink":"https://www.uniprot.org/uniprotkb/P53851/entry","name":"TEX1","description":"Protein TEX1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22839","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30898","identifier":"O13539","identifierLink":"https://www.uniprot.org/uniprotkb/O13539/entry","name":"THP2","description":"THO complex subunit THP2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-8526","identifier":"P17629","identifierLink":"https://www.uniprot.org/uniprotkb/P17629/entry","name":"HPR1","description":"THO complex subunit HPR1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-8906","complexName":"CARD-BCL10-MALT1 complex, CARD14 variant","organismName":"Homo sapiens; 9606","description":"Scaffolding platform that bridges T- and B-cell receptor proximal signaling to the canonical I-kappa-B kinase, NF-kappa-B and JNK pathway in lymphocytes thus triggering the adaptive immune response in lymphocytes and lymphoma cells. Activation of the CARD protein results in its interaction with BCL10 and facilitates its forming of large macromolecular filaments, providing a large scaffold for binding and activation of MALT1, which is the enzymatic caspase-like subunit of the complex. This results in the further downstream activation of a variety of effector molecules. CARD14 is expressed in non-haematopoietic cells, at high levels in the epidermis, in particular keratinocytes, dermal endothelial cells and Langerhans cells.","predictedComplex":false,"interactors":[{"ac":"EBI-1047372","identifier":"Q9UDY8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UDY8/entry","name":"MALT1","description":"Mucosa-associated lymphoid tissue lymphoma translocation protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22576","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-745552","identifier":"Q9BXL6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BXL6/entry","name":"CARD14","description":"Caspase recruitment domain-containing protein 14","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14559","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-958922","identifier":"O95999","identifierLink":"https://www.uniprot.org/uniprotkb/O95999/entry","name":"BCL10","description":"B-cell lymphoma/leukemia 10","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 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6239","xrefs":[{"identifier":"PTHR10535","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-320556","identifier":"Q19826","identifierLink":"https://www.uniprot.org/uniprotkb/Q19826/entry","name":"rpb-8","description":"Probable DNA-directed RNA polymerases I, II, and III subunit RPABC3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10917","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-322538","identifier":"G5ED21","identifierLink":"https://www.uniprot.org/uniprotkb/G5ED21/entry","name":"rpoa-1","description":"DNA-directed RNA polymerase subunit","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR19376","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50437050","identifier":"Q9GR61","identifierLink":"https://www.uniprot.org/uniprotkb/Q9GR61/entry","name":"rpb-10","description":"DNA-directed RNA polymerases I, II, and III subunit RPABC5","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 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6239","xrefs":[{"identifier":"PTHR11239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50559495","identifier":"Q95X83","identifierLink":"https://www.uniprot.org/uniprotkb/Q95X83/entry","name":"rpoa-49","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR14440","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8914","complexName":"Nucleolar exosome complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"3' -5' exo- and endoribonuclease complex that is involved in RNA maturation and degradation which include the removal of unstable and aberrant transcripts and may also regulate the levels of specific transcripts in response to environmental factors. Restricted to processing linear and circular single-stranded RNAs only. RNAs with complex secondary structures, particularly at the 3' end of the molecule, may have to be unwound or pre-processed by co-factors prior to entering the complex. Although some RNAs may be targeted directly to the catalytic subunits, the majority of substrates enter the barrel-like structure of the exosome through a pore at the centre of the cap and are threaded through the central channel in a 3' to 5' orientation. The ribonuclease activity of the catalytic subunits facilitates the degradation process.","predictedComplex":false,"interactors":[{"ac":"EBI-1560441","identifier":"O42872","identifierLink":"https://www.uniprot.org/uniprotkb/O42872/entry","name":"ski6","description":"Exosome complex component ski6","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50644361","identifier":"Q09704","identifierLink":"https://www.uniprot.org/uniprotkb/Q09704/entry","name":"rrp4","description":"Exosome complex component rrp4","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50644396","identifier":"Q10205","identifierLink":"https://www.uniprot.org/uniprotkb/Q10205/entry","name":"rrp43","description":"Exosome complex component rrp43","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50644431","identifier":"Q9P7R3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P7R3/entry","name":"mtr3","description":"Exosome complex component mtr3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50644462","identifier":"O74918","identifierLink":"https://www.uniprot.org/uniprotkb/O74918/entry","name":"rrp45","description":"Exosome complex component rrp45","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50644497","identifier":"O42894","identifierLink":"https://www.uniprot.org/uniprotkb/O42894/entry","name":"rrp46","description":"Exosome complex component rrp46","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11953","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50644528","identifier":"O59821","identifierLink":"https://www.uniprot.org/uniprotkb/O59821/entry","name":"csl4","description":"Exosome complex component csl4","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12686","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50644558","identifier":"O13903","identifierLink":"https://www.uniprot.org/uniprotkb/O13903/entry","name":"rrp40","description":"Exosome complex component rrp40","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR21321","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7997089","identifier":"Q10146","identifierLink":"https://www.uniprot.org/uniprotkb/Q10146/entry","name":"rrp6","description":"Exosome complex exonuclease rrp6","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12124","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7997146","identifier":"P37202","identifierLink":"https://www.uniprot.org/uniprotkb/P37202/entry","name":"dis3","description":"Exosome complex exonuclease dis3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23355","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8993841","identifier":"O60124","identifierLink":"https://www.uniprot.org/uniprotkb/O60124/entry","name":"rrp42","description":"Exosome complex component rrp42","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8916","complexName":"CRL3 E3 ubiquitin ligase complex, SPOP-SPOPL variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SPOP is required to maintain normal cellular growth and development and its targets include the polycomb protein BMI1 (P35226), the apoptosis factor DAXX (Q9UER7), the pancreatic and duodenal homeobox protein PDX1 (P52945), and the Hedgehog signaling transcription factors GLI2 (P10070) and GLI3 (P10071). SPOP forms linear higher-order oligomers which enables it to present multiple MATH domains (IPR002083) for binding to multiple low-affinity motifs in a single substrate (CPX-2300) however binding to SPOPL restricts self-assembly due to the presence of an inhibitory structural element within the SPOPL BACK domain.","predictedComplex":false,"interactors":[{"ac":"EBI-2822161","identifier":"Q6IQ16","identifierLink":"https://www.uniprot.org/uniprotkb/Q6IQ16/entry","name":"SPOPL","description":"Speckle-type POZ protein-like","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24413","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743549","identifier":"O43791","identifierLink":"https://www.uniprot.org/uniprotkb/O43791/entry","name":"SPOP","description":"Speckle-type POZ protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24413","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8917","complexName":"CRL3 E3 ubiquitin ligase complex, SPOPL variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. SPOPL appears to play a role in the regulation of the NOTCH-signalling pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-2822161","identifier":"Q6IQ16","identifierLink":"https://www.uniprot.org/uniprotkb/Q6IQ16/entry","name":"SPOPL","description":"Speckle-type POZ protein-like","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24413","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8918","complexName":"CRL3 E3 ubiquitin ligase complex, KBTBD2 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.CRL3-KBTBD2 target proteins include PIK3R1 (P27986), thus regulating insulin signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-16812775","identifier":"Q8IY47","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IY47/entry","name":"KBTBD2","description":"Kelch repeat and BTB domain-containing protein 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8921","complexName":"TOM40 mitochondrial outer membrane translocase complex","organismName":"Drosophila melanogaster; 7227","description":"Translocase in the outer mitochondrial membrane that mediates the import of precursor protein and mediates inset of some resident outer membrane proteins. Most mitochondrial proteins are synthesised in the cytosol, imported into mitochondria, sorted to one of the four sub-mitochondrial compartments, where they function, and attain their functional native conformation, which is often facilitated by assembly into the membrane or a multi-protein complex.","predictedComplex":false,"interactors":[{"ac":"EBI-115599","identifier":"Q7K036","identifierLink":"https://www.uniprot.org/uniprotkb/Q7K036/entry","name":"Tom7","description":"Mitochondrial import receptor subunit TOM7 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46722","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-127868","identifier":"Q8IRD0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IRD0/entry","name":"Tom5","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-181644","identifier":"Q95RF6","identifierLink":"https://www.uniprot.org/uniprotkb/Q95RF6/entry","name":"Tom20","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12430","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-51874708","identifier":"Q6IGW6","identifierLink":"https://www.uniprot.org/uniprotkb/Q6IGW6/entry","name":"Tom6","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-86299","identifier":"Q9VKC8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VKC8/entry","name":"Tom70","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46208","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-97056","identifier":"Q9U4L6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9U4L6/entry","name":"Tom40","description":"Mitochondrial import receptor subunit TOM40 homolog 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9937884","identifier":"Q9VZL1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VZL1/entry","name":"mge","description":"Mitochondrial import receptor subunit TOM22 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12504","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8923","complexName":"ERF1-ERF3 translation release factor complex, GSPT2 variant","organismName":"Homo sapiens; 9606","description":"Required for the termination of protein synthesis which occurs when one of three stop codons (UAA, UAG or UGA) enters the ribosomal A site. ETF1 stimulates GTP binding to GSPT2, inducing the GTPase activity of eRF3 that couples codon recognition and ETF1 peptidyl-tRNA hydrolysis to ensure rapid and efficient peptide release from the ribosome.","predictedComplex":false,"interactors":[{"ac":"EBI-25820308","identifier":"CHEBI:37565","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:37565","name":"gtp(4-)","description":"GTP(4-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-3869637","identifier":"Q8IYD1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IYD1/entry","name":"GSPT2","description":"Eukaryotic peptide chain release factor GTP-binding subunit ERF3B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-750990","identifier":"P62495","identifierLink":"https://www.uniprot.org/uniprotkb/P62495/entry","name":"ETF1","description":"Eukaryotic peptide chain release factor subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10113","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8924","complexName":"ERF1-ERF3 translation release factor complex, Gspt2 variant","organismName":"Mus musculus; 10090","description":"Required for the termination of protein synthesis which occurs when one of three stop codons (UAA, UAG or UGA) enters the ribosomal A site. Etf1 stimulates GTP binding to Gspt2, inducing the GTPase activity of Gspt2 that couples codon recognition and Etf1 peptidyl-tRNA hydrolysis to ensure rapid and efficient peptide release from the ribosome.","predictedComplex":false,"interactors":[{"ac":"EBI-25820308","identifier":"CHEBI:37565","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:37565","name":"gtp(4-)","description":"GTP(4-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-4309564","identifier":"Q149F3","identifierLink":"https://www.uniprot.org/uniprotkb/Q149F3/entry","name":"Gspt2","description":"Eukaryotic peptide chain release factor GTP-binding subunit ERF3B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8737530","identifier":"Q8BWY3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BWY3/entry","name":"Etf1","description":"Eukaryotic peptide chain release factor subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10113","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8925","complexName":"ERF1-ERF3 translation termination complex","organismName":"Drosophila melanogaster; 7227","description":"Required for the termination of protein synthesis which occurs when one of three stop codons (UAA, UAG or UGA) enters the ribosomal A site. eRF1 stimulates GTP binding to eRF3, inducing the GTPase activity of eRF3 that couples codon recognition and peptidyl-tRNA hydrolysis mediated by eRF1 to ensure rapid and efficient peptide release on the ribosome.","predictedComplex":false,"interactors":[{"ac":"EBI-146901","identifier":"Q9VPH7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VPH7/entry","name":"eRF1","description":"Eukaryotic peptide chain release factor subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10113","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-192162","identifier":"Q9VK85","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VK85/entry","name":"eRF3","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25820308","identifier":"CHEBI:37565","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:37565","name":"gtp(4-)","description":"GTP(4-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-8926","complexName":"TOM40 mitochondrial outer membrane translocase complex, testis-specific variant","organismName":"Drosophila melanogaster; 7227","description":"Translocase in the outer mitochondrial membrane that mediates the import of precursor protein and mediates inset of some resident outer membrane proteins. Most mitochondrial proteins are synthesised in the cytosol, imported into mitochondria, sorted to one of the four sub-mitochondrial compartments, where they function, and attain their functional native conformation, which is often facilitated by assembly into the membrane or a multi-protein complex.","predictedComplex":false,"interactors":[{"ac":"EBI-115599","identifier":"Q7K036","identifierLink":"https://www.uniprot.org/uniprotkb/Q7K036/entry","name":"Tom7","description":"Mitochondrial import receptor subunit TOM7 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46722","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-127868","identifier":"Q8IRD0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IRD0/entry","name":"Tom5","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-51874708","identifier":"Q6IGW6","identifierLink":"https://www.uniprot.org/uniprotkb/Q6IGW6/entry","name":"Tom6","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-52217359","identifier":"A1Z6L1","identifierLink":"https://www.uniprot.org/uniprotkb/A1Z6L1/entry","name":"tomboy40","description":"Mitochondrial import receptor subunit TOM40 homolog 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52217379","identifier":"Q9VGX9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VGX9/entry","name":"tomboy20","description":"TOMM20-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12430","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-86299","identifier":"Q9VKC8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VKC8/entry","name":"Tom70","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR46208","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9937884","identifier":"Q9VZL1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VZL1/entry","name":"mge","description":"Mitochondrial import receptor subunit TOM22 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12504","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8927","complexName":"CRL3 E3 ubiquitin ligase complex, KBTBD4 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.CRL3-KBTBD4 target proteins include components of the LSD1/RCOR1 corepressor complex for proteasomal degradation, hence re-establishing the transcripition-activating dimethyl-lysine-4 histone and acetyl-lysine-27 histone H3 epigenetic marks.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-725970","identifier":"Q9NVX7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NVX7/entry","name":"KBTBD4","description":"Kelch repeat and BTB domain-containing protein 4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47195","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8928","complexName":"Kinetochore MIS12 complex, Nnf1b variant","organismName":"Drosophila melanogaster; 7227","description":"Required for normal chromosome alignment and segregation, kinetochore formation during mitosis, proper kinetochore microtubule attachments and for the spindle assembly checkpoint. Binds to the centromeric protein CENP-C (Q9VHP9) to create the foundation on which the mitotic kinetochore is constructed and enable the nucleation of the KMN (Knl1, Mis12, and Ndc80 complex) network.","predictedComplex":false,"interactors":[{"ac":"EBI-15108077","identifier":"Q9VS01","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VS01/entry","name":"Mis12","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-15108099","identifier":"Q8IPW3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IPW3/entry","name":"Nnf1b","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-9630827","identifier":"A4V2Z1","identifierLink":"https://www.uniprot.org/uniprotkb/A4V2Z1/entry","name":"nsl1","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]}]},{"complexAC":"CPX-8930","complexName":"NXF1-NXT1 mRNA nuclear export factor complex","organismName":"Drosophila melanogaster; 7227","description":"Mediates the export of bulk mRNA through direct interactions with both the mRNA cargo and nuclear pore proteins that contain characteristic phenylalanine-glycine repeating sequence motifs (FG-nucleoporins).","predictedComplex":false,"interactors":[{"ac":"EBI-144932","identifier":"Q9U1H9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9U1H9/entry","name":"sbr","description":"Nuclear RNA export factor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10662","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-160435","identifier":"Q9V3H8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V3H8/entry","name":"Nxt1","description":"NTF2-related export protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12612","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8931","complexName":"Transmembrane tumor necrosis factor complex","organismName":"Homo sapiens; 9606","description":"Potent pro-inflammatory cytokine capable of exerting pleiotropic effects on a variety of cell types. Belongs to the tumour necrosis factor (TNF) superfamily of type II transmembrane proteins. \r\n\r\nMainly secreted by macrophages, T helper 1 and natural killer cells, it is expressed on activated macrophages and lymphocytes. Generated as a precursor form known as transmembrane TNF(mTNF, this complex), TACE (ADAM17) cleavage of mTNF results in the release of a soluble form (sTNF, CPX-8826) with the residual cytoplasmic domain of mTNF migrating back into the nucleus of mTNF producing cells. sTNF exerts its functions through either type-1 (TNR1A, P19438) or type-2 (TNR1B, P20333)  TNF receptors and while mTNF can act through either receptor type, its activities are mainly mediated through TNR1B, its primary biological target.\r\n\r\nBoth the soluble and the transmembrane forms play a role in inflammatory responses and whilst mTNF exerts its biological function through cell-to-cell contact to moderate inflammation, sTNF, acts at sites remote from the TNF-producing cells to drive inflammation.\r\n\r\nBoth protective and pathogenic, it induces cell death in response to microbial infection but behaves aberrantly when induced as a result of environmental or genetic factors, thereby driving the pathogenesis of inflammatory disorders. \r\n\r\nCytotoxic effects mediated by mTNF include lung injury induced in the alveolar macrophages of HIV patients, yet mTNF offers protection from Mycobacterium tuberculosis infection.","predictedComplex":false,"interactors":[{"ac":"EBI-52222143","identifier":"P01375-PRO_0000034423","identifierLink":"https://www.uniprot.org/uniprotkb/P01375-PRO_0000034423/entry","name":"TNF","description":"Tumor necrosis factor, membrane form","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-8934","complexName":"Panoramix-induced co-transcriptional silencing complex","organismName":"Drosophila melanogaster; 7227","description":"Directs piRNA-guided co-transcriptional gene silencing (TGS) of transposon insertions, anchoring Piwi‐(RNA‐induced silencing complex) to target RNAs through the Nxf2 LRR domain (IPR001611). Tethering of the complex to nascent RNA induces heterochromatin formation independent of Piwi and piRNAs","predictedComplex":false,"interactors":[{"ac":"EBI-156442","identifier":"Q24117","identifierLink":"https://www.uniprot.org/uniprotkb/Q24117/entry","name":"ctp","description":"Dynein light chain 1, cytoplasmic","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-160435","identifier":"Q9V3H8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V3H8/entry","name":"Nxt1","description":"NTF2-related export protein","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12612","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-184428","identifier":"Q9W2H9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W2H9/entry","name":"Panx","description":"Protein panoramix","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-3415272","identifier":"Q9VV73","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VV73/entry","name":"nxf2","description":"Nuclear RNA export factor 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10662","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8935","complexName":"CRL3 E3 ubiquitin ligase complex, KBTBD6-KBTBD7 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.CRL3-KBTBD6/7 target proteins include TIAM1 (Q13009), a RAC1-specific guanine exchange factor which controls actin rearrangements and cell motility. Recruitment of the complex to the plasma membrane is dependent on member of the GABARAP protein family.","predictedComplex":false,"interactors":[{"ac":"EBI-2514778","identifier":"Q86V97","identifierLink":"https://www.uniprot.org/uniprotkb/Q86V97/entry","name":"KBTBD6","description":"Kelch repeat and BTB domain-containing protein 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-473695","identifier":"Q8WVZ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WVZ9/entry","name":"KBTBD7","description":"Kelch repeat and BTB domain-containing protein 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8936","complexName":"Interleukin-6 antagonist complex","organismName":"Homo sapiens; 9606","description":"Principal member of the IL-6 superfamily, a multifunctional cytokine which promotes T cell activation, B cell differentiation and modulates acute-phase responses. IL-6 plays fundamental roles in immune response, inflammation, hematopoiesis, and bone homeostasis under homeostatic conditions. \r\n\r\nDimeric IL-6 has an increased affinity for soluble IL-6RA but are thought to have a decreased ability to bind IL6ST/gp130, and thus considered an IL-6 antagonist. Binding of the monomeric form of IL-6 to its specific IL-6RA and the signal-tranducing glycoprotein component IL6ST results in three distinct modes of IL-6-mediated signalling: classic IL-6 signalling, trans-IL-6 signalling and cluster-IL-6 signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-720533","identifier":"P05231","identifierLink":"https://www.uniprot.org/uniprotkb/P05231/entry","name":"IL6","description":"Interleukin-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48494","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8938","complexName":"MEX67-NXT1 mRNA nuclear export factor complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Mediates the export of bulk mRNA through direct interactions with both the mRNA cargo and nuclear pore proteins that contain characteristic phenylalanine-glycine repeating sequence motifs (FG-nucleoporins).","predictedComplex":false,"interactors":[{"ac":"EBI-21244774","identifier":"Q9Y8G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y8G3/entry","name":"mex67","description":"mRNA export factor mex67","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10662","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-54453966","identifier":"P0CAN8","identifierLink":"https://www.uniprot.org/uniprotkb/P0CAN8/entry","name":"nxt1","description":"NTF2-related export protein 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12612","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8939","complexName":"HipHop-HOAP telomere-capping complex","organismName":"Drosophila melanogaster; 7227","description":"Binds to the double stranded portion of telomeric chromatin and recruits Su(var)205/Heterochromatin Protein 1 (P05205), a structural  component of heterochromatin involved in gene repression, to telomeres. Also recruits the MTV complex (CPX-8944) to form the terminin telomere-capping complex, which binds to chromosome ends in a sequence-independent manner and prevents telomere fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-103483","identifier":"Q7JWP6","identifierLink":"https://www.uniprot.org/uniprotkb/Q7JWP6/entry","name":"HipHop","description":"HP1-HOAP-interacting protein","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-104820","identifier":"Q95RV2","identifierLink":"https://www.uniprot.org/uniprotkb/Q95RV2/entry","name":"cav","description":"Telomere-binding protein cav","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]}]},{"complexAC":"CPX-8940","complexName":"Ribosome biogenesis complex","organismName":"Homo sapiens; 9606","description":"Serves as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, thus regulating protein translation in cells differentiating to become neural crest cells.","predictedComplex":false,"interactors":[{"ac":"EBI-396105","identifier":"Q13428","identifierLink":"https://www.uniprot.org/uniprotkb/Q13428/entry","name":"TCOF1","description":"Treacle protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20787","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-396155","identifier":"Q14978","identifierLink":"https://www.uniprot.org/uniprotkb/Q14978/entry","name":"NOLC1","description":"Nucleolar and coiled-body phosphoprotein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23216","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6657662","identifier":"P61328","identifierLink":"https://www.uniprot.org/uniprotkb/P61328/entry","name":"FGF12","description":"Fibroblast growth factor 12","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11486","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8941","complexName":"CRL3 E3 ubiquitin ligase complex, KBTBD8 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.CRL3-KBTBD8 monoubiquitylates NOLC1 (Q14978) and its paralogue TCOF1 (Q13428), driving the formation of the ribosome biogenesis complex (CPX-8940)","predictedComplex":false,"interactors":[{"ac":"EBI-21328977","identifier":"Q8NFY9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NFY9/entry","name":"KBTBD8","description":"Kelch repeat and BTB domain-containing protein 8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8942","complexName":"CRL3 E3 ubiquitin ligase complex, KBTBD3 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.","predictedComplex":false,"interactors":[{"ac":"EBI-1390557","identifier":"Q8NAB2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NAB2/entry","name":"KBTBD3","description":"Kelch repeat and BTB domain-containing protein 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8943","complexName":"CoREST transcriptional corepressor complex, RCOR1-HDAC1 variant","organismName":"Homo sapiens; 9606","description":"Class I histone deacetylase complex unique in containing both histone demethylase and deacetylase enzymes, KDM1A and HDAC1/2 respectively. Acts as a transcriptional repressor, by acting as an epigenetic eraser removing methyl and acetyl groups from histone tails. This results in the loss of binding sites for regulatory reader proteins and causes chromatin compaction by restoring the positive charge on histone tails. Regulates neuronal differentiation gene expression and stem cell fate and development.","predictedComplex":false,"interactors":[{"ac":"EBI-301834","identifier":"Q13547","identifierLink":"https://www.uniprot.org/uniprotkb/Q13547/entry","name":"HDAC1","description":"Histone deacetylase 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-710124","identifier":"O60341","identifierLink":"https://www.uniprot.org/uniprotkb/O60341/entry","name":"KDM1A","description":"Lysine-specific histone demethylase 1A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-926563","identifier":"Q9UKL0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UKL0/entry","name":"RCOR1","description":"REST corepressor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16089","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-8944","complexName":"MTV complex","organismName":"Drosophila melanogaster; 7227","description":"Binds single-stranded DNA in a sequence independent manner, protecting the DNA from cleavage by endonucleases. Binds the HipHop-HOAP complex (CPX-8939) to form terminin telomere-capping complex which binds to chromosome ends in a sequence-independent manner and prevents telomere fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-15755079","identifier":"B7Z0L8","identifierLink":"https://www.uniprot.org/uniprotkb/B7Z0L8/entry","name":"moi","description":"Protein modigliani","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-163870","identifier":"Q9VTZ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VTZ2/entry","name":"ver","description":"Protein verrocchio","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13989","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-183700","identifier":"E1JH25","identifierLink":"https://www.uniprot.org/uniprotkb/E1JH25/entry","name":"tea","description":"Protein telomere ends associated","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]}]},{"complexAC":"CPX-8945","complexName":"Lymphotoxin-alpha-TNFRSF1A receptor complex","organismName":"Homo sapiens; 9606","description":"Receptor complex whose primary role is in lymphoid organ development, organization and the maintenance of lymphoid microenvironments to promote host defense, and inflammation. LTA mediates its effects through one of three receptors: TNFRSF1A (this complex), TNFRSF1B (CPX-9221) and TNFRSF14 (CPX-9222). A death domain (DD) contained within the cytoplasmic tail of TNFRSF1A allows it to recruit TRADD (TNFR1-associated DD, Q15628) and its associated molecules which predominantly results in cell survival through NF-KB-NIK or MAPK activation. Apoptosis is initiated through TRADD's interaction with FADD (Q13158).\r\n\r\nLTA is produced predominantly by activated innate and adaptive immune cells, and its effects are mediated by TNFRSF1A which is expressed on most cells, including tumour cell types.\r\n\r\nTNFRSF1A signalling leads to cell death and canonical NFKB-mediated inflammatory processes, as well as the development and progression of autoimmune diseases.","predictedComplex":false,"interactors":[{"ac":"EBI-299451","identifier":"P19438","identifierLink":"https://www.uniprot.org/uniprotkb/P19438/entry","name":"TNFRSF1A","description":"Tumor necrosis factor receptor superfamily member 1A","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46861","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-524105","identifier":"P01374","identifierLink":"https://www.uniprot.org/uniprotkb/P01374/entry","name":"LTA","description":"Lymphotoxin-alpha","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11471","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8947","complexName":"Lymphotoxin-alpha-beta-LTBR receptor complex","organismName":"Homo sapiens; 9606","description":"Asymmetric receptor complex which plays a broad role in thymic function including the development and maintenance of lymphoid organs as well as lymph node remodelling and the induction of IFNG (P01579) and T cell responses during systemic viral infections. The complex's effects are mediated by activating NF-KB. LTA-LTB-LTBR signalling also promotes apoptosis via TRAF3 (Q13114) and TRAF5 (O00463).\r\n\r\nExpressed by non-hematopoeitic and follicular dendritic cells, dysregulation of LTA and LTB expression on the surface on subsets of activated T and B cells and NK cells is responsible for the pathogenesis of autoimmune diseases.","predictedComplex":false,"interactors":[{"ac":"EBI-3509981","identifier":"P36941","identifierLink":"https://www.uniprot.org/uniprotkb/P36941/entry","name":"LTBR","description":"Tumor necrosis factor receptor superfamily member 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47607","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-524105","identifier":"P01374","identifierLink":"https://www.uniprot.org/uniprotkb/P01374/entry","name":"LTA","description":"Lymphotoxin-alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11471","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-524217","identifier":"Q06643","identifierLink":"https://www.uniprot.org/uniprotkb/Q06643/entry","name":"LTB","description":"Lymphotoxin-beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11471","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8962","complexName":"19S proteasome regulatory complex","organismName":"Rattus norvegicus; 10116","description":"Functions as a proteasome regulator when bound to the barrel-shaped 20S Proteasome to form the 26S Proteasome. Recognises and deubiquitinates substrates as they enter the 20S catalytic core, thereby enabling protein degradation and maintaining cellular protein homeostasis.\r\n\r\nAbundantly found as free 19S near synapses, where there is a large demand for protein turnover. Independently regulates synaptic proteins in the absence of the 20S core proteasome. Free 19S moonlights as a deubiquitinase (DUB) by binding and deubiquitynating lysine 63-ubiquitin (Lys63-ub) a non-proteasome-targeting ubiquitin linkage in AMPARs (alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor) to regulate synaptic transmission.","predictedComplex":false,"interactors":[{"ac":"EBI-22247004","identifier":"F1LMZ8","identifierLink":"https://www.uniprot.org/uniprotkb/F1LMZ8/entry","name":"Psmd11","description":"26S proteasome non-ATPase regulatory subunit 11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR10678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2640482","identifier":"Q4FZT9","identifierLink":"https://www.uniprot.org/uniprotkb/Q4FZT9/entry","name":"Psmd2","description":"26S proteasome non-ATPase regulatory subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR10943","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2640503","identifier":"B0BN93","identifierLink":"https://www.uniprot.org/uniprotkb/B0BN93/entry","name":"Psmd13","description":"26S proteasome non-ATPase regulatory subunit 13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR10539","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2640515","identifier":"A6HIT6","identifierLink":"https://www.uniprot.org/uniprotkb/A6HIT6/entry","name":"Psmd3","description":"26S proteasome non-ATPase regulatory subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-2640530","identifier":"Q9ESH1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ESH1/entry","name":"Psmd4","description":"26S proteasome non-ATPase regulatory subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-2640568","identifier":"Q5XIC6","identifierLink":"https://www.uniprot.org/uniprotkb/Q5XIC6/entry","name":"Psmd12","description":"26S proteasome non-ATPase regulatory subunit 12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR10855","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2640579","identifier":"A0A0G2JZJ1","identifierLink":"https://www.uniprot.org/uniprotkb/A0A0G2JZJ1/entry","name":"Psmd14","description":"26S proteasome non-ATPase regulatory subunit 14","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR10410","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2649804","identifier":"D4AEH3","identifierLink":"https://www.uniprot.org/uniprotkb/D4AEH3/entry","name":"Psmd7","description":"26S proteasome non-ATPase regulatory subunit 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-357586","identifier":"P62193","identifierLink":"https://www.uniprot.org/uniprotkb/P62193/entry","name":"Psmc1","description":"26S proteasome regulatory subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357761","identifier":"P62198","identifierLink":"https://www.uniprot.org/uniprotkb/P62198/entry","name":"Psmc5","description":"26S proteasome regulatory subunit 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52326001","identifier":"G3V6W6","identifierLink":"https://www.uniprot.org/uniprotkb/G3V6W6/entry","name":"Psmc6","description":"26S proteasome regulatory subunit 10B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52326078","identifier":"F1LMQ3","identifierLink":"https://www.uniprot.org/uniprotkb/F1LMQ3/entry","name":"Psmd8","description":"26S proteasome non-ATPase regulatory subunit 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR12387","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52330318","identifier":"A0A0G2K2A5","identifierLink":"https://www.uniprot.org/uniprotkb/A0A0G2K2A5/entry","name":"Uchl5","description":"Ubiquitin carboxyl-terminal hydrolase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR10589","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-915698","identifier":"O88761","identifierLink":"https://www.uniprot.org/uniprotkb/O88761/entry","name":"Psmd1","description":"26S proteasome non-ATPase regulatory subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR10943","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-918567","identifier":"Q63347","identifierLink":"https://www.uniprot.org/uniprotkb/Q63347/entry","name":"Psmc2","description":"26S proteasome regulatory subunit 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-918627","identifier":"Q63569","identifierLink":"https://www.uniprot.org/uniprotkb/Q63569/entry","name":"Psmc3","description":"26S proteasome regulatory subunit 6A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-918637","identifier":"Q63570","identifierLink":"https://www.uniprot.org/uniprotkb/Q63570/entry","name":"Psmc4","description":"26S proteasome regulatory subunit 6B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-919152","identifier":"Q6PCT9","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PCT9/entry","name":"Psmd6","description":"26S proteasome non-ATPase regulatory subunit 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-920050","identifier":"Q9JMB5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JMB5/entry","name":"Adrm1","description":"Proteasomal ubiquitin receptor ADRM1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR12225","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8964","complexName":"19S proteasome regulatory complex","organismName":"Homo sapiens; 9606","description":"The major proteasome regulator when bound to the barrel-shaped 20S Proteasome (CPX-8806) to form the 26S proteasome (single-capped, CPX-5993) or the 30S Proteasome (double-capped, CPX-9086). Recognises and deubiquitinates substrates as they enter the 20S catalytic core, thereby enabling protein degradation and maintaining cellular protein homeostasis. \r\n\r\nAbundantly found as free 19S near synapses, where there is a large demand for protein turnover. Free 19S is thought to have a moonlighting role as a deubiquitinase (DUB) and independently regulates synaptic proteins in the absence of the 20S core proteasome.\r\n\r\nThe 19S regulatory particle is comprised of 19 integral subunits including six proteasome AAA-ATPases (PSMC1-6) and 13 non-ATPase subunits.  PSMD2, PSMD4 and ADRM1 bind to conjugated ubiquitin tags on a protein, while the DUBs, USP14 and UCHL5 (and PSMD14 when bound to 20S) remove ubiquitin modifications and facilitate degradation of the conjugated substrate, thereby enabling the 26S proteasome to degrade substrates in a highly regulated ubiquitin-dependent manner, ensuring its role as the major activator for intracellular proteolysis.","predictedComplex":false,"interactors":[{"ac":"EBI-356070","identifier":"Q9UNM6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UNM6/entry","name":"PSMD13","description":"26S proteasome non-ATPase regulatory subunit 13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10539","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357598","identifier":"P62191","identifierLink":"https://www.uniprot.org/uniprotkb/P62191/entry","name":"PSMC1","description":"26S proteasome regulatory subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357622","identifier":"O43242","identifierLink":"https://www.uniprot.org/uniprotkb/O43242/entry","name":"PSMD3","description":"26S proteasome non-ATPase regulatory subunit 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10758","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357648","identifier":"Q13200","identifierLink":"https://www.uniprot.org/uniprotkb/Q13200/entry","name":"PSMD2","description":"26S proteasome non-ATPase regulatory subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10943","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357659","identifier":"P51665","identifierLink":"https://www.uniprot.org/uniprotkb/P51665/entry","name":"PSMD7","description":"26S proteasome non-ATPase regulatory subunit 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10540","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357669","identifier":"P62333","identifierLink":"https://www.uniprot.org/uniprotkb/P62333/entry","name":"PSMC6","description":"26S proteasome regulatory subunit 10B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357745","identifier":"P62195","identifierLink":"https://www.uniprot.org/uniprotkb/P62195/entry","name":"PSMC5","description":"26S proteasome regulatory subunit 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357816","identifier":"O00231","identifierLink":"https://www.uniprot.org/uniprotkb/O00231/entry","name":"PSMD11","description":"26S proteasome non-ATPase regulatory subunit 11","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357874","identifier":"Q99460","identifierLink":"https://www.uniprot.org/uniprotkb/Q99460/entry","name":"PSMD1","description":"26S proteasome non-ATPase regulatory subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10943","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359304","identifier":"P48556","identifierLink":"https://www.uniprot.org/uniprotkb/P48556/entry","name":"PSMD8","description":"26S proteasome non-ATPase regulatory subunit 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12387","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359318","identifier":"P55036","identifierLink":"https://www.uniprot.org/uniprotkb/P55036/entry","name":"PSMD4","description":"26S proteasome non-ATPase regulatory subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10223","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359701","identifier":"Q15008","identifierLink":"https://www.uniprot.org/uniprotkb/Q15008/entry","name":"PSMD6","description":"26S proteasome non-ATPase regulatory subunit 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14145","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359710","identifier":"P35998","identifierLink":"https://www.uniprot.org/uniprotkb/P35998/entry","name":"PSMC2","description":"26S proteasome regulatory subunit 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359720","identifier":"P17980","identifierLink":"https://www.uniprot.org/uniprotkb/P17980/entry","name":"PSMC3","description":"26S proteasome regulatory subunit 6A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359733","identifier":"O00232","identifierLink":"https://www.uniprot.org/uniprotkb/O00232/entry","name":"PSMD12","description":"26S proteasome non-ATPase regulatory subunit 12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10855","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-722193","identifier":"O00487","identifierLink":"https://www.uniprot.org/uniprotkb/O00487/entry","name":"PSMD14","description":"26S proteasome non-ATPase regulatory subunit 14","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10410","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743997","identifier":"P43686","identifierLink":"https://www.uniprot.org/uniprotkb/P43686/entry","name":"PSMC4","description":"26S proteasome regulatory subunit 6B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-79819","identifier":"P60896","identifierLink":"https://www.uniprot.org/uniprotkb/P60896/entry","name":"SEM1","description":"26S proteasome complex subunit SEM1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-954387","identifier":"Q16186","identifierLink":"https://www.uniprot.org/uniprotkb/Q16186/entry","name":"ADRM1","description":"Proteasomal ubiquitin receptor ADRM1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12225","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8965","complexName":"30S proteasome complex","organismName":"Rattus norvegicus; 10116","description":"Multi-enzyme complex that functions as the primary degradation machinery for the selective turnover of surplus or damaged proteins within the cell. Proteins targeted for degradation are covalently labelled with polyubiquitin chains which are recognized and removed by the proteasome. The core contains the protease active sites (chymotrypsin-like, trypsin-like and peptidylglutamyl-peptide hydrolysing) that perform the proteolysis reactions in an internal chamber. The regulatory particles act as a discriminating gateway for potential substrates.\r\n\r\nThis complex is composed of the 20S Proteasome and two 19S regulatory particles. The 19S regulatory particle (CPX-8962) is the major activator that allows the 20S Proteasome to degrade almost any protein tagged with the small protein modifier ubiquitin. The 19S recognises and deubiquitinates substrates as they enter the 20S catalytic core, thereby enabling protein degradation and maintaining cellular protein homeostasis. Attachment of the 19S to one end of the 20S forms the 26S proteasome (single-capped), and two ends, the 30S Proteasome (double-capped, this complex).\r\n\r\nWhile both 19S regulatory particles can engage with a protein substrate and be functional, it is thought that the proteasome function is more efficient if the opposite side to substrate entry side serves for peptide exit. Thus, concurrent functionality of both 19S particles may be mutually exclusive and the 30S Proteasome may function most efficiently as a single capped 26S Proteasome.","predictedComplex":false,"interactors":[{"ac":"EBI-22247004","identifier":"F1LMZ8","identifierLink":"https://www.uniprot.org/uniprotkb/F1LMZ8/entry","name":"Psmd11","description":"26S proteasome non-ATPase regulatory subunit 11","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR10678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2640482","identifier":"Q4FZT9","identifierLink":"https://www.uniprot.org/uniprotkb/Q4FZT9/entry","name":"Psmd2","description":"26S proteasome non-ATPase regulatory subunit 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR10943","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2640503","identifier":"B0BN93","identifierLink":"https://www.uniprot.org/uniprotkb/B0BN93/entry","name":"Psmd13","description":"26S proteasome non-ATPase regulatory subunit 13","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR10539","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2640515","identifier":"A6HIT6","identifierLink":"https://www.uniprot.org/uniprotkb/A6HIT6/entry","name":"Psmd3","description":"26S proteasome non-ATPase regulatory subunit 3","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-2640530","identifier":"Q9ESH1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ESH1/entry","name":"Psmd4","description":"26S proteasome non-ATPase regulatory subunit 4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-2640568","identifier":"Q5XIC6","identifierLink":"https://www.uniprot.org/uniprotkb/Q5XIC6/entry","name":"Psmd12","description":"26S proteasome non-ATPase regulatory subunit 12","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR10855","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2640579","identifier":"A0A0G2JZJ1","identifierLink":"https://www.uniprot.org/uniprotkb/A0A0G2JZJ1/entry","name":"Psmd14","description":"26S proteasome non-ATPase regulatory subunit 14","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR10410","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2649804","identifier":"D4AEH3","identifierLink":"https://www.uniprot.org/uniprotkb/D4AEH3/entry","name":"Psmd7","description":"26S proteasome non-ATPase regulatory subunit 7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-357586","identifier":"P62193","identifierLink":"https://www.uniprot.org/uniprotkb/P62193/entry","name":"Psmc1","description":"26S proteasome regulatory subunit 4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357761","identifier":"P62198","identifierLink":"https://www.uniprot.org/uniprotkb/P62198/entry","name":"Psmc5","description":"26S proteasome regulatory subunit 8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357805","identifier":"P60901","identifierLink":"https://www.uniprot.org/uniprotkb/P60901/entry","name":"Psma6","description":"Proteasome subunit alpha type-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52326001","identifier":"G3V6W6","identifierLink":"https://www.uniprot.org/uniprotkb/G3V6W6/entry","name":"Psmc6","description":"26S proteasome regulatory subunit 10B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52326078","identifier":"F1LMQ3","identifierLink":"https://www.uniprot.org/uniprotkb/F1LMQ3/entry","name":"Psmd8","description":"26S proteasome non-ATPase regulatory subunit 8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR12387","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52326153","identifier":"D3ZHW9","identifierLink":"https://www.uniprot.org/uniprotkb/D3ZHW9/entry","name":"Sem1","description":"26S proteasome complex subunit SEM1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR16771","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52326197","identifier":"P18422","identifierLink":"https://www.uniprot.org/uniprotkb/P18422/entry","name":"Psma3","description":"Proteasome subunit alpha type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-915698","identifier":"O88761","identifierLink":"https://www.uniprot.org/uniprotkb/O88761/entry","name":"Psmd1","description":"26S proteasome non-ATPase regulatory subunit 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR10943","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-916719","identifier":"P17220","identifierLink":"https://www.uniprot.org/uniprotkb/P17220/entry","name":"Psma2","description":"Proteasome subunit alpha type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-916756","identifier":"P18420","identifierLink":"https://www.uniprot.org/uniprotkb/P18420/entry","name":"Psma1","description":"Proteasome subunit alpha type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-916762","identifier":"P18421","identifierLink":"https://www.uniprot.org/uniprotkb/P18421/entry","name":"Psmb1","description":"Proteasome subunit beta type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR32194","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-916847","identifier":"P21670","identifierLink":"https://www.uniprot.org/uniprotkb/P21670/entry","name":"Psma4","description":"Proteasome subunit alpha type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-917094","identifier":"P28075","identifierLink":"https://www.uniprot.org/uniprotkb/P28075/entry","name":"Psmb5","description":"Proteasome subunit beta type-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-917288","identifier":"P34064","identifierLink":"https://www.uniprot.org/uniprotkb/P34064/entry","name":"Psma5","description":"Proteasome subunit alpha type-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-917294","identifier":"P34067","identifierLink":"https://www.uniprot.org/uniprotkb/P34067/entry","name":"Psmb4","description":"Proteasome subunit beta type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-917459","identifier":"P40112","identifierLink":"https://www.uniprot.org/uniprotkb/P40112/entry","name":"Psmb3","description":"Proteasome subunit beta type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-917465","identifier":"P40307","identifierLink":"https://www.uniprot.org/uniprotkb/P40307/entry","name":"Psmb2","description":"Proteasome subunit beta type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-917581","identifier":"P48004","identifierLink":"https://www.uniprot.org/uniprotkb/P48004/entry","name":"Psma7","description":"Proteasome subunit alpha type-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-918567","identifier":"Q63347","identifierLink":"https://www.uniprot.org/uniprotkb/Q63347/entry","name":"Psmc2","description":"26S proteasome regulatory subunit 7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-918627","identifier":"Q63569","identifierLink":"https://www.uniprot.org/uniprotkb/Q63569/entry","name":"Psmc3","description":"26S proteasome regulatory subunit 6A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-918637","identifier":"Q63570","identifierLink":"https://www.uniprot.org/uniprotkb/Q63570/entry","name":"Psmc4","description":"26S proteasome regulatory subunit 6B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR23073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-918772","identifier":"P28073","identifierLink":"https://www.uniprot.org/uniprotkb/P28073/entry","name":"Psmb6","description":"Proteasome subunit beta type-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-919152","identifier":"Q6PCT9","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PCT9/entry","name":"Psmd6","description":"26S proteasome non-ATPase regulatory subunit 6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[]},{"ac":"EBI-919930","identifier":"Q9JHW0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JHW0/entry","name":"Psmb7","description":"Proteasome subunit beta type-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-920050","identifier":"Q9JMB5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9JMB5/entry","name":"Adrm1","description":"Proteasomal ubiquitin receptor ADRM1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR12225","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9001","complexName":"PA28-gamma single-capped 20S proteasome complex","organismName":"Homo sapiens; 9606","description":"Multi-enzyme complex that functions as the primary degradation machinery for the selective turnover of surplus or damaged proteins within the cell. The core contains the protease active sites (chymotrypsin-like, trypsin-like and peptidylglutamyl-peptide hydrolyzing) that perform the proteolysis reactions in an internal chamber. Regulatory particles referred to as 'caps' act as a discriminating gateway for potential substrates.\r\n\r\nThis complex is formed upon the endogenous proteasomal activator, PA28, a 28 kDa protein binding to the 20S proteasome (CPX-8806). PA28 exists as three highly homologous isoforms, alpha, beta and gamma (Q06323, Q9UL46 and P61289 respectively), which differ significantly in their biochemical and biological properties. PA28-gamma is thought to be the most similar to the common PA28 ancestor and likely to have retained its original functions. PA28-gamma is prevalent in the nucleus and is integral to enhancing degradation rates in diverse cellular processes including cell growth and proliferation, apoptosis, chromatin structure and organization and response to DNA damage. PA28-gamma binds in an ubiquitin- and ATP-independent manner to either one (single-cap, this complex) or both ends (double-capped, CPX-9022) of the 20S Proteasome, but the efficiency of substrate processing by single and double-capped proteasomes in not known. Binding of the activator modifies the 20S peptidase and opens its outer alpha-ring gates allowing substrate entry to the antechamber. PA28-gamma also modifies the proteolytic activities of the 20S Proteasome.\r\n\r\nComplex regulates protein degradation either in a regulated manner upon specific molecular cues or acts on damaged and disordered proteins. Plays a key role under oxidative stress conditions to degrade damaged and unfolded proteins. Promotes proteasomal degradation of several important regulatory proteins including SRC-3 and the tumour suppressor p53, as well as growth-related proteins such as the cyclin-dependent kinase inhibitors p21, p19 and p16 and c-Myc.\r\n\r\nPA28-gamma subunit is a key regulator of cell growth and proliferation and apoptosis. Dysregulation of PA28-gamma results in induction of malignant tumours in several cancers. PA28-gamma promotes the degradation of multiple proteins including p53 via MDM2-mediated interaction but over-expression of PA28-gamma leads to carcinogenesis through its ability to modulate the Wnt/b-catenin pathway. \r\n\r\nPA28-gamma in association with PA200, plays a key role in male fertility by their ability to regulate sperm motility.","predictedComplex":false,"interactors":[{"ac":"EBI-348380","identifier":"P25788","identifierLink":"https://www.uniprot.org/uniprotkb/P25788/entry","name":"PSMA3","description":"Proteasome subunit alpha type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355475","identifier":"P28066","identifierLink":"https://www.uniprot.org/uniprotkb/P28066/entry","name":"PSMA5","description":"Proteasome subunit alpha type-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355546","identifier":"P61289","identifierLink":"https://www.uniprot.org/uniprotkb/P61289/entry","name":"PSME3","description":"Proteasome activator complex subunit 3","stochiometry":"minValue: 7, maxValue: 7","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10660","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357793","identifier":"P60900","identifierLink":"https://www.uniprot.org/uniprotkb/P60900/entry","name":"PSMA6","description":"Proteasome subunit alpha type-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357828","identifier":"P28074","identifierLink":"https://www.uniprot.org/uniprotkb/P28074/entry","name":"PSMB5","description":"Proteasome subunit beta type-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359288","identifier":"P28072","identifierLink":"https://www.uniprot.org/uniprotkb/P28072/entry","name":"PSMB6","description":"Proteasome subunit beta type-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359310","identifier":"P25789","identifierLink":"https://www.uniprot.org/uniprotkb/P25789/entry","name":"PSMA4","description":"Proteasome subunit alpha type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359335","identifier":"P49721","identifierLink":"https://www.uniprot.org/uniprotkb/P49721/entry","name":"PSMB2","description":"Proteasome subunit beta type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359352","identifier":"P25786","identifierLink":"https://www.uniprot.org/uniprotkb/P25786/entry","name":"PSMA1","description":"Proteasome subunit alpha type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372273","identifier":"P20618","identifierLink":"https://www.uniprot.org/uniprotkb/P20618/entry","name":"PSMB1","description":"Proteasome subunit beta type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32194","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603262","identifier":"P25787","identifierLink":"https://www.uniprot.org/uniprotkb/P25787/entry","name":"PSMA2","description":"Proteasome subunit alpha type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603272","identifier":"O14818","identifierLink":"https://www.uniprot.org/uniprotkb/O14818/entry","name":"PSMA7","description":"Proteasome subunit alpha type-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603319","identifier":"Q99436","identifierLink":"https://www.uniprot.org/uniprotkb/Q99436/entry","name":"PSMB7","description":"Proteasome subunit beta type-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603340","identifier":"P49720","identifierLink":"https://www.uniprot.org/uniprotkb/P49720/entry","name":"PSMB3","description":"Proteasome subunit beta type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603350","identifier":"P28070","identifierLink":"https://www.uniprot.org/uniprotkb/P28070/entry","name":"PSMB4","description":"Proteasome subunit beta type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9002","complexName":"PA28-alphabeta single-capped 20S proteasome complex","organismName":"Homo sapiens; 9606","description":"Multi-enzyme complex that functions as the primary degradation machinery for the selective turnover of surplus or damaged proteins within the cell. The core contains the protease active sites (chymotrypsin-like, trypsin-like and peptidylglutamyl-peptide hydrolyzing) that perform the proteolysis reactions in an internal chamber. Regulatory particles referred to as 'caps' act as a discriminating gateway for potential substrates.\r\n\r\nThis complex is formed upon the endogenous proteasomal activator, PA28, a 28 kDa protein binding to the 20S proteasome (CPX-8806). PA28 exists as three highly homologous isoforms, alpha, beta and gamma (Q06323, Q9UL46 and P61289 respectively). The three subunits differ significantly in their biochemical and biological properties. PA28-alpha and PA28-beta favour the release of peptide products by the proteasome and are specifically involved in optimizing MHC class 1 antigen presentation. PA28-alpha and PA28-beta bind in an ATP-independent manner to either one (single-cap, this complex) or both ends (double-capped, CPX-8842) of the of the 20S proteasome, but the efficiency of substrate processing by single and double-capped proteasomes in not known. Binding of the activator modifies the 20S peptidase and opens its outer alpha-ring gates allowing substrate entry to the antechamber through an internal activation loop. \r\n\r\nRegulates protein degradation either in a regulated manner upon specific molecular cues or acts on damaged and disordered proteins. Plays a key role under oxidative stress conditions to degrade damaged and unfolded proteins and is up-regulated by interferon-gamma during antigen presentation.\r\n\r\nTumorigenesis of PA28-alpha is unclear but up-regulation of the subunit is associated with several cancers, including ovarian, prostate and oral squamous cell carcinoma (OSCC), and interestingly, silencing it suppressed OSCC cell growth and metastasis.","predictedComplex":false,"interactors":[{"ac":"EBI-348380","identifier":"P25788","identifierLink":"https://www.uniprot.org/uniprotkb/P25788/entry","name":"PSMA3","description":"Proteasome subunit alpha type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355475","identifier":"P28066","identifierLink":"https://www.uniprot.org/uniprotkb/P28066/entry","name":"PSMA5","description":"Proteasome subunit alpha type-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357793","identifier":"P60900","identifierLink":"https://www.uniprot.org/uniprotkb/P60900/entry","name":"PSMA6","description":"Proteasome subunit alpha type-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357828","identifier":"P28074","identifierLink":"https://www.uniprot.org/uniprotkb/P28074/entry","name":"PSMB5","description":"Proteasome subunit beta type-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359288","identifier":"P28072","identifierLink":"https://www.uniprot.org/uniprotkb/P28072/entry","name":"PSMB6","description":"Proteasome subunit beta type-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359310","identifier":"P25789","identifierLink":"https://www.uniprot.org/uniprotkb/P25789/entry","name":"PSMA4","description":"Proteasome subunit alpha type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359335","identifier":"P49721","identifierLink":"https://www.uniprot.org/uniprotkb/P49721/entry","name":"PSMB2","description":"Proteasome subunit beta type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359352","identifier":"P25786","identifierLink":"https://www.uniprot.org/uniprotkb/P25786/entry","name":"PSMA1","description":"Proteasome subunit alpha type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372273","identifier":"P20618","identifierLink":"https://www.uniprot.org/uniprotkb/P20618/entry","name":"PSMB1","description":"Proteasome subunit beta type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32194","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603262","identifier":"P25787","identifierLink":"https://www.uniprot.org/uniprotkb/P25787/entry","name":"PSMA2","description":"Proteasome subunit alpha type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603272","identifier":"O14818","identifierLink":"https://www.uniprot.org/uniprotkb/O14818/entry","name":"PSMA7","description":"Proteasome subunit alpha type-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603319","identifier":"Q99436","identifierLink":"https://www.uniprot.org/uniprotkb/Q99436/entry","name":"PSMB7","description":"Proteasome subunit beta type-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603340","identifier":"P49720","identifierLink":"https://www.uniprot.org/uniprotkb/P49720/entry","name":"PSMB3","description":"Proteasome subunit beta type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603350","identifier":"P28070","identifierLink":"https://www.uniprot.org/uniprotkb/P28070/entry","name":"PSMB4","description":"Proteasome subunit beta type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712149","identifier":"Q06323","identifierLink":"https://www.uniprot.org/uniprotkb/Q06323/entry","name":"PSME1","description":"Proteasome activator complex subunit 1","stochiometry":"minValue: 3, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10660","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-741630","identifier":"Q9UL46","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UL46/entry","name":"PSME2","description":"Proteasome activator complex subunit 2","stochiometry":"minValue: 3, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10660","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9003","complexName":"20S immunoproteasome complex","organismName":"Homo sapiens; 9606","description":"Multi-enzyme complex that functions as the primary degradation machinery for the selective turnover of surplus or damaged proteins within the cell. \r\n\r\nFound only in jawed vertebrates, formed upon exposure to inflammatory stimuli such as interferon-gamma (IFN-g) or tumour necrosis factor, the proteolytic activity of the 20S immunoproteasome (20Si) differs from its standard 20S (CPX-8806) counterpart with the constitutive subunits beta-1 (P28072), beta-2 (Q99436), and beta-5 (P28074) replaced by its immune counterparts beta-1i (P28065), beta-2i (P40306), and beta-5i (P28062), respectively. \r\n\r\nConstitutively expressed in lymphoid tissues at high levels but requires induction by pro-inflammatory cytokines such as IFN-g in non-lymphoid tissues. Has lower caspase-like activity than the standard 20S Proteasome but a higher chymotrypsin-like and trypsin-like activity, resulting in alternative cleavage of proteins, to generate peptides with hydrophobic or basic C-termini, which are preferred by major histocompatibility complex (MHC) class I.\r\n\r\nExpressed by medullary thymic epithelial cells (mTECs), which contribute to the establishment of self-tolerance in T cells. Implicated in proteasome-mediated generation of CD8+ T cell epitopes thereby expanding the diversity of the epitopes presented by MHC class I molecules through a mechanism known as PCPS (proteasome-catalyzed peptide splicing), with up to one-third of self-peptides presented on the cell surface generated by PCPS . Plays a role in macrophage activation and T-cell differentiation, as well as the differentiation of non-immune cells like skeletal muscle cells, and the preservation of general homeostasis. \r\n\r\nImplicated in disorders such as cancer, neurodegerative and autoimmune diseases. Immunoproteasome-specific inhibitors targeting beta-5i have demonstrated some success at the pre-clinical stage for the treatment of diseases such as colitis, colitis-associated cancer and rheumatoid arthritis.","predictedComplex":false,"interactors":[{"ac":"EBI-348380","identifier":"P25788","identifierLink":"https://www.uniprot.org/uniprotkb/P25788/entry","name":"PSMA3","description":"Proteasome subunit alpha type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355475","identifier":"P28066","identifierLink":"https://www.uniprot.org/uniprotkb/P28066/entry","name":"PSMA5","description":"Proteasome subunit alpha type-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357793","identifier":"P60900","identifierLink":"https://www.uniprot.org/uniprotkb/P60900/entry","name":"PSMA6","description":"Proteasome subunit alpha type-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359310","identifier":"P25789","identifierLink":"https://www.uniprot.org/uniprotkb/P25789/entry","name":"PSMA4","description":"Proteasome subunit alpha type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359335","identifier":"P49721","identifierLink":"https://www.uniprot.org/uniprotkb/P49721/entry","name":"PSMB2","description":"Proteasome subunit beta type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359352","identifier":"P25786","identifierLink":"https://www.uniprot.org/uniprotkb/P25786/entry","name":"PSMA1","description":"Proteasome subunit alpha type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372273","identifier":"P20618","identifierLink":"https://www.uniprot.org/uniprotkb/P20618/entry","name":"PSMB1","description":"Proteasome subunit beta type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32194","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372294","identifier":"P28062","identifierLink":"https://www.uniprot.org/uniprotkb/P28062/entry","name":"PSMB8","description":"Proteasome subunit beta type-8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603262","identifier":"P25787","identifierLink":"https://www.uniprot.org/uniprotkb/P25787/entry","name":"PSMA2","description":"Proteasome subunit alpha type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603272","identifier":"O14818","identifierLink":"https://www.uniprot.org/uniprotkb/O14818/entry","name":"PSMA7","description":"Proteasome subunit alpha type-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603300","identifier":"P28065","identifierLink":"https://www.uniprot.org/uniprotkb/P28065/entry","name":"PSMB9","description":"Proteasome subunit beta type-9","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603329","identifier":"P40306","identifierLink":"https://www.uniprot.org/uniprotkb/P40306/entry","name":"PSMB10","description":"Proteasome subunit beta type-10","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603340","identifier":"P49720","identifierLink":"https://www.uniprot.org/uniprotkb/P49720/entry","name":"PSMB3","description":"Proteasome subunit beta type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603350","identifier":"P28070","identifierLink":"https://www.uniprot.org/uniprotkb/P28070/entry","name":"PSMB4","description":"Proteasome subunit beta type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9004","complexName":"20S thymoproteasome complex","organismName":"Homo sapiens; 9606","description":"Multi-enzyme complex that functions as the primary degradation machinery for the selective turnover of surplus or damaged proteins within the cell. \r\n\r\nAn immune-type proteasome expressed exclusively and constitutively expressed in the cortex of the thymus by cortical thymic epithelial cells (cTECs). The beta-5i (P28062) subunit is replaced by the cTEC-specific beta-5t (A5LHX3) subunit  along with beta-1i (P28065) and beta-2i (P40306) subunits.. The thymoproteasome is essential for the optimal production and repertoire formation of CD8+ cells, and their homeostasis. Thymoproteasome-generated self-peptides associated with \r\nMHC class I molecules expressed by cTECs are thought to contribute to this positive selection of CD8+ cells.\r\n\r\nSpecific to the thymoproteasome, the beta-5t subunit is a useful diagnostic marker in tracking disease progression of certain thymic epthelial tumours.","predictedComplex":false,"interactors":[{"ac":"EBI-19951687","identifier":"A5LHX3","identifierLink":"https://www.uniprot.org/uniprotkb/A5LHX3/entry","name":"PSMB11","description":"Proteasome subunit beta type-11","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348380","identifier":"P25788","identifierLink":"https://www.uniprot.org/uniprotkb/P25788/entry","name":"PSMA3","description":"Proteasome subunit alpha type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355475","identifier":"P28066","identifierLink":"https://www.uniprot.org/uniprotkb/P28066/entry","name":"PSMA5","description":"Proteasome subunit alpha type-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357793","identifier":"P60900","identifierLink":"https://www.uniprot.org/uniprotkb/P60900/entry","name":"PSMA6","description":"Proteasome subunit alpha type-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359310","identifier":"P25789","identifierLink":"https://www.uniprot.org/uniprotkb/P25789/entry","name":"PSMA4","description":"Proteasome subunit alpha type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359335","identifier":"P49721","identifierLink":"https://www.uniprot.org/uniprotkb/P49721/entry","name":"PSMB2","description":"Proteasome subunit beta type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359352","identifier":"P25786","identifierLink":"https://www.uniprot.org/uniprotkb/P25786/entry","name":"PSMA1","description":"Proteasome subunit alpha type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372273","identifier":"P20618","identifierLink":"https://www.uniprot.org/uniprotkb/P20618/entry","name":"PSMB1","description":"Proteasome subunit beta type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32194","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603262","identifier":"P25787","identifierLink":"https://www.uniprot.org/uniprotkb/P25787/entry","name":"PSMA2","description":"Proteasome subunit alpha type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603272","identifier":"O14818","identifierLink":"https://www.uniprot.org/uniprotkb/O14818/entry","name":"PSMA7","description":"Proteasome subunit alpha type-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603300","identifier":"P28065","identifierLink":"https://www.uniprot.org/uniprotkb/P28065/entry","name":"PSMB9","description":"Proteasome subunit beta type-9","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603329","identifier":"P40306","identifierLink":"https://www.uniprot.org/uniprotkb/P40306/entry","name":"PSMB10","description":"Proteasome subunit beta type-10","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603340","identifier":"P49720","identifierLink":"https://www.uniprot.org/uniprotkb/P49720/entry","name":"PSMB3","description":"Proteasome subunit beta type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603350","identifier":"P28070","identifierLink":"https://www.uniprot.org/uniprotkb/P28070/entry","name":"PSMB4","description":"Proteasome subunit beta type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9021","complexName":"20S spermatoproteasome complex","organismName":"Homo sapiens; 9606","description":"Multi-enzyme complex that functions as the primary degradation machinery for the selective turnover of surplus or damaged proteins within the cell. \r\n\r\nSpecifically found in the testis, spermatoproteasomes (s20S) are comprised of the constitutive 20S Proteasome subunits (alpha 1-3 and 5-6 and beta 1-7), as well as a novel alpha-4s subunit (Q8TAA3) in lieu of the alpha-4 subunit (O14818). The s20S associates with proteasomal activators to form large (19S-s20S-PA200, hybrid) and small s20S-PA200 (single-capped), PA200-s20S-PA200 (double-capped) spermatoproteasomal complexes. \r\n\r\nMammalian s20S are known to degrade acetylated histones through association with PA200 (Q14997) and play a role in DNA damage repair in spermatocytes and the maturation of spermatids. Promotes acetylation-dependent degradation of histones through PA200's BRDL (bromodomain like) region, thereby participating actively in the exchange of histones during spermatogenesis. Essential for the degradation of meiotic proteins RAD51 and RPA1 at late prophase I and the progression of meiosis I during spermatogenesis. Localizes to the synaptonemal complex, a 'zipper-like' structure that holds homologous chromosome pairs in synapsis during meiotic prophase I.\r\n\r\nLoss of PA200 in mouse models revealed defects in spermatogenesis in meiotic spermatocytes as well as during postmeiotic haploid spermatids maturation, with a marked reduction in male fertility.","predictedComplex":false,"interactors":[{"ac":"EBI-16579257","identifier":"Q8TAA3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAA3/entry","name":"PSMA8","description":"Proteasome subunit alpha-type 8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348380","identifier":"P25788","identifierLink":"https://www.uniprot.org/uniprotkb/P25788/entry","name":"PSMA3","description":"Proteasome subunit alpha type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355475","identifier":"P28066","identifierLink":"https://www.uniprot.org/uniprotkb/P28066/entry","name":"PSMA5","description":"Proteasome subunit alpha type-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357793","identifier":"P60900","identifierLink":"https://www.uniprot.org/uniprotkb/P60900/entry","name":"PSMA6","description":"Proteasome subunit alpha type-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357828","identifier":"P28074","identifierLink":"https://www.uniprot.org/uniprotkb/P28074/entry","name":"PSMB5","description":"Proteasome subunit beta type-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359288","identifier":"P28072","identifierLink":"https://www.uniprot.org/uniprotkb/P28072/entry","name":"PSMB6","description":"Proteasome subunit beta type-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359310","identifier":"P25789","identifierLink":"https://www.uniprot.org/uniprotkb/P25789/entry","name":"PSMA4","description":"Proteasome subunit alpha type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359335","identifier":"P49721","identifierLink":"https://www.uniprot.org/uniprotkb/P49721/entry","name":"PSMB2","description":"Proteasome subunit beta type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359352","identifier":"P25786","identifierLink":"https://www.uniprot.org/uniprotkb/P25786/entry","name":"PSMA1","description":"Proteasome subunit alpha type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372273","identifier":"P20618","identifierLink":"https://www.uniprot.org/uniprotkb/P20618/entry","name":"PSMB1","description":"Proteasome subunit beta type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32194","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603262","identifier":"P25787","identifierLink":"https://www.uniprot.org/uniprotkb/P25787/entry","name":"PSMA2","description":"Proteasome subunit alpha type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603319","identifier":"Q99436","identifierLink":"https://www.uniprot.org/uniprotkb/Q99436/entry","name":"PSMB7","description":"Proteasome subunit beta type-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603340","identifier":"P49720","identifierLink":"https://www.uniprot.org/uniprotkb/P49720/entry","name":"PSMB3","description":"Proteasome subunit beta type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603350","identifier":"P28070","identifierLink":"https://www.uniprot.org/uniprotkb/P28070/entry","name":"PSMB4","description":"Proteasome subunit beta type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9022","complexName":"PA28-gamma double-capped 20S proteasome complex","organismName":"Homo sapiens; 9606","description":"Multi-enzyme complex that functions as the primary degradation machinery for the selective turnover of surplus or damaged proteins within the cell. The core contains the protease active sites (chymotrypsin-like, trypsin-like and peptidylglutamyl-peptide hydrolyzing) that perform the proteolysis reactions in an internal chamber. Regulatory particles referred to as 'caps' act as a discriminating gateway for potential substrates.\r\n\r\nThis complex is formed upon the endogenous proteasomal activator, PA28, a 28 kDa protein binding to the 20S proteasome (CPX-8806). PA28 exists as three highly homologous isoforms, alpha, beta and gamma (Q06323, Q9UL46 and P61289 respectively), which differ significantly in their biochemical and biological properties. PA28-gamma is thought to be the most similar to the common PA28 ancestor and likely to have retained its original functions. PA28-gamma is prevalent in the nucleus and is integral to enhancing degradation rates in diverse cellular processes including cell growth and proliferation, apoptosis, chromatin structure and organization and response to DNA damage. PA28-gamma binds in an ubiquitin- and ATP-independent manner to either one (single-cap, CPX-9001) or both ends (double-capped, this complex) of the 20S Proteasome, but the efficiency of substrate processing by single and double-capped proteasomes in not known. Binding of the activator modifies the 20S peptidase and opens its outer alpha-ring gates allowing substrate entry to the antechamber. PA28 also modifies the proteolytic activities of the 20S Proteasome.\r\n\r\nComplex regulates protein degradation either in a regulated manner upon specific molecular cues or acts on damaged and disordered proteins. Plays a key role under oxidative stress conditions to degrade damaged and unfolded proteins. Promotes proteasomal degradation of several important regulatory proteins including SRC-3 and the tumour suppressor p53, as well as growth-related proteins such as the cyclin-dependent kinase inhibitors p21, p19 and p16 and c-Myc.\r\n\r\nPA28-gamma subunit is a key regulator of cell growth and proliferation and apoptosis. Dysregulation of PA28-gamma results in induction of malignant tumours in several cancers. PA28-gamma promotes the degradation of multiple proteins including p53 via MDM2-mediated interaction but over-expression of PA28-gamma leads to carcinogenesis through its ability to modulate the Wnt/b-catenin pathway.\r\n\r\nPA28-gamma in association with PA200, plays a key role in male fertility by their ability to regulate sperm motility.","predictedComplex":false,"interactors":[{"ac":"EBI-348380","identifier":"P25788","identifierLink":"https://www.uniprot.org/uniprotkb/P25788/entry","name":"PSMA3","description":"Proteasome subunit alpha type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355475","identifier":"P28066","identifierLink":"https://www.uniprot.org/uniprotkb/P28066/entry","name":"PSMA5","description":"Proteasome subunit alpha type-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355546","identifier":"P61289","identifierLink":"https://www.uniprot.org/uniprotkb/P61289/entry","name":"PSME3","description":"Proteasome activator complex subunit 3","stochiometry":"minValue: 14, maxValue: 14","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10660","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357793","identifier":"P60900","identifierLink":"https://www.uniprot.org/uniprotkb/P60900/entry","name":"PSMA6","description":"Proteasome subunit alpha type-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357828","identifier":"P28074","identifierLink":"https://www.uniprot.org/uniprotkb/P28074/entry","name":"PSMB5","description":"Proteasome subunit beta type-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359288","identifier":"P28072","identifierLink":"https://www.uniprot.org/uniprotkb/P28072/entry","name":"PSMB6","description":"Proteasome subunit beta type-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359310","identifier":"P25789","identifierLink":"https://www.uniprot.org/uniprotkb/P25789/entry","name":"PSMA4","description":"Proteasome subunit alpha type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359335","identifier":"P49721","identifierLink":"https://www.uniprot.org/uniprotkb/P49721/entry","name":"PSMB2","description":"Proteasome subunit beta type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359352","identifier":"P25786","identifierLink":"https://www.uniprot.org/uniprotkb/P25786/entry","name":"PSMA1","description":"Proteasome subunit alpha type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372273","identifier":"P20618","identifierLink":"https://www.uniprot.org/uniprotkb/P20618/entry","name":"PSMB1","description":"Proteasome subunit beta type-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32194","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603262","identifier":"P25787","identifierLink":"https://www.uniprot.org/uniprotkb/P25787/entry","name":"PSMA2","description":"Proteasome subunit alpha type-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603272","identifier":"O14818","identifierLink":"https://www.uniprot.org/uniprotkb/O14818/entry","name":"PSMA7","description":"Proteasome subunit alpha type-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603319","identifier":"Q99436","identifierLink":"https://www.uniprot.org/uniprotkb/Q99436/entry","name":"PSMB7","description":"Proteasome subunit beta type-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603340","identifier":"P49720","identifierLink":"https://www.uniprot.org/uniprotkb/P49720/entry","name":"PSMB3","description":"Proteasome subunit beta type-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603350","identifier":"P28070","identifierLink":"https://www.uniprot.org/uniprotkb/P28070/entry","name":"PSMB4","description":"Proteasome subunit beta type-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9042","complexName":"Mitochondrial 2-oxoglutarate dehydrogenase complex, ODGH variant","organismName":"Drosophila melanogaster; 7227","description":"Catalyzes the oxidative decarboxylation of alpha-ketoglutarate to succinyl-CoA, NADH and CO2 in the tricarboxylic acid (TCA) cycle. Succinyl-CoA is then converted to succinate by succinyl-CoA synthetase. The enzyme complex thus generates metabolites and reduced electron carriers for oxidative phosphorylation.","predictedComplex":false,"interactors":[{"ac":"EBI-110434","identifier":"Q9VVL7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVL7/entry","name":"Dld","description":"Dihydrolipoyl dehydrogenase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22912","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16416616","identifier":"CHEBI:83088","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:83088","name":"(r)-lipoate","description":"(R)-lipoate","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-195174","identifier":"Q9VGQ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VGQ1/entry","name":"Dlst","description":"Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR43416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52360856","identifier":"A8JNU6","identifierLink":"https://www.uniprot.org/uniprotkb/A8JNU6/entry","name":"Ogdh1","description":"2-oxoglutarate dehydrogenase, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23152","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9691551","identifier":"CHEBI:58937","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58937","name":"thiamine(1+) diphosphate(3-)","description":"thiamine(1+) diphosphate(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-9043","complexName":"Mitochondrial 2-oxoglutarate dehydrogenase complex, CG33791 variant","organismName":"Drosophila melanogaster; 7227","description":"Catalyzes the oxidative decarboxylation of alpha-ketoglutarate to succinyl-CoA, NADH and CO2 in the tricarboxylic acid (TCA) cycle. Succinyl-CoA is then converted to succinate by succinyl-CoA synthetase. The enzyme complex thus generates metabolites and reduced electron carriers for oxidative phosphorylation.","predictedComplex":false,"interactors":[{"ac":"EBI-110434","identifier":"Q9VVL7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVL7/entry","name":"Dld","description":"Dihydrolipoyl dehydrogenase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22912","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16416616","identifier":"CHEBI:83088","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:83088","name":"(r)-lipoate","description":"(R)-lipoate","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-195174","identifier":"Q9VGQ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VGQ1/entry","name":"Dlst","description":"Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR43416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3405854","identifier":"Q95T35","identifierLink":"https://www.uniprot.org/uniprotkb/Q95T35/entry","name":"Ogdh2","description":"2-oxoglutarate dehydrogenase, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23152","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9691551","identifier":"CHEBI:58937","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58937","name":"thiamine(1+) diphosphate(3-)","description":"thiamine(1+) diphosphate(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-9044","complexName":"Mitochondrial 2-oxoglutarate dehydrogenase complex,CG1544 variant","organismName":"Drosophila melanogaster; 7227","description":"Catalyzes the oxidative decarboxylation of alpha-ketoglutarate to succinyl-CoA, NADH and CO2 in the tricarboxylic acid (TCA) cycle. Succinyl-CoA is then converted to succinate by succinyl-CoA synthetase. The enzyme complex thus generates metabolites and reduced electron carriers for oxidative phosphorylation.","predictedComplex":false,"interactors":[{"ac":"EBI-110434","identifier":"Q9VVL7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVL7/entry","name":"Dld","description":"Dihydrolipoyl dehydrogenase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR22912","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16416616","identifier":"CHEBI:83088","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:83088","name":"(r)-lipoate","description":"(R)-lipoate","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-166909","identifier":"Q9VA02","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VA02/entry","name":"Oadh","description":"Probable 2-oxoadipate dehydrogenase complex component E1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23152","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-195174","identifier":"Q9VGQ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VGQ1/entry","name":"Dlst","description":"Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR43416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9691551","identifier":"CHEBI:58937","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58937","name":"thiamine(1+) diphosphate(3-)","description":"thiamine(1+) diphosphate(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-9061","complexName":"Mitochondrial 2-oxoglutarate dehydrogenase complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the oxidative decarboxylation of alpha-ketoglutarate to succinyl-CoA, NADH and CO2 in the tricarboxylic acid (TCA) cycle. 2-oxoglutarate is decarboxylated by the thiamine pyrophosphate (TPP)-containing E1 OGDH and the resulting 2-succinyl intermediate is transferred to the flexible lipoyl domain of E2 DLST. DLST transfers the succinyl functional group from its lipoyl domain onto CoA-SH generating succinyl-CoA. In a final reaction, the lipoyl domain of DLST is re-oxidized by E3 DLD, a FAD-containing subunit that transfers electrons to NAD+ producing NADH Succinyl-CoA is then converted to succinate by succinyl-CoA synthetase. The enzyme complex thus generates metabolites and reduced electron carriers for oxidative phosphorylation.","predictedComplex":false,"interactors":[{"ac":"EBI-11020727","identifier":"P82909","identifierLink":"https://www.uniprot.org/uniprotkb/P82909/entry","name":"KGD4","description":"Alpha-ketoglutarate dehydrogenase component 4","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31601","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-351007","identifier":"P36957","identifierLink":"https://www.uniprot.org/uniprotkb/P36957/entry","name":"DLST","description":"Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial","stochiometry":"minValue: 24, maxValue: 24","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353366","identifier":"P09622","identifierLink":"https://www.uniprot.org/uniprotkb/P09622/entry","name":"DLD","description":"Dihydrolipoyl dehydrogenase, mitochondrial","stochiometry":"minValue: 12, maxValue: 12","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22912","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-747213","identifier":"Q02218","identifierLink":"https://www.uniprot.org/uniprotkb/Q02218/entry","name":"OGDH","description":"2-oxoglutarate dehydrogenase complex component E1","stochiometry":"minValue: 16, maxValue: 16","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23152","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":"minValue: 12, maxValue: 12","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9691551","identifier":"CHEBI:58937","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58937","name":"thiamine(1+) diphosphate(3-)","description":"thiamine(1+) diphosphate(3-)","stochiometry":"minValue: 16, maxValue: 16","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-10261","complexName":"Interleukin-20 receptor-ligand type 2 complex","organismName":"Homo sapiens; 9606","description":"Pleiotropic cytokine-receptor complex which plays a role in regulating tissue inflammation, angiogenesis, hemopoiesis, and epidermal cell and keratinocyte differentiation  The bioactive complex is primarily formed through crosstalk between IL20 cytokine producing immune cells and receptor complex expressing epthelial cells. Complex formation results in the transphosphorylation of JAK1 and TYK2, which in turn leads to the phosphorylation and activation of transcription factors STAT3 which subsequently translocates into the nucleus where it induces the transcription of target genes.\r\n\r\nThe restricted expression pattern of the receptors which bind IL20 subfamily of cytokines (IL19, IL20, IL22, IL24 and IL26) determines their unique biology and distinguishes them from the larger family of IL10 members. This also underlies their complex role in the pathophysiology of diseases such as IBD, where IL22RA1 and IL22 (Q9GZX6) are implicated but IL20 is not.","predictedComplex":false,"interactors":[{"ac":"EBI-14022785","identifier":"Q9NYY1-PRO_0000015381","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NYY1-PRO_0000015381/entry","name":"IL20","description":"Interleukin-20","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-14022792","identifier":"Q6UXL0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6UXL0/entry","name":"IL20RB","description":"Interleukin-20 receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3940749","identifier":"Q8N6P7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N6P7/entry","name":"IL22RA1","description":"Interleukin-22 receptor subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-833","complexName":"Interleukin-21 receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Transmembrane complex formed on the binding of an extracellular interleukin-21 (IL21) to its receptor. Ligand binding results in the assembly of the complete complex where signalling is dependent upon IL21 binding to the unique ligand-binding IL21R and the common-gamma chain receptor, IL2RG. IL21R and IL2RG dimerization leads to the transphosphorylation of Janus kinases, JAK1 and JAK3, which in turn leads to the phosphorylation and activation of transcription factors, Signal transducer and activator of transcription 3, STAT3 and, to a lesser extent, STAT1 and STAT5, which subsequently translocate into the nucleus where they induce the transcription of target genes. In addition to the JAK/STAT pathway, IL21 also signals via the phosphoinositide 3-kinase (PI3K) and mitogen-activated protein kinase (MAPK) pathways.\r\n\r\nIL21 mediates signalling through the IL21 receptor, exerting pleiotropic effects on B, CD4 T cells, cytotoxic CD8 T and natural killer (NK) cells. IL21 activates T follicular helper cells and B cells to promote germinal centre response and thereby the formation of immunological memory.\r\n\r\nImplicated in multiple autoimmune disorders including systemic lupus erythematosus, rheumatoid arthritis, multiple sclerosis and inflammatory bowel disease, but capable of stimulating antiviral and antitumor responses.\r\nIL21 signalling strength correlates with antibody production and IL21 signalling is considered important in antibody production post-immunisation.","predictedComplex":false,"interactors":[{"ac":"EBI-12558959","identifier":"Q9HBE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HBE5/entry","name":"IL21R","description":"Interleukin-21 receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23037","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6595560","identifier":"Q9HBE4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HBE4/entry","name":"IL21","description":"Interleukin-21","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14356","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-80475","identifier":"P31785","identifierLink":"https://www.uniprot.org/uniprotkb/P31785/entry","name":"IL2RG","description":"Cytokine receptor common subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10306","complexName":"Interleukin-22 receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Transmembrane proinflammatory cytokine receptor complex. Primarily impacts non-hematopoietic epithelial cells and fiborblasts where it has a profound impact on tissue regeneration post injury. IL22 function is regulated by the restricted expression of its receptor, IL22RA1 on epithelial cells and some monoctyic subsets. IL22RA2 (Q969J5), a soluble form of IL22RA1 also binds IL22 and antagonize the effector functions of IL22. IL22 signals through the JAK-STAT pathway, utilizing JAK1/Tyk2 and primarily STAT3, but it can also activate the MAPK pathways.\r\n\r\nElevated levels of IL22 expression have been implicated in the pathology of malignancy and psoriasis.","predictedComplex":false,"interactors":[{"ac":"EBI-11175900","identifier":"Q08334","identifierLink":"https://www.uniprot.org/uniprotkb/Q08334/entry","name":"IL10RB","description":"Interleukin-10 receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3940749","identifier":"Q8N6P7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N6P7/entry","name":"IL22RA1","description":"Interleukin-22 receptor subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8040250","identifier":"Q9GZX6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9GZX6/entry","name":"IL22","description":"Interleukin-22","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48488","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-383","complexName":"Interleukin-23 receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Receptor complex that activates and stimulates proliferation of a wide range of lymphocytes, in particular memory T cells and Th17 cells. The IL23 ligand complex (CPX-3290) binds the receptors chains IL12RB1 and IL23R which are associated with the kinases TYK2 and JAK2, respectively. Transphosphorylation of IL23R and the JAK-family kinases initiates the JAK-STAT signaling cascade via phosphorylation and heterodimerisation of STAT3 and STAT4 (P40763/Q14765). This ultimately leads to the activation of transcription of interferon-gamma or Interleukin-17. Associated with the pathogenesis of autoimmune inflammations, including rheumatoid and Lyme arthritis, multiple sclerosis, psoriasis, and inflammatory bowel disease as well as mycobacterial diseases of varying severity, primarily bacillus Calmette-Guerin and Salmonella infections.","predictedComplex":false,"interactors":[{"ac":"EBI-11665075","identifier":"P29460-PRO_0000010930","identifierLink":"https://www.uniprot.org/uniprotkb/P29460-PRO_0000010930/entry","name":"IL12B","description":"Interleukin-12 subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-11665249","identifier":"Q9NPF7-PRO_0000259488","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPF7-PRO_0000259488/entry","name":"IL23A","description":"Interleukin-23 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-11665910","identifier":"Q5VWK5-PRO_0000268662","identifierLink":"https://www.uniprot.org/uniprotkb/Q5VWK5-PRO_0000268662/entry","name":"IL23R","description":"Interleukin-23 receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-11665915","identifier":"P42701-PRO_0000010917","identifierLink":"https://www.uniprot.org/uniprotkb/P42701-PRO_0000010917/entry","name":"IL12RB1","description":"Interleukin-12 receptor subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-10310","complexName":"Interleukin-24 receptor-ligand complex, type 1","organismName":"Homo sapiens; 9606","description":"Pleiotropic cytokine-receptor complex with diverse roles in immune response, tissue homeostasis, host defense, and oncogenesis. Cytokine binding to its receptor complex initiates signalling, primarily triggering the JAK/STAT pathway recruiting JAK1/Tyk2 and STAT1(P42224) and STAT3(P40763) to mediate cell differentiation, proliferation and apoptosis, but it can also utilise the MAPK pathway to mediate tumour suppressive effects.\r\n\r\nIL24 is expressed in a variety of immune cells as well as epithelial cells such as keratinocytes and fibroblasts.\r\n\r\nElevated levels of IL24 is associated with many pro-inflammatory and autoimmune diseases such as psoriasis and rheumatoid arthiritis but it can also play a protective anti-inflammatory role such as in multiple sclerosis where IL24 deficiency leads to experimental autoimmune encephalomyelitis.","predictedComplex":false,"interactors":[{"ac":"EBI-14022792","identifier":"Q6UXL0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6UXL0/entry","name":"IL20RB","description":"Interleukin-20 receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2933034","identifier":"Q9UHF4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UHF4/entry","name":"IL20RA","description":"Interleukin-20 receptor subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3915542","identifier":"Q13007","identifierLink":"https://www.uniprot.org/uniprotkb/Q13007/entry","name":"IL24","description":"Interleukin-24","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48482","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10311","complexName":"Interleukin-24 receptor-ligand complex, type 2","organismName":"Homo sapiens; 9606","description":"Pleiotropic cytokine-receptor complex with diverse roles in immune response, tissue homeostasis, host defense, and oncogenesis. Cytokine binding to its receptor complex initiates signalling, primarily triggering the JAK/STAT pathway recruiting JAK1/Tyk2 and STAT1(P42224) and STAT3(P40763) to mediate cell differentiation, proliferation and apoptosis, but it can also utilise the MAPK pathway to mediate tumour suppressive effects.\r\n\r\nIL24 is expressed in a variety of immune cells as well as epithelial cells such as keratinocytes and fibroblasts.\r\n\r\nElevated levels of IL24 is associated with many pro-inflammatory and autoimmune diseases such as psoriasis and rheumatoid arthiritis but it can also play a protective anti-inflammatory role such as in multiple sclerosis where IL24 deficiency leads to experimental autoimmune encephalomyelitis.","predictedComplex":false,"interactors":[{"ac":"EBI-14022792","identifier":"Q6UXL0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6UXL0/entry","name":"IL20RB","description":"Interleukin-20 receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3915542","identifier":"Q13007","identifierLink":"https://www.uniprot.org/uniprotkb/Q13007/entry","name":"IL24","description":"Interleukin-24","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48482","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3940749","identifier":"Q8N6P7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N6P7/entry","name":"IL22RA1","description":"Interleukin-22 receptor subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8836","complexName":"Interleukin-27 receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Transmembrane complex formed on the binding of the dimeric, extracellular interleukin-27 (IL-27, CPX-8822) to its receptor composed of IL-6RB (gp130) and the IL-27RA chains. Ligand binding results in the assembly of the complete complex, inducing the transphosphorylation of JAK1/2 molecules and phosphorylation of the cytoplasmic tails of the receptors. STAT monomers bind to the phosphorylated site of the receptor and are phosphorylated by JAK. Phosphorylated STATs dissociate from the receptors, dimerize, and translocate into the nucleus where they induce the transcription of target genes. IL-27 activation of STATs is dependent on the cell-type and activation state, for example, STAT1, STAT3, STAT5 and low amounts of STAT4 are activated by IL-27 in CD4+ cells. IL-27 induction of T helper 1 (Th1) differentiation is thought to occur through the p38 MAPK/T-bet and ICAM-1/LFA-1/ERK1/2 signaling cascade. \r\n\r\nA pleiotropic cytokine with both anti- and pro-inflammatory activity, IL-27 is capable of exerting both innate and adaptive immune responses.\r\n\r\nIn myeloid cells, IL-27 possesses both pro-apoptotic functions and anti-apoptotic functions through activation of STAT1 and STAT3, respectively. \r\n\r\nIncreases neuronal survival in various diseases and injuries of the central nervous system (CNS) and IL-27 binding to gp130 plays a critical role in reducing ischemia reperfusion injury through the activation of STAT3, to promote the expression of anti-apoptotic protein BCL2.","predictedComplex":false,"interactors":[{"ac":"EBI-1030834","identifier":"P40189","identifierLink":"https://www.uniprot.org/uniprotkb/P40189/entry","name":"IL6ST","description":"Interleukin-6 receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15887997","identifier":"Q8NEV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NEV9/entry","name":"IL27","description":"Interleukin-27 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20879","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-19045531","identifier":"Q6UWB1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6UWB1/entry","name":"IL27RA","description":"Interleukin-27 receptor subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48423","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742959","identifier":"Q14213","identifierLink":"https://www.uniprot.org/uniprotkb/Q14213/entry","name":"EBI3","description":"Interleukin-27 subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48483","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10316","complexName":"Interleukin-26 receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Receptor-cytokine complex thought to function both as a driver and an effector of inflammation. IL26 binding to its receptor complex induces JAK1/TYK2 signalling leading to activation of STAT1/STAT3. Monomeric and dimeric IL26 are both functional, but are thought to differ in their ability to activate epithelial cells and monocytes, as well as in their binding locations to form the functional receptor-ligand complex.\r\n\r\nPrimarily secreted by pathogenic T helper 1 (Th1), Th17 and CD4+ cells, IL26 activity is restricted by the expression of its receptor IL20R1 to epithelial cells and some myeloid cells. The inability of immune cells to express IL20R1 is thought to lend IL26 to alternative ways (CPX-10317) to mediate its proinflammatory effects in IL20R1-negative cells. \r\n\r\nIL26 is considered to be a master regulator of inflammation but one that could also be a catalyst for driving chronic inflammatory disorders. In addition to the proinflammatory effects it mediates, IL26 functions as a kinocidin or antimicrobial protein (AMP) with strong antimicrobial and bactericidal effects, particularly on Gram-positive bacteria, through its capacity to form pores in bacterial membranes.","predictedComplex":false,"interactors":[{"ac":"EBI-11175900","identifier":"Q08334","identifierLink":"https://www.uniprot.org/uniprotkb/Q08334/entry","name":"IL10RB","description":"Interleukin-10 receptor subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2933034","identifier":"Q9UHF4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UHF4/entry","name":"IL20RA","description":"Interleukin-20 receptor subunit alpha","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-54772883","identifier":"Q9NPH9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPH9/entry","name":"IL26","description":"Interleukin-26","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48482","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6013","complexName":"Interferon lambda receptor-ligand complex, IFNL3 variant","organismName":"Homo sapiens; 9606","description":"Receptor-ligand complex whose formation is triggered in response to viral infection to engage downstream signalling pathways that activate anti-viral responses. Following complex assembly TYK2 (P29597) and/or members of the JAK family of tyrosine-protein kinases  are activated by reciprocal transphosphorylation. Subsequently, they phosphorylate several tyrosine residues in the membrane-distal, intracellular domains of IFNLR1 and IL10RB, which, in turn, recruit further effector proteins that propagate downstream signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-11175900","identifier":"Q08334","identifierLink":"https://www.uniprot.org/uniprotkb/Q08334/entry","name":"IL10RB","description":"Interleukin-10 receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11668104","identifier":"Q8IZI9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IZI9/entry","name":"IFNL3","description":"Interferon lambda-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31943","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373215","identifier":"Q8IU57","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IU57/entry","name":"IFNLR1","description":"Interferon lambda receptor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10334","complexName":"Interleukin-35 receptor ligand type 1 complex","organismName":"Homo sapiens; 9606","description":"Inhibitory cytokine-receptor complex that plays a key role in immune regulation by promoting the expansion of regulatory T cells (Tregs) and Bregs, while simultaneously suppressing effector T cells, Th1 cells, Th17 cells and macrophages. IL35 signals through four receptors: IL12RB2 homodimers, IL6ST homodimers, IL12RB2/IL6ST heterodimers (this complex) and IL12RB2/IL27RA (Q6UWB1). Although homodimeric receptors partially mediate IL35's immunosuppressive signalling, maximal function is effected by the IL12RB2-IL6ST heterodimer. IL35 binding to IL12RB2-IL6ST induces immunosuppressive effects on Treg cells mediated through JAK1/JAK2 and STAT1/STAT4. Heterodimerization of the receptor phosphorylated by JAK1 and JAK2 promotes expression of IL12A and EBI3 leading to the generation of Foxp3-negative IL35-producing induced Treg (iTr35) cells, thereby creating a positive feedback loop to induce further iTr35 cell differentiation resulting in infectious tolerance.\r\n\r\nSuppresses autoimmune diseases by converting resting B- and T-cells into IL10 (P22301) and IL35-producing Breg and Treg cells.","predictedComplex":false,"interactors":[{"ac":"EBI-1030834","identifier":"P40189","identifierLink":"https://www.uniprot.org/uniprotkb/P40189/entry","name":"IL6ST","description":"Interleukin-6 receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59037816","identifier":"CPX-25744","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-25744","name":"Interleukin-35 complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-7045630","identifier":"Q99665","identifierLink":"https://www.uniprot.org/uniprotkb/Q99665/entry","name":"IL12RB2","description":"Interleukin-12 receptor subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10335","complexName":"Interleukin-35 receptor ligand type 2 complex","organismName":"Homo sapiens; 9606","description":"Inhibitory cytokine-receptor complex found predominanatly on B-cells, that plays a key role in immune regulation by promoting the expansion of regulatory B cells (Bregs), while simultaneously suppressing effector T cells, Th1 cells, Th17 cells and macrophages. IL35 signals through four receptors: IL12RB2 homodimers, IL6ST (P40189) homodimers, IL12RB2/IL6ST heterodimers and IL12RB2/IL27RA (this complex). IL35 binding to IL12RB2/IL27RA induces IL12A and EBI3 transcription and the activation of the JAK-STAT pathway through JAK1/JAK2 and STAT1/STAT3 (P42224/P40763). IL35 initiates infectious tolerance, whereby continuous generation of IL35-producing Bregs establishes a positive feedback loop to amplify its immunoregulatory signals.\r\n\r\nSuppresses autoimmune diseases by converting resting B- and T-cells into IL10 (P22301) and IL35-producting Breg and Treg cells.","predictedComplex":false,"interactors":[{"ac":"EBI-19045531","identifier":"Q6UWB1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6UWB1/entry","name":"IL27RA","description":"Interleukin-27 receptor subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48423","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59037816","identifier":"CPX-25744","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-25744","name":"Interleukin-35 complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-7045630","identifier":"Q99665","identifierLink":"https://www.uniprot.org/uniprotkb/Q99665/entry","name":"IL12RB2","description":"Interleukin-12 receptor subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10336","complexName":"Interleukin-35 receptor ligand type 3 complex","organismName":"Homo sapiens; 9606","description":"Inhibitory cytokine-receptor complex that plays a key role in immune regulation by suppressing effector T cells, Th1 cells, Th17 cells and macrophages. IL35 signals through four receptors: IL12RB2 homodimers, IL6ST homodimers, and heterodimers comprised of IL12RB2/IL6ST and IL12RB2/IL27RA. IL35 binding to IL12RB2 homodimers (this complex) induces IL12A and EBI3 transcription and the activation of the JAK-STAT pathway through JAK2/STAT4 phosphorylation. Although IL12RB2 homodimers partially mediate IL35-led immunosuppressive signalling, maximal function is effected by the IL12RB2-IL6ST heterodimer.","predictedComplex":false,"interactors":[{"ac":"EBI-59037816","identifier":"CPX-25744","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-25744","name":"Interleukin-35 complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-7045630","identifier":"Q99665","identifierLink":"https://www.uniprot.org/uniprotkb/Q99665/entry","name":"IL12RB2","description":"Interleukin-12 receptor subunit beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10337","complexName":"Interleukin-35 receptor ligand type 4 complex","organismName":"Homo sapiens; 9606","description":"Inhibitory cytokine-receptor complex that plays a key role in immune regulation by suppressing effector T cells, Th1 cells, Th17 cells and macrophages. IL35 is thought to signal through four receptors: IL12RB2 homodimers, IL6ST homodimers and heterodimers comprised of IL12RB2/IL6ST and IL12RB2/IL27RA (Q99665/Q6UWB1). IL35 binding to IL6ST homodimers (this complex) induces IL12A and EBI3 transcription and the activation of the JAK-STAT pathway through JAK1/STAT1 (P42224) phosphorylation. Although IL6ST homodimers partially mediate IL35-led immunosuppressive signalling, maximal function is effected by the IL12RB2-IL6ST heterodimer.","predictedComplex":false,"interactors":[{"ac":"EBI-1030834","identifier":"P40189","identifierLink":"https://www.uniprot.org/uniprotkb/P40189/entry","name":"IL6ST","description":"Interleukin-6 receptor subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59037816","identifier":"CPX-25744","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-25744","name":"Interleukin-35 complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-25726","complexName":"mTNF-TNR1A receptor-ligand core complex, BIRC3 variant","organismName":"Homo sapiens; 9606","description":"A membrane-bound tumor necrosis factor-receptor signaling complex (Complex I) formed on the binding of the membrane-bound form of the pro-inflammatory cytokine, tumour necrosis factor (mTNF, CPX-8932). This activates the mitogen-activated protein kinase  and nuclear factor-kappa-B (NF-kappa-B) signalling pathways, leading to proinflammatory gene expression and promoting cell survival. The Ripoptosome (CPX-1907, Complex II) originates from the dissociation of Complex I components from the receptor and promotes cell apoptosis. \r\n\r\nTNF, a key regulator of T regulatory cells, is mainly secreted by macrophages, T helper 1 and natural killer cells, while its receptor component TNFRSF1A is ubiquitously expressed on almost all human tissues.\r\n\r\nIntracellular signaling is triggered by ligand-bound receptors assembling into higher-order clusters. Soluble TNFA triggers more robust clustering of TNFR1 than membrane-bound ligand. TNFR1-mediated signaling is therefore generally caused by the activation due to sTNFA over mTNFA. TNFA-TNFRSF1A signalling complex formation is indirectly influenced by TNFA-TNFRSF1B activation and the cross-talk between the receptor complexes is central to cell-survival, proliferation or death.","predictedComplex":false,"interactors":[{"ac":"EBI-355744","identifier":"Q12933","identifierLink":"https://www.uniprot.org/uniprotkb/Q12933/entry","name":"TRAF2","description":"TNF receptor-associated factor 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358507","identifier":"Q13546","identifierLink":"https://www.uniprot.org/uniprotkb/Q13546/entry","name":"RIPK1","description":"Receptor-interacting serine/threonine-protein kinase 1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44329","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359215","identifier":"Q15628","identifierLink":"https://www.uniprot.org/uniprotkb/Q15628/entry","name":"TRADD","description":"Tumor necrosis factor receptor type 1-associated DEATH domain protein","stochiometry":"minValue: 3, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14913","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-517709","identifier":"Q13489","identifierLink":"https://www.uniprot.org/uniprotkb/Q13489/entry","name":"BIRC3","description":"Baculoviral IAP repeat-containing protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52219099","identifier":"P19438-PRO_0000034543","identifierLink":"https://www.uniprot.org/uniprotkb/P19438-PRO_0000034543/entry","name":"TNFRSF1A","description":"Tumor necrosis factor receptor superfamily member 1A, membrane form","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-52222100","identifier":"CPX-8931","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-8931","name":"Transmembrane tumor necrosis factor complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-523498","identifier":"O00463","identifierLink":"https://www.uniprot.org/uniprotkb/O00463/entry","name":"TRAF5","description":"TNF receptor-associated factor 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25727","complexName":"mTNF-TNR1B receptor-ligand core complex, BIRC3 variant","organismName":"Homo sapiens; 9606","description":"A membrane-bound tumor necrosis factor-receptor signaling complex formed on the binding of the membrane-bound form of the pro-inflammatory cytokine, tumour necrosis factor (mTNF, CPX-8931). TNFRSF1B is similar in its extracellular structure to TNFRSF1A (P19438) at the mTNF and sTNF binding sites, but it lacks the death domain found in TNFRSF1A. Instead, TNFRSF1B containss a TNF receptor associated factor (TRAF) binding site. mNF-stimulated  TNFRSF1B complexes recruit TRAF2-BIRC2/3, reducing their availability for triggering MAP3K14/NIK (Q99558) degradation. As a result, NIK accumulates and drives NF-kappa-B signaling. Aggregation of the TNF-TNFR2 complexes brings two or more TRAF2-BIRC2/3 complexes into proximity, enabling BIRC2/3 transactivation of their E3 ligase activity resulting in Lys-63-ubiquitination of TRAF2. This generates docking sites for classical NF-kappa-B signaling-stimulating kinases. \r\nTNFA is a key regulator of T regulatory cells, mainly secreted by macrophages, T helper 1 and natural killer cells, and while TNFRSF1A is ubiquitously expressed, TNFRSF1B is mainly expressed by immune cells, neurons and endothelial cells.","predictedComplex":false,"interactors":[{"ac":"EBI-355744","identifier":"Q12933","identifierLink":"https://www.uniprot.org/uniprotkb/Q12933/entry","name":"TRAF2","description":"TNF receptor-associated factor 2","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-517709","identifier":"Q13489","identifierLink":"https://www.uniprot.org/uniprotkb/Q13489/entry","name":"BIRC3","description":"Baculoviral IAP repeat-containing protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52222100","identifier":"CPX-8931","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-8931","name":"Transmembrane tumor necrosis factor complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-52222339","identifier":"P20333-PRO_0000034548","identifierLink":"https://www.uniprot.org/uniprotkb/P20333-PRO_0000034548/entry","name":"TNFRSF1B","description":"Tumor necrosis factor receptor superfamily member 1b, membrane form","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-25728","complexName":"Elongator holoenzyme complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"N-acetyltransferase which acts to form modified wobble uridines in tRNA, such as 5-methoxycarbonylmethyl-uridine (mcm5U), 5-methoxycarbonylmethyl-2-thio-uridine (mcm5s2U), and 5-carbamoylmethyl-uridine (ncm5U). These sites influence the recognition rate and affinity between incoming tRNAs and codons in the A site of the translating ribosome, stablizing transient pausing events thus supporting proper domain folding of the nascent polypeptide chains during the elongation phase of the ribosome‐mediated translation process.","predictedComplex":false,"interactors":[{"ac":"EBI-1190636","identifier":"O59704","identifierLink":"https://www.uniprot.org/uniprotkb/O59704/entry","name":"elp1","description":"Elongator complex protein 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12747","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59035532","identifier":"O94533","identifierLink":"https://www.uniprot.org/uniprotkb/O94533/entry","name":"elp2","description":"Elongator complex protein 2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR44111","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59035550","identifier":"O14023","identifierLink":"https://www.uniprot.org/uniprotkb/O14023/entry","name":"elp3","description":"Elongator complex protein 3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11135","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59035573","identifier":"Q9USP1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9USP1/entry","name":"elp4","description":"Elongator complex protein 4","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12896","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59035589","identifier":"O94495","identifierLink":"https://www.uniprot.org/uniprotkb/O94495/entry","name":"iki1","description":"Elongator complex protein 5","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15641","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59035603","identifier":"O74385","identifierLink":"https://www.uniprot.org/uniprotkb/O74385/entry","name":"elp6","description":"Elongator complex protein 6 homolog","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR16184","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25729","complexName":"TAK1-TAB complex, TAB2 variant","organismName":"Homo sapiens; 9606","description":"Serine/threonine kinase complex that activates nuclear factor-kappa B and mitogen-activated protein kinase (MAPK) pathways in response to various signals, such as cytokines and chemokines, and regulates inflammasomes.","predictedComplex":false,"interactors":[{"ac":"EBI-358643","identifier":"Q15750","identifierLink":"https://www.uniprot.org/uniprotkb/Q15750/entry","name":"TAB1","description":"TGF-beta-activated kinase 1 and MAP3K7-binding protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13832","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358684","identifier":"O43318","identifierLink":"https://www.uniprot.org/uniprotkb/O43318/entry","name":"MAP3K7","description":"Mitogen-activated protein kinase kinase kinase 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46716","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358708","identifier":"Q9NYJ8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NYJ8/entry","name":"TAB2","description":"TGF-beta-activated kinase 1 and MAP3K7-binding protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46253","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25730","complexName":"TAK1-TAB complex, TAB3 variant","organismName":"Homo sapiens; 9606","description":"Serine/threonine kinase complex that activates nuclear factor-kappa B and mitogen-activated protein kinase (MAPK) pathways in response to various signals, such as cytokines and chemokines, and regulates inflammasomes.","predictedComplex":false,"interactors":[{"ac":"EBI-358643","identifier":"Q15750","identifierLink":"https://www.uniprot.org/uniprotkb/Q15750/entry","name":"TAB1","description":"TGF-beta-activated kinase 1 and MAP3K7-binding protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13832","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358684","identifier":"O43318","identifierLink":"https://www.uniprot.org/uniprotkb/O43318/entry","name":"MAP3K7","description":"Mitogen-activated protein kinase kinase kinase 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46716","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359964","identifier":"Q8N5C8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N5C8/entry","name":"TAB3","description":"TGF-beta-activated kinase 1 and MAP3K7-binding protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46253","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25731","complexName":"DNA ligase IV complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"DNA ligase which catalyses the final ligation step in the non-homologous end-joining DNA repair pathway. Ligates DNA strands to restore the continuity of the chromosome in non-homologous end joining DNA double-strand break repair.","predictedComplex":false,"interactors":[{"ac":"EBI-59036104","identifier":"O74833","identifierLink":"https://www.uniprot.org/uniprotkb/O74833/entry","name":"lig4","description":"DNA ligase 4","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR45997","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59036136","identifier":"Q92361","identifierLink":"https://www.uniprot.org/uniprotkb/Q92361/entry","name":"xrc4","description":"Non-homologous end-joining factor xrc4","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]}]},{"complexAC":"CPX-25732","complexName":"MICOS mitochondrial contact site and cristae organizing system complex, MIC10A variant","organismName":"Drosophila melanogaster; 7227","description":"Required to maintain the folding of the mitochondrial inner membrane into cristae, crista junctions, inner membrane architecture, and the formation of contact sites to the outer mitochondrial membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-149315","identifier":"Q9VA18","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VA18/entry","name":"Chchd3","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-167726","identifier":"Q9VVH3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVH3/entry","name":"QIL1","description":"MICOS complex subunit MIC13 homolog QIL1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR31816","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-280677","identifier":"P91928","identifierLink":"https://www.uniprot.org/uniprotkb/P91928/entry","name":"Mitofilin","description":"MICOS complex subunit Mic60","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15415","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59036511","identifier":"Q9VY65","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VY65/entry","name":"Mic10a","description":"MICOS complex subunit MIC10","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-88342","identifier":"Q9VEY5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VEY5/entry","name":"Mic26-27","description":"MICOS complex subunit","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14564","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25733","complexName":"MICOS mitochondrial contact site and cristae organizing system complex, MIC10B variant","organismName":"Drosophila melanogaster; 7227","description":"Required to maintain the folding of the mitochondrial inner membrane into cristae, crista junctions, inner membrane architecture, and the formation of contact sites to the outer mitochondrial membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-149315","identifier":"Q9VA18","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VA18/entry","name":"Chchd3","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-167726","identifier":"Q9VVH3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVH3/entry","name":"QIL1","description":"MICOS complex subunit MIC13 homolog QIL1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR31816","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-280677","identifier":"P91928","identifierLink":"https://www.uniprot.org/uniprotkb/P91928/entry","name":"Mitofilin","description":"MICOS complex subunit Mic60","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15415","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59036538","identifier":"Q8SY69","identifierLink":"https://www.uniprot.org/uniprotkb/Q8SY69/entry","name":"Mic10b","description":"MICOS complex subunit MIC10","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-88342","identifier":"Q9VEY5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VEY5/entry","name":"Mic26-27","description":"MICOS complex subunit","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14564","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25735","complexName":"MICOS mitochondrial contact site and cristae organizing system complex, MIC10C variant","organismName":"Drosophila melanogaster; 7227","description":"Required to maintain the folding of the mitochondrial inner membrane into cristae, crista junctions, inner membrane architecture, and the formation of contact sites to the outer mitochondrial membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-146992","identifier":"Q9W1B2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W1B2/entry","name":"Mic10c","description":"MICOS complex subunit MIC10","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-149315","identifier":"Q9VA18","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VA18/entry","name":"Chchd3","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR21588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-167726","identifier":"Q9VVH3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVH3/entry","name":"QIL1","description":"MICOS complex subunit MIC13 homolog QIL1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR31816","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-280677","identifier":"P91928","identifierLink":"https://www.uniprot.org/uniprotkb/P91928/entry","name":"Mitofilin","description":"MICOS complex subunit Mic60","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15415","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-88342","identifier":"Q9VEY5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VEY5/entry","name":"Mic26-27","description":"MICOS complex subunit","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR14564","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25736","complexName":"SMC5-SMC6 SUMO ligase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"SUMO ligase complex with a role in homologous recombination (HR) and replication. Required for chromosome segregation at repetitive sequences.  Localizes to repetitive elements such as the rDNA and telomeres  where is is thought to promote and resolve HR-dependent intermediates using ATP-hydrolysis to symmetrically reel DNA into loops.","predictedComplex":false,"interactors":[{"ac":"EBI-603745","identifier":"P53692","identifierLink":"https://www.uniprot.org/uniprotkb/P53692/entry","name":"smc6","description":"Structural maintenance of chromosomes protein 6","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR19306","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-603756","identifier":"O13710","identifierLink":"https://www.uniprot.org/uniprotkb/O13710/entry","name":"smc5","description":"Structural maintenance of chromosomes protein 5","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR45916","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-605440","identifier":"Q53EK2","identifierLink":"https://www.uniprot.org/uniprotkb/Q53EK2/entry","name":"nse1","description":"Non-structural maintenance of chromosomes element 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR20973","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-605449","identifier":"Q4PIR3","identifierLink":"https://www.uniprot.org/uniprotkb/Q4PIR3/entry","name":"nse2","description":"E3 SUMO-protein ligase nse2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR21330","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-605466","identifier":"Q9Y7U4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y7U4/entry","name":"nse3","description":"Non-structural maintenance of chromosome element 3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11736","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-605484","identifier":"Q6BDR8","identifierLink":"https://www.uniprot.org/uniprotkb/Q6BDR8/entry","name":"nse4","description":"Non-structural maintenance of chromosome element 4","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR16140","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25737","complexName":"CERF chromatin remodelling complex, Smarca5 variant","organismName":"Mus musculus; 10090","description":"Chromatin remodelling complex which plays a role in neural tube closure and reproduction. CERF complex facilitates the perturbation of chromatin structure in an ATP-dependent manner.\r\n\r\nCerc2 Loss-of-function mutations results in lethal neural tube defect and is associated with suboptimal spermatogenesis in mice that reach adulthood.","predictedComplex":false,"interactors":[{"ac":"EBI-11786531","identifier":"E9Q2Z1","identifierLink":"https://www.uniprot.org/uniprotkb/E9Q2Z1/entry","name":"Cecr2","description":"Chromatin remodeling regulator CECR2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR47092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-927547","identifier":"Q91ZW3","identifierLink":"https://www.uniprot.org/uniprotkb/Q91ZW3/entry","name":"Smarca5","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25738","complexName":"CERF chromatin remodelling complex, SMARCA5 variant","organismName":"Homo sapiens; 9606","description":"Chromatin remodelling complex which plays a role in neural tube closure and reproduction. CERF complex facilitates the perturbation of chromatin structure in an ATP-dependent manner.","predictedComplex":false,"interactors":[{"ac":"EBI-11784677","identifier":"Q9BXF3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BXF3/entry","name":"CECR2","description":"Chromatin remodeling regulator CECR2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352588","identifier":"O60264","identifierLink":"https://www.uniprot.org/uniprotkb/O60264/entry","name":"SMARCA5","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25739","complexName":"Survival motor neuron complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Molecular chaperone that plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, thus playing an important role in the splicing of cellular pre-mRNAs.","predictedComplex":false,"interactors":[{"ac":"EBI-59037244","identifier":"Q09808","identifierLink":"https://www.uniprot.org/uniprotkb/Q09808/entry","name":"smn1","description":"SMN complex subunit smn1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR39267","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59037260","identifier":"P0CU08","identifierLink":"https://www.uniprot.org/uniprotkb/P0CU08/entry","name":"yip11","description":"SMN complex subunit yip11/gem2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12794","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59037277","identifier":"Q9USY8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9USY8/entry","name":"gem8","description":"Uncharacterized protein C16H5.15","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR40642","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59037288","identifier":"G2TRK8","identifierLink":"https://www.uniprot.org/uniprotkb/G2TRK8/entry","name":"gem6","description":"Uncharacterized protein new12","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-59037299","identifier":"G2TRR1","identifierLink":"https://www.uniprot.org/uniprotkb/G2TRR1/entry","name":"gem7","description":"Gem-associated protein 7 homolog","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR14679","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25743","complexName":"Chromatin assembly factor 1 complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Catalyzes de novo assembly of nucleosomes onto newly synthesized DNA, involved in chromatin assembly following both DNA replication and some forms of DNA repair. Binds modified histones H3 and H4 and deposits them as a tetramer, preferentially onto replicating DNA, in a step coupled to the replication process. This is followed by deposition of a pair of dimers of histones H2A and H2B mediated by other factor(s) in a process not necessarily coupled to DNA replication. The histone core of nucleosomes consists of two copies of each of histones H2A, H2B, H3 and H4. CAF-1 nucleosome deposition is thought to be involved in heterochromatic silencing.","predictedComplex":false,"interactors":[{"ac":"EBI-1560762","identifier":"Q1MTN9","identifierLink":"https://www.uniprot.org/uniprotkb/Q1MTN9/entry","name":"pcf1","description":"Chromatin assembly factor 1 subunit A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15272","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16123749","identifier":"O13985","identifierLink":"https://www.uniprot.org/uniprotkb/O13985/entry","name":"pcf2","description":"Chromatin assembly factor 1 subunit B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15271","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59037649","identifier":"Q9Y825","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y825/entry","name":"pcf3","description":"Histone-binding protein pcf3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-382","complexName":"Interleukin-12-receptor ligand complex","organismName":"Homo sapiens; 9606","description":"Receptor complex that activates and stimulates proliferation of a wide range of lymphocytes, in particular natural killer cells and T helper 1 (Th1) cells. The IL12 ligand complex (CPX-381) binds the receptors chains IL12RB1 and IL12RB2 which are associated with the kinases TYK2 and JAK2, respectively. Transphosphorylation of IL12RB2 and the JAK-family kinases initiates the JAK-STAT signaling cascade via phosphorylation and homodimerisation of STAT3/STAT4 (P40763/Q14765). This ultimately leads to the activation of transcription of interferon-gamma which, in turn, stimulates production of IL12 leading to a positive regulation loop. Mutations in IL12B and IL12RB1 can lead to mycobacterial diseases of varying severity, primarily bacillus Calmette-Guerin and Salmonella infections.","predictedComplex":false,"interactors":[{"ac":"EBI-11664485","identifier":"CPX-381","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-381","name":"Interleukin-12 complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-11665915","identifier":"P42701-PRO_0000010917","identifierLink":"https://www.uniprot.org/uniprotkb/P42701-PRO_0000010917/entry","name":"IL12RB1","description":"Interleukin-12 receptor subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-11665925","identifier":"Q99665-PRO_0000010920","identifierLink":"https://www.uniprot.org/uniprotkb/Q99665-PRO_0000010920/entry","name":"IL12RB2","description":"Interleukin-12 receptor subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-25744","complexName":"Interleukin-35 complex","organismName":"Homo sapiens; 9606","description":"Inhibitory cytokine complex that plays a key role in immune regulation by promoting the expansion of regulatory T cells (Tregs) and Bregs, while simultaneously suppressing effector T cells, Th1 cells, Th17 cells and macrophages. IL35 signals through four receptors: IL12RB2 (Q99665) homodimers, IL6ST (P40189) homodimers, IL12RB2/IL6ST heterodimers and IL12RB2/IL27RA (Q6UWB1). \r\n\r\nThe complex is constitutively secreted by Tregs but not T effector cells and suppresses autoimmune diseases by converting resting B- and T-cells into IL10 (P22301) and IL35-producing Breg and Treg cells.","predictedComplex":false,"interactors":[{"ac":"EBI-1029636","identifier":"P29459","identifierLink":"https://www.uniprot.org/uniprotkb/P29459/entry","name":"IL12A","description":"Interleukin-12 subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48485","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742959","identifier":"Q14213","identifierLink":"https://www.uniprot.org/uniprotkb/Q14213/entry","name":"EBI3","description":"Interleukin-27 subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48483","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25745","complexName":"SREBP-SCAP transcription regulator complex, SREBF1 variant","organismName":"Homo sapiens; 9606","description":"When the cell is enriched with cholesterol, SCAP binds and stabilizes full-length SREBF1/2 and is anchored in the endoplasmic reticulum (ER) by formation of the SREBP-SCAP-INSIG complex (CPX-25749/CPX-25750). Under conditions of low sterols, the SREBP-SCAP complex is translocated by COPII (CPX-2360)-coated vesicles from the ER to the Golgi where SREBF1/2 is proteolytically cleaved and freed from the membrane to activate the transcription of genes involved in fatty acids and cholesterol biosynthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-6190187","identifier":"Q12770","identifierLink":"https://www.uniprot.org/uniprotkb/Q12770/entry","name":"SCAP","description":"Sterol regulatory element-binding protein cleavage-activating protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46378","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-948313","identifier":"P36956","identifierLink":"https://www.uniprot.org/uniprotkb/P36956/entry","name":"SREBF1","description":"Sterol regulatory element-binding protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46062","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25746","complexName":"CST complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Acts to suppress aberrant telomerase and recombination activities at telomeres, restricting telomerase action via its sumoylation-mediated interaction with the telomeric DNA-binding protein Tpz1 (O14246). Promotes DNA synthesis at telomeres to limit single-strand DNA accumulation.","predictedComplex":false,"interactors":[{"ac":"EBI-1553734","identifier":"Q0E7J7","identifierLink":"https://www.uniprot.org/uniprotkb/Q0E7J7/entry","name":"stn1","description":"Protein stn1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13989","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1567530","identifier":"P0C5Y7","identifierLink":"https://www.uniprot.org/uniprotkb/P0C5Y7/entry","name":"ten1","description":"Protein ten1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]}]},{"complexAC":"CPX-25747","complexName":"SREBP-SCAP-INSIG sequestering complex, INSIG1-SREBF2 variant","organismName":"Homo sapiens; 9606","description":"When the cell is enriched with cholesterol, the SCAP SREBF2 complex (CPX-25721)  is anchored in the endoplasmic reticulum (ER) by formation of the SREBP-SCAP-INSIG complex. The association between SCAP and INSIG requires oxysterols such as 25-hydroxycholesterol or, less favorably, cholesterol Under conditions of low sterols, INSIG-SCAP disassociate and the SREBP-SCAP complex is translocated by COPII (CPX-2360)-coated vesicles from the ER to the Golgi where SREBF2 is proteolytically cleaved and freed from the membrane to activate the transcription of genes involved in cholesterol biosynthesis. INSIG1 is transcriptionally regulated by SREBPs and is abundant in cells.","predictedComplex":false,"interactors":[{"ac":"EBI-2368702","identifier":"CHEBI:42977","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:42977","name":"25-hydroxycholesterol","description":"25-hydroxycholesterol","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-59026029","identifier":"CPX-25721","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-25721","name":"SREBP-SCAP transcription regulator complex, SREBF2 variant","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-6252425","identifier":"O15503","identifierLink":"https://www.uniprot.org/uniprotkb/O15503/entry","name":"INSIG1","description":"Insulin-induced gene 1 protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15301","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25748","complexName":"SREBP-SCAP-INSIG sequestering complex, INSIG2-SREBF2 variant","organismName":"Homo sapiens; 9606","description":"When the cell is enriched with cholesterol, the SREBP2-SCAP complex (CPX-25721) is anchored in the endoplasmic reticulum (ER) by the formation of this complex. The association between SCAP and INSIG requires oxysterols such as 25-hydroxycholesterol or, less favorably, cholesterol Under conditions of low sterols, INSIG-SCAP disassociate and the SREBP-SCAP complex is translocated by COPII (CPX-2360)-coated vesicles from the ER to the Golgi where SREBF2 is proteolytically cleaved and freed from the membrane to activate the transcription of genes involved in cholesterol biosynthesis. is ubiquitously expressed at a low level in cells and may act as the regulator of SCAP/SREBP pathway at the basal level.","predictedComplex":false,"interactors":[{"ac":"EBI-2368702","identifier":"CHEBI:42977","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:42977","name":"25-hydroxycholesterol","description":"25-hydroxycholesterol","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-59026029","identifier":"CPX-25721","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-25721","name":"SREBP-SCAP transcription regulator complex, SREBF2 variant","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-8503746","identifier":"Q9Y5U4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5U4/entry","name":"INSIG2","description":"Insulin-induced gene 2 protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15301","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25749","complexName":"SREBP-SCAP-INSIG sequestering complex, INSIG2-SREBF1 variant","organismName":"Homo sapiens; 9606","description":"When the cell is enriched with cholesterol, the SREBP1-SCAP complex (CPX-25745) is anchored in the endoplasmic reticulum (ER) by the formation of this complex. The association between SCAP and INSIG requires oxysterols such as 25-hydroxycholesterol or, less favorably, cholesterol Under conditions of low sterols, INSIG-SCAP disassociate and the SREBP-SCAP complex is translocated by COPII (CPX-2360)-coated vesicles from the ER to the Golgi where SREBF1 is proteolytically cleaved and freed from the membrane to activate the transcription of genes involved in fatty acid and cholesterol biosynthesis. is ubiquitously expressed at a low level in cells and may act as the regulator of SCAP/SREBP pathway at the basal level.","predictedComplex":false,"interactors":[{"ac":"EBI-2368702","identifier":"CHEBI:42977","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:42977","name":"25-hydroxycholesterol","description":"25-hydroxycholesterol","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-59037891","identifier":"CPX-25745","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-25745","name":"SREBP-SCAP transcription regulator complex, SREBF1 variant","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-8503746","identifier":"Q9Y5U4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y5U4/entry","name":"INSIG2","description":"Insulin-induced gene 2 protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15301","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25750","complexName":"SREBP-SCAP-INSIG sequestering complex, INSIG1-SREBF1 variant","organismName":"Homo sapiens; 9606","description":"When the cell is enriched with cholesterol, the SCAP SREBF1 complex (CPX-25745)  is anchored in the endoplasmic reticulum (ER) by formation of the SREBP-SCAP-INSIG complex. The association between SCAP and INSIG requires oxysterols such as 25-hydroxycholesterol or, less favorably, cholesterol Under conditions of low sterols, INSIG-SCAP disassociate and the SREBP-SCAP complex is translocated by COPII (CPX-2360)-coated vesicles from the ER to the Golgi where SREBF1 is proteolytically cleaved and freed from the membrane to activate the transcription of genes involved in faaty acid and cholesterol biosynthesis. INSIG1 is transcriptionally regulated by SREBPs and is abundant in cells.","predictedComplex":false,"interactors":[{"ac":"EBI-2368702","identifier":"CHEBI:42977","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:42977","name":"25-hydroxycholesterol","description":"25-hydroxycholesterol","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-59037891","identifier":"CPX-25745","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-25745","name":"SREBP-SCAP transcription regulator complex, SREBF1 variant","description":null,"stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-6252425","identifier":"O15503","identifierLink":"https://www.uniprot.org/uniprotkb/O15503/entry","name":"INSIG1","description":"Insulin-induced gene 1 protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15301","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25751","complexName":"Mitochondrial isocitrate dehydrogenase complex (NAD+)","organismName":"Drosophila melanogaster; 7227","description":"Tricarboxylic acid cycle enzyme which catalyzes the conversion of threo-Ds-isocitrate to alpha-ketoglutarate and carbon dioxide, important for regulatory control of mitochondrial energy metabolism. Allosterically regulated, activated by citrate and ADP, inhibited by ATP. There are two binding sites per tetramer for each of its ligands: isocitrate, Mn2+, NAD, ADP, NADH, and NADPH. During the oxidative decarboxylation, NAD reacts with Mn2+-isocitrate. The active sites are shared between the Mn2+-binding alpha and gamma subunits and between the NAD-binding alpha and beta subunits. The allosteric activator ADP has been found to be associated with only the beta and gamma subunits.","predictedComplex":false,"interactors":[{"ac":"EBI-109813","identifier":"Q8MT18","identifierLink":"https://www.uniprot.org/uniprotkb/Q8MT18/entry","name":"Idh3g","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11835","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-157405","identifier":"Q9VD58","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VD58/entry","name":"Idh3b","description":"Isocitric dehydrogenase subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11835","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-162527","identifier":"Q9VWH4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VWH4/entry","name":"Idh3a","description":"Probable isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11835","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9097897","identifier":"CHEBI:60240","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60240","name":"divalent metal cation","description":"divalent metal cation","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-25752","complexName":"AMPK complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Energy sensor serine/threonine kinase that plays a key role in regulating cellular energy metabolism. Energy stress manifests as a drop in the ratio of adenosine triphosphate (ATP) to AMP/ADP, which activates AMPK's kinase activity, allowing it to upregulate ATP-generating catabolic pathways and to reduce energy-consuming catabolic pathways and cellular programs: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators.","predictedComplex":false,"interactors":[{"ac":"EBI-1387265","identifier":"O74536","identifierLink":"https://www.uniprot.org/uniprotkb/O74536/entry","name":"ssp2","description":"SNF1-like protein kinase ssp2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR24343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1387281","identifier":"Q10343","identifierLink":"https://www.uniprot.org/uniprotkb/Q10343/entry","name":"cbs2","description":"5'-AMP-activated protein kinase subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13780","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15664758","identifier":"P78789","identifierLink":"https://www.uniprot.org/uniprotkb/P78789/entry","name":"amk2","description":"5'-AMP-activated protein kinase subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25753","complexName":"AMPK complex","organismName":"Drosophila melanogaster; 7227","description":"Energy sensor serine/threonine kinase that plays a key role in regulating cellular energy metabolism. Energy stress manifests as a drop in the ratio of adenosine triphosphate (ATP) to AMP/ADP, which activates AMPK's kinase activity, allowing it to upregulate ATP-generating catabolic pathways and to reduce energy-consuming catabolic pathways and cellular programs: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators.","predictedComplex":false,"interactors":[{"ac":"EBI-111605","identifier":"O18645","identifierLink":"https://www.uniprot.org/uniprotkb/O18645/entry","name":"AMPKalpha","description":"non-specific serine/threonine protein kinase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR24343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-26787466","identifier":"Q7JQX9","identifierLink":"https://www.uniprot.org/uniprotkb/Q7JQX9/entry","name":"SNF4Agamma","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-90118","identifier":"A1Z7Q8","identifierLink":"https://www.uniprot.org/uniprotkb/A1Z7Q8/entry","name":"alc","description":"5'-AMP-activated protein kinase subunit beta-1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10343","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25754","complexName":"Nucleosome complex, H2A type 1 variant","organismName":"Homo sapiens; 9606","description":"Nucleosome core particle (NCP), fundamental structural unit of chromatin. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability.","predictedComplex":false,"interactors":[{"ac":"EBI-1390628","identifier":"P0C0S8","identifierLink":"https://www.uniprot.org/uniprotkb/P0C0S8/entry","name":"H2AC11","description":"Histone H2A type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23430","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302023","identifier":"P62805","identifierLink":"https://www.uniprot.org/uniprotkb/P62805/entry","name":"H4C16","description":"Histone H4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10484","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6150252","identifier":"P06899","identifierLink":"https://www.uniprot.org/uniprotkb/P06899/entry","name":"H2BC11","description":"Histone H2B type 1-J","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23428","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-79722","identifier":"P68431","identifierLink":"https://www.uniprot.org/uniprotkb/P68431/entry","name":"H3C1","description":"Histone H3.1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11426","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9636457","identifier":"CHEBI:4705","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:4705","name":"double-stranded dna","description":"double-stranded DNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-25755","complexName":"Hexasome complex","organismName":"Homo sapiens; 9606","description":"Noncanonical nucleosome complex with six instead of eight histones which functions to compact and control access to DNA. Stable hexasomes can be formed adjacent to nucleosomes; although hexasomes can be formed as an intermediary of nucleosome assembly, hexasomes can also be formed by histone chaperones and chromatin remodelling complexes.","predictedComplex":false,"interactors":[{"ac":"EBI-302023","identifier":"P62805","identifierLink":"https://www.uniprot.org/uniprotkb/P62805/entry","name":"H4C16","description":"Histone H4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10484","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-354552","identifier":"P62807","identifierLink":"https://www.uniprot.org/uniprotkb/P62807/entry","name":"H2BC10","description":"Histone H2B type 1-C/E/F/G/I","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23428","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-725259","identifier":"Q93077","identifierLink":"https://www.uniprot.org/uniprotkb/Q93077/entry","name":"H2AC6","description":"Histone H2A type 1-C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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284812","xrefs":[{"identifier":"PTHR14513","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15903288","identifier":"P79005","identifierLink":"https://www.uniprot.org/uniprotkb/P79005/entry","name":"taz1","description":"Telomere length regulator taz1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-15953947","identifier":"Q10432","identifierLink":"https://www.uniprot.org/uniprotkb/Q10432/entry","name":"ccq1","description":"Coiled-coil quantitatively-enriched protein 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-8802014","identifier":"O14246","identifierLink":"https://www.uniprot.org/uniprotkb/O14246/entry","name":"tpz1","description":"Protection of telomeres protein tpz1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 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Mediates organization of the cytoskeleton, vesicle transport and fusion, chromosome alignment and segregation, and cytokinesis. Septin complexes also bind and bundle filamentous actin, anchoring and stabilizing actin filaments at the plasma membrane.\r\n\r\nSeptins play wide ranging roles in development and homeostatic biological processes such as cell motility, sperm integrity, neuron development, tissue morphogenesis, and host-pathogen interactions.\r\n\r\nSeptins are thought to play a protective role in stabilizing epithelial and endothelial barriers to limit immune cell exposure during tissue inflammation in response to enironmental pathogens. Mutations in septins have also been implicated in cancer and neurodegenerative diseases.","predictedComplex":false,"interactors":[{"ac":"EBI-2009373","identifier":"Q16181","identifierLink":"https://www.uniprot.org/uniprotkb/Q16181/entry","name":"SEPTIN7","description":"Septin-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-741220","identifier":"Q15019","identifierLink":"https://www.uniprot.org/uniprotkb/Q15019/entry","name":"SEPTIN2","description":"Septin-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-745901","identifier":"Q14141","identifierLink":"https://www.uniprot.org/uniprotkb/Q14141/entry","name":"SEPTIN6","description":"Septin-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-851542","identifier":"Q9UHD8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UHD8/entry","name":"SEPTIN9","description":"Septin-9","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25759","complexName":"Protein farnesyltransferase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Catalyzes the transfer of a 15-carbon lipid, the farnesyl moiety, from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X (CaaX box).\r\n\r\nThe hydrophobic farnesyl moiety aids membrane attachment of the target proteins which include many essential signal transduction proteins, including members of the Ras superfamily. Farnesylation is essential both for normal functioning of these proteins, and for the transforming activity of oncogenic mutants.","predictedComplex":false,"interactors":[{"ac":"EBI-59039461","identifier":"O60052","identifierLink":"https://www.uniprot.org/uniprotkb/O60052/entry","name":"cwp1","description":"Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59039479","identifier":"O13782","identifierLink":"https://www.uniprot.org/uniprotkb/O13782/entry","name":"cpp1","description":"Protein farnesyltransferase subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11774","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-25760","complexName":"Protein geranylgeranyltransferase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Catalyzes the transfer of a 20-carbon lipid, the geranyl-geranyl moiety, from geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X (CaaX box). The Zn2+ is required for peptide, but not for isoprenoid, substrate binding.\r\n\r\nThe hydrophobic geranyl-geranyl moiety aids membrane attachment of the target proteins which include many essential signal transduction proteins, including members of the Ras superfamily.","predictedComplex":false,"interactors":[{"ac":"EBI-59039461","identifier":"O60052","identifierLink":"https://www.uniprot.org/uniprotkb/O60052/entry","name":"cwp1","description":"Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59039515","identifier":"P32434","identifierLink":"https://www.uniprot.org/uniprotkb/P32434/entry","name":"cwg2","description":"Geranylgeranyl transferase type-1 subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11774","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-25761","complexName":"Septin complex, octamer variant, SEPT2-SEPT6-SEPT-7-SEPT3","organismName":"Homo sapiens; 9606","description":"Cytoskeletal complex that polymerizes to form filaments. Mediates organization of the cytoskeleton, vesicle transport and fusion, chromosome alignment and segregation, and cytokinesis. Septin complexes also bind and bundle filamentous actin, anchoring and stabilizing actin filaments at the plasma membrane.\r\n\r\nSeptins play wide ranging roles in development and homeostatic biological processes such as cell motility, sperm integrity, neuron development, tissue morphogenesis, and host-pathogen interactions.\r\n\r\nSeptins are thought to play a protective role in stabilizing epithelial and endothelial barriers to limit immune cell exposure during tissue inflammation in response to environmental pathogens. Mutations in septins have also been implicated in cancer and neurodegenerative diseases.","predictedComplex":false,"interactors":[{"ac":"EBI-2009373","identifier":"Q16181","identifierLink":"https://www.uniprot.org/uniprotkb/Q16181/entry","name":"SEPTIN7","description":"Septin-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727037","identifier":"Q9UH03","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UH03/entry","name":"SEPTIN3","description":"Neuronal-specific septin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-741220","identifier":"Q15019","identifierLink":"https://www.uniprot.org/uniprotkb/Q15019/entry","name":"SEPTIN2","description":"Septin-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-745901","identifier":"Q14141","identifierLink":"https://www.uniprot.org/uniprotkb/Q14141/entry","name":"SEPTIN6","description":"Septin-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25762","complexName":"Short transient receptor potential channel complex,TRPC1-TRPC4 variant","organismName":"Homo sapiens; 9606","description":"Non-selective, multimeric cation channel permeable by Na+ and Ca2+. Activators and modulators of channel activity may include endogenous and dietary lipids and metal ions such as Zn2+. Appear to play a role in a wide range of cellular processes that require calcium signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-929504","identifier":"Q9UBN4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UBN4/entry","name":"TRPC4","description":"Short transient receptor potential channel 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-929665","identifier":"P48995","identifierLink":"https://www.uniprot.org/uniprotkb/P48995/entry","name":"TRPC1","description":"Short transient receptor potential channel 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25763","complexName":"Phosphatidylinositol 3-kinase complex, class III, type I","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"A phosphatidylinositol 3-kinase complex that specifically phosphorylates 1-phosphatidyl-1D-myo-inositol(1-) (CHEBI:57880) in an ATP- and Mn(2+)-dependent manner. Functions in autophagy.","predictedComplex":false,"interactors":[{"ac":"EBI-59041242","identifier":"O42862","identifierLink":"https://www.uniprot.org/uniprotkb/O42862/entry","name":"atg14","description":"Autophagy-related protein 14","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13664","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59041267","identifier":"P87117","identifierLink":"https://www.uniprot.org/uniprotkb/P87117/entry","name":"atg6","description":"Vacuolar protein sorting-associated protein atg6","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12768","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59041316","identifier":"P50520","identifierLink":"https://www.uniprot.org/uniprotkb/P50520/entry","name":"pik3","description":"Phosphatidylinositol 3-kinase pik3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59041358","identifier":"O42900","identifierLink":"https://www.uniprot.org/uniprotkb/O42900/entry","name":"vps15","description":"Serine/threonine-protein kinase vps15","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR17583","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59046735","identifier":"O94427","identifierLink":"https://www.uniprot.org/uniprotkb/O94427/entry","name":"atg38","description":"PtdIns3K complex I subunit atg38","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]}]},{"complexAC":"CPX-25764","complexName":"Mitochondrial proton translocating ATP synthase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Acts to convert the energy of oxidation-reduction reactions of the electron transport chain (respiration) to the phosphorylation of ADP. 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Thus, the flow of protons though F0 is coupled to the synthesis of ATP.","predictedComplex":false,"interactors":[{"ac":"EBI-2477760","identifier":"O94390","identifierLink":"https://www.uniprot.org/uniprotkb/O94390/entry","name":"atp7","description":"ATP synthase subunit d, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12700","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59041646","identifier":"P22068","identifierLink":"https://www.uniprot.org/uniprotkb/P22068/entry","name":"atp2","description":"ATP synthase subunit beta, mitochondrial","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15184","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59041672","identifier":"O13931","identifierLink":"https://www.uniprot.org/uniprotkb/O13931/entry","name":"atp18","description":"ATP synthase subunit J, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28060","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59041684","identifier":"O74479","identifierLink":"https://www.uniprot.org/uniprotkb/O74479/entry","name":"atp5","description":"ATP synthase subunit 5, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11910","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59041698","identifier":"O74754","identifierLink":"https://www.uniprot.org/uniprotkb/O74754/entry","name":"atp3","description":"ATP synthase subunit gamma, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11693","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59041715","identifier":"O94377","identifierLink":"https://www.uniprot.org/uniprotkb/O94377/entry","name":"atp17","description":"ATP synthase subunit f, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28161","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59041727","identifier":"P21535","identifierLink":"https://www.uniprot.org/uniprotkb/P21535/entry","name":"atp6","description":"ATP synthase subunit a","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11410","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59041745","identifier":"P21537","identifierLink":"https://www.uniprot.org/uniprotkb/P21537/entry","name":"atp9","description":"ATP synthase subunit 9, mitochondrial","stochiometry":"minValue: 10, maxValue: 10","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59041761","identifier":"P24487","identifierLink":"https://www.uniprot.org/uniprotkb/P24487/entry","name":"atp1","description":"ATP synthase subunit alpha, mitochondrial","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR48082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59041785","identifier":"Q9P6R6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P6R6/entry","name":"atp16","description":"ATP synthase subunit delta, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13822","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59041801","identifier":"C6Y4A3","identifierLink":"https://www.uniprot.org/uniprotkb/C6Y4A3/entry","name":"atp19","description":"ATP synthase subunit K, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28074","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59041812","identifier":"O59673","identifierLink":"https://www.uniprot.org/uniprotkb/O59673/entry","name":"atp14","description":"ATP synthase subunit H, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28207","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59041824","identifier":"O94373","identifierLink":"https://www.uniprot.org/uniprotkb/O94373/entry","name":"atp4","description":"ATP synthase subunit 4, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12733","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59041838","identifier":"P21536","identifierLink":"https://www.uniprot.org/uniprotkb/P21536/entry","name":"atp8","description":"ATP synthase protein 8","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR36101","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59041850","identifier":"P87316","identifierLink":"https://www.uniprot.org/uniprotkb/P87316/entry","name":"atp15","description":"Putative ATP synthase subunit epsilon, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12448","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59041863","identifier":"Q09774","identifierLink":"https://www.uniprot.org/uniprotkb/Q09774/entry","name":"atp20","description":"ATP synthase subunit g, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-59041875","identifier":"Q9URV6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9URV6/entry","name":"tim11","description":"ATP synthase subunit e, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]}]},{"complexAC":"CPX-25765","complexName":"Short transient receptor potential channel complex, TRPC1-TRPC5 variant","organismName":"Homo sapiens; 9606","description":"Non-selective, multimeric cation channel permeable by Na+ and Ca2+. Activators and modulators of channel activity may include endogenous and dietary lipids and metal ions such as Zn2+. Appear to play a role in a wide range of cellular processes that require calcium signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-929550","identifier":"Q9UL62","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UL62/entry","name":"TRPC5","description":"Short transient receptor potential channel 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-929665","identifier":"P48995","identifierLink":"https://www.uniprot.org/uniprotkb/P48995/entry","name":"TRPC1","description":"Short transient receptor potential channel 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25766","complexName":"Septin complex, hexamer variant, SEPT2-SEPT6-SEPT-7","organismName":"Homo sapiens; 9606","description":"Cytoskeletal complex that polymerizes to form filaments. Mediates organization of the cytoskeleton, vesicle transport and fusion, chromosome alignment and segregation, and cytokinesis. Septin complexes also bind and bundle filamentous actin, anchoring and stabilizing actin filaments at the plasma membran.\r\n\r\nSeptins play wide ranging roles in development and homeostatic biological processes such as cell motility, sperm integrity, neuron development, tissue morphogenesis, and host-pathogen interactions.\r\n\r\nSeptins are thought to play a protective role in stabilizing epithelial and endothelial barriers to limit immune cell exposure during tissue inflammation in response to enironmental pathogens. Mutations in septins have also been implicated in cancer and neurodegenerative diseases.","predictedComplex":false,"interactors":[{"ac":"EBI-2009373","identifier":"Q16181","identifierLink":"https://www.uniprot.org/uniprotkb/Q16181/entry","name":"SEPTIN7","description":"Septin-7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-741220","identifier":"Q15019","identifierLink":"https://www.uniprot.org/uniprotkb/Q15019/entry","name":"SEPTIN2","description":"Septin-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-745901","identifier":"Q14141","identifierLink":"https://www.uniprot.org/uniprotkb/Q14141/entry","name":"SEPTIN6","description":"Septin-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25767","complexName":"Prefoldin co-chaperone complex","organismName":"Homo sapiens; 9606","description":"Multi-functional complex that plays a key role in proteostasis, acting as a co-chaperone to assist protein folding, assembly and stabilization. Prefoldin-like (PFDL) complex (this complex) and Prefoldin (PFDN, CPX-6149) are thought to interact with the PAQosome (CPX-6145) which is crucial for the stable assembly and maturation of large RNA-binding protein assemblies, and multiple phosphatidylinositol 3-kinase-related kinase (PIK3) complexes.\r\n\r\nOverexpression of prefoldins is associated with certain types of cancers.","predictedComplex":false,"interactors":[{"ac":"EBI-307050","identifier":"Q9NUG6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NUG6/entry","name":"PDRG1","description":"p53 and DNA damage-regulated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21162","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356919","identifier":"O60925","identifierLink":"https://www.uniprot.org/uniprotkb/O60925/entry","name":"PFDN1","description":"Prefoldin subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20903","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356973","identifier":"O15212","identifierLink":"https://www.uniprot.org/uniprotkb/O15212/entry","name":"PFDN6","description":"Prefoldin subunit 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21431","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357275","identifier":"Q99471","identifierLink":"https://www.uniprot.org/uniprotkb/Q99471/entry","name":"PFDN5","description":"Prefoldin subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12674","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357430","identifier":"P61758","identifierLink":"https://www.uniprot.org/uniprotkb/P61758/entry","name":"VBP1","description":"Prefoldin subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12409","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359873","identifier":"Q9UHV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UHV9/entry","name":"PFDN2","description":"Prefoldin subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13303","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25769","complexName":"TAP antigen peptide transporter complex","organismName":"Homo sapiens; 9606","description":"ABC (ATP binding cassette) transporter that functions as a molecular calliper selecting antigenic peptides according to length for ATP-mediated transport from the cytoplasm into the endoplasmic reticulum where the transient peptide-loading complex selects high affinity peptides for MHC Class 1 presentation. \r\n\r\nHomozygous mutations in the TAP1 and TAP2 genes are associated with progressive autosomal recessive immunologic disorders ('MHC Class 1 deficiency 1' and 'MHC Class 1 deficiency 2', respectively) which lead to bronciectasis and respiratory failure.","predictedComplex":false,"interactors":[{"ac":"EBI-747259","identifier":"Q03518","identifierLink":"https://www.uniprot.org/uniprotkb/Q03518/entry","name":"TAP1","description":"Antigen peptide transporter 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24221","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-780781","identifier":"Q03519","identifierLink":"https://www.uniprot.org/uniprotkb/Q03519/entry","name":"TAP2","description":"Antigen peptide transporter 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24221","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25770","complexName":"Cytosolic tRNA wobble base thiouridylase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Required for the 2-thiolation of cytosolic tRNA, specifically the uridine at the first anticodon position (U34) of glutamate, lysine, and glutamine tRNAs, which is believed to be crucial for both restriction of wobble in the corresponding split codon box and efficient codon-anticodon interaction. May act by catalyzing the adenylation of tRNAs","predictedComplex":false,"interactors":[{"ac":"EBI-15696976","identifier":"O94282","identifierLink":"https://www.uniprot.org/uniprotkb/O94282/entry","name":"ncs6","description":"Cytoplasmic tRNA 2-thiolation protein 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11807","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15697002","identifier":"Q9UUC7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UUC7/entry","name":"ctu2","description":"Cytoplasmic tRNA 2-thiolation protein 2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR20882","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25771","complexName":"MRH5C complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Translational activator complex which binds to and causes the association of both the small subunit of the mitoribosome (mtSSU) and cox1 (P07657) mRNA.","predictedComplex":false,"interactors":[{"ac":"EBI-59046663","identifier":"O74356","identifierLink":"https://www.uniprot.org/uniprotkb/O74356/entry","name":"mrh5","description":"Mitochondrial translation ATP-dependent RNA helicase mrh5","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR24031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59046678","identifier":"O14275","identifierLink":"https://www.uniprot.org/uniprotkb/O14275/entry","name":"ppr4","description":"Mitochondrial cox1 translation regulator ppr4","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR47938","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59046694","identifier":"O14204","identifierLink":"https://www.uniprot.org/uniprotkb/O14204/entry","name":"mtf2","description":"Mitochondrial translation factor 2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR39468","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59046710","identifier":"Q9UT03","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UT03/entry","name":"sls1","description":"Mitochondrial translation factor sls1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]}]},{"complexAC":"CPX-25772","complexName":"Phosphatidylinositol 3-kinase complex, class III, type II","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"A phosphatidylinositol 3-kinase complex that specifically phosphorylates 1-phosphatidyl-1D-myo-inositol(1-) (CHEBI:57880) in an ATP- and Mn(2+)-dependent manner. May function in vacuolar protein sorting.","predictedComplex":false,"interactors":[{"ac":"EBI-59041267","identifier":"P87117","identifierLink":"https://www.uniprot.org/uniprotkb/P87117/entry","name":"atg6","description":"Vacuolar protein sorting-associated protein atg6","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12768","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59041298","identifier":"O60149","identifierLink":"https://www.uniprot.org/uniprotkb/O60149/entry","name":"vps38","description":"Vacuolar protein sorting-associated protein 38","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15157","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59041316","identifier":"P50520","identifierLink":"https://www.uniprot.org/uniprotkb/P50520/entry","name":"pik3","description":"Phosphatidylinositol 3-kinase pik3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10048","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59041358","identifier":"O42900","identifierLink":"https://www.uniprot.org/uniprotkb/O42900/entry","name":"vps15","description":"Serine/threonine-protein kinase vps15","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR17583","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25773","complexName":"Atg1/ULK1 protein kinase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Central regulator of autophagy initiation. Essential for recruitment of Atg proteins to the pre-autophagosomal structure, the putative site for autophagosome formation, under starvation condition, resulting in the sequestration of cytoplasmic proteins and organelles for bulk degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-16158534","identifier":"O36019","identifierLink":"https://www.uniprot.org/uniprotkb/O36019/entry","name":"atg13","description":"Autophagy protein 13","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13430","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16158557","identifier":"O13978","identifierLink":"https://www.uniprot.org/uniprotkb/O13978/entry","name":"atg101","description":"Autophagy-related protein 101","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13292","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21242201","identifier":"O42651","identifierLink":"https://www.uniprot.org/uniprotkb/O42651/entry","name":"atg17","description":"Autophagy-related protein 17","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28005","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21244543","identifier":"O14261","identifierLink":"https://www.uniprot.org/uniprotkb/O14261/entry","name":"taf1","description":"Taz1-interacting factor 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59047074","identifier":"Q9Y7T4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y7T4/entry","name":"atg1","description":"Serine/threonine-protein kinase atg1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR24348","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25774","complexName":"CCR4-NOT mRNA deadenylase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Major cellular mRNA deadenylase complex, removing polyA tails that protect transcripts from degradation and promotes translation in the cytoplasm. The complex is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation, and general transcription regulation, potentially by promoting the resumption of elongation of arrested RNAPII when it encounters transcriptional blocks in vivo. The deadenylation and ubiquitinylation activities of the complex independently mediate gene repression, maintain heterochromatin integrity and ensure its efficient propagation within the mating type locus and at subtelomeres.","predictedComplex":false,"interactors":[{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-21243119","identifier":"Q92368","identifierLink":"https://www.uniprot.org/uniprotkb/Q92368/entry","name":"rcd1","description":"Cell differentiation protein rcd1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12262","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59072187","identifier":"O74874","identifierLink":"https://www.uniprot.org/uniprotkb/O74874/entry","name":"ccr4","description":"CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12121","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59072211","identifier":"O74856","identifierLink":"https://www.uniprot.org/uniprotkb/O74856/entry","name":"caf1","description":"Poly(A) ribonuclease pop2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10797","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59072240","identifier":"O13870","identifierLink":"https://www.uniprot.org/uniprotkb/O13870/entry","name":"not3","description":"General negative regulator of transcription subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23326","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59072258","identifier":"P87240","identifierLink":"https://www.uniprot.org/uniprotkb/P87240/entry","name":"not2","description":"General negative regulator of transcription subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23326","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59072274","identifier":"P87112","identifierLink":"https://www.uniprot.org/uniprotkb/P87112/entry","name":"not1","description":"General negative regulator of transcription subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13162","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59072298","identifier":"Q09818","identifierLink":"https://www.uniprot.org/uniprotkb/Q09818/entry","name":"yac4","description":"Putative general negative regulator of transcription C16C9.04c","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12603","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-25775","complexName":"Short transient receptor potential channel complex,TRPC1-TRPC4-TRPC5 variant","organismName":"Homo sapiens; 9606","description":"Non-selective, multimeric cation channel permeable by Na+ and Ca2+. Activators and modulators of channel activity may include endogenous and dietary lipids and metal ions such as Zn2+. Appear to play a role in a wide range of cellular processes that require calcium signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-929504","identifier":"Q9UBN4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UBN4/entry","name":"TRPC4","description":"Short transient receptor potential channel 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-929550","identifier":"Q9UL62","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UL62/entry","name":"TRPC5","description":"Short transient receptor potential channel 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-929665","identifier":"P48995","identifierLink":"https://www.uniprot.org/uniprotkb/P48995/entry","name":"TRPC1","description":"Short transient receptor potential channel 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25776","complexName":"Short transient receptor potential channel complex, TRPC5 variant","organismName":"Homo sapiens; 9606","description":"Non-selective, multimeric cation channel permeable by Na+ and Ca2+. Activators and modulators of channel activity may include endogenous and dietary lipids and metal ions such as Zn2+. Appears to play a role in a wide range of cellular processes that require calcium signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-929550","identifier":"Q9UL62","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UL62/entry","name":"TRPC5","description":"Short transient receptor potential channel 5","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25777","complexName":"RITS transcriptional silencing complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"RNAi effector complex. Dcr1 (Q09884)-processed siRNAs bind to the complex where Ago1 endonuclease activity cleaves the passenger strand siRNA forming an effector complex. This then targets specific chromosome regions by sequence-specific interactions involving either siRNA-DNA or siRNA-nascent transcript base pairing. The complex also acts as a platform for binding of Clr4 E3 ubiquitin ligase/methyltransferase complex (CPX-9241) resulting in heterochromatin formation and the RNA-dependent RNA polymerase complex to promote the synthesis of double-stranded RNA.","predictedComplex":false,"interactors":[{"ac":"EBI-421832","identifier":"Q10103","identifierLink":"https://www.uniprot.org/uniprotkb/Q10103/entry","name":"chp1","description":"Chromo domain-containing protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR22812","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-422882","identifier":"O74957","identifierLink":"https://www.uniprot.org/uniprotkb/O74957/entry","name":"ago1","description":"Protein argonaute","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR22891","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-423002","identifier":"O94687","identifierLink":"https://www.uniprot.org/uniprotkb/O94687/entry","name":"tas3","description":"RNA-induced transcriptional silencing complex protein tas3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]}]},{"complexAC":"CPX-25778","complexName":"Short transient receptor potential channel complex, TRPC4 variant","organismName":"Homo sapiens; 9606","description":"Non-selective, multimeric cation channel permeable by Na+ and Ca2+. Activators and modulators of channel activity may include endogenous and dietary lipids and metal ions such as Zn2+. Appear to play a role in a wide range of cellular processes that require calcium signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-929504","identifier":"Q9UBN4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UBN4/entry","name":"TRPC4","description":"Short transient receptor potential channel 4","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25779","complexName":"Argonaute siRNA chaperone complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Chaperone complex required for the assembly of heterochromatin and silencing of reporter genes inserted in the pericentromeric region of chromosomes. Binds double-stranded, rather than single-stranded siRNAs, and loads these molecule onto the RITS complex (CPX-25777).","predictedComplex":false,"interactors":[{"ac":"EBI-15624131","identifier":"Q9P7B8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P7B8/entry","name":"arb1","description":"Argonaute-binding protein 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-15624152","identifier":"Q10271","identifierLink":"https://www.uniprot.org/uniprotkb/Q10271/entry","name":"arb2","description":"Argonaute-binding protein 2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR21357","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-422882","identifier":"O74957","identifierLink":"https://www.uniprot.org/uniprotkb/O74957/entry","name":"ago1","description":"Protein argonaute","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR22891","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25780","complexName":"RNA-directed RNA polymerase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"RNA-dependent RNA polymerase activity required for the association of siRNAs with the RITS complex (CPX-25777) and for centromeric gene silencing. Synthesizes double-stranded RNA nascent transcripts from repetitive regions of the genome during S phase of the cell cycle. The RNase III–like enzyme Dcr1 (Q09884) then processes these double-stranded RNAs into siRNAs. The helicase hrr1 may increasie the processivity of rdp1 on its RNA templates.","predictedComplex":false,"interactors":[{"ac":"EBI-15624169","identifier":"O74465","identifierLink":"https://www.uniprot.org/uniprotkb/O74465/entry","name":"hrr1","description":"Helicase required for RNAi-mediated heterochromatin assembly 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10887","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15977521","identifier":"O74518","identifierLink":"https://www.uniprot.org/uniprotkb/O74518/entry","name":"cid12","description":"Poly(A) RNA polymerase cid12","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2652374","identifier":"O14227","identifierLink":"https://www.uniprot.org/uniprotkb/O14227/entry","name":"rdp1","description":"RNA-dependent RNA polymerase 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23079","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25781","complexName":"RAVE complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Mediates both the biosynthetic assembly and the glucose-induced reassembly of the V-ATPase (CPX-1193). Binds to V1 released from the vacuolar membrane by glucose deprivation and releases V1 upon glucose readdition. Appears to be aiding cytosolic V1 complexes to assemble with V0 at the membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-1172248","identifier":"Q9Y709","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y709/entry","name":"skp1","description":"Suppressor of kinetochore protein 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11165","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59048077","identifier":"Q9Y817","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y817/entry","name":"rav1","description":"Regulator of V-ATPase in vacuolar membrane protein 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13950","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59048096","identifier":"O74387","identifierLink":"https://www.uniprot.org/uniprotkb/O74387/entry","name":"rav2","description":"Regulator of V-ATPase in vacuolar membrane protein 2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13618","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25782","complexName":"SNARE complex STX17-SNAP29-VAMP8","organismName":"Homo sapiens; 9606","description":"SNARE complex required for the fusion of the double-membraned autophagosome with the single-membraned lysosome during starvation-induced bulk autophagy. Mediates membrane fusion through the spontaneous assembly of four complementary SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) motifs. SNAREs bind to each other in-trans, that is, with SNAREs anchored in each apposed tethered membrane. The assembly process leads to a tight connection between the fusing membranes and initiates membrane fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-2797775","identifier":"P56962","identifierLink":"https://www.uniprot.org/uniprotkb/P56962/entry","name":"STX17","description":"Syntaxin-17","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-490676","identifier":"O95721","identifierLink":"https://www.uniprot.org/uniprotkb/O95721/entry","name":"SNAP29","description":"Synaptosomal-associated protein 29","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727028","identifier":"Q9BV40","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BV40/entry","name":"VAMP8","description":"Vesicle-associated membrane protein 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25783","complexName":"SNARE complex STX17-SNAP29-VAMP7","organismName":"Homo sapiens; 9606","description":"SNARE complex required for the fusion of the double-membraned autophagosome with the single-membraned lysosome during starvation-induced bulk autophagy. Mediates membrane fusion through the spontaneous assembly of four complementary SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) motifs. SNAREs bind to each other in-trans, that is, with SNAREs anchored in each apposed tethered membrane. The assembly process leads to a tight connection between the fusing membranes and initiates membrane fusion..","predictedComplex":false,"interactors":[{"ac":"EBI-1052205","identifier":"P51809","identifierLink":"https://www.uniprot.org/uniprotkb/P51809/entry","name":"VAMP7","description":"Vesicle-associated membrane protein 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21136","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2797775","identifier":"P56962","identifierLink":"https://www.uniprot.org/uniprotkb/P56962/entry","name":"STX17","description":"Syntaxin-17","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-490676","identifier":"O95721","identifierLink":"https://www.uniprot.org/uniprotkb/O95721/entry","name":"SNAP29","description":"Synaptosomal-associated protein 29","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25785","complexName":"SWI5-SWI2 mating-type switching complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Selectively enables one of two cis-acting recombination enhancers, SRE2 adjacent to mat2-P or SRE3 adjacent to mat3-M thus designating a preferred heterochromatic donor cassette, mat2-P or mat3-M in a cell-type-specific manner.. Homothallic strains are either of the P or M mating-type and switch their mating type during vegetative growth. The complex localizes to SRE3 independently of Swi6 (P40381) or to SRE2 which is dependent on the presence of Swi6, to promote the strand exchange reaction required for mating-type switching. May also stimulate Rad51(P36601)-driven strand invasion.","predictedComplex":false,"interactors":[{"ac":"EBI-926902","identifier":"Q9UUB7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UUB7/entry","name":"swi5","description":"Mating-type switching protein swi5","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-926914","identifier":"Q10668","identifierLink":"https://www.uniprot.org/uniprotkb/Q10668/entry","name":"swi2","description":"Mating-type switching protein swi2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25786","complexName":"SNARE priming complex STX17-SNAP29-YKT6","organismName":"Homo sapiens; 9606","description":"Forms a SNARE priming complex on autophagosomes. preparing STX17 and SNAP29 in an optimal conformation to facilitate their subsequent interaction with VAMP8 on lysosomes ensuring efficient membrane fusion. As lysosomes approach the autophagosomes, VAMP8 displaces YKT6 from the priming complex, leading to the formation of a fusogenic SNARE complex, STX17-SNAP29-VAMP8 (CPX-25782).","predictedComplex":false,"interactors":[{"ac":"EBI-2797775","identifier":"P56962","identifierLink":"https://www.uniprot.org/uniprotkb/P56962/entry","name":"STX17","description":"Syntaxin-17","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4402903","identifier":"O15498","identifierLink":"https://www.uniprot.org/uniprotkb/O15498/entry","name":"YKT6","description":"Synaptobrevin homolog YKT6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45806","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-490676","identifier":"O95721","identifierLink":"https://www.uniprot.org/uniprotkb/O95721/entry","name":"SNAP29","description":"Synaptosomal-associated protein 29","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26028","complexName":"Mitochondrial CCA tRNA nucleotidyltransferase 1 complex","organismName":"Homo sapiens; 9606","description":"Responsible for the the addition of a CCA triplet at the 3'-end of mitochondrial tRNA which is required  for aminoacylation.and tRNA maturation. This immediately follows tRNA 5′- and 3'-processing by the RNase P (CPX-6155) and RNase Z (CPX-2240) complexes respectively. The 3′-CCA is an RNase Z antideterminant, which is recognized and not removed by ELAC2 to avoid futile cycling of the tRNAs between this complex and RNase Z.","predictedComplex":false,"interactors":[{"ac":"EBI-2107046","identifier":"Q7L0Y3","identifierLink":"https://www.uniprot.org/uniprotkb/Q7L0Y3/entry","name":"TRMT10C","description":"tRNA methyltransferase 10 homolog C","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13563","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25827394","identifier":"CHEBI:10668","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:10668","name":"trna precursor","description":"tRNA precursor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2839106","identifier":"Q96Q11","identifierLink":"https://www.uniprot.org/uniprotkb/Q96Q11/entry","name":"TRNT1","description":"CCA tRNA nucleotidyltransferase 1, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46173","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-79964","identifier":"Q99714","identifierLink":"https://www.uniprot.org/uniprotkb/Q99714/entry","name":"HSD17B10","description":"3-hydroxyacyl-CoA dehydrogenase type-2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43658","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26030","complexName":"DNA replication factor C complex, ATAD5 variant","organismName":"Homo sapiens; 9606","description":"DNA-dependent ATPase clamp-unloader complex that acts to remove PCNA (P12004, CPX-538) remaining on DNA after the completion of DNA replication and repair during the S phase of the cell cycle. The complex binds to DNA-loaded PCNA to induce opening of the PCNA ring, leading to the release of ATAD5-RFC bound-PCNA. ATAD5-RFC is thought to unload PCNA many-fold more efficiently than the canonical RFC complex (CPX-415). PCNA release from the chromatin after chromosomal duplication is crucial in preventing inappropriate recruitment of replication enzymes and preventing premature termination of DNA replication.\r\n\r\nAdditionally, ATAD5-RFC also participates in de-ubiquiniation of ubiquinated PCNA (Ub-PCNA) to aid in the removal of chromatin-bound Ub-PCNA from DNA to resume normal DNA replication after bypass.","predictedComplex":false,"interactors":[{"ac":"EBI-1055010","identifier":"P40938","identifierLink":"https://www.uniprot.org/uniprotkb/P40938/entry","name":"RFC3","description":"Replication factor C subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10980241","identifier":"Q96QE3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96QE3/entry","name":"ATAD5","description":"ATPase family AAA domain-containing protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23389","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-476409","identifier":"P35250","identifierLink":"https://www.uniprot.org/uniprotkb/P35250/entry","name":"RFC2","description":"Replication factor C subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-476655","identifier":"P35249","identifierLink":"https://www.uniprot.org/uniprotkb/P35249/entry","name":"RFC4","description":"Replication factor C subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712376","identifier":"P40937","identifierLink":"https://www.uniprot.org/uniprotkb/P40937/entry","name":"RFC5","description":"Replication factor C subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26034","complexName":"DSC E3 ubiquitin ligase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Required for the proteolytic cleavage of the sre1 transcriptional activator (Q9UUD1) to release the soluble transcription factor from the membrane. The sre1/SREBP-SCAP transcription regulator complex (CPX-25718) forms in the endoplasmic reticulum (ER). Under conditions of low sterols or low oxygen, the complex translocates from the ER to the Golgi where sre1 is proteolytically cleaved and freed to act as a master regulator of cellular lipid homeostasis which plays a critical role in the cells adaptation to hypoxia. cdc48 binds to the Dsc E3 ligase complex through the UBX domain of dsc5 and is required for sre1 cleavage under low oxygen","predictedComplex":false,"interactors":[{"ac":"EBI-61100749","identifier":"O43085","identifierLink":"https://www.uniprot.org/uniprotkb/O43085/entry","name":"dsc1","description":"DSC E3 ubiquitin ligase complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR22763","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61100771","identifier":"Q9UTK7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UTK7/entry","name":"dsc2","description":"DSC E3 ubiquitin ligase complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-61100785","identifier":"Q9HE10","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HE10/entry","name":"dsc3","description":"DSC E3 ubiquitin ligase complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28049","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61100800","identifier":"O14175","identifierLink":"https://www.uniprot.org/uniprotkb/O14175/entry","name":"dsc4","description":"DSC E3 ubiquitin ligase complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR39405","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61100819","identifier":"O74498","identifierLink":"https://www.uniprot.org/uniprotkb/O74498/entry","name":"ucp10","description":"UBX domain-containing protein 10","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23322","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26352","complexName":"Dynactin complex","organismName":"Homo sapiens; 9606","description":"Recruited to autoinhibited dynein, a retrograde microtubule motor complex, by a coiled-coil-containing adaptor (Bicaudal-D or Hook family) protein to form the tripartite dynein-dynactin-adaptor assembly which activates the processive, unidirectional movement of dynein. Dynactin and dynein contribute to a number of motility associated events including endomembrane movement, nuclear envelope breakdown, and mitotic spindle assembly.\r\n\r\nMutations in DCTN1 have been implicated in several neurodegenerative diseases. Co-localization of DCTN1 in Lewy body pathology has been associated with Perry syndrome, motor neuron diseases and progressive supranuclear palsy.","predictedComplex":false,"interactors":[{"ac":"EBI-2134033","identifier":"Q9UJW0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UJW0/entry","name":"DCTN4","description":"Dynactin subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13034","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2559415","identifier":"O00399","identifierLink":"https://www.uniprot.org/uniprotkb/O00399/entry","name":"DCTN6","description":"Dynactin subunit 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13072","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2559426","identifier":"Q9NZ32","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZ32/entry","name":"ACTR10","description":"Actin-related protein 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347442","identifier":"O75935","identifierLink":"https://www.uniprot.org/uniprotkb/O75935/entry","name":"DCTN3","description":"Dynactin subunit 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28360","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48432173","identifier":"CPX-8695","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-8695","name":"F-actin capping protein complex, CAPZA1 variant","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-715074","identifier":"Q13561","identifierLink":"https://www.uniprot.org/uniprotkb/Q13561/entry","name":"DCTN2","description":"Dynactin subunit 2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724352","identifier":"Q14203","identifierLink":"https://www.uniprot.org/uniprotkb/Q14203/entry","name":"DCTN1","description":"Dynactin subunit 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18916","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-747324","identifier":"Q9BTE1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BTE1/entry","name":"DCTN5","description":"Dynactin subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46126","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-774234","identifier":"P61163","identifierLink":"https://www.uniprot.org/uniprotkb/P61163/entry","name":"ACTR1A","description":"Alpha-centractin","stochiometry":"minValue: 8, maxValue: 8","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26353","complexName":"SHOC2-HRAS-PPP1CA complex","organismName":"Homo sapiens; 9606","description":"Holophosphatase complex which dephosphorylates members of RAF family proteins, RAF1 (P04049), BRAF (P15056) and ARAF (P10398) at key inhibitory phosphorylation sites Ser-259, Ser-365 and Ser-214, respectively, while eliminating inhibitory phosphorylation on RAF family proteins to potentiate MAPK signalling. Functions as a key regulator of RTK-RAS signalling, a pathway which regulates cell proliferation and survival through the MAP kinase cascade. \r\n\r\nMutations mapped to protein-protein interfaces in the complex impair complex formation and stabilization. Gain-of-function and loss-of-function mutations in SHOC2 are linked to driving RASopathy and RAS-driven cancers including colorectal cancers.","predictedComplex":false,"interactors":[{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-25820308","identifier":"CHEBI:37565","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:37565","name":"gtp(4-)","description":"GTP(4-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-350145","identifier":"P01112","identifierLink":"https://www.uniprot.org/uniprotkb/P01112/entry","name":"HRAS","description":"GTPase HRas","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24070","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357253","identifier":"P62136","identifierLink":"https://www.uniprot.org/uniprotkb/P62136/entry","name":"PPP1CA","description":"Serine/threonine-protein phosphatase PP1-alpha catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11668","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-993879","identifier":"Q9UQ13","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UQ13/entry","name":"SHOC2","description":"Leucine-rich repeat protein SHOC-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45752","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26354","complexName":"SHOC2-NRAS-PPP1CA complex","organismName":"Homo sapiens; 9606","description":"Holophosphatase complex which dephosphorylates members of RAF family proteins, RAF1 (P04049), BRAF (P15056) and ARAF (P10398) at key inhibitory phosphorylation sites Ser-259, Ser-365 and Ser-214, respectively, while eliminating inhibitory phosphorylation on RAF family proteins to potentiate MAPK signalling. Functions as a key regulator of RTK-RAS signalling, a pathway which regulates cell proliferation and survival through the MAP kinase cascade. \r\n\r\nMutations mapped to protein-protein interfaces in the complex impair complex formation and stabilization. Gain-of-function and loss-of-function mutations in SHOC2 are linked to driving RASopathy and RAS-driven cancers including colorectal cancers.","predictedComplex":false,"interactors":[{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-25820308","identifier":"CHEBI:37565","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:37565","name":"gtp(4-)","description":"GTP(4-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-357253","identifier":"P62136","identifierLink":"https://www.uniprot.org/uniprotkb/P62136/entry","name":"PPP1CA","description":"Serine/threonine-protein phosphatase PP1-alpha catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11668","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-721993","identifier":"P01111","identifierLink":"https://www.uniprot.org/uniprotkb/P01111/entry","name":"NRAS","description":"GTPase NRas","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24070","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-993879","identifier":"Q9UQ13","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UQ13/entry","name":"SHOC2","description":"Leucine-rich repeat protein SHOC-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45752","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26355","complexName":"SHOC2-KRAS-PPP1CA complex","organismName":"Homo sapiens; 9606","description":"Holophosphatase complex which dephosphorylates members of RAF family proteins, RAF1 (P04049), BRAF (P15056) and ARAF (P10398) at key inhibitory phosphorylation sites Ser-259, Ser-365 and Ser-214, respectively, while eliminating inhibitory phosphorylation on RAF family proteins to potentiate MAPK signalling. Functions as a key regulator of RTK-RAS signalling, a pathway which regulates cell proliferation and survival through the MAP kinase cascade. \r\n\r\nMutations mapped to protein-protein interfaces in the complex impair complex formation and stabilization. Gain-of-function and loss-of-function mutations in SHOC2 are linked to driving RASopathy and RAS-driven cancers including colorectal cancers.","predictedComplex":false,"interactors":[{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-25820308","identifier":"CHEBI:37565","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:37565","name":"gtp(4-)","description":"GTP(4-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-357253","identifier":"P62136","identifierLink":"https://www.uniprot.org/uniprotkb/P62136/entry","name":"PPP1CA","description":"Serine/threonine-protein phosphatase PP1-alpha catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11668","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-367415","identifier":"P01116","identifierLink":"https://www.uniprot.org/uniprotkb/P01116/entry","name":"KRAS","description":"GTPase KRas","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24070","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-993879","identifier":"Q9UQ13","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UQ13/entry","name":"SHOC2","description":"Leucine-rich repeat protein SHOC-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45752","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26356","complexName":"DNA replication factor C complex, CHTF18 variant","organismName":"Homo sapiens; 9606","description":"DNA-dependent ATPase clamp-loader complex specific for leading strand DNA synthesis but also establishing cohesion between sister chromatids. Binds the leading strand DNA POLE (Q07864) which stimulates the complex to load DNA polymerase processivity factor PCNA (P12004, CPX-538) onto primed and gapped leading strand DNA in an ATP-dependent manner. CTF18-RFC has a lower PCNA loading activity than the canonical RFC complex (CPX-415).","predictedComplex":false,"interactors":[{"ac":"EBI-1055010","identifier":"P40938","identifierLink":"https://www.uniprot.org/uniprotkb/P40938/entry","name":"RFC3","description":"Replication factor C subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11143782","identifier":"Q9BVC3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BVC3/entry","name":"DSCC1","description":"Sister chromatid cohesion protein DCC1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13395","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1237523","identifier":"Q8WVB6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WVB6/entry","name":"CHTF18","description":"Chromosome transmission fidelity protein 18 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23389","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3920309","identifier":"P0CG13","identifierLink":"https://www.uniprot.org/uniprotkb/P0CG13/entry","name":"CHTF8","description":"Chromosome transmission fidelity protein 8 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28605","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-476409","identifier":"P35250","identifierLink":"https://www.uniprot.org/uniprotkb/P35250/entry","name":"RFC2","description":"Replication factor C subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-476655","identifier":"P35249","identifierLink":"https://www.uniprot.org/uniprotkb/P35249/entry","name":"RFC4","description":"Replication factor C subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712376","identifier":"P40937","identifierLink":"https://www.uniprot.org/uniprotkb/P40937/entry","name":"RFC5","description":"Replication factor C subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26357","complexName":"Dynein-2 complex, light-chain variant 1","organismName":"Homo sapiens; 9606","description":"Multi-protein molecular motor. Dynein-2 is one of three major classes of dynein, which share a conserved motor domain that couples ATP hydrolysis with conformational changes to power movement of cargoes along microtubules within cilia. Dynein-2 is vital for the assembly and powering of retrograde intra-flagellar transport of cargoes from the tip of cilia and flagella to the base for recycling or degradation .\r\n\r\nActs as a negative regulator of the Toll-like receptor and IL1R1 (P14778) signalling pathways. Inhibits the MAP3K7 (O43318) induced NF-kappa-B activation pathway.\r\n\r\nMutations in dynein's intermediate chains (ICs), light IC and the heavy chain (HC) DYNC2H1 are associated microcephaly, as well as a subset of skeletal-ciliopathies encompassing a wide spectrum of human diseases including primary ciliary dyskinesia and short-rib thoracic dysplasia.","predictedComplex":false,"interactors":[{"ac":"EBI-1176455","identifier":"P63172","identifierLink":"https://www.uniprot.org/uniprotkb/P63172/entry","name":"DYNLT1","description":"Dynein light chain Tctex-type 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2512957","identifier":"Q8NCM8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NCM8/entry","name":"DYNC2H1","description":"Cytoplasmic dynein 2 heavy chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2556085","identifier":"Q8WVS4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WVS4/entry","name":"DYNC2I1","description":"Cytoplasmic dynein 2 intermediate chain 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16022","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2556091","identifier":"Q96EX3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96EX3/entry","name":"DYNC2I2","description":"Cytoplasmic dynein 2 intermediate chain 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2692044","identifier":"Q8WW35","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WW35/entry","name":"DYNLT2B","description":"Dynein light chain Tctex-type protein 2B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-349105","identifier":"P63167","identifierLink":"https://www.uniprot.org/uniprotkb/P63167/entry","name":"DYNLL1","description":"Dynein light chain 1, cytoplasmic","stochiometry":"minValue: 2, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372128","identifier":"Q9NP97","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NP97/entry","name":"DYNLRB1","description":"Dynein light chain roadblock-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8568003","identifier":"Q8TCX1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TCX1/entry","name":"DYNC2LI1","description":"Cytoplasmic dynein 2 light intermediate chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13236","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26360","complexName":"Dynein-2 complex, light-chain variant 2","organismName":"Homo sapiens; 9606","description":"Multi-protein molecular motor. 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Inhibits the MAP3K7 (O43318) induced NF-kappa-B activation pathway.\r\n\r\nMutations in dynein's intermediate chains (ICs), light IC and the heavy chain (HC) DYNC2H1 are associated microcephaly, as well as a subset of skeletal-ciliopathies encompassing a wide spectrum of human diseases including primary ciliary dyskinesia and short-rib thoracic dysplasia.","predictedComplex":false,"interactors":[{"ac":"EBI-1176455","identifier":"P63172","identifierLink":"https://www.uniprot.org/uniprotkb/P63172/entry","name":"DYNLT1","description":"Dynein light chain Tctex-type 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2512957","identifier":"Q8NCM8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NCM8/entry","name":"DYNC2H1","description":"Cytoplasmic dynein 2 heavy chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2556085","identifier":"Q8WVS4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WVS4/entry","name":"DYNC2I1","description":"Cytoplasmic dynein 2 intermediate chain 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16022","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2556091","identifier":"Q96EX3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96EX3/entry","name":"DYNC2I2","description":"Cytoplasmic dynein 2 intermediate chain 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2692044","identifier":"Q8WW35","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WW35/entry","name":"DYNLT2B","description":"Dynein light chain Tctex-type protein 2B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372128","identifier":"Q9NP97","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NP97/entry","name":"DYNLRB1","description":"Dynein light chain roadblock-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742371","identifier":"Q96FJ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96FJ2/entry","name":"DYNLL2","description":"Dynein light chain 2, cytoplasmic","stochiometry":"minValue: 2, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8568003","identifier":"Q8TCX1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TCX1/entry","name":"DYNC2LI1","description":"Cytoplasmic dynein 2 light intermediate chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13236","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26361","complexName":"Dynein-2 complex, light-chain variant 3","organismName":"Homo sapiens; 9606","description":"Multi-protein molecular motor. 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Inhibits the MAP3K7 (O43318) induced NF-kappa-B activation pathway.\r\n\r\nMutations in dynein's intermediate chains (ICs), light IC and the heavy chain (HC) DYNC2H1 are associated microcephaly, as well as a subset of skeletal-ciliopathies encompassing a wide spectrum of human diseases including primary ciliary dyskinesia and short-rib thoracic dysplasia.","predictedComplex":false,"interactors":[{"ac":"EBI-2512957","identifier":"Q8NCM8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NCM8/entry","name":"DYNC2H1","description":"Cytoplasmic dynein 2 heavy chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2556085","identifier":"Q8WVS4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WVS4/entry","name":"DYNC2I1","description":"Cytoplasmic dynein 2 intermediate chain 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16022","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2556091","identifier":"Q96EX3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96EX3/entry","name":"DYNC2I2","description":"Cytoplasmic dynein 2 intermediate chain 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2692044","identifier":"Q8WW35","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WW35/entry","name":"DYNLT2B","description":"Dynein light chain Tctex-type protein 2B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372128","identifier":"Q9NP97","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NP97/entry","name":"DYNLRB1","description":"Dynein light chain roadblock-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742371","identifier":"Q96FJ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96FJ2/entry","name":"DYNLL2","description":"Dynein light chain 2, cytoplasmic","stochiometry":"minValue: 2, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743027","identifier":"P51808","identifierLink":"https://www.uniprot.org/uniprotkb/P51808/entry","name":"DYNLT3","description":"Dynein light chain Tctex-type 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8568003","identifier":"Q8TCX1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TCX1/entry","name":"DYNC2LI1","description":"Cytoplasmic dynein 2 light intermediate chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13236","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26362","complexName":"Dynein-2 complex, light-chain variant 4","organismName":"Homo sapiens; 9606","description":"Multi-protein molecular motor. Dynein-2 is one of three major classes of dynein, which share a conserved motor domain that couples ATP hydrolysis with conformational changes to power movement of cargoes along microtubules within cilia. Dynein-2 is vital for the assembly and powering of retrograde intra-flagellar transport of cargoes from the tip of cilia and flagella to the base for recycling or degradation .\r\n\r\nActs as a negative regulator of the Toll-like receptor and IL1R1 (P14778) signalling pathways. Inhibits the MAP3K7 (O43318) induced NF-kappa-B activation pathway.\r\n\r\nMutations in dynein's intermediate chains (ICs), light IC and the heavy chain (HC) DYNC2H1 are associated microcephaly, as well as a subset of skeletal-ciliopathies encompassing a wide spectrum of human diseases including primary ciliary dyskinesia and short-rib thoracic dysplasia.","predictedComplex":false,"interactors":[{"ac":"EBI-2512957","identifier":"Q8NCM8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NCM8/entry","name":"DYNC2H1","description":"Cytoplasmic dynein 2 heavy chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2556085","identifier":"Q8WVS4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WVS4/entry","name":"DYNC2I1","description":"Cytoplasmic dynein 2 intermediate chain 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16022","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2556091","identifier":"Q96EX3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96EX3/entry","name":"DYNC2I2","description":"Cytoplasmic dynein 2 intermediate chain 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2692044","identifier":"Q8WW35","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WW35/entry","name":"DYNLT2B","description":"Dynein light chain Tctex-type protein 2B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-349105","identifier":"P63167","identifierLink":"https://www.uniprot.org/uniprotkb/P63167/entry","name":"DYNLL1","description":"Dynein light chain 1, cytoplasmic","stochiometry":"minValue: 2, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372128","identifier":"Q9NP97","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NP97/entry","name":"DYNLRB1","description":"Dynein light chain roadblock-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743027","identifier":"P51808","identifierLink":"https://www.uniprot.org/uniprotkb/P51808/entry","name":"DYNLT3","description":"Dynein light chain Tctex-type 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8568003","identifier":"Q8TCX1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TCX1/entry","name":"DYNC2LI1","description":"Cytoplasmic dynein 2 light intermediate chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13236","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26363","complexName":"Dynein-2 complex, light-chain variant 5","organismName":"Homo sapiens; 9606","description":"Multi-protein molecular motor. 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Inhibits the MAP3K7 (O43318) induced NF-kappa-B activation pathway.\r\n\r\nMutations in dynein's intermediate chains (ICs), light IC and the heavy chain (HC) DYNC2H1 are associated microcephaly, as well as a subset of skeletal-ciliopathies encompassing a wide spectrum of human diseases including primary ciliary dyskinesia and short-rib thoracic dysplasia.","predictedComplex":false,"interactors":[{"ac":"EBI-1176455","identifier":"P63172","identifierLink":"https://www.uniprot.org/uniprotkb/P63172/entry","name":"DYNLT1","description":"Dynein light chain Tctex-type 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11918120","identifier":"Q8TF09","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TF09/entry","name":"DYNLRB2","description":"Dynein light chain roadblock-type 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2512957","identifier":"Q8NCM8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NCM8/entry","name":"DYNC2H1","description":"Cytoplasmic dynein 2 heavy chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2556085","identifier":"Q8WVS4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WVS4/entry","name":"DYNC2I1","description":"Cytoplasmic dynein 2 intermediate chain 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16022","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2556091","identifier":"Q96EX3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96EX3/entry","name":"DYNC2I2","description":"Cytoplasmic dynein 2 intermediate chain 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2692044","identifier":"Q8WW35","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WW35/entry","name":"DYNLT2B","description":"Dynein light chain Tctex-type protein 2B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-349105","identifier":"P63167","identifierLink":"https://www.uniprot.org/uniprotkb/P63167/entry","name":"DYNLL1","description":"Dynein light chain 1, cytoplasmic","stochiometry":"minValue: 2, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8568003","identifier":"Q8TCX1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TCX1/entry","name":"DYNC2LI1","description":"Cytoplasmic dynein 2 light intermediate chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13236","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26364","complexName":"Dynein-2 complex, light-chain variant 6","organismName":"Homo sapiens; 9606","description":"Multi-protein molecular motor. Dynein-2 is one of three major classes of dynein, which share a conserved motor domain that couples ATP hydrolysis with conformational changes to power movement of cargoes along microtubules within cilia. Dynein-2 is vital for the assembly and powering of retrograde intra-flagellar transport of cargoes from the tip of cilia and flagella to the base for recycling or degradation .\r\n\r\nActs as a negative regulator of the Toll-like receptor and IL1R1 (P14778) signalling pathways. Inhibits the MAP3K7 (O43318) induced NF-kappa-B activation pathway.\r\n\r\nMutations in dynein's intermediate chains (ICs), light IC and the heavy chain (HC) DYNC2H1 are associated microcephaly, as well as a subset of skeletal-ciliopathies encompassing a wide spectrum of human diseases including primary ciliary dyskinesia and short-rib thoracic dysplasia.","predictedComplex":false,"interactors":[{"ac":"EBI-1176455","identifier":"P63172","identifierLink":"https://www.uniprot.org/uniprotkb/P63172/entry","name":"DYNLT1","description":"Dynein light chain Tctex-type 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11918120","identifier":"Q8TF09","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TF09/entry","name":"DYNLRB2","description":"Dynein light chain roadblock-type 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2512957","identifier":"Q8NCM8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NCM8/entry","name":"DYNC2H1","description":"Cytoplasmic dynein 2 heavy chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2556085","identifier":"Q8WVS4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WVS4/entry","name":"DYNC2I1","description":"Cytoplasmic dynein 2 intermediate chain 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16022","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2556091","identifier":"Q96EX3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96EX3/entry","name":"DYNC2I2","description":"Cytoplasmic dynein 2 intermediate chain 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2692044","identifier":"Q8WW35","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WW35/entry","name":"DYNLT2B","description":"Dynein light chain Tctex-type protein 2B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742371","identifier":"Q96FJ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96FJ2/entry","name":"DYNLL2","description":"Dynein light chain 2, cytoplasmic","stochiometry":"minValue: 2, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8568003","identifier":"Q8TCX1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TCX1/entry","name":"DYNC2LI1","description":"Cytoplasmic dynein 2 light intermediate chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13236","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26365","complexName":"Dynein-2 complex, light-chain variant 7","organismName":"Homo sapiens; 9606","description":"Multi-protein molecular motor. Dynein-2 is one of three major classes of dynein, which share a conserved motor domain that couples ATP hydrolysis with conformational changes to power movement of cargoes along microtubules within cilia. Dynein-2 is vital for the assembly and powering of retrograde intra-flagellar transport of cargoes from the tip of cilia and flagella to the base for recycling or degradation .\r\n\r\nActs as a negative regulator of the Toll-like receptor and IL1R1 (P14778) signalling pathways. Inhibits the MAP3K7 (O43318) induced NF-kappa-B activation pathway.\r\n\r\nMutations in dynein's intermediate chains (ICs), light IC and the heavy chain (HC) DYNC2H1 are associated microcephaly, as well as a subset of skeletal-ciliopathies encompassing a wide spectrum of human diseases including primary ciliary dyskinesia and short-rib thoracic dysplasia.","predictedComplex":false,"interactors":[{"ac":"EBI-11918120","identifier":"Q8TF09","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TF09/entry","name":"DYNLRB2","description":"Dynein light chain roadblock-type 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2512957","identifier":"Q8NCM8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NCM8/entry","name":"DYNC2H1","description":"Cytoplasmic dynein 2 heavy chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2556085","identifier":"Q8WVS4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WVS4/entry","name":"DYNC2I1","description":"Cytoplasmic dynein 2 intermediate chain 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16022","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2556091","identifier":"Q96EX3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96EX3/entry","name":"DYNC2I2","description":"Cytoplasmic dynein 2 intermediate chain 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2692044","identifier":"Q8WW35","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WW35/entry","name":"DYNLT2B","description":"Dynein light chain Tctex-type protein 2B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742371","identifier":"Q96FJ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96FJ2/entry","name":"DYNLL2","description":"Dynein light chain 2, cytoplasmic","stochiometry":"minValue: 2, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743027","identifier":"P51808","identifierLink":"https://www.uniprot.org/uniprotkb/P51808/entry","name":"DYNLT3","description":"Dynein light chain Tctex-type 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8568003","identifier":"Q8TCX1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TCX1/entry","name":"DYNC2LI1","description":"Cytoplasmic dynein 2 light intermediate chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13236","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26366","complexName":"Dynein-2 complex, light-chain variant 8","organismName":"Homo sapiens; 9606","description":"Multi-protein molecular motor. Dynein-2 is one of three major classes of dynein, which share a conserved motor domain that couples ATP hydrolysis with conformational changes to power movement of cargoes along microtubules within cilia. Dynein-2 is vital for the assembly and powering of retrograde intra-flagellar transport of cargoes from the tip of cilia and flagella to the base for recycling or degradation .\r\n\r\nActs as a negative regulator of the Toll-like receptor and IL1R1 (P14778) signalling pathways. Inhibits the MAP3K7 (O43318) induced NF-kappa-B activation pathway.\r\n\r\nMutations in dynein's intermediate chains (ICs), light IC and the heavy chain (HC) DYNC2H1 are associated microcephaly, as well as a subset of skeletal-ciliopathies encompassing a wide spectrum of human diseases including primary ciliary dyskinesia and short-rib thoracic dysplasia.","predictedComplex":false,"interactors":[{"ac":"EBI-11918120","identifier":"Q8TF09","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TF09/entry","name":"DYNLRB2","description":"Dynein light chain roadblock-type 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2512957","identifier":"Q8NCM8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NCM8/entry","name":"DYNC2H1","description":"Cytoplasmic dynein 2 heavy chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2556085","identifier":"Q8WVS4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WVS4/entry","name":"DYNC2I1","description":"Cytoplasmic dynein 2 intermediate chain 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16022","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2556091","identifier":"Q96EX3","identifierLink":"https://www.uniprot.org/uniprotkb/Q96EX3/entry","name":"DYNC2I2","description":"Cytoplasmic dynein 2 intermediate chain 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2692044","identifier":"Q8WW35","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WW35/entry","name":"DYNLT2B","description":"Dynein light chain Tctex-type protein 2B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-349105","identifier":"P63167","identifierLink":"https://www.uniprot.org/uniprotkb/P63167/entry","name":"DYNLL1","description":"Dynein light chain 1, cytoplasmic","stochiometry":"minValue: 2, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743027","identifier":"P51808","identifierLink":"https://www.uniprot.org/uniprotkb/P51808/entry","name":"DYNLT3","description":"Dynein light chain Tctex-type 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8568003","identifier":"Q8TCX1","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TCX1/entry","name":"DYNC2LI1","description":"Cytoplasmic dynein 2 light intermediate chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13236","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26367","complexName":"Dynein-1 complex, variant 2","organismName":"Homo sapiens; 9606","description":"Multi-protein molecular motor. Dynein-1 is one of three major classes of dynein, which share a conserved motor domain that couples ATP hydrolysis with conformational changes to power intracellular retrograde movement of cargoes including vesicles and organelles along microtubules within the cytoplasm. Depletion of DYNC1LI1 present in this complex is thought to reduce dynein-1 binding to spindle assembly checkpoint proteins which ensure correct orientation of sister chromatids needed for the proper segregation during anaphase.\r\n\r\nMutations in DYNC1H1 have been implicated in neurological disorders including an axonal form of Charcot-Marie-Tooth disease.","predictedComplex":false,"interactors":[{"ac":"EBI-1176455","identifier":"P63172","identifierLink":"https://www.uniprot.org/uniprotkb/P63172/entry","name":"DYNLT1","description":"Dynein light chain Tctex-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2556107","identifier":"Q9Y6G9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6G9/entry","name":"DYNC1LI1","description":"Cytoplasmic dynein 1 light intermediate chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12688","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-349105","identifier":"P63167","identifierLink":"https://www.uniprot.org/uniprotkb/P63167/entry","name":"DYNLL1","description":"Dynein light chain 1, cytoplasmic","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356015","identifier":"Q14204","identifierLink":"https://www.uniprot.org/uniprotkb/Q14204/entry","name":"DYNC1H1","description":"Cytoplasmic dynein 1 heavy chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372128","identifier":"Q9NP97","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NP97/entry","name":"DYNLRB1","description":"Dynein light chain roadblock-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742998","identifier":"Q13409","identifierLink":"https://www.uniprot.org/uniprotkb/Q13409/entry","name":"DYNC1I2","description":"Cytoplasmic dynein 1 intermediate chain 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26369","complexName":"Dynein-1 complex, variant 3","organismName":"Homo sapiens; 9606","description":"Multi-protein molecular motor. Dynein-1 is one of three major classes of dynein, which share a conserved motor domain that couples ATP hydrolysis with conformational changes to power intracellular retrograde movement of cargoes including vesicles and organelles along microtubules within the cytoplasm.\r\n\r\nMutations in DYNC1H1 have been implicated in neurological disorders including an axonal form of Charcot-Marie-Tooth disease.","predictedComplex":false,"interactors":[{"ac":"EBI-1176455","identifier":"P63172","identifierLink":"https://www.uniprot.org/uniprotkb/P63172/entry","name":"DYNLT1","description":"Dynein light chain Tctex-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-349105","identifier":"P63167","identifierLink":"https://www.uniprot.org/uniprotkb/P63167/entry","name":"DYNLL1","description":"Dynein light chain 1, cytoplasmic","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356015","identifier":"Q14204","identifierLink":"https://www.uniprot.org/uniprotkb/Q14204/entry","name":"DYNC1H1","description":"Cytoplasmic dynein 1 heavy chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366267","identifier":"O14576","identifierLink":"https://www.uniprot.org/uniprotkb/O14576/entry","name":"DYNC1I1","description":"Cytoplasmic dynein 1 intermediate chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372128","identifier":"Q9NP97","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NP97/entry","name":"DYNLRB1","description":"Dynein light chain roadblock-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-715294","identifier":"O43237","identifierLink":"https://www.uniprot.org/uniprotkb/O43237/entry","name":"DYNC1LI2","description":"Cytoplasmic dynein 1 light intermediate chain 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12688","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26370","complexName":"Dynein-1 complex, variant 4","organismName":"Homo sapiens; 9606","description":"Multi-protein molecular motor. Dynein-1 is one of three major classes of dynein, which share a conserved motor domain that couples ATP hydrolysis with conformational changes to power intracellular retrograde movement of cargoes including vesicles and organelles along microtubules within the cytoplasm. Depletion of DYNC1LI1 present in this complex is thought to reduce dynein-1 binding to spindle assembly checkpoint proteins which ensure correct orientation of sister chromatids needed for the proper segregation during anaphase.\r\n\r\nMutations in DYNC1H1 have been implicated in neurological disorders including an axonal form of Charcot-Marie-Tooth disease.","predictedComplex":false,"interactors":[{"ac":"EBI-1176455","identifier":"P63172","identifierLink":"https://www.uniprot.org/uniprotkb/P63172/entry","name":"DYNLT1","description":"Dynein light chain Tctex-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2556107","identifier":"Q9Y6G9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6G9/entry","name":"DYNC1LI1","description":"Cytoplasmic dynein 1 light intermediate chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12688","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-349105","identifier":"P63167","identifierLink":"https://www.uniprot.org/uniprotkb/P63167/entry","name":"DYNLL1","description":"Dynein light chain 1, cytoplasmic","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356015","identifier":"Q14204","identifierLink":"https://www.uniprot.org/uniprotkb/Q14204/entry","name":"DYNC1H1","description":"Cytoplasmic dynein 1 heavy chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366267","identifier":"O14576","identifierLink":"https://www.uniprot.org/uniprotkb/O14576/entry","name":"DYNC1I1","description":"Cytoplasmic dynein 1 intermediate chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372128","identifier":"Q9NP97","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NP97/entry","name":"DYNLRB1","description":"Dynein light chain roadblock-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26371","complexName":"Dynein-1 complex, variant 5","organismName":"Homo sapiens; 9606","description":"Multi-protein molecular motor. Dynein-1 is one of three major classes of dynein, which share a conserved motor domain that couples ATP hydrolysis with conformational changes to power intracellular retrograde movement of cargoes including vesicles and organelles along microtubules within the cytoplasm.\r\n\r\nMutations in DYNC1H1 have been implicated in neurological disorders including an axonal form of Charcot-Marie-Tooth disease.","predictedComplex":false,"interactors":[{"ac":"EBI-1176455","identifier":"P63172","identifierLink":"https://www.uniprot.org/uniprotkb/P63172/entry","name":"DYNLT1","description":"Dynein light chain Tctex-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11918120","identifier":"Q8TF09","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TF09/entry","name":"DYNLRB2","description":"Dynein light chain roadblock-type 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-349105","identifier":"P63167","identifierLink":"https://www.uniprot.org/uniprotkb/P63167/entry","name":"DYNLL1","description":"Dynein light chain 1, cytoplasmic","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356015","identifier":"Q14204","identifierLink":"https://www.uniprot.org/uniprotkb/Q14204/entry","name":"DYNC1H1","description":"Cytoplasmic dynein 1 heavy chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366267","identifier":"O14576","identifierLink":"https://www.uniprot.org/uniprotkb/O14576/entry","name":"DYNC1I1","description":"Cytoplasmic dynein 1 intermediate chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-715294","identifier":"O43237","identifierLink":"https://www.uniprot.org/uniprotkb/O43237/entry","name":"DYNC1LI2","description":"Cytoplasmic dynein 1 light intermediate chain 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12688","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26372","complexName":"Dynein-1 complex, variant 6","organismName":"Homo sapiens; 9606","description":"Multi-protein molecular motor. Dynein-1 is one of three major classes of dynein, which share a conserved motor domain that couples ATP hydrolysis with conformational changes to power intracellular retrograde movement of cargoes including vesicles and organelles along microtubules within the cytoplasm. Depletion of DYNC1LI1 present in this complex is thought to reduce dynein-1 binding to spindle assembly checkpoint proteins which ensure correct orientation of sister chromatids needed for the proper segregation during anaphase.\r\n\r\nMutations in DYNC1H1 have been implicated in neurological disorders including an axonal form of Charcot-Marie-Tooth disease.","predictedComplex":false,"interactors":[{"ac":"EBI-1176455","identifier":"P63172","identifierLink":"https://www.uniprot.org/uniprotkb/P63172/entry","name":"DYNLT1","description":"Dynein light chain Tctex-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11918120","identifier":"Q8TF09","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TF09/entry","name":"DYNLRB2","description":"Dynein light chain roadblock-type 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2556107","identifier":"Q9Y6G9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6G9/entry","name":"DYNC1LI1","description":"Cytoplasmic dynein 1 light intermediate chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12688","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-349105","identifier":"P63167","identifierLink":"https://www.uniprot.org/uniprotkb/P63167/entry","name":"DYNLL1","description":"Dynein light chain 1, cytoplasmic","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356015","identifier":"Q14204","identifierLink":"https://www.uniprot.org/uniprotkb/Q14204/entry","name":"DYNC1H1","description":"Cytoplasmic dynein 1 heavy chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366267","identifier":"O14576","identifierLink":"https://www.uniprot.org/uniprotkb/O14576/entry","name":"DYNC1I1","description":"Cytoplasmic dynein 1 intermediate chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26373","complexName":"Dynein-1 complex, variant 7","organismName":"Homo sapiens; 9606","description":"Multi-protein molecular motor. Dynein-1 is one of three major classes of dynein, which share a conserved motor domain that couples ATP hydrolysis with conformational changes to power intracellular retrograde movement of cargoes including vesicles and organelles along microtubules within the cytoplasm.\r\n\r\nMutations in DYNC1H1 have been implicated in neurological disorders including an axonal form of Charcot-Marie-Tooth disease.","predictedComplex":false,"interactors":[{"ac":"EBI-1176455","identifier":"P63172","identifierLink":"https://www.uniprot.org/uniprotkb/P63172/entry","name":"DYNLT1","description":"Dynein light chain Tctex-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11918120","identifier":"Q8TF09","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TF09/entry","name":"DYNLRB2","description":"Dynein light chain roadblock-type 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-349105","identifier":"P63167","identifierLink":"https://www.uniprot.org/uniprotkb/P63167/entry","name":"DYNLL1","description":"Dynein light chain 1, cytoplasmic","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356015","identifier":"Q14204","identifierLink":"https://www.uniprot.org/uniprotkb/Q14204/entry","name":"DYNC1H1","description":"Cytoplasmic dynein 1 heavy chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-715294","identifier":"O43237","identifierLink":"https://www.uniprot.org/uniprotkb/O43237/entry","name":"DYNC1LI2","description":"Cytoplasmic dynein 1 light intermediate chain 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12688","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742998","identifier":"Q13409","identifierLink":"https://www.uniprot.org/uniprotkb/Q13409/entry","name":"DYNC1I2","description":"Cytoplasmic dynein 1 intermediate chain 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26374","complexName":"Dynein-1 complex, variant 8","organismName":"Homo sapiens; 9606","description":"Multi-protein molecular motor. Dynein-1 is one of three major classes of dynein, which share a conserved motor domain that couples ATP hydrolysis with conformational changes to power intracellular retrograde movement of cargoes including vesicles and organelles along microtubules within the cytoplasm. Depletion of DYNC1LI1 present in this complex is thought to reduce dynein-1 binding to spindle assembly checkpoint proteins which ensure correct orientation of sister chromatids needed for the proper segregation during anaphase.\r\n\r\nMutations in DYNC1H1 have been implicated in neurological disorders including an axonal form of Charcot-Marie-Tooth disease.","predictedComplex":false,"interactors":[{"ac":"EBI-1176455","identifier":"P63172","identifierLink":"https://www.uniprot.org/uniprotkb/P63172/entry","name":"DYNLT1","description":"Dynein light chain Tctex-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11918120","identifier":"Q8TF09","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TF09/entry","name":"DYNLRB2","description":"Dynein light chain roadblock-type 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2556107","identifier":"Q9Y6G9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6G9/entry","name":"DYNC1LI1","description":"Cytoplasmic dynein 1 light intermediate chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12688","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-349105","identifier":"P63167","identifierLink":"https://www.uniprot.org/uniprotkb/P63167/entry","name":"DYNLL1","description":"Dynein light chain 1, cytoplasmic","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356015","identifier":"Q14204","identifierLink":"https://www.uniprot.org/uniprotkb/Q14204/entry","name":"DYNC1H1","description":"Cytoplasmic dynein 1 heavy chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742998","identifier":"Q13409","identifierLink":"https://www.uniprot.org/uniprotkb/Q13409/entry","name":"DYNC1I2","description":"Cytoplasmic dynein 1 intermediate chain 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26377","complexName":"Box C/D snoRNA-Guided RNP methyltransferase complex, FBLL1 variant","organismName":"Homo sapiens; 9606","description":"Small nucleolar RNA (snoRNA) dependent 2'-O-methyltransferase complex. Upon forming a snoRNP complex with a box C/D snoRNA and other core proteins, FBLL1 transfers a methyl group to the 2'-hydroxyl of the ribose moiety in substrate RNAs. Complex plays a role in pre-rRNA cleavage and in 2'-O-methylation of nucleotides at specific positions in rRNAs, snoRNAs, and other RNAs during maturation. \r\n\r\nLoss of FBLL1 in neurons is detrimental to 2'-O-methylation of GAP43 (P17677) mRNA and results in repressed neuronal differentiation, possibly contributing to human diseases linked to nucleotide methylation.","predictedComplex":false,"interactors":[{"ac":"EBI-12520674","identifier":"CHEBI:67040","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:67040","name":"s-adenosyl-l-methioninate","description":"S-adenosyl-L-methioninate","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-12521462","identifier":"CHEBI:133335","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:133335","name":"c/d box small nucleolar rnas","description":"C/D box small nucleolar RNAs","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2880232","identifier":"A6NHQ2","identifierLink":"https://www.uniprot.org/uniprotkb/A6NHQ2/entry","name":"FBLL1","description":"RNA 2'-O-methyltransferase FBLL1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10335","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395469","identifier":"Q9Y2X3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2X3/entry","name":"NOP58","description":"Nucleolar protein 58","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-396034","identifier":"O00567","identifierLink":"https://www.uniprot.org/uniprotkb/O00567/entry","name":"NOP56","description":"Nucleolar protein 56","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712228","identifier":"P55769","identifierLink":"https://www.uniprot.org/uniprotkb/P55769/entry","name":"SNU13","description":"NHP2-like protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26378","complexName":"Dynein-1 complex, variant 9","organismName":"Homo sapiens; 9606","description":"Multi-protein molecular motor. Dynein-1 is one of three major classes of dynein, which share a conserved motor domain that couples ATP hydrolysis with conformational changes to power intracellular retrograde movement of cargoes including vesicles and organelles along microtubules within the cytoplasm.\r\n\r\nMutations in DYNC1H1 have been implicated in neurological disorders including an axonal form of Charcot-Marie-Tooth disease.","predictedComplex":false,"interactors":[{"ac":"EBI-1176455","identifier":"P63172","identifierLink":"https://www.uniprot.org/uniprotkb/P63172/entry","name":"DYNLT1","description":"Dynein light chain Tctex-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356015","identifier":"Q14204","identifierLink":"https://www.uniprot.org/uniprotkb/Q14204/entry","name":"DYNC1H1","description":"Cytoplasmic dynein 1 heavy chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366267","identifier":"O14576","identifierLink":"https://www.uniprot.org/uniprotkb/O14576/entry","name":"DYNC1I1","description":"Cytoplasmic dynein 1 intermediate chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372128","identifier":"Q9NP97","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NP97/entry","name":"DYNLRB1","description":"Dynein light chain roadblock-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-715294","identifier":"O43237","identifierLink":"https://www.uniprot.org/uniprotkb/O43237/entry","name":"DYNC1LI2","description":"Cytoplasmic dynein 1 light intermediate chain 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12688","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742371","identifier":"Q96FJ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96FJ2/entry","name":"DYNLL2","description":"Dynein light chain 2, cytoplasmic","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26379","complexName":"Dynein-1 complex, variant 10","organismName":"Homo sapiens; 9606","description":"Multi-protein molecular motor. Dynein-1 is one of three major classes of dynein, which share a conserved motor domain that couples ATP hydrolysis with conformational changes to power intracellular retrograde movement of cargoes including vesicles and organelles along microtubules within the cytoplasm. Depletion of DYNC1LI1 present in this complex is thought to reduce dynein-1 binding to spindle assembly checkpoint proteins which ensure correct orientation of sister chromatids needed for the proper segregation during anaphase.\r\n\r\nMutations in DYNC1H1 have been implicated in neurological disorders including an axonal form of Charcot-Marie-Tooth disease.","predictedComplex":false,"interactors":[{"ac":"EBI-1176455","identifier":"P63172","identifierLink":"https://www.uniprot.org/uniprotkb/P63172/entry","name":"DYNLT1","description":"Dynein light chain Tctex-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2556107","identifier":"Q9Y6G9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6G9/entry","name":"DYNC1LI1","description":"Cytoplasmic dynein 1 light intermediate chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12688","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356015","identifier":"Q14204","identifierLink":"https://www.uniprot.org/uniprotkb/Q14204/entry","name":"DYNC1H1","description":"Cytoplasmic dynein 1 heavy chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366267","identifier":"O14576","identifierLink":"https://www.uniprot.org/uniprotkb/O14576/entry","name":"DYNC1I1","description":"Cytoplasmic dynein 1 intermediate chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372128","identifier":"Q9NP97","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NP97/entry","name":"DYNLRB1","description":"Dynein light chain roadblock-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742371","identifier":"Q96FJ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96FJ2/entry","name":"DYNLL2","description":"Dynein light chain 2, cytoplasmic","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26380","complexName":"Dynein-1 complex, variant 11","organismName":"Homo sapiens; 9606","description":"Multi-protein molecular motor. Dynein-1 is one of three major classes of dynein, which share a conserved motor domain that couples ATP hydrolysis with conformational changes to power intracellular retrograde movement of cargoes including vesicles and organelles along microtubules within the cytoplasm.\r\n\r\nMutations in DYNC1H1 have been implicated in neurological disorders including an axonal form of Charcot-Marie-Tooth disease.","predictedComplex":false,"interactors":[{"ac":"EBI-1176455","identifier":"P63172","identifierLink":"https://www.uniprot.org/uniprotkb/P63172/entry","name":"DYNLT1","description":"Dynein light chain Tctex-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356015","identifier":"Q14204","identifierLink":"https://www.uniprot.org/uniprotkb/Q14204/entry","name":"DYNC1H1","description":"Cytoplasmic dynein 1 heavy chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372128","identifier":"Q9NP97","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NP97/entry","name":"DYNLRB1","description":"Dynein light chain roadblock-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-715294","identifier":"O43237","identifierLink":"https://www.uniprot.org/uniprotkb/O43237/entry","name":"DYNC1LI2","description":"Cytoplasmic dynein 1 light intermediate chain 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12688","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742371","identifier":"Q96FJ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96FJ2/entry","name":"DYNLL2","description":"Dynein light chain 2, cytoplasmic","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742998","identifier":"Q13409","identifierLink":"https://www.uniprot.org/uniprotkb/Q13409/entry","name":"DYNC1I2","description":"Cytoplasmic dynein 1 intermediate chain 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26381","complexName":"Dynein-1 complex, variant 12","organismName":"Homo sapiens; 9606","description":"Multi-protein molecular motor. Dynein-1 is one of three major classes of dynein, which share a conserved motor domain that couples ATP hydrolysis with conformational changes to power intracellular retrograde movement of cargoes including vesicles and organelles along microtubules within the cytoplasm. Depletion of DYNC1LI1 present in this complex is thought to reduce dynein-1 binding to spindle assembly checkpoint proteins which ensure correct orientation of sister chromatids needed for the proper segregation during anaphase.\r\n\r\nMutations in DYNC1H1 have been implicated in neurological disorders including an axonal form of Charcot-Marie-Tooth disease.","predictedComplex":false,"interactors":[{"ac":"EBI-1176455","identifier":"P63172","identifierLink":"https://www.uniprot.org/uniprotkb/P63172/entry","name":"DYNLT1","description":"Dynein light chain Tctex-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2556107","identifier":"Q9Y6G9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6G9/entry","name":"DYNC1LI1","description":"Cytoplasmic dynein 1 light intermediate chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12688","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356015","identifier":"Q14204","identifierLink":"https://www.uniprot.org/uniprotkb/Q14204/entry","name":"DYNC1H1","description":"Cytoplasmic dynein 1 heavy chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372128","identifier":"Q9NP97","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NP97/entry","name":"DYNLRB1","description":"Dynein light chain roadblock-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742371","identifier":"Q96FJ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96FJ2/entry","name":"DYNLL2","description":"Dynein light chain 2, cytoplasmic","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742998","identifier":"Q13409","identifierLink":"https://www.uniprot.org/uniprotkb/Q13409/entry","name":"DYNC1I2","description":"Cytoplasmic dynein 1 intermediate chain 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26382","complexName":"Dynein-1 complex, variant 13","organismName":"Homo sapiens; 9606","description":"Multi-protein molecular motor. Dynein-1 is one of three major classes of dynein, which share a conserved motor domain that couples ATP hydrolysis with conformational changes to power intracellular retrograde movement of cargoes including vesicles and organelles along microtubules within the cytoplasm.\r\n\r\nMutations in DYNC1H1 have been implicated in neurological disorders including an axonal form of Charcot-Marie-Tooth disease.","predictedComplex":false,"interactors":[{"ac":"EBI-356015","identifier":"Q14204","identifierLink":"https://www.uniprot.org/uniprotkb/Q14204/entry","name":"DYNC1H1","description":"Cytoplasmic dynein 1 heavy chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366267","identifier":"O14576","identifierLink":"https://www.uniprot.org/uniprotkb/O14576/entry","name":"DYNC1I1","description":"Cytoplasmic dynein 1 intermediate chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372128","identifier":"Q9NP97","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NP97/entry","name":"DYNLRB1","description":"Dynein light chain roadblock-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-715294","identifier":"O43237","identifierLink":"https://www.uniprot.org/uniprotkb/O43237/entry","name":"DYNC1LI2","description":"Cytoplasmic dynein 1 light intermediate chain 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12688","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742371","identifier":"Q96FJ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96FJ2/entry","name":"DYNLL2","description":"Dynein light chain 2, cytoplasmic","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743027","identifier":"P51808","identifierLink":"https://www.uniprot.org/uniprotkb/P51808/entry","name":"DYNLT3","description":"Dynein light chain Tctex-type 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26383","complexName":"Dynein-1 complex, variant 14","organismName":"Homo sapiens; 9606","description":"Multi-protein molecular motor. Dynein-1 is one of three major classes of dynein, which share a conserved motor domain that couples ATP hydrolysis with conformational changes to power intracellular retrograde movement of cargoes including vesicles and organelles along microtubules within the cytoplasm. Depletion of DYNC1LI1 present in this complex is thought to reduce dynein-1 binding to spindle assembly checkpoint proteins which ensure correct orientation of sister chromatids needed for the proper segregation during anaphase.\r\n\r\nMutations in DYNC1H1 have been implicated in neurological disorders including an axonal form of Charcot-Marie-Tooth disease.","predictedComplex":false,"interactors":[{"ac":"EBI-2556107","identifier":"Q9Y6G9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6G9/entry","name":"DYNC1LI1","description":"Cytoplasmic dynein 1 light intermediate chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12688","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356015","identifier":"Q14204","identifierLink":"https://www.uniprot.org/uniprotkb/Q14204/entry","name":"DYNC1H1","description":"Cytoplasmic dynein 1 heavy chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366267","identifier":"O14576","identifierLink":"https://www.uniprot.org/uniprotkb/O14576/entry","name":"DYNC1I1","description":"Cytoplasmic dynein 1 intermediate chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372128","identifier":"Q9NP97","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NP97/entry","name":"DYNLRB1","description":"Dynein light chain roadblock-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742371","identifier":"Q96FJ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96FJ2/entry","name":"DYNLL2","description":"Dynein light chain 2, cytoplasmic","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743027","identifier":"P51808","identifierLink":"https://www.uniprot.org/uniprotkb/P51808/entry","name":"DYNLT3","description":"Dynein light chain Tctex-type 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26384","complexName":"Dynein-1 complex, variant 15","organismName":"Homo sapiens; 9606","description":"Multi-protein molecular motor. Dynein-1 is one of three major classes of dynein, which share a conserved motor domain that couples ATP hydrolysis with conformational changes to power intracellular retrograde movement of cargoes including vesicles and organelles along microtubules within the cytoplasm.\r\n\r\nMutations in DYNC1H1 have been implicated in neurological disorders including an axonal form of Charcot-Marie-Tooth disease.","predictedComplex":false,"interactors":[{"ac":"EBI-356015","identifier":"Q14204","identifierLink":"https://www.uniprot.org/uniprotkb/Q14204/entry","name":"DYNC1H1","description":"Cytoplasmic dynein 1 heavy chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372128","identifier":"Q9NP97","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NP97/entry","name":"DYNLRB1","description":"Dynein light chain roadblock-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-715294","identifier":"O43237","identifierLink":"https://www.uniprot.org/uniprotkb/O43237/entry","name":"DYNC1LI2","description":"Cytoplasmic dynein 1 light intermediate chain 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12688","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742371","identifier":"Q96FJ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96FJ2/entry","name":"DYNLL2","description":"Dynein light chain 2, cytoplasmic","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742998","identifier":"Q13409","identifierLink":"https://www.uniprot.org/uniprotkb/Q13409/entry","name":"DYNC1I2","description":"Cytoplasmic dynein 1 intermediate chain 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743027","identifier":"P51808","identifierLink":"https://www.uniprot.org/uniprotkb/P51808/entry","name":"DYNLT3","description":"Dynein light chain Tctex-type 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10322","complexName":"IL33 receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Pleiotropic receptor-cytokine complex which acts as an alarmin and is involved in inflammatory and metabolic disease. IL33 binding to IL1RL1 induces a coformational change that allows IL1RL1 to interact with its co-receptor IL1RAP. Receptor heterodimerization results in the juxtaposition of the intracellular TIR domains of both receptors to activate NFKB and MAPK pathways in target cells driving cell survival, proliferation and AREG (P15514) expression by IL1RL1+ cells. IL33 is thought to be negatively regulated upon sequestration by soluble IL1RL1 (CPX-10324).\r\n\r\nImpaired IL33-IL1R1 signalling is thought to contribute to the pathogenesis of Alzheimer's Disease.","predictedComplex":false,"interactors":[{"ac":"EBI-525939","identifier":"Q9NPH3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPH3/entry","name":"IL1RAP","description":"Interleukin-1 receptor accessory protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724057","identifier":"O95760","identifierLink":"https://www.uniprot.org/uniprotkb/O95760/entry","name":"IL33","description":"Interleukin-33","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21114","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-993762","identifier":"Q01638","identifierLink":"https://www.uniprot.org/uniprotkb/Q01638/entry","name":"IL1RL1","description":"Interleukin-1 receptor-like 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10323","complexName":"54S mitochondrial large ribosomal subunit","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Component of the ribosome, the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). Responsible for the catalytic activity of the ribosome, the peptidyltransferase activity required to catalyze peptide bond formation. The mitochondrial ribosome (mitoribosome) is responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are tethered to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-1190649","identifier":"Q9Y7Z7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y7Z7/entry","name":"mrp15","description":"Large ribosomal subunit protein mL57","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28160","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56891553","identifier":"Q9P7D4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P7D4/entry","name":"aco2","description":"Aconitase-ribosomal protein bL21m fusion protein","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR43160","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56891584","identifier":"Q09724","identifierLink":"https://www.uniprot.org/uniprotkb/Q09724/entry","name":"mrp11","description":"Large ribosomal subunit protein uL10m","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11560","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56891598","identifier":"O14178","identifierLink":"https://www.uniprot.org/uniprotkb/O14178/entry","name":"mrpl40","description":"Large ribosomal subunit protein uL24m","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12903","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56891616","identifier":"Q9UR27","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UR27/entry","name":"mrpl31","description":"Large ribosomal subunit protein mL60","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28271","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56891628","identifier":"O74464","identifierLink":"https://www.uniprot.org/uniprotkb/O74464/entry","name":"mrpl22","description":"Large ribosomal subunit protein uL22m","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 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The exact substrate specificity of the enzyme is determined by the dimeric alpha subunits and is further modulated by the non-catalytic beta homodimer.","predictedComplex":false,"interactors":[{"ac":"EBI-711522","identifier":"Q15102","identifierLink":"https://www.uniprot.org/uniprotkb/Q15102/entry","name":"PAFAH1B3","description":"Platelet-activating factor acetylhydrolase IB subunit alpha1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11852","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-720620","identifier":"P43034","identifierLink":"https://www.uniprot.org/uniprotkb/P43034/entry","name":"PAFAH1B1","description":"Platelet-activating factor acetylhydrolase IB subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10327","complexName":"SWM histone demethylase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"FAD (flavin adenine dinucleotide)-dependent  mono- and di-methylated histone H3K4/H3K9 demethylase complex which localizes specifically at heterochromatic loci and the transcription start sites of actively transcribed genes.  Plays a role in  transcriptional regulation via heterochromatic silencing The complex and maintains the boundary between euchromatin and heterochromatin at the telomeres","predictedComplex":false,"interactors":[{"ac":"EBI-56916161","identifier":"Q9Y802","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y802/entry","name":"lsd1","description":"Lysine-specific histone demethylase 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10742","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56916195","identifier":"Q10135","identifierLink":"https://www.uniprot.org/uniprotkb/Q10135/entry","name":"lsd2","description":"Lysine-specific histone demethylase 2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR42923","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56916223","identifier":"P87233","identifierLink":"https://www.uniprot.org/uniprotkb/P87233/entry","name":"phf1","description":"SWM histone demethylase complex subunit phf1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-56916244","identifier":"Q09908","identifierLink":"https://www.uniprot.org/uniprotkb/Q09908/entry","name":"phf2","description":"SWM histone demethylase complex subunit phf2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12628","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-10328","complexName":"Platelet-activating factor acetylhydrolase IB complex, alpha2-alpha2 variant","organismName":"Homo sapiens; 9606","description":"Catalyzes the hydrolysis of an acetyl ester at the sn-2 position of platelet-activating factor (PAF; 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine)) and its analogs and modulates the action of PAF. The exact substrate specificity of the enzyme is determined by the dimeric alpha subunits and is further modulated by the non-catalytic beta homodimer.","predictedComplex":false,"interactors":[{"ac":"EBI-713724","identifier":"P68402","identifierLink":"https://www.uniprot.org/uniprotkb/P68402/entry","name":"PAFAH1B2","description":"Platelet-activating factor acetylhydrolase IB subunit alpha2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11852","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-720620","identifier":"P43034","identifierLink":"https://www.uniprot.org/uniprotkb/P43034/entry","name":"PAFAH1B1","description":"Platelet-activating factor acetylhydrolase IB subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10329","complexName":"Platelet-activating factor acetylhydrolase IB complex, alpha1-alpha2 variant","organismName":"Homo sapiens; 9606","description":"Catalyzes the hydrolysis of an acetyl ester at the sn-2 position of platelet-activating factor (PAF; 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine) and its analogs and modulates the action of PAF. The exact substrate specificity of the enzyme is determined by the dimeric alpha subunits and is further modulated by the non-catalytic beta homodimer.","predictedComplex":false,"interactors":[{"ac":"EBI-711522","identifier":"Q15102","identifierLink":"https://www.uniprot.org/uniprotkb/Q15102/entry","name":"PAFAH1B3","description":"Platelet-activating factor acetylhydrolase IB subunit alpha1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11852","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-713724","identifier":"P68402","identifierLink":"https://www.uniprot.org/uniprotkb/P68402/entry","name":"PAFAH1B2","description":"Platelet-activating factor acetylhydrolase IB subunit alpha2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11852","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-720620","identifier":"P43034","identifierLink":"https://www.uniprot.org/uniprotkb/P43034/entry","name":"PAFAH1B1","description":"Platelet-activating factor acetylhydrolase IB subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10330","complexName":"Histone H2B ubiquitin ligase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Ubiquitin ligase required for ubiquitination of histone H2B (P04913) Lys-119/123, a  specific tag for epigenetic transcriptional activation and  also a prerequisite for H3K4me and H3K79me formation. H2BK119ub1 also modulates the formation of double-strand breaks during meiosis and is a prerequisite for DNA-damage checkpoint activation. The complex localizes to heterochromatic sequences where it functions with the COMPASS complex to regulate mating-type switching.","predictedComplex":false,"interactors":[{"ac":"EBI-1153034","identifier":"P23566","identifierLink":"https://www.uniprot.org/uniprotkb/P23566/entry","name":"rhp6","description":"Ubiquitin-conjugating enzyme E2 2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR24067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6109150","identifier":"Q9UUI2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UUI2/entry","name":"shf1","description":"Small histone ubiquitination factor 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-6109161","identifier":"Q1MTQ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q1MTQ0/entry","name":"brl1","description":"E3 ubiquitin-protein ligase brl1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23163","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6109185","identifier":"O74563","identifierLink":"https://www.uniprot.org/uniprotkb/O74563/entry","name":"brl2","description":"E3 ubiquitin-protein ligase brl2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23163","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10331","complexName":"Triffosome complex","organismName":"Homo sapiens; 9606","description":"Supramolecular organizing centre (SMOC) thought to assemble in the endosome in response to activated TLR4(O00206) and TLR3(O15455) to facilitate the inducible expression of inflammatory genes. The triffosome is considered to complement myddosome (CPX-10281) activity, through an IRAK4 (Q9NWZ3) scaffold. Activates TRAF6 (Q9Y4K3) leading to prolonged NFKB1 and AP1 activity.","predictedComplex":false,"interactors":[{"ac":"EBI-525927","identifier":"Q86XR7","identifierLink":"https://www.uniprot.org/uniprotkb/Q86XR7/entry","name":"TICAM2","description":"TIR domain-containing adapter molecule 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47230","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-525995","identifier":"Q8IUC6","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IUC6/entry","name":"TICAM1","description":"TIR domain-containing adapter molecule 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47230","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10332","complexName":"PEX2-PEX10-PEX12 ubiquitin ligase complex","organismName":"Drosophila melanogaster; 7227","description":"E3 ubiquitin-ligase complex which forms a retrotranslocation channel required for the export of the PEX5 peroxisomal import -receptor from peroxisomes to the cytosol, promoting PEX5 ( O46085) recycling. When receptor recycling is compromised, the receptor is polyubiquitylated by the complex, extracted from the ligase channel by another ATPase, and degraded by the proteasome.","predictedComplex":false,"interactors":[{"ac":"EBI-105831","identifier":"Q9W0D7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W0D7/entry","name":"Pex10","description":"RING-type E3 ubiquitin transferase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23350","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-143577","identifier":"Q9VSH8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VSH8/entry","name":"Pex2","description":"Peroxisome biogenesis factor 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23350","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2108526","identifier":"Q9VPT5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VPT5/entry","name":"Pex12","description":"Peroxisome assembly protein 12","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10333","complexName":"IL34-CSF1R complex","organismName":"Homo sapiens; 9606","description":"Cytokine-receptor complex. IL34 mediates its effects primarily through CSF1R (this complex), with alternative receptors proposed, PTPRZ1 (P23471) and SDC1 (P18827). IL34 binding to CSF1R results in receptor phosphorylation and homodimerization leading to the activation of several pathways including MAP and SRC kinases, the JAK/STAT, RAS and AMPK1 pathways, thus supporting cell growth, survival of monocytes and their differentiation into macrophages.\r\n\r\nIL34 is expressed in a wide variety of tissues but the highest levels are expressed by neurons and keratinocytes. Predominantly associated with the disease progression of autoimmune diseases such as rheumatoid arthritis and systemic lupus erythematosus as well as, breast and lung cancer, IL34's role in disease progression is disease-dependent with beneficial protective roles in some cancers and Alzheimers disease.","predictedComplex":false,"interactors":[{"ac":"EBI-2835440","identifier":"P07333","identifierLink":"https://www.uniprot.org/uniprotkb/P07333/entry","name":"CSF1R","description":"Macrophage colony-stimulating factor 1 receptor","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-948761","identifier":"Q6ZMJ4","identifierLink":"https://www.uniprot.org/uniprotkb/Q6ZMJ4/entry","name":"IL34","description":"Interleukin-34","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28606","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10338","complexName":"Interleukin-36A receptor ligand complex","organismName":"Homo sapiens; 9606","description":"Proinflammatory cytokine-receptor complex involved in immune cell activation, driving T helper 1 responses, and inducing inflammatory responses at barrier sites such as the skin, lungs and intestines. The complex is formed in a two-step process where IL36A first binds to IL1RL2, and the intermediary binary complex recruits IL1RAP. The ternary complex formation brings the TIR domains of the receptors together which recruit MyD88 (Q99836). This activates NFKB and MAPK signalling. Both IL36RN (Q9UBH0) and IL1F10 (Q8WWZ1) play a role inhibiting IL36 function by binding to IL1RL2, preventing recruitment of IL1RAP.\r\n\r\nDysregulation of IL36 cytokines is associated with inflammatory diseases  such as inflammatory bowel disease (IBD), rheumatoid and psoriatic arthritis, and various inflammatory and infectious skin disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-21648578","identifier":"Q9HB29","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HB29/entry","name":"IL1RL2","description":"Interleukin-1 receptor-like 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-525939","identifier":"Q9NPH3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPH3/entry","name":"IL1RAP","description":"Interleukin-1 receptor accessory protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-58760660","identifier":"Q9UHA7-PRO_0000153644","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UHA7-PRO_0000153644/entry","name":"IL36A","description":"Interleukin-36 alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-10340","complexName":"Interleukin-36B receptor ligand complex","organismName":"Homo sapiens; 9606","description":"Proinflammatory cytokine-receptor complex involved in immune cell activation, driving T helper 1 responses, and inducing inflammatory responses at barrier sites such as the skin, lungs and intestines. The complex is formed in a two-step process where IL36B first binds to IL1RL2, and the intermediary binary complex recruits IL1RAP. The ternary complex formation brings TIR domains of the receptors together which recruit MyD88 (Q99836). This activates NFKB and MAPK signalling. Both IL36RN (Q9UBH0) and IL1F10 (Q8WWZ1) play a role inhibiting IL36 function by binding to IL1RL2, preventing recruitment of IL1RAP.\r\n\r\nDysregulation of IL36 cytokines is associated with inflammatory diseases  such as inflammatory bowel disease (IBD), rheumatoid and psoriatic arthritis, and various inflammatory and infectious skin disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-21648578","identifier":"Q9HB29","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HB29/entry","name":"IL1RL2","description":"Interleukin-1 receptor-like 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-525939","identifier":"Q9NPH3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPH3/entry","name":"IL1RAP","description":"Interleukin-1 receptor accessory protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-58760670","identifier":"Q9NZH7-PRO_0000153646","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZH7-PRO_0000153646/entry","name":"IL36B","description":"Interleukin-36 beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-10341","complexName":"Interleukin-36G receptor ligand complex","organismName":"Homo sapiens; 9606","description":"Proinflammatory cytokine-receptor complex involved in immune cell activation, driving T helper 1 responses, and inducing inflammatory responses at barrier sites such as the skin, lungs and intestines. The complex is formed in a two-step process where IL36G first binds to IL1RL2, and the intermediary binary complex recruits IL1RAP. The ternary complex formation brings TIR domains of the receptors together which recruit MyD88 (Q99836). This activates NFKB and MAPK signalling. Both IL36RN (Q9UBH0) and IL1F10 (Q8WWZ1) play a role inhibiting IL36 function by binding to IL1RL2, preventing recruitment of IL1RAP.\r\n\r\nDysregulation of IL36 cytokines is associated with inflammatory diseases  such as inflammatory bowel disease (IBD), rheumatoid and psoriatic arthritis, and various inflammatory and infectious skin disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-21648578","identifier":"Q9HB29","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HB29/entry","name":"IL1RL2","description":"Interleukin-1 receptor-like 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-525939","identifier":"Q9NPH3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPH3/entry","name":"IL1RAP","description":"Interleukin-1 receptor accessory protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-58760680","identifier":"Q9NZH8-PRO_0000153648","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZH8-PRO_0000153648/entry","name":"IL36G","description":"Interleukin-36 gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-10343","complexName":"Interleukin-36 antagonist complex","organismName":"Homo sapiens; 9606","description":"Buffering complex which negatively regulates the IL36 signalling pathway by blocking IL1RL1-IL1RAP mediated activation of NFKB and MAP kinase pathways. IL36RN performs an antagonistic role by competitively binding to IL1RL1, suppressing IL36 agonist recognition and IL1RAP recruitment. In addition to its inhibitory role, IL36RN can proactively induce upregulation of IL4 (P05112) expression in glial cells.\r\n\r\nLoss-of-function mutations in IL36RN are implicated in DITRA, a recessive autoinflammatory disease characterised by pustular psoriasis.","predictedComplex":false,"interactors":[{"ac":"EBI-21648578","identifier":"Q9HB29","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HB29/entry","name":"IL1RL2","description":"Interleukin-1 receptor-like 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11890","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-58760693","identifier":"Q9UBH0-PRO_0000153642","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UBH0-PRO_0000153642/entry","name":"IL36RN","description":"Interleukin-36 receptor antagonist protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-10344","complexName":"Interleukin-37 receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Anti-inflammatory cytokine-receptor complex that curbs inflammation and modulates metabolic pathways. Abrogates the protective effects of trained immunity, pertaining to the memory associated with innate immunity.","predictedComplex":false,"interactors":[{"ac":"EBI-52374719","identifier":"Q9NZH6-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZH6-1/entry","name":"IL37","description":"Interleukin-37","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-58763213","identifier":"Q13478-PRO_0000015448","identifierLink":"https://www.uniprot.org/uniprotkb/Q13478-PRO_0000015448/entry","name":"IL18R1","description":"Interleukin-18 receptor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-58763226","identifier":"Q6IA17-PRO_0000099065","identifierLink":"https://www.uniprot.org/uniprotkb/Q6IA17-PRO_0000099065/entry","name":"SIGIRR","description":"Single Ig IL-1-related receptor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-10345","complexName":"IL37-SMAD3 transcriptional repressor complex","organismName":"Homo sapiens; 9606","description":"Functions to suppress the innate immune inflammatory response through an intracellular pathway. After stimulation by lipopolysaccharide (LPS), the carboxyl-domain of IL37-isoform B, IL37B (Q9NZH6-1) binds to SMAD3 and is transported to the nucleus where it suppresses activation of the gene expression of inflammatory cytokines. IL37D (Q9NZH6-4) also binds SMAD3 to drive the suppression LPS-induced pro-inflammatory cytokines expression.\r\n\r\nExpression of IL37 in macrophages and epithelial cell is correlated with the suppression of pro-inflammatory cytokines.","predictedComplex":false,"interactors":[{"ac":"EBI-347161","identifier":"P84022","identifierLink":"https://www.uniprot.org/uniprotkb/P84022/entry","name":"SMAD3","description":"Mothers against decapentaplegic homolog 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13703","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3862125","identifier":"Q9NZH6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZH6/entry","name":"IL37","description":"Interleukin-37","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10078","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10346","complexName":"Elongator holoenzyme complex","organismName":"Drosophila melanogaster; 7227","description":"N-acetyltransferase which acts to form modified wobble uridines in tRNA, such as 5-methoxycarbonylmethyl-uridine (mcm5U), 5-methoxycarbonylmethyl-2-thio-uridine (mcm5s2U), and 5-carbamoylmethyl-uridine (ncm5U). These sites influence the recognition rate and affinity between incoming tRNAs and codons in the A site of the translating ribosome, stablizing transient pausing events thus supporting proper domain folding of the nascent polypeptide chains during the elongation phase of the ribosome‐mediated translation process.","predictedComplex":false,"interactors":[{"ac":"EBI-116343","identifier":"Q7K4B3","identifierLink":"https://www.uniprot.org/uniprotkb/Q7K4B3/entry","name":"Elp2","description":"Elongator complex protein 2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR44111","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-135327","identifier":"Q24050","identifierLink":"https://www.uniprot.org/uniprotkb/Q24050/entry","name":"Elp5","description":"Elongator complex protein 5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15641","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-179023","identifier":"Q9VGK7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VGK7/entry","name":"Elp1","description":"Elongator complex protein 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12747","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-85766","identifier":"Q9VFW4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VFW4/entry","name":"Elp6","description":"Elongator complex protein 6","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR16184","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-92248","identifier":"Q9VMQ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VMQ7/entry","name":"Elp4","description":"Elongator complex protein 4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12896","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9964043","identifier":"Q9VQZ6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VQZ6/entry","name":"Elp3","description":"Elongator complex protein 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11135","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10348","complexName":"Interleukin-37 complex","organismName":"Homo sapiens; 9606","description":"Anti-inflammatory cytokine. Powerful inhibitor of inflammation and immunity. Released in an alarmin-like fashion upon stimulation by monocytes. IL37 is thought to autoregulate its anti-inflammatory effects by transitioning from a dimeric to a monomeric state as it moves away from its site of release.\r\n\r\nIL37 is predominantly produced by peripheral blood mononuclear cells but its isoforms (IL37a-e) have a variable expression profile in human blood, with IL37B and IL37C (Q9NZH6-3) detected in PBMCs whilst IL37A (Q9NZH6-2) and IL37E (Q9NZH6-5) are not.","predictedComplex":false,"interactors":[{"ac":"EBI-3862125","identifier":"Q9NZH6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NZH6/entry","name":"IL37","description":"Interleukin-37","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10078","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10799","complexName":"ADAM22-ADAM23-LGI1, trans-synaptic complex","organismName":"Homo sapiens; 9606","description":"Trans-synaptic complex, formed between soluble LGI1 and its receptors ADAM22 (CPX-21307) and ADAM23 (CPX-18972), which regulates excitatory synaptic transmission and neuronal excitability in the brain to maintain normal synaptic function and brain homeostasis. Complex mediates interactions with presynaptic Kv1 channels and postsynaptic AMPARs.  \r\n\r\nADAM23 negatively regulates Kv1.1 currents and limits LGI1 localisation at the axon initial segment (AIS), and it also contributes to neurite outgrowth. In contrast, ADAM22 is positively regulated by LGI1, enhancing Kv1.1 current and being enriched at the AIS. Through its interaction with ADAM22, LGI1 supports normal synaptic function and brain homeostasis. The LGI1-ADAM22 complex also links to AMPA receptors via DLG4 (P78352) to stabilise excitatory synapses and regulate neuronal excitability.\r\n\r\nDysfunction of the complex is linked to epilepsy in infancy and childhood. Disruption of LGI1, either through loss-of-function mutations or autoantibodies, impairs both Kv1 channel and AMPAR function, leading to epilepsies associated with a variety of pathophysiological mechanisms.","predictedComplex":false,"interactors":[{"ac":"EBI-58882459","identifier":"CPX-18972","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-18972","name":"ADAM23-LGI1 synaptic receptor complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-58913217","identifier":"CPX-21307","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-21307","name":"ADAM22-LGI1 synaptic receptor complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-10798","complexName":"GPSM2-INSC complex","organismName":"Homo sapiens; 9606","description":"Key regulator of asymmetric cell division in polarized progenitor cells, a process fundamental for generating diverse cell types. Plays a critical role in establishing and maintaining tissue organization during development. Complex functions as a molecular bridge, coupling polarity signals to the cytoskeletal machinery that orientates the mitotic spindle. INSC and GPSM2 localize apically in a mutually reinforcing manner: GPSM2 stabilizes cortical INSC, while INSC biases the localization of other polarity regulators. This ensures that spindle orientation aligns with apical-basal polarity, enabling the generation of daughter cells with divergent fates, a process essential for neurogenesis, epithelial homeostasis, and stem cell renewal.","predictedComplex":false,"interactors":[{"ac":"EBI-12081118","identifier":"Q1MX18","identifierLink":"https://www.uniprot.org/uniprotkb/Q1MX18/entry","name":"INSC","description":"Protein inscuteable homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21386","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-618655","identifier":"P81274","identifierLink":"https://www.uniprot.org/uniprotkb/P81274/entry","name":"GPSM2","description":"G-protein-signaling modulator 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45954","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-11353","complexName":"MIMP2-TIMP2, metalloproteinase inhibition complex","organismName":"Homo sapiens; 9606","description":"Regulates metalloproteinase activity at the extracellular matrix. TIMP2 regulates MMP2 activity through distinct interactions involving its N- and C-terminal domains. The N-terminal domain binds to the catalytic site of MMP2, inhibiting its enzymatic activity, while the C-terminal domain binds to the hemopexin domain of MMP2 within the cellular activation complex. These interactions are mutually exclusive; one TIMP2 molecule cannot simultaneously bind both the catalytic and hemopexin domains of MMP2. At higher concentrations, TIMP2 inhibits the activation of proMMP-2 (30-109) through two possible mechanisms: by binding to membrane type 1 matrix metalloproteinase (MT1-MMP) via its N-terminal domain and preventing cleavage of the prodomain, or by excess TIMP2 occupying the hemopexin domain of free proMMP2, thereby blocking its integration into the activation complex.","predictedComplex":false,"interactors":[{"ac":"EBI-1033507","identifier":"P16035","identifierLink":"https://www.uniprot.org/uniprotkb/P16035/entry","name":"TIMP2","description":"Metalloproteinase inhibitor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1033518","identifier":"P08253","identifierLink":"https://www.uniprot.org/uniprotkb/P08253/entry","name":"MMP2","description":"72 kDa type IV collagenase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10201","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-11548","complexName":"DBF4-dependent CDC7 kinase complex","organismName":"Homo sapiens; 9606","description":"Serine/threonine-protein kinase essential for the initiation of DNA replication. Associates with replication origins where it phosphorylates components of the prereplicative complex including the MCM helicase (CPX-2940). Phosphorylates the RAD9 component of the checkpoint clamp complex component (CPX-1829)  in response to replication-induced DNA damage.","predictedComplex":false,"interactors":[{"ac":"EBI-372690","identifier":"Q9UBU7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UBU7/entry","name":"DBF4","description":"Protein DBF4 homolog A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-374980","identifier":"O00311","identifierLink":"https://www.uniprot.org/uniprotkb/O00311/entry","name":"CDC7","description":"Cell division cycle 7-related protein kinase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11909","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-11549","complexName":"Huntingtin-HAP40 endosomal complex","organismName":"Homo sapiens; 9606","description":"The HTT-HAP40 complex plays several key biological roles, including maintaining protein stability, regulating intracellular transport, and modulating cellular homeostasis. The complex acts as a RAB5A (P20339) effector, regulating early endosome motility by recruiting kinesins-1 and -3 to facilitate anterograde motility along microtubules, thereby affecting intracellular cargo transport and membrane dynamics.\r\n\r\nBinding of F8A1 to HTT is thought to reduce the aggregation and toxicity of mutant HTT in Huntington’s disease, and to promote its proteasomal degradation via K48-linked ubiquitination.","predictedComplex":false,"interactors":[{"ac":"EBI-466029","identifier":"P42858","identifierLink":"https://www.uniprot.org/uniprotkb/P42858/entry","name":"HTT","description":"Huntingtin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10170","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5663973","identifier":"P23610","identifierLink":"https://www.uniprot.org/uniprotkb/P23610/entry","name":"F8A1","description":"40-kDa huntingtin-associated protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16797","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-11679","complexName":"Obesity factor-receptor complex","organismName":"Homo sapiens; 9606","description":"Mainly produced by adipocytes, LEP acts on LEPR to regulate adipose tissue via hypothalamic control of satiety and energy expenditure, thereby maintaining food intake and body weight homeostasis. The complex is also involved in other processes, including adaptive and innate immune function, reproduction, and bone metabolism. Leptin, therefore, functions as a metabolic switch, linking the body's nutritional status to energy-demanding physiological activities.\r\n\r\nProper functioning of this complex is crucial for preventing obesity and associated secondary diseases such as diabetes, inflammation, cardiovascular disease, and cancer. Human obesity is characterized by elevated serum leptin concentrations, which appear to impair leptin transport into the central nervous system.","predictedComplex":false,"interactors":[{"ac":"EBI-12994693","identifier":"P41159","identifierLink":"https://www.uniprot.org/uniprotkb/P41159/entry","name":"LEP","description":"Leptin","stochiometry":"minValue: 1, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11724","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-518596","identifier":"P48357","identifierLink":"https://www.uniprot.org/uniprotkb/P48357/entry","name":"LEPR","description":"Leptin receptor","stochiometry":"minValue: 1, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-11781","complexName":"Lyric-SND1 RNA regulator complex","organismName":"Homo sapiens; 9606","description":"Regulator of RNA metabolism with potential roles in modulating RNA alternative splicing, maturation, and stability. It inhibits T-cell infiltration and activation by binding to \"TAP1/2\" mRNA and promoting its degradation, thereby preventing formation of the TAP antigen peptide transporter complex (CPX-25769).\r\n\r\nThe complex enhances malignant phenotypes by orchestrating tumour-promoting processes particularly during the initiation phase of tumor development. It is implicated in various cancer types and has been shown to be essential for cancer cell survival under oncogenic stress. \r\n\r\nComplex is implicated in breast and prostate cancer, and is thought to bind and degrade SESN2 (P58004) mRNA, modulating prostate cancer progression through the AMPK/mTOR pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-1044112","identifier":"Q7KZF4","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KZF4/entry","name":"SND1","description":"Staphylococcal nuclease domain-containing protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12302","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1046588","identifier":"Q86UE4","identifierLink":"https://www.uniprot.org/uniprotkb/Q86UE4/entry","name":"MTDH","description":"Protein LYRIC","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23251","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-12100","complexName":"METTL15-RBFA mitochondrial metabolism regulatory complex","organismName":"Homo sapiens; 9606","description":"Mitochondrial assembly factor complex involved in mitochondrial small subunit (SSU) assembly and mitochondrial translation. METTL15 functions as the principal N4-methylcytidine (m4C) methyltransferase in human mitochondria, responsible for modifying C839 in 12S rRNA, RBFA is believed to act as a scaffolding protein, recruited to helices 44 and 45 of the mitochondrial SSU 12S rRNA. The m4C839 modification is thought to stabilize 12S rRNA folding, promoting proper subunit maturation.  Loss of METTL15 impairs mitochondrial translation by disrupting SSU assembly, particularly the incorporation of late-stage components. \r\n\r\nDefects in mitochondrial ribosome assembly are associated with a broad range of mitochondrial diseases and developmental disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-10742528","identifier":"A6NJ78","identifierLink":"https://www.uniprot.org/uniprotkb/A6NJ78/entry","name":"METTL15","description":"12S rRNA N(4)-cytidine methyltransferase METTL15","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11265","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30813205","identifier":"CHEBI:59789","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:59789","name":"s-adenosyl-l-methionine zwitterion","description":"S-adenosyl-L-methionine zwitterion","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-3232108","identifier":"Q8N0V3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N0V3/entry","name":"RBFA","description":"Putative ribosome-binding factor A, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14725","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9494077","identifier":"CHEBI:18111","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18111","name":"ribosomal rna","description":"ribosomal RNA","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-12385","complexName":"Separase-Securin complex","organismName":"Homo sapiens; 9606","description":"Regulates the metaphase-to-anaphase transition during cell cycle progression, playing a role in control of the metaphase-anaphase transition and anaphase onset. Complex formation both activates and inhibits the protease activity of separase/ESPL1 which is responsible for cleaving the RAD21 (O60216) subunit of the cohesin ring that holds sister chromatids together during mitosis. Securin/PTTG1 appears to ensure that separase adopts its proper fold required for proteolytic activity and also promotes subcellular localization of separase to the nucleus. Securin is degraded via ubiquitylation by the anaphase-promoting complex enabling separase to become fully active.","predictedComplex":false,"interactors":[{"ac":"EBI-2551072","identifier":"O95997","identifierLink":"https://www.uniprot.org/uniprotkb/O95997/entry","name":"PTTG1","description":"Securin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10418","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2554882","identifier":"Q14674","identifierLink":"https://www.uniprot.org/uniprotkb/Q14674/entry","name":"ESPL1","description":"Separin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12792","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-12765","complexName":"TASL-SLC15A4, endolysosomal TLR signalling complex","organismName":"Homo sapiens; 9606","description":"Positive regulator of the innate immune response via toll-like receptor (TLR) activation to promote the induction of proinflammatory mediators and type I interferons; Complex formation results in the recruitment and activation of IRF5 (Q13568) downstream of endolysosomal toll-like receptors TLR7, TLR8 and TLR9.","predictedComplex":false,"interactors":[{"ac":"EBI-21895669","identifier":"Q9HAI6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HAI6/entry","name":"TASL","description":"TLR adapter interacting with SLC15A4 on the lysosome","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14889","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4319594","identifier":"Q8N697","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N697/entry","name":"SLC15A4","description":"Solute carrier family 15 member 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11654","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-14323","complexName":"Autophagic ferritin degradation complex","organismName":"Homo sapiens; 9606","description":"Complex formed between NCOA4 and the iron-binding ferritin complex (CPX-26673), directing it to autolysosomes to undergo ferritinophagy (a ferritin-selective autophagy process). Ferritin degradation enables the controlled release and reuse of iron, maintaining iron homeostasis. Iron is released into the labile iron pool, where it is used for essential cellular functions such as DNA synthesis, mitochondrial respiration, and erythropoiesis. The process is tightly regulated and plays a vital role in maintaining iron balance, especially during periods of iron deficiency. When ferritinophagy is disrupted, it can lead to either iron accumulation or depletion.","predictedComplex":false,"interactors":[{"ac":"EBI-67161448","identifier":"CPX-26673","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-26673","name":"FTH1-FTL, Ferritin complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-954501","identifier":"Q13772","identifierLink":"https://www.uniprot.org/uniprotkb/Q13772/entry","name":"NCOA4","description":"Nuclear receptor coactivator 4","stochiometry":"minValue: 1, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR17085","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-15884","complexName":"RAB3 GTPase-activating complex","organismName":"Homo sapiens; 9606","description":"Plays a regulatory role in membrane trafficking, particularly in exocytosis, by acting on RAB GTPases, the master regulators of intracellular vesicle transport. A RAB3 GTPase-activating complex which activates various RAB3 subfamily members (RAB3A, RAB3B, RAB3C and RAB3D), RAB5A and RAB43 by converting active RAB3-GTP to the inactive form RAB3-GDP. Also acts as a guanine nucleotide exchange factor (GEF) which recruits RAB18 (Q9NP72), and promotes the conversion of inactive RAB18-GDP to the active form RAB18-GTP a regulator of lipid droplet metabolism, ER-to-Golgi trafficking, secretion, and autophagy. \r\n\r\nMutations in RAB3GAP1, RAB3GAP2, or RAB18 cause Warburg Micro Syndrome (WMS), a rare recessive disorder marked by microcephaly, cataracts, optic atrophy, spasticity, hypogonadism, and severe developmental delays.","predictedComplex":false,"interactors":[{"ac":"EBI-1053078","identifier":"Q15042","identifierLink":"https://www.uniprot.org/uniprotkb/Q15042/entry","name":"RAB3GAP1","description":"Rab3 GTPase-activating protein catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21422","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-536107","identifier":"Q9H2M9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H2M9/entry","name":"RAB3GAP2","description":"Rab3 GTPase-activating protein non-catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12472","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-16536","complexName":"INSR-IGF1R, hybrid insulin receptor complex","organismName":"Homo sapiens; 9606","description":"Complex regulates glucose homeostasis and normal human growth.\r\n\r\nHybrid receptors are formed when one half (alpha-beta) of INSR pairs with one half (alpha-beta) of the IGF1R. The specific INSR isoform involved, either the long form (P06213-1, INSR-B which includes exon 11) or the short form (P06213-2, INSR-A which excludes exon 11) can influence the ligand-binding and activation properties of the resulting hybrid complex. Hybrids containing INSR-B are reported to be strongly activated by IGF1 (P05019), exhibit low affinity for IGF2 (P01344), and show minimal responsiveness to INS (P01308). In contrast, hybrids involving the INSR-A have been reported in some studies to respond to IGF1, IGF2, and, to a limited extent, INS. However, INS activation of hybrid receptors remains significantly weaker than that of homodimeric INSR, regardless of isoform. The extent to which isoform identity determines hybrid receptor function remains unclear, and INS binding may vary depending on cell type, receptor abundance, and experimental context.\r\n\r\nDysregulation of insulin receptor (INSR) signalling is a well-established contributor to the pathogenesis of diabetes mellitus. In parallel, aberrant activation of the hybrid INS-IGF1R receptors has been implicated in tumourigenesis and cancer progression, as well as in the molecular mechanisms underlying neurodegenerative diseases such as Alzheimer’s disease.","predictedComplex":false,"interactors":[{"ac":"EBI-10818032","identifier":"P06213-PRO_0000016689","identifierLink":"https://www.uniprot.org/uniprotkb/P06213-PRO_0000016689/entry","name":"INSR","description":"Insulin receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-22054038","identifier":"P08069-PRO_0000016682","identifierLink":"https://www.uniprot.org/uniprotkb/P08069-PRO_0000016682/entry","name":"IGF1R","description":"Insulin-like growth factor 1 receptor beta chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-67171059","identifier":"P06213-PRO_0000016687","identifierLink":"https://www.uniprot.org/uniprotkb/P06213-PRO_0000016687/entry","name":"INSR","description":"Insulin receptor subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-67171102","identifier":"P08069-PRO_0000016681","identifierLink":"https://www.uniprot.org/uniprotkb/P08069-PRO_0000016681/entry","name":"IGF1R","description":"Insulin-like growth factor 1 receptor alpha chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-16835","complexName":"AMH-AMHR2 reproduction development complex","organismName":"Homo sapiens; 9606","description":"Plays a crucial role in male sexual differentiation by mediating Mullerian duct regression during fetal development, thereby preventing the formation of internal female reproductive structures. In female sexual development, the complex contributes to ovarian physiology by regulating follicle activation, restraining excessive early folliculogenesis, and maintaining the ovarian reserve.","predictedComplex":false,"interactors":[{"ac":"EBI-3905087","identifier":"P03971","identifierLink":"https://www.uniprot.org/uniprotkb/P03971/entry","name":"AMH","description":"Muellerian-inhibiting factor","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15009","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6423788","identifier":"Q16671","identifierLink":"https://www.uniprot.org/uniprotkb/Q16671/entry","name":"AMHR2","description":"Anti-Muellerian hormone type-2 receptor","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-17570","complexName":"DENR-MCTS1, translation reinitiation complex","organismName":"Homo sapiens; 9606","description":"Translation regulator complex. Promotes translation reinitiation, a process in which the small ribosomal subunit remains on the mRNA after translating an upstream ORF and resumes scanning to initiate at a downstream ORF, typically the main ORF. The complex enables two key steps: dissociation of deacylated tRNAs from post-termination 40S subunits during recycling, and eIF2-independent recruitment of initiator tRNA to the 40S P site. This mechanism regulates translation of over 150 genes and influences biological processes including cell cycle regulation and DNA damage response.","predictedComplex":false,"interactors":[{"ac":"EBI-716076","identifier":"Q9ULC4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ULC4/entry","name":"MCTS1","description":"Malignant T-cell-amplified sequence 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22798","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-716083","identifier":"O43583","identifierLink":"https://www.uniprot.org/uniprotkb/O43583/entry","name":"DENR","description":"Density-regulated protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12789","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-18972","complexName":"ADAM23-LGI1 synaptic receptor complex","organismName":"Homo sapiens; 9606","description":"Synaptic organizing complex which regulates excitatory synaptic transmission and neuronal excitability in the brain. ADAM23 acts as a negative regulator of Kv1.1 currents, removing LGI1 from the axon initial segment (AIS), and appears to have a role in neurite outgrowth. In contrast, ADAM22 is positively regulated by LGI1 (CPX-21307), promoting Kv1.1 currents, and is enriched at the AIS.","predictedComplex":false,"interactors":[{"ac":"EBI-36504810","identifier":"O95970","identifierLink":"https://www.uniprot.org/uniprotkb/O95970/entry","name":"LGI1","description":"Leucine-rich glioma-inactivated protein 1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24367","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8603366","identifier":"O75077","identifierLink":"https://www.uniprot.org/uniprotkb/O75077/entry","name":"ADAM23","description":"Disintegrin and metalloproteinase domain-containing protein 23","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11905","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-18979","complexName":"CAPRIN1-G3BP2, stress granules assembly regulating complex","organismName":"Homo sapiens; 9606","description":"Complex promotes stress granule (SG) formation, a process key to regulating gene expression during cellular stress. Colocalizes in cytoplasmic RNA granules on microtubules and when overexpressed, promotes SG assembly through RNA binding and induction of EIF2A (Q9BY44) phosphorylation.\r\n\r\nPolyadenylated mRNAs, eukaryotic initiation factors (eIFs), and RNA-binding proteins (RBPs) can localize into stress granules in response to a variety of stress-related stimuli leading to the accumulation of translationally stalled mRNA, and dysregulation in mRNA translation plays an important role in the pathogenesis of several neurodevelopmental diseases.","predictedComplex":false,"interactors":[{"ac":"EBI-1044298","identifier":"Q9UN86","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UN86/entry","name":"G3BP2","description":"Ras GTPase-activating protein-binding protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10693","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1047080","identifier":"Q14444","identifierLink":"https://www.uniprot.org/uniprotkb/Q14444/entry","name":"CAPRIN1","description":"Caprin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22922","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-19271","complexName":"BIRC2-DIABLO apoptosis modulator complex","organismName":"Homo sapiens; 9606","description":"Pro-apototic complex, formation of which disrupts the inhibition of caspase activity by BIRC2. Plays a key regulatory role in maintaining the balance between cell survival and programmed cell death under physiological conditions. The complex functions as a modulator of cell fate, contributing to tissue homeostasis, immune regulation, and developmental cell turnover.","predictedComplex":false,"interactors":[{"ac":"EBI-514538","identifier":"Q13490","identifierLink":"https://www.uniprot.org/uniprotkb/Q13490/entry","name":"BIRC2","description":"Baculoviral IAP repeat-containing protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-517508","identifier":"Q9NR28","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NR28/entry","name":"DIABLO","description":"Diablo IAP-binding mitochondrial protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32247","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-19841","complexName":"CEP63-CEP152, centriole duplication regulatory complex","organismName":"Homo sapiens; 9606","description":"The CEP63-CEP152 complex forms a ring-like structure around parental centrioles, a configuration that ensures normal neurodevelopment. The complex plays a critical role in the positive regulating centriole duplication, facilitating the recruitment of key centriole biogenesis proteins to the small pericentriolar material (PCM), helping to ensure the efficient loading of SAS6 (Q6UVJ0), a core structural component of the nascent procentriole. This is considered essential for initiating the formation of new centrioles.","predictedComplex":false,"interactors":[{"ac":"EBI-311012","identifier":"O94986","identifierLink":"https://www.uniprot.org/uniprotkb/O94986/entry","name":"CEP152","description":"Centrosomal protein of 152 kDa","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10337","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-741977","identifier":"Q96MT8","identifierLink":"https://www.uniprot.org/uniprotkb/Q96MT8/entry","name":"CEP63","description":"Centrosomal protein of 63 kDa","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18875","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-20045","complexName":"AP5-Spastizin-spatacsin complex","organismName":"Homo sapiens; 9606","description":"Essential in the formation of lysosomal tubulation and autophagic lysosome reformation. Localized to the late endosome and lysosome membrane, the complex is required for regulaton of free lysosomes and driving membrane remodelling of auto-lysosomal tubules.\r\n\r\nMutations in SPG11, ZFYVE26 and AP5Z1 result in autosomal-recessive hereditary spastic paraplegia characterised by the slow, gradual, progressive weakness and spasticity of the lower limbs. Functional impairment of the complex results in lysosome abnormalities, including endolysosomal accumulation of material and enlargement, lack of free lysosomes available for fusion with autophagosomes and autophagosome accumulation.","predictedComplex":false,"interactors":[{"ac":"EBI-25372368","identifier":"CPX-5181","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-5181","name":"AP-5 Adaptor complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-64039833","identifier":"CPX-26503","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-26503","name":"Spastizin-spatacsin complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-20753","complexName":"Chromosomal passenger complex, AURKC variant","organismName":"Homo sapiens; 9606","description":"A serine/threonine kinase complex essential for accurate chromosome segregation and early cytokinesis. It ensures proper chromosome bi-orientation on the mitotic spindle during metaphase by phosphorylating multiple kinetochore components, thereby destabilizing incorrect, monopolar attachments. The complex also regulates cytokinesis and chromatin-induced spindle assembly. Structurally, it consists of INCENP, BIRC5, CDCA8, and an Aurora kinase, primarily AURKB (see CPX-116), though AURKC (this complex) can perform similar roles in certain cellular contexts, such as during meiosis in germline cells. Disruption of any of these four components leads to structural impairment of the complex and mislocalization from its key mitotic sites, ultimately compromising faithful chromosome segregation and successful cell division.","predictedComplex":false,"interactors":[{"ac":"EBI-307907","identifier":"Q9NQS7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NQS7/entry","name":"INCENP","description":"Inner centromere protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13142","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3926851","identifier":"Q9UQB9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UQB9/entry","name":"AURKC","description":"Aurora kinase C","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24350","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-518823","identifier":"O15392","identifierLink":"https://www.uniprot.org/uniprotkb/O15392/entry","name":"BIRC5","description":"Baculoviral IAP repeat-containing protein 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46771","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-979174","identifier":"Q53HL2","identifierLink":"https://www.uniprot.org/uniprotkb/Q53HL2/entry","name":"CDCA8","description":"Borealin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-21210","complexName":"Methyltransferase complex, METTL3-METTL14","organismName":"Homo sapiens; 9606","description":"N6-methyltransferase complex. Mediates methylation of adenosine residues at the N6 position of some RNAs inside mammalian cells, an event considered as an epitranscriptomic and post-transcriptional regulatory mark. N6-methyladenosine (m6A) modification regulates various biological processes such as the circadian clock, differentiation of embryonic and hematopoietic stem cells, cortical neurogenesis, differentiation of T-cells and primary miRNA processing, and the regulation of DNA damage response (DDR) and genomic stability. \r\n\r\nDysregulated m6A modification and m6A-associated proteins play a complex and contradicting role in driving tumorigenesis and cancer progression. METTL3-METTL14 has also been implicated in musculoskeletal diseases in both an m6A-dependent or independent manner.","predictedComplex":false,"interactors":[{"ac":"EBI-11105430","identifier":"Q86U44","identifierLink":"https://www.uniprot.org/uniprotkb/Q86U44/entry","name":"METTL3","description":"N(6)-adenosine-methyltransferase catalytic subunit METTL3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12520674","identifier":"CHEBI:67040","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:67040","name":"s-adenosyl-l-methioninate","description":"S-adenosyl-L-methioninate","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-6661081","identifier":"Q9HCE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HCE5/entry","name":"METTL14","description":"N(6)-adenosine-methyltransferase non-catalytic subunit METTL14","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13107","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-21307","complexName":"ADAM22-LGI1 synaptic receptor complex","organismName":"Homo sapiens; 9606","description":"Synaptic organizing complex. LGI1 positively modulates the voltage-gated potassium channel (Kv1) through its interaction with ADAM22 to maintain normal synaptic function and brain homeostasis. The complex interacts with AMPA-type glutamate receptors via DLG4 (P78352) intracellularly to maintain normal synaptic signal transmission. Also acts as a key synaptic organizer, anchoring signalling molecules and stabilizing synaptic connections, to ensure normal glutamatergic signalling and neuronal excitability balance, which are essential for normal brain function. \r\n\r\nDysfunction in the LGI1-ADAM22-Kv1 complex is linked to autoimmune limbic encephalitis and epilepsy.","predictedComplex":false,"interactors":[{"ac":"EBI-1567236","identifier":"Q9P0K1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P0K1/entry","name":"ADAM22","description":"Disintegrin and metalloproteinase domain-containing protein 22","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11905","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-36504810","identifier":"O95970","identifierLink":"https://www.uniprot.org/uniprotkb/O95970/entry","name":"LGI1","description":"Leucine-rich glioma-inactivated protein 1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24367","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-21432","complexName":"CAPRIN1-G3BP1, stress granules assembly regulating complex","organismName":"Homo sapiens; 9606","description":"Complex promotes stress granule (SG) formation, a process key to regulating gene expression during cellular stress. Colocalizes in cytoplasmic RNA granules on microtubules and when overexpressed, promotes SG assembly through RNA binding and induction of EIF2A (Q9BY44) phosphorylation.\r\n\r\nPolyadenylated mRNAs, eukaryotic initiation factors (eIFs), and RNA-binding proteins (RBPs) can localize into stress granules in response to a variety of stress-related stimuli leading to the accumulation of translationally stalled mRNA, and dysregulation in mRNA translation plays an important role in the pathogenesis of several neurodevelopmental diseases.","predictedComplex":false,"interactors":[{"ac":"EBI-1047080","identifier":"Q14444","identifierLink":"https://www.uniprot.org/uniprotkb/Q14444/entry","name":"CAPRIN1","description":"Caprin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22922","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1047359","identifier":"Q13283","identifierLink":"https://www.uniprot.org/uniprotkb/Q13283/entry","name":"G3BP1","description":"Ras GTPase-activating protein-binding protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10693","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-21774","complexName":"GPSM1-INSC complex","organismName":"Homo sapiens; 9606","description":"A key regulator of asymmetric cell division in polarized progenitor cells, the complex plays a fundamental role in generating diverse cell types during development. It is essential for cell fate determination and the maintenance of tissue architecture, primarily through its ability to precisely control spindle orientation. \r\n\r\nAdditionally, it may be involved in macroautophagy in intestinal cells and has been implicated in processes related to drug addiction.","predictedComplex":false,"interactors":[{"ac":"EBI-12081118","identifier":"Q1MX18","identifierLink":"https://www.uniprot.org/uniprotkb/Q1MX18/entry","name":"INSC","description":"Protein inscuteable homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21386","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-741455","identifier":"Q86YR5","identifierLink":"https://www.uniprot.org/uniprotkb/Q86YR5/entry","name":"GPSM1","description":"G-protein-signaling modulator 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45954","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-21824","complexName":"CCS-SOD1, oxidative stress response complex","organismName":"Homo sapiens; 9606","description":"The SOD1-CCS complex plays a central role in cellular defense against oxidative stress by facilitating the detoxification of superoxide radicals. CCS specifically recognizes nascent, metal-deficient SOD1 (apo-SOD1) and promotes its maturation through copper delivery and oxidation of the conserved intramolecular disulfide bond. These modifications convert apo-SOD1 into the stable, zinc- and copper-bound holo-enzyme that catalyzes the dismutation of superoxide into hydrogen peroxide and molecular oxygen, thereby maintaining redox homeostasis and protecting the cytosol and mitochondrial intermembrane space from oxidative damage.\r\n\r\nMutations in SOD1 disrupt CCS-mediated maturation and binding, linking the complex to neurodegenerative disease.","predictedComplex":false,"interactors":[{"ac":"EBI-11668690","identifier":"O14618","identifierLink":"https://www.uniprot.org/uniprotkb/O14618/entry","name":"CCS","description":"Copper chaperone for superoxide dismutase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10003","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2008294","identifier":"CHEBI:29036","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29036","name":"copper(2+)","description":"Copper (Cu2+)","stochiometry":"minValue: 3, maxValue: 3","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-990792","identifier":"P00441","identifierLink":"https://www.uniprot.org/uniprotkb/P00441/entry","name":"SOD1","description":"Superoxide dismutase [Cu-Zn]","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10003","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-23349","complexName":"GBA1-SCARB2, lysosomal trafficking complex","organismName":"Homo sapiens; 9606","description":"The GBA1-SCARB2 transport complex forms within the endoplasmic reticulum and travels through the trans-Golgi network to the lysosome where it plays a critical role in lysosomal function and glycosphingolipid metabolism, ensuring proper lysosomal enzyme localization, lipid homeostasis, and glycolipid degradation. \r\n\r\nDisruption of this complex leads to glucocerebroside accumulation, underlying Gaucher disease, Action Myoclonus-Renal Failure (AMRF) syndrome, and increased Parkinson’s disease risk.","predictedComplex":false,"interactors":[{"ac":"EBI-1564609","identifier":"P04062","identifierLink":"https://www.uniprot.org/uniprotkb/P04062/entry","name":"GBA1","description":"Lysosomal acid glucosylceramidase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11069","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1564650","identifier":"Q14108","identifierLink":"https://www.uniprot.org/uniprotkb/Q14108/entry","name":"SCARB2","description":"Lysosome membrane protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11923","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-24049","complexName":"TP63-TP73, transcription regulatory complex","organismName":"Homo sapiens; 9606","description":"Sequence specific DNA binding transcriptional regulator complex. Contributes to maintaining tissue integrity, cell differentiation, and genomic stability. Acts as a tumour‑suppressing regulator, controlling transcription of genes linked to DNA repair, survival, differentiation and stem/progenitor cell maintenance. This complex or its isoforms may engage in skin/epidermal repair. Under certain contexts it can activate some TP53‑target genes including CDKN1A (P38936), BAX (Q07812) and BBC3 (Q9BXH1).","predictedComplex":false,"interactors":[{"ac":"EBI-2337775","identifier":"Q9H3D4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H3D4/entry","name":"TP63","description":"Tumor protein 63","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11447","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-389606","identifier":"O15350","identifierLink":"https://www.uniprot.org/uniprotkb/O15350/entry","name":"TP73","description":"Tumor protein p73","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11447","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-24856","complexName":"GNAI1-RGS14, Gi-signalling regulatory complex","organismName":"Homo sapiens; 9606","description":"A multifunctional signalling assembly in which RGS14 binds GDP-GNAI1₁ stabilizes it in its inactive state and coordinates cross-talk between heterotrimeric G-protein and Ras/MAPK signalling pathways. The complex acts as a regulator of Gi-mediated signalling in neurons and other tissues. GDP-GNAI1 binding to RGS14 also prevents the latters association with centrosomes. GDP-GNAI1 binding results in the translocation of RGS14 from the cytoplasm to the plasma membrane where it acts as a scaffold and regulator of G-protein signalling; translocation switches RGS14's from a potential structural role in centrosomal organization to a dynamic signalling role at the cell surface.","predictedComplex":false,"interactors":[{"ac":"EBI-618639","identifier":"P63096","identifierLink":"https://www.uniprot.org/uniprotkb/P63096/entry","name":"GNAI1","description":"Guanine nucleotide-binding protein G(i) subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10218","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-750603","identifier":"O43566","identifierLink":"https://www.uniprot.org/uniprotkb/O43566/entry","name":"RGS14","description":"Regulator of G-protein signaling 14","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25521","complexName":"RIC1-RGP1 guanyl-nucleotide exchange factor complex","organismName":"Homo sapiens; 9606","description":"Guanine nucleotide exchange factor recruited by RAB33B (Q9H082) to the Golgi membrane to function as a GEF for RAB6A (P20340) activation by exchanging bound GDP for free GTP.","predictedComplex":false,"interactors":[{"ac":"EBI-2823702","identifier":"Q92546","identifierLink":"https://www.uniprot.org/uniprotkb/Q92546/entry","name":"RGP1","description":"RAB6A-GEF complex partner protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12507","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2824467","identifier":"Q4ADV7","identifierLink":"https://www.uniprot.org/uniprotkb/Q4ADV7/entry","name":"RIC1","description":"Guanine nucleotide exchange factor subunit RIC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22746","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25716","complexName":"SHOC2-MRAS-PPP1CA complex","organismName":"Homo sapiens; 9606","description":"Holophosphatase complex which dephosphorylates members of RAF family proteins, RAF1 (P04049), BRAF (P15056) and ARAF (P10398) at key inhibitory phosphorylation sites Ser-259, Ser-365 and Ser-214, respectively, while eliminating inhibitory phosphorylation on RAF family proteins to potentiate MAPK signalling. Functions as a key regulator of RTK-RAS signalling, a pathway which regulates cell proliferation and survival through the MAP kinase cascade. \r\n\r\nMutations mapped to protein-protein interfaces in the complex impair complex formation and stabilization. Gain-of-function and loss-of-function mutations in SHOC2 are linked to driving RASopathy and RAS-driven cancers.","predictedComplex":false,"interactors":[{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-25820308","identifier":"CHEBI:37565","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:37565","name":"gtp(4-)","description":"GTP(4-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-357253","identifier":"P62136","identifierLink":"https://www.uniprot.org/uniprotkb/P62136/entry","name":"PPP1CA","description":"Serine/threonine-protein phosphatase PP1-alpha catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11668","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968728","identifier":"O14807","identifierLink":"https://www.uniprot.org/uniprotkb/O14807/entry","name":"MRAS","description":"Ras-related protein M-Ras","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24070","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-993879","identifier":"Q9UQ13","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UQ13/entry","name":"SHOC2","description":"Leucine-rich repeat protein SHOC-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45752","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25717","complexName":"Macrophage colony-stimulating factor-1 receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Macrophage attractant cytokine-receptor complex that plays a role in the regulation of hematopoietic precursor cell survival, proliferation and differentiation into heterogeneous populations of monocytes, macrophages, dendritic cells, and bone-resorbing osteoclasts. Also plays a key role in inflammation through its ability to promote the release of pro-inflammatory chemokines. Involved in the reorganization of the actin cytoskeleton and cell migration. CSF1 binding to CSF1R results in receptor phosphorylation and dimerization leading to the activation of several pathways including MAP and SRC kinases, the JAK/STAT, RAS and AMPK1 pathways. The CSF1-CSF1R signalling pathway has overlapping effects with the IL34-CSF1R (CPX-10333) pathway to drive macrophage differentiation but differ in their polarization potential.\r\n\r\nUncontrolled expression of CSF1-CSF1R is implicated in both inflammatory diseases, and cancer cell proliferation, invasion and metastases. CSF1-CSFR1 plays a pivotol role in the healthy brain and is essential in brain development, synaptic landscape, infection resolution and neuronal maintenance. CSF1 adjuvant therapy is thought to improve female fertility.","predictedComplex":false,"interactors":[{"ac":"EBI-2835440","identifier":"P07333","identifierLink":"https://www.uniprot.org/uniprotkb/P07333/entry","name":"CSF1R","description":"Macrophage colony-stimulating factor 1 receptor","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2872294","identifier":"P09603","identifierLink":"https://www.uniprot.org/uniprotkb/P09603/entry","name":"CSF1","description":"Macrophage colony-stimulating factor 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10058","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25718","complexName":"SREBP-SCAP transcription regulator complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"scp1 binds and stabilizes full-length sre1 in the endoplasmic reticulum (ER). Under conditions of low sterols or low oxygen, the complex translocates from the ER to the Golgi where sre1 is proteolytically cleaved and freed from the membrane to act as a master regulator of cellular lipid homeostasis which plays a critical role in the cells adaptation to hypoxia.","predictedComplex":false,"interactors":[{"ac":"EBI-59000496","identifier":"O43043","identifierLink":"https://www.uniprot.org/uniprotkb/O43043/entry","name":"scp1","description":"Sterol regulatory element-binding protein cleavage-activating protein","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR46378","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-59000520","identifier":"Q9UUD1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UUD1/entry","name":"sre1","description":"Sterol regulatory element-binding protein 1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR47336","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25719","complexName":"SHOC2-MRAS-PPP1CB complex","organismName":"Homo sapiens; 9606","description":"Holophosphatase complex which dephosphorylates members of RAF family proteins, RAF1 (P04049), BRAF (P15056) and ARAF (P10398) at key inhibitory phosphorylation sites Ser-259, Ser-365 and Ser-214, respectively, while eliminating inhibitory phosphorylation on RAF family proteins to potentiate MAPK signalling. Functions as a key regulator of RTK-RAS signalling, a pathway which regulates cell proliferation and survival through the MAP kinase cascade.\r\n\r\nMutations mapped to protein-protein interfaces in the complex impair complex formation and stabilization. Gain-of-function and loss-of-function mutations in SHOC2 and PPP1CB mutations are linked to driving RASopathy and RAS-driven cancers.","predictedComplex":false,"interactors":[{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-25820308","identifier":"CHEBI:37565","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:37565","name":"gtp(4-)","description":"GTP(4-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-352350","identifier":"P62140","identifierLink":"https://www.uniprot.org/uniprotkb/P62140/entry","name":"PPP1CB","description":"Serine/threonine-protein phosphatase PP1-beta catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11668","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968728","identifier":"O14807","identifierLink":"https://www.uniprot.org/uniprotkb/O14807/entry","name":"MRAS","description":"Ras-related protein M-Ras","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24070","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-993879","identifier":"Q9UQ13","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UQ13/entry","name":"SHOC2","description":"Leucine-rich repeat protein SHOC-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45752","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25720","complexName":"SHOC2-MRAS-PPP1CC complex","organismName":"Homo sapiens; 9606","description":"Holophosphatase complex which dephosphorylates members of RAF family proteins, RAF1 (P04049), BRAF (P15056) and ARAF (P10398) at key inhibitory phosphorylation sites Ser-259, Ser-365 and Ser-214, respectively, while eliminating inhibitory phosphorylation on RAF family proteins to potentiate MAPK signalling. Functions as a key regulator of RTK-RAS signalling, a pathway which regulates cell proliferation and survival through the MAP kinase cascade.\r\n\r\nMutations mapped to protein-protein interfaces in the complex impair complex formation and stabilization. Gain-of-function and loss-of-function mutations in SHOC2 are linked to driving RASopathy and RAS-driven cancers.","predictedComplex":false,"interactors":[{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-25820308","identifier":"CHEBI:37565","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:37565","name":"gtp(4-)","description":"GTP(4-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-356283","identifier":"P36873","identifierLink":"https://www.uniprot.org/uniprotkb/P36873/entry","name":"PPP1CC","description":"Serine/threonine-protein phosphatase PP1-gamma catalytic subunit","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11668","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968728","identifier":"O14807","identifierLink":"https://www.uniprot.org/uniprotkb/O14807/entry","name":"MRAS","description":"Ras-related protein M-Ras","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24070","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-993879","identifier":"Q9UQ13","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UQ13/entry","name":"SHOC2","description":"Leucine-rich repeat protein SHOC-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45752","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25721","complexName":"SREBP-SCAP transcription regulator complex, SREBF2 variant","organismName":"Homo sapiens; 9606","description":"When the cell is enriched with cholesterol. SCAP binds and stabilizes full-length SREBF1/2 and is anchored in the endoplasmic reticulum (ER) by formation of the SREBP-SCAP-INSIG complex (CPX-25747/CPX-25748). Under conditions of low sterols, the SREBP-SCAP complex is translocated by COPII (CPX-2360)-coated vesicles from the ER to the Golgi where SREBF1/2 is proteolytically cleaved and freed from the membrane to activate the transcription of genes involved in cholesterol biosynthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-465059","identifier":"Q12772","identifierLink":"https://www.uniprot.org/uniprotkb/Q12772/entry","name":"SREBF2","description":"Sterol regulatory element-binding protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46062","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6190187","identifier":"Q12770","identifierLink":"https://www.uniprot.org/uniprotkb/Q12770/entry","name":"SCAP","description":"Sterol regulatory element-binding protein cleavage-activating protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46378","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8828","complexName":"sTNF-TNR1A receptor-ligand core complex, BIRC2 variant","organismName":"Homo sapiens; 9606","description":"A membrane-bound tumor necrosis factor-receptor signaling complex (Complex I) formed on the binding of the soluble form of the pro-inflammatory cytokine, tumour necrosis factor (sTNF, CPX-8826). This activates the mitogen-activated protein kinase  and nuclear factor-kappa-B (NF-kappa-B) signalling pathways, leading to proinflammatory gene expression and promoting cell survival. The Ripoptosome (CPX-1907, Complex II) originates from the dissociation of Complex I components from the receptor and promotes cell apoptosis. \r\n\r\nTNF, a key regulator of T regulatory cells, is mainly secreted by macrophages, T helper 1 and natural killer cells, while its receptor component TNFRSF1A is ubiquitously expressed on almost all human tissues.\r\n\r\n\r\nIntracellular signaling is triggered by ligand-bound receptors assembling into higher-order clusters. Soluble TNFA triggers more robust clustering of TNFR1 than membrane-bound ligand. TNFR1-mediated signaling is therefore generally caused by the activation due to sTNFA over mTNFA. TNFA-TNFRSF1A signalling complex formation is indirectly influenced by TNFA-TNFRSF1B activation and the cross-talk between the receptor complexes is central to cell-survival, proliferation or death.","predictedComplex":false,"interactors":[{"ac":"EBI-355744","identifier":"Q12933","identifierLink":"https://www.uniprot.org/uniprotkb/Q12933/entry","name":"TRAF2","description":"TNF receptor-associated factor 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358507","identifier":"Q13546","identifierLink":"https://www.uniprot.org/uniprotkb/Q13546/entry","name":"RIPK1","description":"Receptor-interacting serine/threonine-protein kinase 1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44329","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359215","identifier":"Q15628","identifierLink":"https://www.uniprot.org/uniprotkb/Q15628/entry","name":"TRADD","description":"Tumor necrosis factor receptor type 1-associated DEATH domain protein","stochiometry":"minValue: 3, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14913","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50431755","identifier":"CPX-8826","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-8826","name":"Soluble tumor necrosis factor complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-514538","identifier":"Q13490","identifierLink":"https://www.uniprot.org/uniprotkb/Q13490/entry","name":"BIRC2","description":"Baculoviral IAP repeat-containing protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52219099","identifier":"P19438-PRO_0000034543","identifierLink":"https://www.uniprot.org/uniprotkb/P19438-PRO_0000034543/entry","name":"TNFRSF1A","description":"Tumor necrosis factor receptor superfamily member 1A, membrane form","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-523498","identifier":"O00463","identifierLink":"https://www.uniprot.org/uniprotkb/O00463/entry","name":"TRAF5","description":"TNF receptor-associated factor 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6000","complexName":"Interferon alpha receptor-ligand complex, IFNA6 variant","organismName":"Homo sapiens; 9606","description":"Receptor-ligand complex whose formation is triggered in response to viruses, bacteria or microbial nucleic acids to engage downstream signalling pathways that activate innate and adaptive immune responses. Following complex assembly TYK2 (P29597) and/or members of the JAK family of tyrosine-protein kinases are activated by reciprocal transphosphorylation. Subsequently, they phosphorylate several tyrosine residues in the membrane-distal, intracellular domains of IFNAR1 and IFNAR2, which, in turn, recruit further effector proteins that propagate downstream signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-14133376","identifier":"P05013","identifierLink":"https://www.uniprot.org/uniprotkb/P05013/entry","name":"IFNA6","description":"Interferon alpha-6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1547250","identifier":"P17181","identifierLink":"https://www.uniprot.org/uniprotkb/P17181/entry","name":"IFNAR1","description":"Interferon alpha/beta receptor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-958408","identifier":"P48551","identifierLink":"https://www.uniprot.org/uniprotkb/P48551/entry","name":"IFNAR2","description":"Interferon alpha/beta receptor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5995","complexName":"Interferon alpha receptor-ligand complex, IFNA2 variant","organismName":"Homo sapiens; 9606","description":"Receptor-ligand complex whose formation is triggered in response to viruses, bacteria or microbial nucleic acids to engage downstream signalling pathways that activate innate and adaptive immune responses. Following complex assembly TYK2 (P29597) and/or members of the JAK family of tyrosine-protein kinases are activated by reciprocal transphosphorylation. Subsequently, they phosphorylate several tyrosine residues in the membrane-distal, intracellular domains of IFNAR1 and IFNAR2, which, in turn, recruit further effector proteins that propagate downstream signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-1547250","identifier":"P17181","identifierLink":"https://www.uniprot.org/uniprotkb/P17181/entry","name":"IFNAR1","description":"Interferon alpha/beta receptor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4394394","identifier":"P01563","identifierLink":"https://www.uniprot.org/uniprotkb/P01563/entry","name":"IFNA2","description":"Interferon alpha-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-958408","identifier":"P48551","identifierLink":"https://www.uniprot.org/uniprotkb/P48551/entry","name":"IFNAR2","description":"Interferon alpha/beta receptor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5996","complexName":"Interferon alpha receptor-ligand complex, IFNA1 variant","organismName":"Homo sapiens; 9606","description":"Receptor-ligand complex whose formation is triggered in response to viruses, bacteria or microbial nucleic acids to engage downstream signalling pathways that activate innate and adaptive immune responses. Following complex assembly TYK2 (P29597) and/or members of the JAK family of tyrosine-protein kinases are activated by reciprocal transphosphorylation. Subsequently, they phosphorylate several tyrosine residues in the membrane-distal, intracellular domains of IFNAR1 and IFNAR2, which, in turn, recruit further effector proteins that propagate downstream signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-11478589","identifier":"P01562","identifierLink":"https://www.uniprot.org/uniprotkb/P01562/entry","name":"IFNA13","description":"Interferon alpha-1/13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1547250","identifier":"P17181","identifierLink":"https://www.uniprot.org/uniprotkb/P17181/entry","name":"IFNAR1","description":"Interferon alpha/beta receptor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-958408","identifier":"P48551","identifierLink":"https://www.uniprot.org/uniprotkb/P48551/entry","name":"IFNAR2","description":"Interferon alpha/beta receptor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5997","complexName":"Interferon alpha receptor-ligand complex, IFNA7 variant","organismName":"Homo sapiens; 9606","description":"Receptor-ligand complex whose formation is triggered in response to viruses, bacteria or microbial nucleic acids to engage downstream signalling pathways that activate innate and adaptive immune responses. Following complex assembly TYK2 (P29597) and/or members of the JAK family of tyrosine-protein kinases are activated by reciprocal transphosphorylation. Subsequently, they phosphorylate several tyrosine residues in the membrane-distal, intracellular domains of IFNAR1 and IFNAR2, which, in turn, recruit further effector proteins that propagate downstream signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-1547250","identifier":"P17181","identifierLink":"https://www.uniprot.org/uniprotkb/P17181/entry","name":"IFNAR1","description":"Interferon alpha/beta receptor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21825632","identifier":"P01567","identifierLink":"https://www.uniprot.org/uniprotkb/P01567/entry","name":"IFNA7","description":"Interferon alpha-7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-958408","identifier":"P48551","identifierLink":"https://www.uniprot.org/uniprotkb/P48551/entry","name":"IFNAR2","description":"Interferon alpha/beta receptor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5998","complexName":"Interferon alpha receptor-ligand complex, IFNA4 variant","organismName":"Homo sapiens; 9606","description":"Receptor-ligand complex whose formation is triggered in response to viruses, bacteria or microbial nucleic acids to engage downstream signalling pathways that activate innate and adaptive immune responses. 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Subsequently, they phosphorylate several tyrosine residues in the membrane-distal, intracellular domains of IFNAR1 and IFNAR2, which, in turn, recruit further effector proteins that propagate downstream signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-10194381","identifier":"P05014","identifierLink":"https://www.uniprot.org/uniprotkb/P05014/entry","name":"IFNA4","description":"Interferon alpha-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1547250","identifier":"P17181","identifierLink":"https://www.uniprot.org/uniprotkb/P17181/entry","name":"IFNAR1","description":"Interferon alpha/beta receptor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-958408","identifier":"P48551","identifierLink":"https://www.uniprot.org/uniprotkb/P48551/entry","name":"IFNAR2","description":"Interferon alpha/beta receptor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-5999","complexName":"Interferon alpha receptor-ligand complex, IFNA5 variant","organismName":"Homo sapiens; 9606","description":"Receptor-ligand complex whose formation is triggered in response to viruses, bacteria or microbial nucleic acids to engage downstream signalling pathways that activate innate and adaptive immune responses. 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Subsequently, they phosphorylate several tyrosine residues in the membrane-distal, intracellular domains of IFNAR1 and IFNAR2, which, in turn, recruit further effector proteins that propagate downstream signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-1547250","identifier":"P17181","identifierLink":"https://www.uniprot.org/uniprotkb/P17181/entry","name":"IFNAR1","description":"Interferon alpha/beta receptor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21706713","identifier":"P01569","identifierLink":"https://www.uniprot.org/uniprotkb/P01569/entry","name":"IFNA5","description":"Interferon alpha-5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-958408","identifier":"P48551","identifierLink":"https://www.uniprot.org/uniprotkb/P48551/entry","name":"IFNAR2","description":"Interferon alpha/beta receptor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6001","complexName":"Interferon alpha receptor-ligand complex, IFNA8 variant","organismName":"Homo sapiens; 9606","description":"Receptor-ligand complex whose formation is triggered in response to viruses, bacteria or microbial nucleic acids to engage downstream signalling pathways that activate innate and adaptive immune responses. 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Subsequently, they phosphorylate several tyrosine residues in the membrane-distal, intracellular domains of IFNAR1 and IFNAR2, which, in turn, recruit further effector proteins that propagate downstream signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-1547250","identifier":"P17181","identifierLink":"https://www.uniprot.org/uniprotkb/P17181/entry","name":"IFNAR1","description":"Interferon alpha/beta receptor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18211524","identifier":"P32881","identifierLink":"https://www.uniprot.org/uniprotkb/P32881/entry","name":"IFNA8","description":"Interferon alpha-8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-958408","identifier":"P48551","identifierLink":"https://www.uniprot.org/uniprotkb/P48551/entry","name":"IFNAR2","description":"Interferon alpha/beta receptor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6002","complexName":"Interferon alpha receptor-ligand complex, IFNA10 variant","organismName":"Homo sapiens; 9606","description":"Receptor-ligand complex whose formation is triggered in response to viruses, bacteria or microbial nucleic acids to engage downstream signalling pathways that activate innate and adaptive immune responses. 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Subsequently, they phosphorylate several tyrosine residues in the membrane-distal, intracellular domains of IFNAR1 and IFNAR2, which, in turn, recruit further effector proteins that propagate downstream signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-1547250","identifier":"P17181","identifierLink":"https://www.uniprot.org/uniprotkb/P17181/entry","name":"IFNAR1","description":"Interferon alpha/beta receptor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21831322","identifier":"P01566","identifierLink":"https://www.uniprot.org/uniprotkb/P01566/entry","name":"IFNA10","description":"Interferon alpha-10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-958408","identifier":"P48551","identifierLink":"https://www.uniprot.org/uniprotkb/P48551/entry","name":"IFNAR2","description":"Interferon alpha/beta receptor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6003","complexName":"Interferon alpha receptor-ligand complex, IFNA14 variant","organismName":"Homo sapiens; 9606","description":"Receptor-ligand complex whose formation is triggered in response to viruses, bacteria or microbial nucleic acids to engage downstream signalling pathways that activate innate and adaptive immune responses. 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Subsequently, they phosphorylate several tyrosine residues in the membrane-distal, intracellular domains of IFNAR1 and IFNAR2, which, in turn, recruit further effector proteins that propagate downstream signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-12290903","identifier":"P01570","identifierLink":"https://www.uniprot.org/uniprotkb/P01570/entry","name":"IFNA14","description":"Interferon alpha-14","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1547250","identifier":"P17181","identifierLink":"https://www.uniprot.org/uniprotkb/P17181/entry","name":"IFNAR1","description":"Interferon alpha/beta receptor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-958408","identifier":"P48551","identifierLink":"https://www.uniprot.org/uniprotkb/P48551/entry","name":"IFNAR2","description":"Interferon alpha/beta receptor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6004","complexName":"Interferon alpha receptor-ligand complex, IFNA16 variant","organismName":"Homo sapiens; 9606","description":"Receptor-ligand complex whose formation is triggered in response to viruses, bacteria or microbial nucleic acids to engage downstream signalling pathways that activate innate and adaptive immune responses. 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Subsequently, they phosphorylate several tyrosine residues in the membrane-distal, intracellular domains of IFNAR1 and IFNAR2, which, in turn, recruit further effector proteins that propagate downstream signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-1547250","identifier":"P17181","identifierLink":"https://www.uniprot.org/uniprotkb/P17181/entry","name":"IFNAR1","description":"Interferon alpha/beta receptor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7055360","identifier":"P05015","identifierLink":"https://www.uniprot.org/uniprotkb/P05015/entry","name":"IFNA16","description":"Interferon alpha-16","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-958408","identifier":"P48551","identifierLink":"https://www.uniprot.org/uniprotkb/P48551/entry","name":"IFNAR2","description":"Interferon alpha/beta receptor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6005","complexName":"Interferon alpha receptor-ligand complex, IFNA17 variant","organismName":"Homo sapiens; 9606","description":"Receptor-ligand complex whose formation is triggered in response to viruses, bacteria or microbial nucleic acids to engage downstream signalling pathways that activate innate and adaptive immune responses. 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Subsequently, they phosphorylate several tyrosine residues in the membrane-distal, intracellular domains of IFNAR1 and IFNAR2, which, in turn, recruit further effector proteins that propagate downstream signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-1547250","identifier":"P17181","identifierLink":"https://www.uniprot.org/uniprotkb/P17181/entry","name":"IFNAR1","description":"Interferon alpha/beta receptor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21771978","identifier":"P01571","identifierLink":"https://www.uniprot.org/uniprotkb/P01571/entry","name":"IFNA17","description":"Interferon alpha-17","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-958408","identifier":"P48551","identifierLink":"https://www.uniprot.org/uniprotkb/P48551/entry","name":"IFNAR2","description":"Interferon alpha/beta receptor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6006","complexName":"Interferon alpha receptor-ligand complex, IFNA21 variant","organismName":"Homo sapiens; 9606","description":"Receptor-ligand complex whose formation is triggered in response to viruses, bacteria or microbial nucleic acids to engage downstream signalling pathways that activate innate and adaptive immune responses. 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Subsequently, they phosphorylate several tyrosine residues in the membrane-distal, intracellular domains of IFNAR1 and IFNAR2, which, in turn, recruit further effector proteins that propagate downstream signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-1547250","identifier":"P17181","identifierLink":"https://www.uniprot.org/uniprotkb/P17181/entry","name":"IFNAR1","description":"Interferon alpha/beta receptor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21706776","identifier":"P01568","identifierLink":"https://www.uniprot.org/uniprotkb/P01568/entry","name":"IFNA21","description":"Interferon alpha-21","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-958408","identifier":"P48551","identifierLink":"https://www.uniprot.org/uniprotkb/P48551/entry","name":"IFNAR2","description":"Interferon alpha/beta receptor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6007","complexName":"Interferon beta receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Receptor-ligand complex whose formation is triggered in response to viruses, bacteria or microbial nucleic acids to engage downstream signalling pathways that activate innate and adaptive immune responses. 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Subsequently, they phosphorylate several tyrosine residues in the membrane-distal, intracellular domains of IFNAR1 and IFNAR2, which, in turn, recruit further effector proteins that propagate downstream signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-12383562","identifier":"P01574","identifierLink":"https://www.uniprot.org/uniprotkb/P01574/entry","name":"IFNB1","description":"Interferon beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1547250","identifier":"P17181","identifierLink":"https://www.uniprot.org/uniprotkb/P17181/entry","name":"IFNAR1","description":"Interferon alpha/beta receptor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-958408","identifier":"P48551","identifierLink":"https://www.uniprot.org/uniprotkb/P48551/entry","name":"IFNAR2","description":"Interferon alpha/beta receptor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6008","complexName":"Interferon epsilon receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Receptor-ligand complex whose formation is triggered in response to viruses, bacteria or microbial nucleic acids to engage downstream signalling pathways that activate innate and adaptive immune responses. 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Subsequently, they phosphorylate several tyrosine residues in the membrane-distal, intracellular domains of IFNAR1 and IFNAR2, which, in turn, recruit further effector proteins that propagate downstream signalling. \r\nRequired for maintaining basal levels of IFN-regulated genes, including IRF7 (Q92985) and ISG15 (P05161), in the female reproductive tract.","predictedComplex":false,"interactors":[{"ac":"EBI-1547250","identifier":"P17181","identifierLink":"https://www.uniprot.org/uniprotkb/P17181/entry","name":"IFNAR1","description":"Interferon alpha/beta receptor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21641408","identifier":"Q86WN2","identifierLink":"https://www.uniprot.org/uniprotkb/Q86WN2/entry","name":"IFNE","description":"Interferon epsilon","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-958408","identifier":"P48551","identifierLink":"https://www.uniprot.org/uniprotkb/P48551/entry","name":"IFNAR2","description":"Interferon alpha/beta receptor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6009","complexName":"Interferon kappa receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Receptor-ligand complex whose formation is triggered in response to viruses, bacteria or microbial nucleic acids to engage downstream signalling pathways that activate innate and adaptive immune responses. 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Subsequently, they phosphorylate several tyrosine residues in the membrane-distal, intracellular domains of IFNAR1 and IFNAR2, which, in turn, recruit further effector proteins that propagate downstream signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-1547250","identifier":"P17181","identifierLink":"https://www.uniprot.org/uniprotkb/P17181/entry","name":"IFNAR1","description":"Interferon alpha/beta receptor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4394437","identifier":"P05000","identifierLink":"https://www.uniprot.org/uniprotkb/P05000/entry","name":"IFNW1","description":"Interferon omega-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11691","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-958408","identifier":"P48551","identifierLink":"https://www.uniprot.org/uniprotkb/P48551/entry","name":"IFNAR2","description":"Interferon alpha/beta receptor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6011","complexName":"Interferon lambda receptor-ligand complex, IFNL1 variant","organismName":"Homo sapiens; 9606","description":"Receptor-ligand complex whose formation is triggered in response to viral infection to engage downstream signalling pathways that activate anti-viral responses. 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Subsequently, they phosphorylate several tyrosine residues in the membrane-distal, intracellular domains of IFNLR1 and IL10RB, which, in turn, recruit further effector proteins that propagate downstream signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-11175900","identifier":"Q08334","identifierLink":"https://www.uniprot.org/uniprotkb/Q08334/entry","name":"IL10RB","description":"Interleukin-10 receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11474210","identifier":"Q8IU54","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IU54/entry","name":"IFNL1","description":"Interferon lambda-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31943","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373215","identifier":"Q8IU57","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IU57/entry","name":"IFNLR1","description":"Interferon lambda receptor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6012","complexName":"Interferon lambda receptor-ligand complex, IFNL2 variant","organismName":"Homo sapiens; 9606","description":"Receptor-ligand complex whose formation is triggered in response to viral infection to engage downstream signalling pathways that activate anti-viral responses. Following complex assembly TYK2 (P29597) and/or members of the JAK family of tyrosine-protein kinases are activated by reciprocal transphosphorylation. Subsequently, they phosphorylate several tyrosine residues in the membrane-distal, intracellular domains of IFNLR1 and IL10RB, which, in turn, recruit further effector proteins that propagate downstream signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-11175900","identifier":"Q08334","identifierLink":"https://www.uniprot.org/uniprotkb/Q08334/entry","name":"IL10RB","description":"Interleukin-10 receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21880197","identifier":"Q8IZJ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IZJ0/entry","name":"IFNL2","description":"Interferon lambda-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31943","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373215","identifier":"Q8IU57","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IU57/entry","name":"IFNLR1","description":"Interferon lambda receptor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6014","complexName":"Interferon lambda receptor-ligand complex, IFNL4 variant","organismName":"Homo sapiens; 9606","description":"Receptor-ligand complex whose formation is triggered in response to viral infection to engage downstream signalling pathways that activate anti-viral responses. Following complex assembly, TYK2 (P29597) and/or members of the JAK family of tyrosine-protein kinases  are activated by reciprocal transphosphorylation. Subsequently, they phosphorylate several tyrosine residues in the membrane-distal, intracellular domains of IFNLR1 and IL10RB, which, in turn, recruit further effector proteins that propagate downstream signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-11175900","identifier":"Q08334","identifierLink":"https://www.uniprot.org/uniprotkb/Q08334/entry","name":"IL10RB","description":"Interleukin-10 receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25756703","identifier":"K9M1U5","identifierLink":"https://www.uniprot.org/uniprotkb/K9M1U5/entry","name":"IFNL4","description":"Interferon lambda-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31943","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373215","identifier":"Q8IU57","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IU57/entry","name":"IFNLR1","description":"Interferon lambda receptor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6015","complexName":"Interferon gamma receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Receptor-ligand complex whose formation is triggered in response to infectious agents to engage downstream signalling pathways that activate immune responses. Following complex assembly JAK1 (P23458) and JAK2 (O60674) are activated by reciprocal transphosphorylation. Subsequently, they phosphorylate several tyrosine residues in the membrane-distal, intracellular domains of IFNGR1 and IFNGR2, which, in turn, recruit further effector proteins that propagate downstream signalling.","predictedComplex":false,"interactors":[{"ac":"EBI-1030755","identifier":"P15260","identifierLink":"https://www.uniprot.org/uniprotkb/P15260/entry","name":"IFNGR1","description":"Interferon gamma receptor 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25759536","identifier":"CPX-6024","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-6024","name":"Interferon gamma complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-3905457","identifier":"P38484","identifierLink":"https://www.uniprot.org/uniprotkb/P38484/entry","name":"IFNGR2","description":"Interferon gamma receptor 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-646","complexName":"Interleukin-2 receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Transmembrane complex formed on the binding of extracellular interleukin-2 (IL-2) to a differentially expressed receptor which can be composed of up to three distinct receptor chains: IL2RA (alpha-chain, IL2RB (beta-chain) and IL2RG (gamma-chain), where IL2RB and IL2RG are essential for signal transduction, whilst IL2RA plays a key role in cytokine presentation to the signaling receptors. Ligand binding results in the assembly of the complete complex, inducing signal transduction through three different signaling pathways: the JAK-STAT pathway, the PI3K/Akt/mTOR pathway and the MAPK/ERK pathway. Binding to IL-2 stimulates phosphorylation of three critical tyrosine residues on the cytoplasmic tail of IL2RB as well as tyrosine phosphorylation of the JAKs. Activation of the JAK/STAT signaling cascade is through IL-2RB-JAK1 and IL-2RG-JAK3 recruitment of predominantly STAT5A and STAT5B. \r\n\r\nOriginally recognized for its ability to stimulate lymphocyte proliferation, the IL-2-IL2R pathway is an integral regulator of healthy and pathalogical immune responses but also plays a key role in regulating the homeostasis of regulatory T cells (T-regs), which express the IL-2R constitutively. \r\n\r\nWhilst, IL2 shares several actions with IL15, such as stimulating cytotoxic T cells and Natural Killer (NK) cell proliferation, they are not functionally redundant. IL-2 favours maintaining T-reg homeostasis and regulating T helper (Th) differentiation whereas IL-15 favors expansion of CD8 memory cells, NK cells, and NKT cells.\r\n\r\nImmune activation leads to the shedding of IL2RA, leaving behind a soluble form of IL2R (sIL-2R). Increased levels of sIL2R are considered to be indicative of an on-going immune response making it a useful biomarker for monitoring disease progression. sIL-2R's role in providing immunity or governing self-tolerance is unclear and it is capable of either functioning as a decoy-receptor that reduces the bio-availability of IL2, or enabling in trans activation by presenting IL2 to dimeric IL2R expressing immune cells.","predictedComplex":false,"interactors":[{"ac":"EBI-12508717","identifier":"P60568","identifierLink":"https://www.uniprot.org/uniprotkb/P60568/entry","name":"IL2","description":"Interleukin-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48487","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2866779","identifier":"P14784","identifierLink":"https://www.uniprot.org/uniprotkb/P14784/entry","name":"IL2RB","description":"Interleukin-2 receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23037","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-80475","identifier":"P31785","identifierLink":"https://www.uniprot.org/uniprotkb/P31785/entry","name":"IL2RG","description":"Cytokine receptor common subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8614302","identifier":"P01589","identifierLink":"https://www.uniprot.org/uniprotkb/P01589/entry","name":"IL2RA","description":"Interleukin-2 receptor subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10573","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9224","complexName":"Interleukin-3 receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Transmembrane complex formed on the binding of a monomeric extracellular interleukin-3 (IL3) to its receptor composed of IL3A and CSF2RB. Ligand binding results in the assembly of the complete complex, inducing the transphosphorylation of JAK2 molecules as well as phosphorylation of the cytoplasmic tails of the receptors. STAT5 monomers bind to the phosphorylated site of the receptor and are phosphorylated by JAK2. Phosphorylated STAT5 dissociates from the receptors, dimerizes, and the dimer translocates into the nucleus where it induces the transcription of target genes. IL3 can also mediate its signal through the c-myc and Ras pathways.\r\n\r\nThe pleiotropic cytokine-receptor complex is implicated in the physiological inflammation for pathogen clearance but also the pathophysiology of inflammatory and autoimmune diseases. Produced mainly by activated T cells to stimulate the growth and differentiation of several multi-potential haematopoietic cells. \r\n\r\nIL3 is thought to fuel acute inflammation to create a cytokine storm. IL3 has been implicated in immune disorders including, sepsis, colitis and acts as a predictive marker for SARS-CoV-2.","predictedComplex":false,"interactors":[{"ac":"EBI-1757512","identifier":"P26951","identifierLink":"https://www.uniprot.org/uniprotkb/P26951/entry","name":"IL3RA","description":"Interleukin-3 receptor subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1809771","identifier":"P32927","identifierLink":"https://www.uniprot.org/uniprotkb/P32927/entry","name":"CSF2RB","description":"Cytokine receptor common subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23037","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1811718","identifier":"P08700","identifierLink":"https://www.uniprot.org/uniprotkb/P08700/entry","name":"IL3","description":"Interleukin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48489","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8834","complexName":"Interleukin-4 receptor-ligand type-1 complex","organismName":"Homo sapiens; 9606","description":"Transmembrane complex formed on the binding of an extracellular interleukin-4 (IL4) to either a type-1 IL4 receptor composed of IL4R and IL2RG or a type-2 IL4 receptor, composed of IL4R and IL13RA1 (CPX-624). Ligand binding results in the assembly of the complete complex, which induces signaling mediated principally through the IL4R chain and involves activation of the transcription factor, signal transducer and activator of transcription-6 (STAT6). \r\n\r\nIL4 binding to the type-1 IL4 receptor induces the phosphorylation of the Janus kinase, JAK1 associated with the IL4R chain and JAK3 associated with the IL2RG. JAK1/JAK3 subsequently phosphorylate IL4R itself, as well as STAT6, resulting in STAT6 translocation to the nucleus and transcription of IL4-responsive genes.\r\n\r\nIL4 mediated signalling through the IL4R generates immunity to helminthic infections and enables the inactivation of toxins. \r\n\r\nExpressed in neurons, IL4R plays a key role in modulating neuronal death through STAT6 activation during ischemic attacks. Stimulating microglial phagocytosis, IL4 enables efficient clearance of apoptotic neurons allowing for repair. Systemic administration of IL4 has been shown to reduce ischemic lesions and improves neurologic function after a stroke.","predictedComplex":false,"interactors":[{"ac":"EBI-367009","identifier":"P24394","identifierLink":"https://www.uniprot.org/uniprotkb/P24394/entry","name":"IL4R","description":"Interleukin-4 receptor subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23037","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-367025","identifier":"P05112","identifierLink":"https://www.uniprot.org/uniprotkb/P05112/entry","name":"IL4","description":"Interleukin-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47401","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-80475","identifier":"P31785","identifierLink":"https://www.uniprot.org/uniprotkb/P31785/entry","name":"IL2RG","description":"Cytokine receptor common subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-624","complexName":"Interleukin-4 receptor-ligand type-2 complex","organismName":"Homo sapiens; 9606","description":"Transmembrane complex formed on the binding of extracellular interleukin-4 (IL4) to either a type-1 IL4 receptor composed of IL4R and IL2RG (CPX-8834) or a type-2 IL4 receptor, composed of IL4R and IL13RA1. Ligand binding results in the assembly of the complete complex, which induces signalling mediated principally through the IL4R chain and involves activation of the transcription factor, signal transducer and activator of transcription-6 (STAT6). \r\n\r\nSignalling via the type-2 receptor occurs upon IL4 binding to IL4R first and then recruiting IL13RA1 to form the signalling complex. IL4 binding to IL4RAinduces the phosphorylation of JAK1 and JAK2 associated with IL4R and TYK2 associated with IL13RA1, resulting in STAT6 phosphorylation and translocation to the nucleus and transcription of IL4-responsive genes.\r\n\r\nIL4 mediated signalling through the IL4 receptor generates immunity to helminthic infections and enables the inactivation of toxins. \r\n\r\nExpressed in neurons, IL4R plays a key role in modulating neuronal death through STAT6 activation during ischemic attacks. Stimulating microglial phagocytosis, IL4 enables efficient clearance of apoptotic neurons allowing for repair. Systemic administration of IL4 has been shown to reduce ischemic lesions and improves neurologic function after a stroke.","predictedComplex":false,"interactors":[{"ac":"EBI-1391535","identifier":"P78552","identifierLink":"https://www.uniprot.org/uniprotkb/P78552/entry","name":"IL13RA1","description":"Interleukin-13 receptor subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-367009","identifier":"P24394","identifierLink":"https://www.uniprot.org/uniprotkb/P24394/entry","name":"IL4R","description":"Interleukin-4 receptor subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23037","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-367025","identifier":"P05112","identifierLink":"https://www.uniprot.org/uniprotkb/P05112/entry","name":"IL4","description":"Interleukin-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47401","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-623","complexName":"Interleukin-6-mIL6R-mIL6ST receptor-ligand classical signalling complex","organismName":"Homo sapiens; 9606","description":"Symmetrical 2:2:2 complex formed on the binding of interleukin-6 (IL6) to the IL6 specific alpha receptor (IL6R) and the signal transducing component, IL6ST (glycoprotein 130, gp130). IL6 binds to IL6R with low affinity but the IL6:IL6R dimer binds to IL6ST with high affinity resulting in trimer formation. A hexameric complex is formed upon the interaction between IL6 of one trimer and the D1 domain on site-3 of IL6ST of the other trimer. \r\n\r\nIL6R exists as soluble (sIL6R) and membrane bound mIL6R, and complex formation results in the induction of either a pro-inflammatory trans-signalling pathway (CPX-8967), or a classical anti-inflammatory signalling cascade (CPX-623, this complex) leading to protective and regenerative outcomes, respectively. \r\n\r\nLigand-receptor assembly results in the formation of the complete complex, inducing the transphosphorylation of IL6ST-associated JAK1/2 and TYK2 molecules as well as phosphorylation of the cytoplasmic tails of the IL6ST receptor. Phosphorylated STAT3 dissociates from the receptors, dimerize and translocate into the nucleus where they induce the transcription of IL6 target genes. IL6-induced trans- and classical signalling is indifferent in canonical intracellular JAK-STAT pathway, but trans-signalling is considered to be the more potent of the two. The ratio of mIL6R to IL6ST on a cell's surface decides how trans- and classical signalling are sensed by a cell.\r\n\r\nIL6 is a pleiotropic cytokine involved in regulating inflammatory responses as well as co-ordinating developmental, metabolic and neuronal processes. Plays an essential role in B-cell differentiation and modulation of acute-phase responses. Involved in lymphocyte and monocyte differentiation. Acts on B-cells, T-cells, hepatocytes, hematopoietic progenitor cells and cells of the CNS.  \r\n\r\nDysregulation of the IL6 signalling pathway and in particular JAK1/STAT3 activity is associated with diseases such as Rheumatoid arthritis (RA), inflammatory bowel disease (IBD), and various cancers. The IL6/JAK/STAT3 signalling pathway is aberrantly overactive in patients with chronic inflammatory conditions and in those with haematopoietic malignancies or solid tumours, and targeting components of the IL6/JAK/STAT3 pathway has been shown to inhibit growth of tumour cells and relieve immunosuppression in the tumour microenvironment.","predictedComplex":false,"interactors":[{"ac":"EBI-1030834","identifier":"P40189","identifierLink":"https://www.uniprot.org/uniprotkb/P40189/entry","name":"IL6ST","description":"Interleukin-6 receptor subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52333540","identifier":"P08887-PRO_0000010895","identifierLink":"https://www.uniprot.org/uniprotkb/P08887-PRO_0000010895/entry","name":"IL6R","description":"Interleukin-6 receptor subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-720533","identifier":"P05231","identifierLink":"https://www.uniprot.org/uniprotkb/P05231/entry","name":"IL6","description":"Interleukin-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48494","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8969","complexName":"Interleukin-6 sIL6R-sIL6ST buffering receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Symmetrical 2:2:2 complex formed on the binding of interleukin-6 (IL6) to the IL6 specific alpha receptor (IL6R) and the signal transducing component, IL6ST (glycoprotein 130, gp130). IL6 binds to IL6R with low affinity but the IL6:IL6R dimer binds to IL6ST with high affinity resulting in trimer formation. A hexameric complex is formed upon the interaction between IL6 of one trimer and the D1 domain on site-3 of IL6ST of the other trimer. \r\n\r\nIL6R exists in soluble (sIL6R) and membrane bound (mIL6R) forms, and complex formation results in the induction of either a pro-inflammatory trans-signalling pathway (CPX-8967), or a classical anti-inflammatory signalling cascade (CPX-623) leading to protective and regenerative outcomes, respectively. IL6ST also exists in both soluble (sIL6ST) and membrane bounds forms, but unlike sIL6R, sIL6ST antagonizes IL6 induced signalling. sIL6ST together with sIL6R constitute a buffer system, where the presence of excess sIL6R favours trans-signalling, but an excess of sIL6ST, blocks IL6 induced signalling. \r\n\r\nLigand-receptor assembly results in the formation of the complete complex, inducing the transphosphorylation of IL6ST-associated JAK1/2 and TYK2 molecules as well as phosphorylation of the cytoplasmic tails of the IL6ST receptor. Phosphorylated STAT3 dissociates from the receptors, dimerize and translocate into the nucleus where they induce the transcription of IL6 target genes.\r\n\r\nIL6 is a pleiotropic cytokine involved in regulating inflammatory responses as well as co-ordinating developmental, metabolic and neuronal processes. Plays an essential role in B-cell differentiation and modulation of acute-phase responses. Involved in lymphocyte and monocyte differentiation. Acts on B-cells, T-cells, hepatocytes, hematopoietic progenitor cells and cells of the CNS. \r\n\r\nDysregulation of the IL6 signalling pathway and in particular JAK1/STAT3 activity is associated with diseases such as Rheumatoid arthritis (RA), inflammatory bowel disease (IBD), and various cancers. The IL6/JAK/STAT3 signalling pathway is aberrantly overactive in patients with chronic inflammatory conditions and in those with haematopoietic malignancies or solid tumours, and targeting components of the IL6/JAK/STAT3 pathway has been shown to inhibit growth of tumour cells and relieve immunosuppression in the tumour microenvironment.","predictedComplex":false,"interactors":[{"ac":"EBI-52312520","identifier":"P08887-PRO_0000450730","identifierLink":"https://www.uniprot.org/uniprotkb/P08887-PRO_0000450730/entry","name":"IL6R","description":"Soluble interleukin-6 receptor subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-52333529","identifier":"P40189-2","identifierLink":"https://www.uniprot.org/uniprotkb/P40189-2/entry","name":"IL6ST","description":"Interleukin-6 receptor subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-720533","identifier":"P05231","identifierLink":"https://www.uniprot.org/uniprotkb/P05231/entry","name":"IL6","description":"Interleukin-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48494","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8967","complexName":"Interleukin-6 sIL6R-mIL6ST receptor-ligand trans-signalling complex","organismName":"Homo sapiens; 9606","description":"Symmetrical 2:2:2 complex formed on the binding of interleukin-6 (IL6) to the IL6 specific alpha receptor (IL6R) and the signal transducing component, IL6ST (glycoprotein 130, gp130). IL6 binds to IL6R with low affinity but the IL6:IL6R dimer binds to IL6ST with high affinity resulting in trimer formation. A hexameric complex is formed upon the interaction between IL6 of one trimer and the D1 domain on site-3 of IL6ST of the other trimer. \r\n\r\nIL6R exists in soluble (sIL6R) and membrane bound (mIL6R) forms, and complex formation results in the induction of either a pro-inflammatory trans-signalling pathway (CPX-8967, this complex), or a classical anti-inflammatory signalling cascade (CPX-623) leading to protective and regenerative outcomes, respectively. \r\n\r\nLigand-receptor assembly results in the formation of the complete complex, inducing the transphosphorylation of IL6ST-associated JAK1/2 and TYK2 molecules as well as phosphorylation of the cytoplasmic tails of the IL6ST receptor. Phosphorylated STAT3 dissociates from the receptors, dimerize and translocate into the nucleus where they induce the transcription of IL6 target genes. IL6-induced trans- and classical signalling is indifferent in canonical intracellular JAK-STAT pathway, but trans-signalling is considered to be the more potent of the two. The ratio of mIL6R to IL6ST on a cell's surface decides how trans- and classical signalling are sensed by a cell. \r\n\r\nIL6 is a pleiotropic cytokine involved in regulating inflammatory responses as well as co-ordinating developmental, metabolic and neuronal processes. Plays an essential role in B-cell differentiation and modulation of acute-phase responses. Involved in lymphocyte and monocyte differentiation. Acts on B-cells, T-cells, hepatocytes, hematopoietic progenitor cells and cells of the CNS. Acts to increase the breakdown of fats and improve insulin resistance in its role as a myokine. \r\n\r\nTrans-signalling is considered the primary mechanism through which IL6 signalling promotes tumourigenesis in multiple cancers. Dysregulation of the IL6 signalling pathway and in particular JAK1/STAT3 activity is associated with diseases such as Rheumatoid arthritis (RA), inflammatory bowel disease (IBD), type 2 diabetes and various cancers. The IL6/JAK/STAT3 signalling pathway is aberrantly overactive in patients with chronic inflammatory conditions and in those with haematopoietic malignancies or solid tumours, and targeting components of the IL6/JAK/STAT3 pathway has been shown to inhibit growth of tumour cells and relieve immunosuppression in the tumour microenvironment.","predictedComplex":false,"interactors":[{"ac":"EBI-15742214","identifier":"P40189-1","identifierLink":"https://www.uniprot.org/uniprotkb/P40189-1/entry","name":"IL6ST","description":"Interleukin-6 receptor subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-52312520","identifier":"P08887-PRO_0000450730","identifierLink":"https://www.uniprot.org/uniprotkb/P08887-PRO_0000450730/entry","name":"IL6R","description":"Soluble interleukin-6 receptor subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-720533","identifier":"P05231","identifierLink":"https://www.uniprot.org/uniprotkb/P05231/entry","name":"IL6","description":"Interleukin-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48494","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8968","complexName":"Membrane bound interleukin-6 mIL6R receptor-ligand cluster-signalling complex","organismName":"Homo sapiens; 9606","description":"Symmetrical 2:2:2 complex formed on the binding of interleukin-6 (IL6) to the IL6 specific alpha receptor (IL6R) and the signal transducing component, IL6ST (glycoprotein 130, gp130). IL6 binds to IL6R with low affinity but the IL6:IL6R dimer binds to IL6ST with high affinity resulting in trimer formation. A hexameric complex is formed upon the interaction between IL6 of one trimer and the D1 domain on site-3 of IL6ST of the other trimer. \r\n\r\nIL6R exists in soluble (sIL6R) and membrane bound (mIL6R) forms, and complex formation results in the induction of either a pro-inflammatory trans-signalling pathway (CPX-8967), or a classical anti-inflammatory signalling cascade (CPX-623) leading to protective and regenerative outcomes, respectively. This complex (CPX-8968) is involved in cluster signalling, a third mechanism of IL6 signalling where preformed complexes of membrane-bound IL6-mIL6R on one cell (transmitting cell) activate an IL6ST receptor on another neighbouring cell (receiving cell) to initiate signal transduction. IL6 cluster signalling can be neutralized upon soluble IL6ST binding directly to the IL6-IL6R complex on a transmitting cell.\r\n\r\nLigand-receptor assembly results in the formation of the complete complex, inducing the transphosphorylation of IL6ST-associated JAK1/2 and TYK2 molecules as well as phosphorylation of the cytoplasmic tails of the IL6ST receptor. Phosphorylated STAT3 dissociates from the receptors, dimerize and translocate into the nucleus where they induce the transcription of IL6 target genes. \r\n\r\nIL6 is a pleiotropic cytokine involved in regulating inflammatory responses as well as co-ordinating developmental, metabolic and neuronal processes. Plays an essential role in B-cell differentiation and modulation of acute-phase responses. Involved in lymphocyte and monocyte differentiation. Acts on B-cells, T-cells, hepatocytes, hematopoietic progenitor cells and cells of the CNS. Cluster-signalling mediates the priming of pathogenic T-helper 17 cells. \r\n\r\nDysregulation of the IL6 signalling pathway and in particular JAK1/STAT3 activity is associated with diseases such as Rheumatoid arthritis (RA), inflammatory bowel disease (IBD), and various cancers. The IL6/JAK/STAT3 signalling pathway is aberrantly overactive in patients with chronic inflammatory conditions and in those with haematopoietic malignancies or solid tumours, and targeting components of the IL6/JAK/STAT3 pathway has been shown to inhibit growth of tumour cells and relieve immunosuppression in the tumour microenvironment.","predictedComplex":false,"interactors":[{"ac":"EBI-15742214","identifier":"P40189-1","identifierLink":"https://www.uniprot.org/uniprotkb/P40189-1/entry","name":"IL6ST","description":"Interleukin-6 receptor subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-52338235","identifier":"P05231-PRO_0000015582","identifierLink":"https://www.uniprot.org/uniprotkb/P05231-PRO_0000015582/entry","name":"IL6","description":"Interleukin-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-52338286","identifier":"P08887-1","identifierLink":"https://www.uniprot.org/uniprotkb/P08887-1/entry","name":"IL6R","description":"Interleukin-6 receptor subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-9102","complexName":"Interleukin-7 mIL7R-IL2RG receptor-ligand signalling complex","organismName":"Homo sapiens; 9606","description":"Transmembrane complex formed on the binding of extracellular interleukin-7 (IL7) to its high-affinity receptor, IL7R and the shared IL2RG. Ligand binding results in the assembly of the complete complex, inducing the transphosphorylation of JAK1/JAK3 molecules as well as phosphorylation of the cytoplasmic tails of the receptors. STAT5 (P42229) monomers then bind to the phosphorylated site of the receptor and are phosphorylated by JAK1, while PIK3R associated with survival signalling, interacts with JAK3. Phosphorylated STATs dissociates from the receptors, dimerize and translocate into the nucleus where they induce the transcription of target genes.\r\n\r\nIL7 is a key regulator of immune homeostasis, critical for B cell development, and IL7 signalling is essential for the proliferation and survival of memory and naive T cells, as well as T cell development in the thymus. A potent immunomodulator of tumours, it has both the ability to eradicate tumours but also exert strong pro-tumour effects. \r\n\r\nThere are two major isoforms of IL7R, the membrane-bound IL7R (mIL7R, P16871-1) and an alternatively spliced soluble IL7R (sIL7R, P16871-4) lacking the transmembrane region encoding exon 6 (CPX-493). Competition between mIL7R and sIL7R, which binds IL7 with greater affinity, diminishes STAT5 phosphorylation and therefore excessive signalling but increases overall bioavailability of the limited resource IL7. \r\n\r\nIL7 signalling contributes to autoimmunity and has been implicated as a cofactor in multiple sclerosis, autoimmune-related colitis, diabetes and lupus. IL7R associated insertion/deletion mutations have been linked to Philadelphia chromosome-like acute lymphoblastic leukemia (Ph-like ALL), a high-risk sub-type of B-ALL, as well as T-ALL.","predictedComplex":false,"interactors":[{"ac":"EBI-52368501","identifier":"P13232-PRO_0000015623","identifierLink":"https://www.uniprot.org/uniprotkb/P13232-PRO_0000015623/entry","name":"IL7","description":"Interleukin-7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-52368614","identifier":"P16871-1","identifierLink":"https://www.uniprot.org/uniprotkb/P16871-1/entry","name":"IL7R","description":"Interleukin-7 receptor subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-80475","identifier":"P31785","identifierLink":"https://www.uniprot.org/uniprotkb/P31785/entry","name":"IL2RG","description":"Cytokine receptor common subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-493","complexName":"Interleukin-7 sIL7RA-IL2RG receptor-ligand potentiating complex","organismName":"Homo sapiens; 9606","description":"Complex formed on the binding of extracellular interleukin-7 (IL7) to its receptor composed of a soluble form of IL7R (sIL7R) and the shared IL2RG. \r\n\r\nIL7 is expressed in lymphoid as well as in non-lymphoid sites, and is a key regulator of immune homeostasis. IL7 is critical for B cell development, and tonic IL7 signalling is essential for the proliferation and survival of memory and naive T cells, as well as T cell development in the thymus. A potent immunomodulator of tumours, it has both the ability to eradicate tumours but also exert strong pro-tumour effects. \r\n\r\nThere are two major isoforms of IL7R, the membrane-bound IL7R (mIL-7R, p16871-1, CPX-9102) and an alternatively spliced sIL7R lacking the transmembrane region encoding exon 6 (p16871-4). sIL7R circulates at a high molar excess compared with IL7 in healthy humans and binds IL7 with moderate affinity to diminish the availability of free IL7. The competition diminishes STAT5 phosphorylation and therefore excessive signalling but increases overall bioavailability of the limited resource IL7. \r\n\r\nIL7 signalling contributes to autoimmunity and has been implicated as a cofactor in multiple sclerosis, autoimmune colitis autoimmune diabetes and lupus. Individuals with a predisposing IL7R genotype have increased rates of IL7R mRNA splicing resulting in elevated levels of sIL7R and are thought to be at increased risk of autoimmune disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-52368501","identifier":"P13232-PRO_0000015623","identifierLink":"https://www.uniprot.org/uniprotkb/P13232-PRO_0000015623/entry","name":"IL7","description":"Interleukin-7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-52368513","identifier":"P16871-4","identifierLink":"https://www.uniprot.org/uniprotkb/P16871-4/entry","name":"IL7R","description":"Interleukin-7 receptor subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-80475","identifier":"P31785","identifierLink":"https://www.uniprot.org/uniprotkb/P31785/entry","name":"IL2RG","description":"Cytokine receptor common subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-742","complexName":"Interleukin-10 receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Interleukin-10, a pleiotropic cytokine with a role in promoting both anti-inflammatory and pro-inflammatory responses, exerts its function upon binding to its receptor complex, IL10R. Secreted as a homodimer, IL10 activates signaling in receiver cells by engaging two copies of a heterodimeric receptor complex consisting of a high-affinity, IL10 specific receptor subunit, IL10RA, and a low-affinity, shared receptor subunit, IL10RB. IL10RB is essential for signal transduction and is a common receptor for IFNG (P01579) and other IL10 family members including IL22, IL26, IFNL1, IFNL2 and IFNL3. \r\n\r\nIL10 drives the dimerization of IL10RA and IL10RB, resulting in the transphosphorylation of members of the JAK family of tyrosine-protein kinases as well as phosphorylation of the cytoplasmic tails of the receptors and activation of the transcription factor signal transducer and activator of transcription STAT3 and to a slightly lesser extent STAT1, which mediate the diverse functional effects of IL10.\r\n\r\nThe limiting factor for IL10 signaling is the formation of the ternary IL10-IL10RA-IL10RB complex, thought to be influenced both by the affinity of the IL10-IL10RB interaction, as well as the quantity of IL10RB on the cell surface.","predictedComplex":false,"interactors":[{"ac":"EBI-1031632","identifier":"P22301","identifierLink":"https://www.uniprot.org/uniprotkb/P22301/entry","name":"IL10","description":"Interleukin-10","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48482","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1031656","identifier":"Q13651","identifierLink":"https://www.uniprot.org/uniprotkb/Q13651/entry","name":"IL10RA","description":"Interleukin-10 receptor subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11175900","identifier":"Q08334","identifierLink":"https://www.uniprot.org/uniprotkb/Q08334/entry","name":"IL10RB","description":"Interleukin-10 receptor subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8932","complexName":"mTNF-TNR1A receptor-ligand core complex, BIRC2 variant","organismName":"Homo sapiens; 9606","description":"A membrane-bound tumour necrosis factor-receptor signalling complex (Complex I) formed on the binding of the membrane-bound form of the pro-inflammatory cytokine, tumour necrosis factor (mTNF, CPX-8931). This activates the mitogen-activated protein kinase  and nuclear factor-kappa-B (NF-kappa-B) signalling pathways, leading to proinflammatory gene expression and promoting cell survival. The Ripoptosome (CPX-1907, Complex II) originates from the dissociation of Complex I components from the receptor and promotes cell apoptosis. \r\n\r\nTNF, a key regulator of T regulatory cells, is mainly secreted by macrophages, T helper 1 and natural killer cells, while its receptor component TNFRSF1A is ubiquitously expressed on almost all human tissues.\r\n\r\nIntracellular signaling is triggered by ligand-bound receptors assembling into higher-order clusters. Soluble TNFA triggers more robust clustering of TNFR1 than membrane-bound ligand. TNFR1-mediated signaling is therefore generally caused by the activation due to sTNFA over mTNFA. TNFA-TNFRSF1A signalling complex formation is indirectly influenced by TNFA-TNFRSF1B activation and the cross-talk between the receptor complexes is central to cell-survival, proliferation or death.","predictedComplex":false,"interactors":[{"ac":"EBI-355744","identifier":"Q12933","identifierLink":"https://www.uniprot.org/uniprotkb/Q12933/entry","name":"TRAF2","description":"TNF receptor-associated factor 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358507","identifier":"Q13546","identifierLink":"https://www.uniprot.org/uniprotkb/Q13546/entry","name":"RIPK1","description":"Receptor-interacting serine/threonine-protein kinase 1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44329","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359215","identifier":"Q15628","identifierLink":"https://www.uniprot.org/uniprotkb/Q15628/entry","name":"TRADD","description":"Tumor necrosis factor receptor type 1-associated DEATH domain protein","stochiometry":"minValue: 3, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14913","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-514538","identifier":"Q13490","identifierLink":"https://www.uniprot.org/uniprotkb/Q13490/entry","name":"BIRC2","description":"Baculoviral IAP repeat-containing protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52219099","identifier":"P19438-PRO_0000034543","identifierLink":"https://www.uniprot.org/uniprotkb/P19438-PRO_0000034543/entry","name":"TNFRSF1A","description":"Tumor necrosis factor receptor superfamily member 1A, membrane form","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-52222100","identifier":"CPX-8931","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-8931","name":"Transmembrane tumor necrosis factor complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-523498","identifier":"O00463","identifierLink":"https://www.uniprot.org/uniprotkb/O00463/entry","name":"TRAF5","description":"TNF receptor-associated factor 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-25723","complexName":"sTNF-TNR1A receptor-ligand core complex, BIRC3 variant","organismName":"Homo sapiens; 9606","description":"A membrane-bound tumor necrosis factor-receptor signaling complex (Complex I) formed on the binding of the soluble form of the pro-inflammatory cytokine, tumour necrosis factor (sTNF, CPX-8826). This activates the mitogen-activated protein kinase  and nuclear factor-kappa-B (NF-kappa-B) signalling pathways, leading to proinflammatory gene expression and promoting cell survival. The Ripoptosome (CPX-1907, Complex II) originates from the dissociation of Complex I components from the receptor and promotes cell apoptosis. \r\n\r\nTNF, a key regulator of T regulatory cells, is mainly secreted by macrophages, T helper 1 and natural killer cells, while its receptor component TNFRSF1A is ubiquitously expressed on almost all human tissues.\r\n\r\nIntracellular signaling is triggered by ligand-bound receptors assembling into higher-order clusters. Soluble TNFA triggers more robust clustering of TNFR1 than membrane-bound ligand. TNFR1-mediated signaling is therefore generally caused by the activation due to sTNFA over mTNFA. TNFA-TNFRSF1A signalling complex formation is indirectly influenced by TNFA-TNFRSF1B activation and the cross-talk between the receptor complexes is central to cell-survival, proliferation or death.","predictedComplex":false,"interactors":[{"ac":"EBI-355744","identifier":"Q12933","identifierLink":"https://www.uniprot.org/uniprotkb/Q12933/entry","name":"TRAF2","description":"TNF receptor-associated factor 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358507","identifier":"Q13546","identifierLink":"https://www.uniprot.org/uniprotkb/Q13546/entry","name":"RIPK1","description":"Receptor-interacting serine/threonine-protein kinase 1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44329","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-359215","identifier":"Q15628","identifierLink":"https://www.uniprot.org/uniprotkb/Q15628/entry","name":"TRADD","description":"Tumor necrosis factor receptor type 1-associated DEATH domain protein","stochiometry":"minValue: 3, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14913","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-50431755","identifier":"CPX-8826","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-8826","name":"Soluble tumor necrosis factor complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-517709","identifier":"Q13489","identifierLink":"https://www.uniprot.org/uniprotkb/Q13489/entry","name":"BIRC3","description":"Baculoviral IAP repeat-containing protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52219099","identifier":"P19438-PRO_0000034543","identifierLink":"https://www.uniprot.org/uniprotkb/P19438-PRO_0000034543/entry","name":"TNFRSF1A","description":"Tumor necrosis factor receptor superfamily member 1A, membrane form","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-523498","identifier":"O00463","identifierLink":"https://www.uniprot.org/uniprotkb/O00463/entry","name":"TRAF5","description":"TNF receptor-associated factor 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9601","complexName":"CXCL8-CXCR1 receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Chemotactic receptor complex involved in neutrophil activation. CXCL8 is a member of the ELR+ CXC subfamily of chemokines known to activate neutrophils and dimerise under physiological conditions. CXCL8 mediates its effects through binding to its G-protein coupled receptors, CXCR1 (this complex) and CXCR2 (CPX-9821). \r\n\r\nCXCL8 is secreted by cells at sites of injury and infection to trigger a transient increase in cytosolic calcium in neutrophils via a GTP-binding protein and chemotaxis through both CXCR1 and CXCR2, but only CXCR1 can mediate phospholipase D activation and respiratory burst.","predictedComplex":false,"interactors":[{"ac":"EBI-3905522","identifier":"P25024","identifierLink":"https://www.uniprot.org/uniprotkb/P25024/entry","name":"CXCR1","description":"C-X-C chemokine receptor type 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10489","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3917999","identifier":"P10145","identifierLink":"https://www.uniprot.org/uniprotkb/P10145/entry","name":"CXCL8","description":"Interleukin-8","stochiometry":"minValue: 1, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12015","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9821","complexName":"CXCL8-CXCR2 receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Chemotactic receptor complex involved in neutrophil activation. CXCL8 is a member of the ELR+ CXC subfamily of chemokines known to activate neutrophils and dimerise under physiological conditions. CXCL8 mediates its effects through binding to its G-protein coupled receptors, CXCR1 (CPX-9601) and CXCR2 (this complex).\r\n\r\nCXCL8 is secreted by cells at sites of injury and infection to trigger a transient increase in cytosolic calcium in neutrophils via a GTP-binding protein and chemotaxis through both CXCR1 and CXCR2, but only CXCR1 can mediate phospholipase D activation and respiratory burst.","predictedComplex":false,"interactors":[{"ac":"EBI-2835281","identifier":"P25025","identifierLink":"https://www.uniprot.org/uniprotkb/P25025/entry","name":"CXCR2","description":"C-X-C chemokine receptor type 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10489","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3917999","identifier":"P10145","identifierLink":"https://www.uniprot.org/uniprotkb/P10145/entry","name":"CXCL8","description":"Interleukin-8","stochiometry":"minValue: 1, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12015","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9781","complexName":"Interleukin 11-mIL11RA-IL-6ST receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Cytokine-receptor complex. IL11 binds to a membrane-bound form of its specific receptor component, mIL11RA and recruits the ubiquitously expressed IL6ST to activate signalling via IL6ST's Tyr-759 initiating either the apoptotic MAPK (ERK) pathway, or to a lesser extent, the pro-survival STAT3 pathway.\r\n\r\nIL11 is produced by fibroblasts and epithelial cells in addition to various immune cell types. It is classically-associated with a  regenerative role in megakaryocytopoiesis but has also been critically implicated in the tumourigenesis of gastrointestinal and epithelial cancers.\r\n\r\nIL11 is thought to be a contributor in driving the pathogenesis of autoimmune inflammatory diseases such as rheumatoid arthiritis and multiple sclerosis as well as chronic inflammatory conditions such as asthma.","predictedComplex":false,"interactors":[{"ac":"EBI-1030834","identifier":"P40189","identifierLink":"https://www.uniprot.org/uniprotkb/P40189/entry","name":"IL6ST","description":"Interleukin-6 receptor subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55034476","identifier":"Q14626-PRO_0000010913","identifierLink":"https://www.uniprot.org/uniprotkb/Q14626-PRO_0000010913/entry","name":"IL11RA","description":"Interleukin-11 receptor subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-751694","identifier":"P20809","identifierLink":"https://www.uniprot.org/uniprotkb/P20809/entry","name":"IL11","description":"Interleukin-11","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16922","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-9721","complexName":"Interleukin 11-sIL11RA-IL-6ST receptor-ligand trans-signalling complex","organismName":"Homo sapiens; 9606","description":"Trans-signalling cytokine-receptor complex that acts as an agonist to induce signalling in cells that do not express membrane-bound IL11RA (mIL11RA). IL11 binds to a soluble form of its specific receptor component, sIL11RA and recruits the ubiquitously expressed IL6ST to activate signalling via IL6ST's tyrosine residue Tyr-759 initiating the apoptotic MAPK (ERK) pathway, or to a lesser extent, the pro-survival STAT3 pathway. sIL11RA is formed either by proteolysis of mIL11RA by ADAM10 (O14672) at Arginine 355, or directly secreted from cells after alternative mRNA splicing.\r\n\r\nIL11 is produced by fibroblasts and epithelial cells in addition to various immune cell types. It is classically-associated with a regenerative role in megakaryocytopoiesis but has also been critically implicated in the tumourigenesis of gastrointestinal and epithelial cancers. The exact role of IL11 mediated trans-signalling is yet to be elucidated but it is thought that IL11 trans-signalling may drive disease conditions.","predictedComplex":false,"interactors":[{"ac":"EBI-1030834","identifier":"P40189","identifierLink":"https://www.uniprot.org/uniprotkb/P40189/entry","name":"IL6ST","description":"Interleukin-6 receptor subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-55034297","identifier":"Q14626-PRO_0000450688","identifierLink":"https://www.uniprot.org/uniprotkb/Q14626-PRO_0000450688/entry","name":"IL11RA","description":"Soluble interleukin-11 receptor subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-751694","identifier":"P20809","identifierLink":"https://www.uniprot.org/uniprotkb/P20809/entry","name":"IL11","description":"Interleukin-11","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16922","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-844","complexName":"Interleukin-13 receptor-ligand alpha 1 complex","organismName":"Homo sapiens; 9606","description":"Transmembrane type 2 receptor complex. Ligand binding first to IL13RA1 followed by IL4R results in the assembly of the complete complex, inducing the transphosphorylation of  TYK2 (P29597) and/or members of the JAK family of tyrosine-protein kinases as well as phosphorylation of the cytoplasmic tails of the receptors. STAT6 (P42226) monomers bind to the phosphorylated site of the receptor and are phosphorylated by JAK1/TYK2. Phosphorylated STAT6 dissociates from the receptors, dimerizes and translocates into the nucleus where it induces the transcription of target genes. IL13 also binds IL13RA2 (CPX-847) with high affinity to inhibit response to IL13 through the IL13RA1-IL4R heterodimer.\r\n\r\nA pleiotropic cytokine produced by many hematopoietic and non-hematopoietic cell types, IL13, is associated with Type 2 diseases and has been shown to be important in the pathogenesis of asthma, allergy and other eosinophilic disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-1391535","identifier":"P78552","identifierLink":"https://www.uniprot.org/uniprotkb/P78552/entry","name":"IL13RA1","description":"Interleukin-13 receptor subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1647828","identifier":"P35225","identifierLink":"https://www.uniprot.org/uniprotkb/P35225/entry","name":"IL13","description":"Interleukin-13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48486","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-367009","identifier":"P24394","identifierLink":"https://www.uniprot.org/uniprotkb/P24394/entry","name":"IL4R","description":"Interleukin-4 receptor subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23037","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-627","complexName":"Interleukin-15 receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Transmembrane complex formed on the binding of extracellular interleukin-15 (IL15) to its receptor (IL15R). IL15 binding to the unique high affinity IL15RA and the shared IL2RB and IL2RG subunits results in the assembly of the complete complex, inducing activation of Janus kinases, JAK1 and JAK3, resulting in the phosphorylation of STAT3 via IL2RB and of STAT5 via IL2RG. This causes activation of PI3K/Akt/mTOR and Ras/Raf/MAPK signaling cascades, resulting in an anti-apoptotic program. Other signalling pathways include, PDGFR and IL15/Akt/XBP1 to mediate Natural Killer (NK) cell survival, and the trans-endocytosis of the membrane-associated IL15-IL15RA complex into NK cells, leading to the activation of STAT5 and subsequent induction of proliferation and survival signals.\r\n\r\nIL15 is a pleiotropic cytokine expressed constitutively by monocytes, macrophages, dendritic cells (DCs), keratinocytes, epidermal skin cells, fibroblasts, various epithelial cells, bone marrow stromal cells, and nerve cells. \r\n\r\nIL15 binding to IL15R mediates signalling activities including the proliferation of Natural Killer (NK) cells, NK-T cells, CD8+ cytotoxic T cells, memory-T cells, intestinal intraepithelial lymphocytes and large granular lymphocytes. \r\n\r\nThought to have a role in respiratory diseases such as sarcoidosis and tuberculosis through its role in Th1-driven-inflammation, IL15 also negatively regulates apoptosis and its anti-tumour potential makes it an attractive target for cancer immunotherapy.","predictedComplex":false,"interactors":[{"ac":"EBI-2866779","identifier":"P14784","identifierLink":"https://www.uniprot.org/uniprotkb/P14784/entry","name":"IL2RB","description":"Interleukin-2 receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23037","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-80475","identifier":"P31785","identifierLink":"https://www.uniprot.org/uniprotkb/P31785/entry","name":"IL2RG","description":"Cytokine receptor common subunit gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-980274","identifier":"P40933","identifierLink":"https://www.uniprot.org/uniprotkb/P40933/entry","name":"IL15","description":"Interleukin-15","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14356","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-980354","identifier":"Q13261","identifierLink":"https://www.uniprot.org/uniprotkb/Q13261/entry","name":"IL15RA","description":"Interleukin-15 receptor subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15060","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2805","complexName":"sTNF:TNR1B receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Complex formed on the binding of the soluble form of the pro-inflammatory cytokine, Tumour necrosis factor alpha (sTNFa, CPX-8826) to its type-2 receptor (TNFRSF1B, P20333). \r\n\r\nTNF, a key regulator of T regulatory cells, is mainly secreted by macrophages, T helper 1 and natural killer cells, and while TNFRSF1A (P19438) is ubiquitously expressed, TNFRSF1B is mainly expressed by immune cells, neurons and endothelial cells.\r\n\r\nTNFRSF1B is similar in its extracellular structure to TNFRSF1A at the mTNF (transmembrane TNF, CPX-8931) and sTNF binding sites, but it lacks the death domain (DD) found in TNFRSF1A that is central to its intracellular signalling activities. Instead, TNFRSF1B holds a TNF receptor associated factor (TRAF) binding site, allowing it to interact directly with TRAF2 and TRAF1 or TRAF3. Lacking the DD, TNFRSF1B cannot trigger cell death, instead uses TRAF to activate the NF-KB and MAPK signalling cascade, most frequently resulting in cell proliferation and survival.\r\n\r\nsTNF is relatively poor at activating TNFRSF1B but complex formation between mTNF and TNFRSF1B can induce reverse signalling where TNFRSF1B binding mTNF results in phosphorylation within the ligand-bearing cell, resulting in triggering the NF-KB signalling cascade.\r\n\r\nTNF-TNFRSF1B activation indirectly influences the formation of TNF-TNFRSF1A signalling complexes and the cross-talk between the receptor complexes is central to cell-survival, proliferation or death.","predictedComplex":false,"interactors":[{"ac":"EBI-2905409","identifier":"P01375-PRO_0000034424","identifierLink":"https://www.uniprot.org/uniprotkb/P01375-PRO_0000034424/entry","name":"TNF","description":"Tumor necrosis factor, soluble form","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-52222339","identifier":"P20333-PRO_0000034548","identifierLink":"https://www.uniprot.org/uniprotkb/P20333-PRO_0000034548/entry","name":"TNFRSF1B","description":"Tumor necrosis factor receptor superfamily member 1b, membrane form","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-10221","complexName":"Interleukin-19 receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Cytokine receptor complex that polarizes adaptive immunity to promote an anti-inflammatory phenotype. IL19 binding to its receptor complex, IL20RA-IL20RB initiates downstream signalling mediated by JAK1, Tyk2 and STAT3  (P40763) phosphorylation. IL19 inhibits IFNG (P01579) production by down-regulating antigen presenting capacity and enhancing M2 macrophage polarization to promote T helper 2 (Th2) cell differentiation through IL4 (P05112) and IL13 (P35225) up-regulation and suppression of Th1 and Th17 cell differentiation.\r\n\r\nThe bioactive complex is formed through crosstalk between IL19 cytokine producing immune cells and receptor complex expressing epthelial cells and in particular, vascular cells, in which it is thought to exhibit vasculo-protective effects. IL19 exerts contrasting effects on immunity wherein it exerts anti-inflammatory effects to hamper hyperactivation of innate and acquired immunity in inflammatory bowel disease (IBD) but exacerbates disease by a positive feedback loop in the case of asthma.","predictedComplex":false,"interactors":[{"ac":"EBI-14022792","identifier":"Q6UXL0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6UXL0/entry","name":"IL20RB","description":"Interleukin-20 receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14023330","identifier":"Q9UHD0-PRO_0000015379","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UHD0-PRO_0000015379/entry","name":"IL19","description":"Interleukin-19","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2933034","identifier":"Q9UHF4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UHF4/entry","name":"IL20RA","description":"Interleukin-20 receptor subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-10241","complexName":"Interleukin-20 receptor-ligand Type 1 complex","organismName":"Homo sapiens; 9606","description":"Pleiotropic cytokine-receptor complex which plays a role in regulating tissue inflammation, angiogenesis, hemopoiesis, and epidermal cell and keratinocyte differentiation The bioactive complex is formed through crosstalk between IL20 cytokine producing immune cells and receptor complex expressing epthelial cells. Complex formation results in the transphosphorylation of JAK1 and TYK2, which in turn leads to the phosphorylation and activation of transcription factors STAT3 which subsequently translocates into the nucleus where it induces the transcription of target genes.\r\n\r\nDysregulation of IL20-mediated signalling is implicated in the pathophysiology of psoriasis, rheumatoid arthritis and atherosclerosis. IL20's arteriogenic and angiogenic properties may be important in treating ischemic disease.","predictedComplex":false,"interactors":[{"ac":"EBI-14022752","identifier":"Q9NYY1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NYY1/entry","name":"IL20","description":"Interleukin-20","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48482","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14022792","identifier":"Q6UXL0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6UXL0/entry","name":"IL20RB","description":"Interleukin-20 receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2933034","identifier":"Q9UHF4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UHF4/entry","name":"IL20RA","description":"Interleukin-20 receptor subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8933","complexName":"mTNF-TNR1B receptor-ligand core complex, BIRC2 variant","organismName":"Homo sapiens; 9606","description":"A membrane-bound tumor necrosis factor-receptor signaling complex formed on the binding of the membrane-bound form of the pro-inflammatory cytokine, tumour necrosis factor (mTNF, CPX-8931). TNFRSF1B is similar in its extracellular structure to TNFRSF1A (P19438) at the mTNF and sTNF binding sites, but it lacks the death domain found in TNFRSF1A. Instead, TNFRSF1B containss a TNF receptor associated factor (TRAF) binding site. mNF-stimulated  TNFRSF1B complexes recruit TRAF2-BIRC2/3, reducing their availability for triggering MAP3K14/NIK (Q99558) degradation. As a result, NIK accumulates and drives NF-kappa-B signaling. Aggregation of the TNF-TNFR2 complexes brings two or more TRAF2-BIRC2/3 complexes into proximity, enabling BIRC2/3 transactivation of their E3 ligase activity resulting in Lys-63-ubiquitination of TRAF2. This generates docking sites for classical NF-kappa-B signaling-stimulating kinases. \r\nTNFA is a key regulator of T regulatory cells, mainly secreted by macrophages, T helper 1 and natural killer cells, and while TNFRSF1A (P19438) is ubiquitously expressed, TNFRSF1B is mainly expressed by immune cells, neurons and endothelial cells.","predictedComplex":false,"interactors":[{"ac":"EBI-355744","identifier":"Q12933","identifierLink":"https://www.uniprot.org/uniprotkb/Q12933/entry","name":"TRAF2","description":"TNF receptor-associated factor 2","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-514538","identifier":"Q13490","identifierLink":"https://www.uniprot.org/uniprotkb/Q13490/entry","name":"BIRC2","description":"Baculoviral IAP repeat-containing protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10044","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-52222100","identifier":"CPX-8931","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-8931","name":"Transmembrane tumor necrosis factor complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-52222339","identifier":"P20333-PRO_0000034548","identifierLink":"https://www.uniprot.org/uniprotkb/P20333-PRO_0000034548/entry","name":"TNFRSF1B","description":"Tumor necrosis factor receptor superfamily member 1b, membrane form","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-26505","complexName":"Fatty-acyl-CoA synthase","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. Consists of a multifunctional enzyme composed of two non-identical alpha and beta subunits which are organized in an alpha6beta6 complex with 6 sites of fatty acid synthesis. The alpha subunit, FAS2, contains domains for acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. The beta subunit, FAS 1, contains domains for [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase.","predictedComplex":false,"interactors":[{"ac":"EBI-2105971","identifier":"Q10289","identifierLink":"https://www.uniprot.org/uniprotkb/Q10289/entry","name":"fas2","description":"Fatty acid synthase subunit alpha","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10982","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64040153","identifier":"Q9UUG0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UUG0/entry","name":"fas1","description":"Fatty acid synthase subunit beta","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10982","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26506","complexName":"Minor Spliceosomal Pre-B complex","organismName":"Homo sapiens; 9606","description":"Precursor pre-catalytic Minor spliceosome (pre-B) complex. The Minor spliceosome catalyses the removal of an atypical (U12) class of eukaryotic precursor-mRNA (pre-mRNA) introns and is thought to excise approximately 1 in 300 introns in human pre-mRNA. U12 introns constitute roughly 0.5% of all introns, and are recognizable by their non-consensus AT-AC termini as well as a high degree of conservation at the 5' splice site. U12-dependent introns are thought to be evolutionarily ancient but absent in many species including model organisms such as Caenorhabditis elegans and Saccharomyces cerevisiae. \r\n\r\nThe minor spliceosome contains several specific low-abundance snRNPs, including U11, U12, U4atac, U6atac and the common U5 snRNP also present in the major spliceosome. U12-type intron containing genes are mainly related to information processing functions, including DNA replication and repair, transcription, RNA processing, and translation, but can also be found in genes related to cytoskeletal organization, vesicular transport, and voltage-gated ion channel activity.","predictedComplex":false,"interactors":[{"ac":"EBI-10309345","identifier":"Q9NX01","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NX01/entry","name":"TXNL4B","description":"Thioredoxin-like protein 4B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12052","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1044822","identifier":"Q53GS9","identifierLink":"https://www.uniprot.org/uniprotkb/Q53GS9/entry","name":"USP39","description":"Ubiquitin carboxyl-terminal hydrolase 39","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21646","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1045395","identifier":"O75643","identifierLink":"https://www.uniprot.org/uniprotkb/O75643/entry","name":"SNRNP200","description":"U5 small nuclear ribonucleoprotein 200 kDa helicase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24075","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11028020","identifier":"Q86UT8","identifierLink":"https://www.uniprot.org/uniprotkb/Q86UT8/entry","name":"CENATAC","description":"Centrosomal AT-AC splicing factor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31198","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1567797","identifier":"Q8WWY3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WWY3/entry","name":"PRPF31","description":"U4/U6 small nuclear ribonucleoprotein Prp31","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13904","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16411676","identifier":"URS000075ADBA_9606","identifierLink":"http://rnacentral.org/rna/URS000075ADBA_9606","name":"rnu4atac","description":"U4atac small nuclear RNA (U12-dependent splicing)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small nuclear rna","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-27124791","identifier":"URS0000631BD4_9606","identifierLink":"http://rnacentral.org/rna/URS0000631BD4_9606","name":"u5_human_snrna","description":"U5 spliceosomal RNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small nuclear rna","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2876632","identifier":"Q6IEG0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6IEG0/entry","name":"SNRNP48","description":"U11/U12 small nuclear ribonucleoprotein 48 kDa protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21402","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-297993","identifier":"P62316","identifierLink":"https://www.uniprot.org/uniprotkb/P62316/entry","name":"SNRPD2","description":"Small nuclear ribonucleoprotein Sm D2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12777","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348082","identifier":"P62304","identifierLink":"https://www.uniprot.org/uniprotkb/P62304/entry","name":"SNRPE","description":"Small nuclear ribonucleoprotein E","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11193","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356900","identifier":"P62306","identifierLink":"https://www.uniprot.org/uniprotkb/P62306/entry","name":"SNRPF","description":"Small nuclear ribonucleoprotein F","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357897","identifier":"Q15029","identifierLink":"https://www.uniprot.org/uniprotkb/Q15029/entry","name":"EFTUD2","description":"116 kDa U5 small nuclear ribonucleoprotein component","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR42908","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372177","identifier":"P62314","identifierLink":"https://www.uniprot.org/uniprotkb/P62314/entry","name":"SNRPD1","description":"Small nuclear ribonucleoprotein Sm D1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372458","identifier":"P14678","identifierLink":"https://www.uniprot.org/uniprotkb/P14678/entry","name":"SNRPB","description":"Small nuclear ribonucleoprotein-associated proteins B and B'","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372789","identifier":"P62318","identifierLink":"https://www.uniprot.org/uniprotkb/P62318/entry","name":"SNRPD3","description":"Small nuclear ribonucleoprotein Sm D3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395940","identifier":"Q13523","identifierLink":"https://www.uniprot.org/uniprotkb/Q13523/entry","name":"PRP4K","description":"Serine/threonine-protein kinase PRP4 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24056","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-536755","identifier":"O94906","identifierLink":"https://www.uniprot.org/uniprotkb/O94906/entry","name":"PRPF6","description":"Pre-mRNA-processing factor 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11246","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-538479","identifier":"Q6P2Q9","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P2Q9/entry","name":"PRPF8","description":"Pre-mRNA-processing-splicing factor 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11140","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-538492","identifier":"Q96DI7","identifierLink":"https://www.uniprot.org/uniprotkb/Q96DI7/entry","name":"SNRNP40","description":"U5 small nuclear ribonucleoprotein 40 kDa protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44006","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-540096","identifier":"Q9BUQ8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BUQ8/entry","name":"DDX23","description":"Probable ATP-dependent RNA helicase DDX23","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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The SIN is a signaling network consisting of a GTPase and a cascade of kinases assembled at the spindle pole body which promotes cytokinetic ring function and stability.","predictedComplex":false,"interactors":[{"ac":"EBI-1542434","identifier":"O74388","identifierLink":"https://www.uniprot.org/uniprotkb/O74388/entry","name":"ynvd","description":"Uncharacterized protein C3H7.13","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-16132377","identifier":"Q9UT08","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UT08/entry","name":"paa1","description":"Protein phosphatase PP2A regulatory subunit A","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64041636","identifier":"O13665","identifierLink":"https://www.uniprot.org/uniprotkb/O13665/entry","name":"far11","description":"Factor arrest protein 11","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64041655","identifier":"Q10298","identifierLink":"https://www.uniprot.org/uniprotkb/Q10298/entry","name":"yd44","description":"Putative serine/threonine-protein phosphatase C22H10.04","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64041679","identifier":"O14043","identifierLink":"https://www.uniprot.org/uniprotkb/O14043/entry","name":"yeya","description":"Uncharacterized protein C2C4.10c","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-64041690","identifier":"O94560","identifierLink":"https://www.uniprot.org/uniprotkb/O94560/entry","name":"ygd1","description":"Uncharacterized WD repeat-containing protein C1773.01","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15653","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26509","complexName":"Minor Spliceosomal B-act complex","organismName":"Homo sapiens; 9606","description":"Catalytically activated Minor spliceosome (B-act) complex. 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-2","xrefs":[]},{"ac":"EBI-61277930","identifier":"CPX-26447","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-26447","name":"Retention and splicing complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-624585","identifier":"P62308","identifierLink":"https://www.uniprot.org/uniprotkb/P62308/entry","name":"SNRPG","description":"Small nuclear ribonucleoprotein G","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-632715","identifier":"Q13573","identifierLink":"https://www.uniprot.org/uniprotkb/Q13573/entry","name":"SNW1","description":"SNW domain-containing protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12096","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-63983305","identifier":"URS00006ECA78_9606","identifierLink":"http://rnacentral.org/rna/URS00006ECA78_9606","name":"rna, u12 small nuclear (rnu12)","description":"Homo sapiens (human) RNA, U12 small nuclear (RNU12)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small nuclear rna","organismName":"Homo sapiens; 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284812","xrefs":[{"identifier":"PTHR22599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1563447","identifier":"Q09898","identifierLink":"https://www.uniprot.org/uniprotkb/Q09898/entry","name":"sid2","description":"Serine/threonine-protein kinase sid2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR24356","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26511","complexName":"Protein geranylgeranyltransferase type III complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the transfer of a 20-hydrocarbon geranyl-geranyl moiety from a geranyl-geranyl pyrophosphate to a protein having the C-terminal sequence -XXCC, -XCXC and -CCXX , where both cysteines may become modified. Transfers a geranylgeranyl group to mono-farnesylated YKT6 (O15498), generating doubly prenylated YKT6 ensuring the assembly of the Golgi SNARE complex.","predictedComplex":false,"interactors":[{"ac":"EBI-2860334","identifier":"Q7Z6K3","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z6K3/entry","name":"PTAR1","description":"Protein prenyltransferase alpha subunit repeat-containing protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11129","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-536715","identifier":"P53611","identifierLink":"https://www.uniprot.org/uniprotkb/P53611/entry","name":"RABGGTB","description":"Geranylgeranyl transferase type-2 subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11774","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26512","complexName":"TORC1 serine/threonine protein kinase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 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284812","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2014333","identifier":"Q9HDW0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HDW0/entry","name":"toc1","description":"Target of rapamycin complex 1 subunit toc1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-2014341","identifier":"O74428","identifierLink":"https://www.uniprot.org/uniprotkb/O74428/entry","name":"tco89","description":"Target of rapamycin complex 1 subunit tco89","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-2014352","identifier":"P87141","identifierLink":"https://www.uniprot.org/uniprotkb/P87141/entry","name":"mip1","description":"Target of rapamycin complex 1 subunit mip1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12848","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26513","complexName":"TORC2 serine/threonine protein kinase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Serine/threonine-protein kinase signalling complex required for responses to starvation and stress conditions.","predictedComplex":false,"interactors":[{"ac":"EBI-1186105","identifier":"Q9P7Y9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P7Y9/entry","name":"sin1","description":"Target of rapamycin complex 2 subunit sin1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13335","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1564139","identifier":"O74184","identifierLink":"https://www.uniprot.org/uniprotkb/O74184/entry","name":"pop3","description":"Target of rapamycin complex subunit wat1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR19842","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2014420","identifier":"O14356","identifierLink":"https://www.uniprot.org/uniprotkb/O14356/entry","name":"tor1","description":"Serine/threonine-protein kinase tor1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2014448","identifier":"O74547","identifierLink":"https://www.uniprot.org/uniprotkb/O74547/entry","name":"bit61","description":"Target of rapamycin complex 2 subunit bit61","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR32428","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64044343","identifier":"Q09743","identifierLink":"https://www.uniprot.org/uniprotkb/Q09743/entry","name":"ste20","description":"Target of rapamycin complex 2 subunit ste20","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13298","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26514","complexName":"Casein kinase II, ckb1 variant","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Serine/threonine-protein kinase complex involved in regulation of cell cycle progression. CK2 may also have role(s) in inhibiting apoptosis. Phosphorylates serine or threonine residues proximal to acidic amino acids (consensus Ser-Xaa-Xaa-Acidic where acidic residue may be Glu, Asp, pSer or pTYr).","predictedComplex":false,"interactors":[{"ac":"EBI-2014393","identifier":"P40231","identifierLink":"https://www.uniprot.org/uniprotkb/P40231/entry","name":"cka1","description":"Casein kinase II subunit alpha","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR24054","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64044582","identifier":"P40232","identifierLink":"https://www.uniprot.org/uniprotkb/P40232/entry","name":"ckb1","description":"Casein kinase II subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26515","complexName":"Casein kinase II, ckb2 variant","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Serine/threonine-protein kinase complex involved in regulation of cell cycle progression. CK2 may also have role(s) in inhibiting apoptosis. Phosphorylates serine or threonine residues proximal to acidic amino acids (consensus Ser-Xaa-Xaa-Acidic where acidic residue may be Glu, Asp, pSer or pTYr).","predictedComplex":false,"interactors":[{"ac":"EBI-2014393","identifier":"P40231","identifierLink":"https://www.uniprot.org/uniprotkb/P40231/entry","name":"cka1","description":"Casein kinase II subunit alpha","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR24054","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64044622","identifier":"O94281","identifierLink":"https://www.uniprot.org/uniprotkb/O94281/entry","name":"ckb2","description":"Casein kinase II subunit beta-2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26516","complexName":"RAG guanosine triphosphatase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"GTPase which is tethered to vacuole membranes through its association with the Lam/Ragulator complex (CPX-26512). Plays a role in TORC1 signalling, modulating cellular response to nutrients.","predictedComplex":false,"interactors":[{"ac":"EBI-21245422","identifier":"O74824","identifierLink":"https://www.uniprot.org/uniprotkb/O74824/entry","name":"gtr1","description":"GTP-binding protein gtr1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11259","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25820308","identifier":"CHEBI:37565","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:37565","name":"gtp(4-)","description":"GTP(4-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-64044661","identifier":"O74544","identifierLink":"https://www.uniprot.org/uniprotkb/O74544/entry","name":"gtr2","description":"GTP-binding protein gtr2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11259","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26517","complexName":"RAG guanosine triphosphatase complex","organismName":"Drosophila melanogaster; 7227","description":"GTPase which is tethered to vacuole membranes through its association with the Lam/Ragulator complex (CPX-26512). Plays a role in TORC1 signalling, modulating cellular response to nutrients.","predictedComplex":false,"interactors":[{"ac":"EBI-109317","identifier":"Q7K519","identifierLink":"https://www.uniprot.org/uniprotkb/Q7K519/entry","name":"RagC-D","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11259","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-166206","identifier":"Q9VHJ4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VHJ4/entry","name":"RagA-B","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11259","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25820308","identifier":"CHEBI:37565","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:37565","name":"gtp(4-)","description":"GTP(4-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-37001918","identifier":"CHEBI:58189","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58189","name":"gdp(3-)","description":"GDP(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26518","complexName":"RUNX-CBFB transcription factor complex, RUNX1 variant","organismName":"Homo sapiens; 9606","description":"Transcription factor complex that plays an essential role in haemopoiesis. The RUNX protein binds to binds to TGTGGNNN core sequences, typically TGTGGTTT or TGTGGTCA. DNA binding is stabilised by the presence of CBFB.","predictedComplex":false,"interactors":[{"ac":"EBI-718750","identifier":"Q13951","identifierLink":"https://www.uniprot.org/uniprotkb/Q13951/entry","name":"CBFB","description":"Core-binding factor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10276","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-925904","identifier":"Q01196","identifierLink":"https://www.uniprot.org/uniprotkb/Q01196/entry","name":"RUNX1","description":"Runt-related transcription factor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11950","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26519","complexName":"RUNX-CBFB transcription factor complex, RUNX2 variant","organismName":"Homo sapiens; 9606","description":"Transcription factor complex that plays an essential role in osteogenesis and is essential for the formation of mature osteocytes and for controlling the expression of genes required for mineralization of the bone extracellular matrix. The RUNX protein binds to binds to TGTGGNNN core sequences, typically TGTGGTTT or TGTGGTCA. DNA binding is stabilised by the presence of CBFB.","predictedComplex":false,"interactors":[{"ac":"EBI-718750","identifier":"Q13951","identifierLink":"https://www.uniprot.org/uniprotkb/Q13951/entry","name":"CBFB","description":"Core-binding factor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10276","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-976402","identifier":"Q13950","identifierLink":"https://www.uniprot.org/uniprotkb/Q13950/entry","name":"RUNX2","description":"Runt-related transcription factor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11950","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26520","complexName":"RUNX-CBFB transcription factor complex, RUNX3 variant","organismName":"Homo sapiens; 9606","description":"Transcription factor complex that plays an essential role in the in the DNA damage response by regulating positively regulates homologous recombination repair. The RUNX protein binds to binds to TGTGGNNN core sequences, typically TGTGGTTT or TGTGGTCA. DNA binding is stabilised by the presence of CBFB.","predictedComplex":false,"interactors":[{"ac":"EBI-718750","identifier":"Q13951","identifierLink":"https://www.uniprot.org/uniprotkb/Q13951/entry","name":"CBFB","description":"Core-binding factor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10276","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-925990","identifier":"Q13761","identifierLink":"https://www.uniprot.org/uniprotkb/Q13761/entry","name":"RUNX3","description":"Runt-related transcription factor 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11950","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26523","complexName":"GATOR1 complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"GTPase activating complex which functions as an inhibitor of the amino acid-sensing branch of the TORC1 pathway. In response to amino acid depletion,  the complex strongly increases GTP hydrolysis by RRAGAB within the heterodimeric Rag complex (CPX-26516) converting the protein to its inactive GDP-bound form. This releases TORC1 (CPX-26512) from the lysosomal surface and inhibits TORC1 signaling The GATOR1 complex is negatively regulated by GATOR2 complex (CPX-26527).","predictedComplex":false,"interactors":[{"ac":"EBI-64045896","identifier":"Q9HGM7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HGM7/entry","name":"nprl3","description":"Nitrogen permease regulator 3-like protein","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13153","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64045934","identifier":"O42857","identifierLink":"https://www.uniprot.org/uniprotkb/O42857/entry","name":"npr2","description":"Nitrogen permease regulator 2 homolog","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12991","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64045946","identifier":"O74788","identifierLink":"https://www.uniprot.org/uniprotkb/O74788/entry","name":"iml1","description":"Vacuolar membrane-associated protein iml1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13179","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26524","complexName":"SNARE complex STX4-SNAP29-SEC22b","organismName":"Homo sapiens; 9606","description":"SNARE complex required for the fusion of the double-membraned autophagosome with the single-membraned lysosome during starvation-induced bulk autophagy. Mediates membrane fusion through the spontaneous assembly of four complementary SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) motifs. SNAREs bind to each other in-trans, that is, with SNAREs anchored in each apposed tethered membrane. The assembly process leads to a tight connection between the fusing membranes and initiates membrane fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-1058865","identifier":"O75396","identifierLink":"https://www.uniprot.org/uniprotkb/O75396/entry","name":"SEC22B","description":"Vesicle-trafficking protein SEC22b","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45837","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-490676","identifier":"O95721","identifierLink":"https://www.uniprot.org/uniprotkb/O95721/entry","name":"SNAP29","description":"Synaptosomal-associated protein 29","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744942","identifier":"Q12846","identifierLink":"https://www.uniprot.org/uniprotkb/Q12846/entry","name":"STX4","description":"Syntaxin-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26526","complexName":"Septin1-Septin2-pnut complex","organismName":"Drosophila melanogaster; 7227","description":"Complex regulates actomyosin ring assembly, contraction and disassembly during cell wound repair, playing a key role in preventing cell damage and death during physiological and environmental stresses. Interacts with F-actin and promotes its bundling and bending.\r\n\r\nComplex formation and function is regulated by Anillin (Q9V4P1).","predictedComplex":false,"interactors":[{"ac":"EBI-120528","identifier":"P42207","identifierLink":"https://www.uniprot.org/uniprotkb/P42207/entry","name":"Septin1","description":"Septin-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-171301","identifier":"P40797","identifierLink":"https://www.uniprot.org/uniprotkb/P40797/entry","name":"pnut","description":"Protein peanut","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-188936","identifier":"P54359","identifierLink":"https://www.uniprot.org/uniprotkb/P54359/entry","name":"Septin2","description":"Septin-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26527","complexName":"GATOR2 complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Functions as an activator of the amino acid-sensing branch of the TORC1 pathway. Indirectly activates TORC1 (CPX-26512) through the inhibition of the GATOR1 complex (CPX-26523).","predictedComplex":false,"interactors":[{"ac":"EBI-1563760","identifier":"Q10099","identifierLink":"https://www.uniprot.org/uniprotkb/Q10099/entry","name":"seh1","description":"Nucleoporin seh1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11024","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21245957","identifier":"O94319","identifierLink":"https://www.uniprot.org/uniprotkb/O94319/entry","name":"sec13","description":"Protein transport protein sec13","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11024","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64045966","identifier":"O13686","identifierLink":"https://www.uniprot.org/uniprotkb/O13686/entry","name":"wdr59","description":"Uncharacterized RWD, RING finger and WD repeat-containing protein C11E3.05","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR46170","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64046148","identifier":"Q09866","identifierLink":"https://www.uniprot.org/uniprotkb/Q09866/entry","name":"yag1","description":"Uncharacterized WD repeat-containing protein C12G12.01c","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR16453","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64046168","identifier":"O14186","identifierLink":"https://www.uniprot.org/uniprotkb/O14186/entry","name":"ydsb","description":"Uncharacterized WD repeat-containing protein C4F8.11","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR46200","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26528","complexName":"Ragulator complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Involved in amino acid sensing and activation of TORC1 (CPX-26512) promoting cell growth in response to growth factors, energy levels, and amino acids. Ragulator functions as a guanine nucleotide exchange factor activating the small Rag GTPase Gtr1-Gtr2 (CPX-26516).","predictedComplex":false,"interactors":[{"ac":"EBI-64046190","identifier":"Q9Y7J2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y7J2/entry","name":"yoi5","description":"Uncharacterized protein C1778.05c","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13323","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64046208","identifier":"C6Y4A8","identifierLink":"https://www.uniprot.org/uniprotkb/C6Y4A8/entry","name":"yaep","description":"Uncharacterized protein C23D3.16","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-64046217","identifier":"C6Y4C6","identifierLink":"https://www.uniprot.org/uniprotkb/C6Y4C6/entry","name":"ygsq","description":"Uncharacterized protein C29A10.17","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-64046226","identifier":"G2TRJ4","identifierLink":"https://www.uniprot.org/uniprotkb/G2TRJ4/entry","name":"tam1","description":"Uncharacterized protein tam1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]}]},{"complexAC":"CPX-26529","complexName":"Septin4-Septin5-pnut complex","organismName":"Drosophila melanogaster; 7227","description":"Complex regulates actomyosin ring assembly, contraction and disassembly during cell wound repair, playing a key role in preventing cell damage and death during physiological and environmental stresses. Interacts with F-actin and promotes its bundling and bending. \r\n\r\nAnillin (Q9V4P1) regulates formation and function of the Septin1-Septin2-pnut complex (CPX-26526) but not the Septin4-Septin5-pnut complex (this complex).","predictedComplex":false,"interactors":[{"ac":"EBI-118172","identifier":"Q0KHR7","identifierLink":"https://www.uniprot.org/uniprotkb/Q0KHR7/entry","name":"Septin4","description":"Septin","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-171301","identifier":"P40797","identifierLink":"https://www.uniprot.org/uniprotkb/P40797/entry","name":"pnut","description":"Protein peanut","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-57037503","identifier":"Q7KLG8","identifierLink":"https://www.uniprot.org/uniprotkb/Q7KLG8/entry","name":"Septin5","description":"Septin","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR18884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26530","complexName":"Thrombopoietin receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Class I cytokine receptor-ligand complex essential for hematopoietic stem cell maintenance and the primary driver of megakaryocyte differentiation and platelet production. Signal transduction is initiated by associated Janus kinase (JAK) proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-3929175","identifier":"P40225","identifierLink":"https://www.uniprot.org/uniprotkb/P40225/entry","name":"THPO","description":"Thrombopoietin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10560","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6511486","identifier":"P40238","identifierLink":"https://www.uniprot.org/uniprotkb/P40238/entry","name":"MPL","description":"Thrombopoietin receptor","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23037","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26531","complexName":"Erythropoietin receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Class I cytokine receptor-ligand complex essential for the production of erythrocytes in the bone marrow.  Signal transduction is initiated by associated Janus kinase (JAK) proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-1027362","identifier":"P01588","identifierLink":"https://www.uniprot.org/uniprotkb/P01588/entry","name":"EPO","description":"Erythropoietin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10370","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-617321","identifier":"P19235","identifierLink":"https://www.uniprot.org/uniprotkb/P19235/entry","name":"EPOR","description":"Erythropoietin receptor","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23037","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26532","complexName":"Neuronal nicotinic acetylcholine receptor complex, alpha6-beta4","organismName":"Homo sapiens; 9606","description":"Ligand-gated ion channel receptor complex that is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron. Mediates fast, short-lived synaptic transmission of neurotransmitters.\r\n\r\nFound in the sensory neurons of dorsal root ganglia, agonists such as nicotine (CHEBI:18723) and its synthetic derivative, tebanicline (CHEBI:234304) act as effective analgesics to modulation pain.","predictedComplex":false,"interactors":[{"ac":"EBI-9008629","identifier":"Q15825","identifierLink":"https://www.uniprot.org/uniprotkb/Q15825/entry","name":"CHRNA6","description":"Neuronal acetylcholine receptor subunit alpha-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9009018","identifier":"P30926","identifierLink":"https://www.uniprot.org/uniprotkb/P30926/entry","name":"CHRNB4","description":"Neuronal acetylcholine receptor subunit beta-4","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26533","complexName":"FACT complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"A heterodimeric H2A-H2B histone chaperone, that helps reorganize nucleosomes in an ATP independent fashion. It promotes histone removal, deposition and replacement on chromatin. Due to its role in chromatin dynamics, it has a role in many cellular processes related to chromatin: DNA replication, DNA damage and repair, transcription initiation and elongation.","predictedComplex":false,"interactors":[{"ac":"EBI-64046663","identifier":"O94529","identifierLink":"https://www.uniprot.org/uniprotkb/O94529/entry","name":"pob3","description":"FACT complex subunit pob3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR45849","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7414132","identifier":"O94267","identifierLink":"https://www.uniprot.org/uniprotkb/O94267/entry","name":"spt16","description":"FACT complex subunit spt16","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13980","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26534","complexName":"MWP complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Anchors microtubule minus ends to mitotic spindle pole bodies. The complex may also act as a physical barrier resisting the outward pushing forces generated by Cut7/kinesin-5.","predictedComplex":false,"interactors":[{"ac":"EBI-64046939","identifier":"Q92376","identifierLink":"https://www.uniprot.org/uniprotkb/Q92376/entry","name":"klp1","description":"Kinesin-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR24115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64046976","identifier":"Q9P6R4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P6R4/entry","name":"mug172","description":"Meiotically up-regulated gene 172 protein","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-64046992","identifier":"Q96WW0","identifierLink":"https://www.uniprot.org/uniprotkb/Q96WW0/entry","name":"ynh9","description":"Uncharacterized WD repeat-containing protein C32H8.09","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR16220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26535","complexName":"Muscle-type nicotinic acetylcholine receptor complex, alpha1-beta1-delta-epsilon","organismName":"Homo sapiens; 9606","description":"Ligand-gated ion channel receptor complex. Found in the post-synaptic membrane of neuromuscular junctions, it is sensitive to endogenous achetylcholine and exogenous nicotinic agents. Ligand binding causes a conformational change of the receptor resulting in the formation of a pore that is permeable to Na+ and/or Ca2+ (inward) and K+ (outward) thereby depolarising the neuron and ultimately producing muscle contractions. Mediates fast, short-lived synaptic transmission of neurotransmitters at the foetal extra-junctional, non-innervated muscle but acts slower than the adult receptor.\r\n\r\nMutations in several of the actylcholine receptor genes are implicated in Congenital myasthenic syndrome, a disorder of the postsynaptic neuromuscular junction, characterized by early-onset muscle weakness of variable severity.","predictedComplex":false,"interactors":[{"ac":"EBI-11173019","identifier":"Q04844","identifierLink":"https://www.uniprot.org/uniprotkb/Q04844/entry","name":"CHRNE","description":"Acetylcholine receptor subunit epsilon","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724218","identifier":"P11230","identifierLink":"https://www.uniprot.org/uniprotkb/P11230/entry","name":"CHRNB1","description":"Acetylcholine receptor subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008819","identifier":"P02708","identifierLink":"https://www.uniprot.org/uniprotkb/P02708/entry","name":"CHRNA1","description":"Acetylcholine receptor subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008829","identifier":"Q07001","identifierLink":"https://www.uniprot.org/uniprotkb/Q07001/entry","name":"CHRND","description":"Acetylcholine receptor subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26536","complexName":"Serine/threonine-protein phosphatase 2A complex, B56 alpha variant","organismName":"Homo sapiens; 9606","description":"Serine/threonine protein phosphatase complex with a central role in maintaining cellular homeostasis. PP2A-B56 has been associated with maintenance of sister chromatid cohesion, regulation of kinetochore-microtubule attachment and with chromosome biorientation.","predictedComplex":false,"interactors":[{"ac":"EBI-302388","identifier":"P30153","identifierLink":"https://www.uniprot.org/uniprotkb/P30153/entry","name":"PPP2R1A","description":"Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-641666","identifier":"Q15172","identifierLink":"https://www.uniprot.org/uniprotkb/Q15172/entry","name":"PPP2R5A","description":"Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10257","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712311","identifier":"P67775","identifierLink":"https://www.uniprot.org/uniprotkb/P67775/entry","name":"PPP2CA","description":"Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26537","complexName":"TRAMP complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Recognises and bind to pre-ribosomal RNA and snoRNAs leading to their rapid degradation by the nuclear exosome (CPX-8914). Adds a short oligo(A) tail to the RNA which is assumed to make it a better substrate for 3'-end degradation.","predictedComplex":false,"interactors":[{"ac":"EBI-64047437","identifier":"Q9P795","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P795/entry","name":"air1","description":"Protein air1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR46543","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64047461","identifier":"Q9UTN3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UTN3/entry","name":"cid14","description":"Poly(A) RNA polymerase cid14","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8993773","identifier":"O14232","identifierLink":"https://www.uniprot.org/uniprotkb/O14232/entry","name":"mtr4","description":"ATP-dependent RNA helicase mtr4","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12131","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26538","complexName":"SepSecS-tRNASec complex","organismName":"Homo sapiens; 9606","description":"O-phosphoseryl-tRNA:selenocysteinyl-tRNA synthase (SepSecS) complex. SepSecS catalyzes the terminal reaction of selenocysteine; SepSecS converts a phosphoseryl (Sep) group into the selenocysteinyl (Sec) moiety in a process which requires selenocysteine tRNA (tRNASec) and the cofactor, pyridoxal-5-phosphate (PLP). Sec-tRNASec, the product of SepSecS catalysis, is an obligate substrate for selenoprotein synthesis, implying that the catalytic activity of SepSecS is crucial for selenoproteome integrity.","predictedComplex":false,"interactors":[{"ac":"EBI-6163446","identifier":"Q9HD40","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HD40/entry","name":"SEPSECS","description":"O-phosphoseryl-tRNA(Sec) selenium transferase","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12944","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64047511","identifier":"URS00001DA281_9606","identifierLink":"http://rnacentral.org/rna/URS00001DA281_9606","name":"(human) trna-sec (anticodon tca) 1-1 (tru-tca1-1)","description":"Homo sapiens (human) tRNA-SeC (anticodon TCA) 1-1 (TRU-TCA1-1)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"transfer rna","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-8852014","identifier":"CHEBI:597326","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:597326","name":"pyridoxal 5'-phosphate(2-)","description":"pyridoxal 5'-phosphate(2-)","stochiometry":"minValue: 4, maxValue: 4","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26539","complexName":"COP9 signalosome complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes.","predictedComplex":false,"interactors":[{"ac":"EBI-3647868","identifier":"O94308","identifierLink":"https://www.uniprot.org/uniprotkb/O94308/entry","name":"csn1","description":"COP9 signalosome complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR14145","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3648006","identifier":"Q9HFR0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HFR0/entry","name":"csn2","description":"COP9 signalosome complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10678","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3648151","identifier":"O13895","identifierLink":"https://www.uniprot.org/uniprotkb/O13895/entry","name":"csn4","description":"COP9 signalosome complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10855","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64048346","identifier":"Q9UT51","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UT51/entry","name":"csn3","description":"COP9 signalosome complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10758","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64048362","identifier":"O94454","identifierLink":"https://www.uniprot.org/uniprotkb/O94454/entry","name":"csn5","description":"COP9 signalosome complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10410","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64048381","identifier":"Q9UUJ7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UUJ7/entry","name":"csn71","description":"COP9 signalosome complex subunit 7","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15350","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968340","identifier":"CHEBI:29105","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29105","name":"zinc(2+)","description":"zinc(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26541","complexName":"Chemerin-CMKLR1 receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Chemotactic adipokine-receptor-ligand complex which displays chemotactic activity towards a subset of leukocytes. Chemerin moderates its function through the canonical CMKLR1 receptor (this complex) to mediate G protein and ARRB1 (P49407) signalling, initiating secondary messenger pathways including the MAPK pathway playing crucial roles in adipogenesis and inflammation.  Also implicated in the regulation of several immune-metabolic processes and diseases including, obesity, diabetes, Alzheimer's disease, multiple sclreosis and cancer.\r\n\r\nChemerin also effects its functions through the CMKLR2 receptor (CPX-26542). Despite the high sequence identity shared by the two receptors, their signalling properties and biological functions are distinct.\r\n\r\nLevels of Chemerin and its processing is thought to correlate with insulin resistance and higher Chemerin levels suspected in patients with type 2 Diabetes.","predictedComplex":false,"interactors":[{"ac":"EBI-28951773","identifier":"Q99969","identifierLink":"https://www.uniprot.org/uniprotkb/Q99969/entry","name":"RARRES2","description":"Retinoic acid receptor responder protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15106","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-54573926","identifier":"Q99788","identifierLink":"https://www.uniprot.org/uniprotkb/Q99788/entry","name":"CMKLR1","description":"Chemerin-like receptor 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24225","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26542","complexName":"Chemerin-CMKLR2 receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Chemotactic adipokine-receptor-ligand complex which displays chemotactic activity towards a subset of leukocytes. Receptor-ligand binding activates G protein and ARRB1 (P49407) signalling, initiating secondary messenger pathways including the MAPK pathway playing crucial roles in adipogenesis and inflammation.  Also implicated in the regulation of several immune-metabolic processes and diseases including, obesity, diabetes, Alzheimer's disease, multiple sclreosis and cancer.\r\n\r\nChemerin moderates its function through the canonical CMKLR1 (CPX-26541) receptor, but it also effects its functions through the CMKLR2 receptor (this complex). Despite the high sequence identity shared by the two receptors, their signalling properties and biological functions are distinct. CMKLR2 can be activated by binding to chemerin but with a lower potency than CMKLR1, and ARRB1 recruitment by CMKLR2 is of a smaller maginute than CMKLR1.\r\n\r\nLevels of Chemerin and its processing is thought to correlate with insulin resistance and higher Chemerin levels suspected in patients with type 2 Diabetes.","predictedComplex":false,"interactors":[{"ac":"EBI-11477864","identifier":"P46091","identifierLink":"https://www.uniprot.org/uniprotkb/P46091/entry","name":"CMKLR2","description":"Chemerin-like receptor 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24229","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28951773","identifier":"Q99969","identifierLink":"https://www.uniprot.org/uniprotkb/Q99969/entry","name":"RARRES2","description":"Retinoic acid receptor responder protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15106","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26543","complexName":"GTPase-activating BFA1-BUB2 complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Acts as a two-component GTPase-activating complex for spg1 (P87027) GTPase, thus regulating the induction of septum formation at G2 and pre-START stages of mitosis.","predictedComplex":false,"interactors":[{"ac":"EBI-1997311","identifier":"Q10951","identifierLink":"https://www.uniprot.org/uniprotkb/Q10951/entry","name":"byr4","description":"Protein byr4","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR35140","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1997321","identifier":"P36618","identifierLink":"https://www.uniprot.org/uniprotkb/P36618/entry","name":"cdc16","description":"Cell division control protein 16","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR22957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26544","complexName":"Nuclear mitotic cohesin complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Required for sister chromatid cohesion during cell division, which enables cells to attach sister kinetochores  to microtubules with opposing polarity (bi-orientation) and subsequently resists the tendency of these microtubules to pull chromatids toward opposite spindle poles. Before the commencement of replication, the cohesin complex is loaded onto DNA. The arms of the psm1/3 (SMC1/3) molecules embrace the DNA, forming a ring of approx. 40 nm diameter. The head domains of psm1 and psm3 are locked together by rad21/SCC1. Cohesion might be generated as the replication fork passes through the ring, entrapping both sister chromatids inside. At the metaphase to anaphase transition, rad211 is cleaved by separase, thereby opening the lock of the psm1/3 head domains. The ring opens and sister chromatids can be pulled to opposite spindle poles.","predictedComplex":false,"interactors":[{"ac":"EBI-1131314","identifier":"O13816","identifierLink":"https://www.uniprot.org/uniprotkb/O13816/entry","name":"psc3","description":"Cohesin subunit psc3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11199","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1151879","identifier":"O42649","identifierLink":"https://www.uniprot.org/uniprotkb/O42649/entry","name":"psm3","description":"Structural maintenance of chromosomes protein 3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR43977","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1151900","identifier":"O94383","identifierLink":"https://www.uniprot.org/uniprotkb/O94383/entry","name":"psm1","description":"Structural maintenance of chromosomes protein 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR18937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1152045","identifier":"P30776","identifierLink":"https://www.uniprot.org/uniprotkb/P30776/entry","name":"rad21","description":"Cohesin subunit rad21","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12585","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26545","complexName":"Chemerin-CCRL2 receptor-ligand scavenger complex","organismName":"Homo sapiens; 9606","description":"Chemerin-scavenger receptor complex. CCRL2 binds chemerin with high-affinity but at a lower affinity than CMKLR1 (Q99788) or CMKLR2 (P46091), forming a nonfunctional chemerin receptor complex which serves as a scavenger and does not mediate transmembrane signalling. However, CCRL2 is able establish concentration gradients by binding and delivering chemerin, thus allowing its involvement in a variety of functions. CCRL2's functions is dependent on CMKLR1 expression.","predictedComplex":false,"interactors":[{"ac":"EBI-13623298","identifier":"O00421","identifierLink":"https://www.uniprot.org/uniprotkb/O00421/entry","name":"CCRL2","description":"C-C chemokine receptor-like 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10489","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28951773","identifier":"Q99969","identifierLink":"https://www.uniprot.org/uniprotkb/Q99969/entry","name":"RARRES2","description":"Retinoic acid receptor responder protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15106","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26546","complexName":"SCC2-SCC4 cohesin loader complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Required for the stable association of the nuclear mitotic cohesin complex (CPX-26546) with DNA and ensures its enrichment at the mitotic spindle of the centromere thus ensuring correct segregation of the sister chromatids into the daughter cells during cell replication.","predictedComplex":false,"interactors":[{"ac":"EBI-16083239","identifier":"Q09725","identifierLink":"https://www.uniprot.org/uniprotkb/Q09725/entry","name":"mis4","description":"Sister chromatid cohesion protein mis4","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR21704","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64072190","identifier":"O94459","identifierLink":"https://www.uniprot.org/uniprotkb/O94459/entry","name":"ssl3","description":"MAU2 chromatid cohesion factor homolog","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR21394","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26547","complexName":"Nonclassical MHC Ib complex, HLA-E-B2M","organismName":"Homo sapiens; 9606","description":"Antigen-presenting major histocompatibility complex which presents the bound peptide antigen to CD8+ cytotoxic T-lymphocytes .The complex assembles in the endoplasmic reticulum  and is transported to the cell surface. Presents a signal sequence peptide from the classical MHC Ia molecules (VL9) to NKG2x-CD94 receptors expressed on natural killer (NK) cells and specific CD8 T cell populations this regulating NK cell-mediated lysis","predictedComplex":false,"interactors":[{"ac":"EBI-64073190","identifier":"CHEBI:166824","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:166824","name":"peptide antigen","description":"peptide antigen","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-714718","identifier":"P61769","identifierLink":"https://www.uniprot.org/uniprotkb/P61769/entry","name":"B2M","description":"Beta-2-microglobulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19944","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-726583","identifier":"P13747","identifierLink":"https://www.uniprot.org/uniprotkb/P13747/entry","name":"HLA-E","description":"HLA class I histocompatibility antigen, alpha chain E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16675","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26548","complexName":"Nonclassical MHC Ib complex, HLA-F-B2M","organismName":"Homo sapiens; 9606","description":"Antigen-presenting major histocompatibility complex which presents the bound peptide antigen to CD8+ cytotoxic T-lymphocytes. The complex assembles in the endoplasmic reticulum  and is transported to the cell surface. Peptide-bound HLA-F-B2M acts as a ligand for LILRB1 inhibitory receptor, a major player in maternal-fetal tolerance.","predictedComplex":false,"interactors":[{"ac":"EBI-2811134","identifier":"P30511","identifierLink":"https://www.uniprot.org/uniprotkb/P30511/entry","name":"HLA-F","description":"HLA class I histocompatibility antigen, alpha chain F","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16675","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64073190","identifier":"CHEBI:166824","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:166824","name":"peptide antigen","description":"peptide antigen","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-714718","identifier":"P61769","identifierLink":"https://www.uniprot.org/uniprotkb/P61769/entry","name":"B2M","description":"Beta-2-microglobulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19944","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26549","complexName":"Nonclassical MHC Ib complex, HLA-G-B2M","organismName":"Homo sapiens; 9606","description":"Antigen-presenting major histocompatibility complex which presents the bound peptide antigen to CD8+ cytotoxic T-lymphocytes. The complex assembles in the endoplasmic reticulum and is transported to the cell surface. Peptide-bound HLA-G-B2M complex acts as a ligand for inhibitory/activating KIR2DL4 (Q99706), LILRB1 (Q8NHL6) and LILRB2 (Q8N423) receptors on uterine immune cells to promote fetal development while maintaining maternal-fetal tolerance.","predictedComplex":false,"interactors":[{"ac":"EBI-1043063","identifier":"P17693","identifierLink":"https://www.uniprot.org/uniprotkb/P17693/entry","name":"HLA-G","description":"HLA class I histocompatibility antigen, alpha chain G","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16675","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64073190","identifier":"CHEBI:166824","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:166824","name":"peptide antigen","description":"peptide antigen","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-714718","identifier":"P61769","identifierLink":"https://www.uniprot.org/uniprotkb/P61769/entry","name":"B2M","description":"Beta-2-microglobulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19944","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2876","complexName":"Ribonuclease MRP complex","organismName":"Homo sapiens; 9606","description":"Essential endoribonuclease  closely related to RNAse P complex (CPX-2877). RNAse MRP is involved in the processing of precursor ribosomal RNAs (pre-rRNA) at ITS1 site 2, mitochondrial RNAs and certain messenger RNAs. The RNA subunit RMRP is a catalytically active ribozyme that is capable of both recognizing and cleaving substrates. \r\n\r\nPOP4, RPP14, POP5, RPP20, RPP30, RPP38, RPP40, and RMRP are required for pre-rRNA ITS1 site 2 cleavage. \r\n\r\nMutations in RMRP or in the complex's promoter regions of its proteins components or the protein components themselves are associated with ribosomopathies.","predictedComplex":false,"interactors":[{"ac":"EBI-10986855","identifier":"Q32NC0","identifierLink":"https://www.uniprot.org/uniprotkb/Q32NC0/entry","name":"C18orf21","description":"UPF0711 protein C18orf21","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31402","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2514392","identifier":"Q6NW34","identifierLink":"https://www.uniprot.org/uniprotkb/Q6NW34/entry","name":"NEPRO","description":"Nucleolus and neural progenitor protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR34761","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366477","identifier":"O95707","identifierLink":"https://www.uniprot.org/uniprotkb/O95707/entry","name":"POP4","description":"Ribonuclease P protein subunit p29","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13348","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366493","identifier":"P78345","identifierLink":"https://www.uniprot.org/uniprotkb/P78345/entry","name":"RPP38","description":"Ribonuclease P protein subunit p38","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46948","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366505","identifier":"O75818","identifierLink":"https://www.uniprot.org/uniprotkb/O75818/entry","name":"RPP40","description":"Ribonuclease P protein subunit p40","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15396","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366525","identifier":"Q969H6","identifierLink":"https://www.uniprot.org/uniprotkb/Q969H6/entry","name":"POP5","description":"Ribonuclease P/MRP protein subunit POP5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15441","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366542","identifier":"O95059","identifierLink":"https://www.uniprot.org/uniprotkb/O95059/entry","name":"RPP14","description":"Ribonuclease P protein subunit p14","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15441","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366553","identifier":"P78346","identifierLink":"https://www.uniprot.org/uniprotkb/P78346/entry","name":"RPP30","description":"Ribonuclease P protein subunit p30","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13031","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366570","identifier":"Q9BUL9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BUL9/entry","name":"RPP25","description":"Ribonuclease P protein subunit p25","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13516","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366574","identifier":"O75817","identifierLink":"https://www.uniprot.org/uniprotkb/O75817/entry","name":"POP7","description":"Ribonuclease P protein subunit p20","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15314","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-366741","identifier":"Q99575","identifierLink":"https://www.uniprot.org/uniprotkb/Q99575/entry","name":"POP1","description":"Ribonucleases P/MRP protein subunit POP1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22731","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9875627","identifier":"URS000075C8FA_9606","identifierLink":"http://rnacentral.org/rna/URS000075C8FA_9606","name":"rmrp_human_rna","description":"RNA component of mitochondrial RNA processing endoribonuclease","stochiometry":null,"interactorType":"small nucleolar rna","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-26550","complexName":"Centriole forming tubulin complex","organismName":"Homo sapiens; 9606","description":"Plays a direct role in forming and/or maintaining centriole structure by regulating triplet microtubule formation and stability. Acts as a positive regulator of the hedgehog signalling pathway in primary cilia.","predictedComplex":false,"interactors":[{"ac":"EBI-11280109","identifier":"Q9UJT1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UJT1/entry","name":"TUBD1","description":"Tubulin delta chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21629784","identifier":"Q9UJT0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UJT0/entry","name":"TUBE1","description":"Tubulin epsilon chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3247115","identifier":"Q86SX3","identifierLink":"https://www.uniprot.org/uniprotkb/Q86SX3/entry","name":"TEDC1","description":"Tubulin epsilon and delta complex protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR35076","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8465456","identifier":"Q7L2K0","identifierLink":"https://www.uniprot.org/uniprotkb/Q7L2K0/entry","name":"TEDC2","description":"Tubulin epsilon and delta complex protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14870","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26552","complexName":"U5 small nuclear ribonucleoprotein complex, AAR2 variant","organismName":"Homo sapiens; 9606","description":"A form of the U5 snRNP (CPX-26421), that is mainly found in the cytoplasm. The spliceosome is a highly dynamic structure, assembled by sequential binding and release of the small nuclear RNAs and protein factors which removes intronic sequence from pre-mRNA.\r\n\r\nAAR2 may play a role in preventing the premature association of the U4/U6 di-snRNP complex (CPX-26418) with pre-U5 snRNP components, and AAR2 is thought to be exclusively associated with U5 snRNPs (this complex) but not with the U4/U6.U5 tri-snRNP (CPX-2391). In man, AAR2 is thought to play a role in the spliceosomal assembly process beyond that of a placeholder to prevent premature assembly of SNRNP200 as in yeast complex (CPX-29, CPX-30); AAR2's ability to impede transition to the next stage of U5 snRNP formation may in turn impede gene expression.","predictedComplex":false,"interactors":[{"ac":"EBI-1045395","identifier":"O75643","identifierLink":"https://www.uniprot.org/uniprotkb/O75643/entry","name":"SNRNP200","description":"U5 small nuclear ribonucleoprotein 200 kDa helicase","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24075","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-297993","identifier":"P62316","identifierLink":"https://www.uniprot.org/uniprotkb/P62316/entry","name":"SNRPD2","description":"Small nuclear ribonucleoprotein Sm D2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12777","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348082","identifier":"P62304","identifierLink":"https://www.uniprot.org/uniprotkb/P62304/entry","name":"SNRPE","description":"Small nuclear ribonucleoprotein E","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11193","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356900","identifier":"P62306","identifierLink":"https://www.uniprot.org/uniprotkb/P62306/entry","name":"SNRPF","description":"Small nuclear ribonucleoprotein F","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357897","identifier":"Q15029","identifierLink":"https://www.uniprot.org/uniprotkb/Q15029/entry","name":"EFTUD2","description":"116 kDa U5 small nuclear ribonucleoprotein component","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR42908","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372177","identifier":"P62314","identifierLink":"https://www.uniprot.org/uniprotkb/P62314/entry","name":"SNRPD1","description":"Small nuclear ribonucleoprotein Sm D1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372458","identifier":"P14678","identifierLink":"https://www.uniprot.org/uniprotkb/P14678/entry","name":"SNRPB","description":"Small nuclear ribonucleoprotein-associated proteins B and B'","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372789","identifier":"P62318","identifierLink":"https://www.uniprot.org/uniprotkb/P62318/entry","name":"SNRPD3","description":"Small nuclear ribonucleoprotein Sm D3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-538479","identifier":"Q6P2Q9","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P2Q9/entry","name":"PRPF8","description":"Pre-mRNA-processing-splicing factor 8","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11140","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61264774","identifier":"URS000075BAAE_9606","identifierLink":"http://rnacentral.org/rna/URS000075BAAE_9606","name":"rna, u5a small nuclear 1 (rnu5a-1)","description":"Homo sapiens (human) RNA, U5A small nuclear 1 (RNU5A-1)","stochiometry":null,"interactorType":"small nuclear rna","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-624585","identifier":"P62308","identifierLink":"https://www.uniprot.org/uniprotkb/P62308/entry","name":"SNRPG","description":"Small nuclear ribonucleoprotein G","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-748721","identifier":"Q9Y312","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y312/entry","name":"AAR2","description":"Protein AAR2 homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12689","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26553","complexName":"LSM2-8 complex","organismName":"Homo sapiens; 9606","description":"The hetero-heptameric complex of seven Lsm proteins (Lsm2-8) affects the processing of small stable RNAs (including tRNAs, rRNAs) and pre-mRNAs in the nucleus. The complex is part of the U6 snRNP, where it binds to the U6 RNA and contributes to stabilizing the U6 snRNA and chaperoning it through the splicing process. The LSM2-8 complex (this complex) is thought to pre-exist in the cell and act as chaperone for U6 spliceosomal RNA (CPX-26415). The cytoplasmic LSM1-7 complex (CPX-26554) initiates mRNA decay.","predictedComplex":false,"interactors":[{"ac":"EBI-347416","identifier":"Q9Y333","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y333/entry","name":"LSM2","description":"U6 snRNA-associated Sm-like protein LSm2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347779","identifier":"O95777","identifierLink":"https://www.uniprot.org/uniprotkb/O95777/entry","name":"LSM8","description":"U6 snRNA-associated Sm-like protein LSm8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348239","identifier":"P62310","identifierLink":"https://www.uniprot.org/uniprotkb/P62310/entry","name":"LSM3","description":"U6 snRNA-associated Sm-like protein LSm3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13110","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348372","identifier":"Q9UK45","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK45/entry","name":"LSM7","description":"U6 snRNA-associated Sm-like protein LSm7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372521","identifier":"Q9Y4Z0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4Z0/entry","name":"LSM4","description":"U6 snRNA-associated Sm-like protein LSm4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373007","identifier":"Q9Y4Y9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4Y9/entry","name":"LSM5","description":"U6 snRNA-associated Sm-like protein LSm5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373310","identifier":"P62312","identifierLink":"https://www.uniprot.org/uniprotkb/P62312/entry","name":"LSM6","description":"U6 snRNA-associated Sm-like protein LSm6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26554","complexName":"LSM1-7 complex","organismName":"Homo sapiens; 9606","description":"LSM1-7 is a complex conserved in all eukaryotes and has similar function to the homohexamer Hfq in bacteria. It is an important part of cytoplasmic mRNA degradation. It preferentially binds oligo-adenylated (but not poly-A) mRNAs at their 3'-end and promotes decapping at the 5'-end thereby directing the mRNA for degradation through the 5' to 3' pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-347416","identifier":"Q9Y333","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y333/entry","name":"LSM2","description":"U6 snRNA-associated Sm-like protein LSm2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347619","identifier":"O15116","identifierLink":"https://www.uniprot.org/uniprotkb/O15116/entry","name":"LSM1","description":"U6 snRNA-associated Sm-like protein LSm1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348239","identifier":"P62310","identifierLink":"https://www.uniprot.org/uniprotkb/P62310/entry","name":"LSM3","description":"U6 snRNA-associated Sm-like protein LSm3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13110","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348372","identifier":"Q9UK45","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK45/entry","name":"LSM7","description":"U6 snRNA-associated Sm-like protein LSm7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372521","identifier":"Q9Y4Z0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4Z0/entry","name":"LSM4","description":"U6 snRNA-associated Sm-like protein LSm4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373007","identifier":"Q9Y4Y9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4Y9/entry","name":"LSM5","description":"U6 snRNA-associated Sm-like protein LSm5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373310","identifier":"P62312","identifierLink":"https://www.uniprot.org/uniprotkb/P62312/entry","name":"LSM6","description":"U6 snRNA-associated Sm-like protein LSm6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26555","complexName":"LSM2-8 complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Hetero-heptameric complex of seven LSM proteins (LSM2-8) which affects the processing of small stable RNAs (including tRNAs, rRNAs) and pre-mRNAs in the nucleus. The complex is a core part of the U6 snRNP (CPX-26415), where it binds to the U6 RNA and contributes to stabilizing the U6 snRNA and chaperoning it through the splicing process. The LSM2-8 complex is thought to pre-exist in the cell and bind to U6 as a complex.","predictedComplex":false,"interactors":[{"ac":"EBI-1560482","identifier":"Q9Y7M4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y7M4/entry","name":"lsm3","description":"LSM complex subunit lsm3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13110","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-539326","identifier":"O74483","identifierLink":"https://www.uniprot.org/uniprotkb/O74483/entry","name":"lsm8","description":"LSM2-LSM8 complex subunit lsm8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61254278","identifier":"O14352","identifierLink":"https://www.uniprot.org/uniprotkb/O14352/entry","name":"lsm4","description":"LSM complex subunit lsm4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61254315","identifier":"O42978","identifierLink":"https://www.uniprot.org/uniprotkb/O42978/entry","name":"lsm5","description":"LSM complex subunit lsm5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR20971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61254349","identifier":"Q9UUI1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UUI1/entry","name":"lsm6","description":"LSM complex subunit lsm6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61254385","identifier":"O74499","identifierLink":"https://www.uniprot.org/uniprotkb/O74499/entry","name":"lsm7","description":"LSM complex subunit lsm7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61254434","identifier":"O94408","identifierLink":"https://www.uniprot.org/uniprotkb/O94408/entry","name":"lsm2","description":"LSM complex subunit lsm2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26556","complexName":"Growth hormone receptor-ligand complex","organismName":"Homo sapiens; 9606","description":"Receptor-ligand complex which regulates postnatal body growth. metabolism, organ development, and sexual maturation. Activates JAK2/STAT5 signalling to stimulate production of insulin-like growth factor 1 (P05019) and increase levels of glucose and free fatty acids","predictedComplex":false,"interactors":[{"ac":"EBI-1026046","identifier":"P01241","identifierLink":"https://www.uniprot.org/uniprotkb/P01241/entry","name":"GH1","description":"Somatotropin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11417","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-286316","identifier":"P10912","identifierLink":"https://www.uniprot.org/uniprotkb/P10912/entry","name":"GHR","description":"Growth hormone receptor","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23036","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26558","complexName":"LSM1-7, PATL1 complex","organismName":"Homo sapiens; 9606","description":"LSM1-7-Pat1 is a complex conserved in all eukaryotes. LSM1-7 complex (CPX-26554) associates with PATL1 to modulate mRNA degradation. The complex preferentially binds oligo-adenylated (but not poly-A) mRNAs at their 3' end and promotes decapping at the 5' end thereby directing the mRNA for degradation through the 5' to 3' pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-2562092","identifier":"Q86TB9","identifierLink":"https://www.uniprot.org/uniprotkb/Q86TB9/entry","name":"PATL1","description":"Protein PAT1 homolog 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21551","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347416","identifier":"Q9Y333","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y333/entry","name":"LSM2","description":"U6 snRNA-associated Sm-like protein LSm2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347619","identifier":"O15116","identifierLink":"https://www.uniprot.org/uniprotkb/O15116/entry","name":"LSM1","description":"U6 snRNA-associated Sm-like protein LSm1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348239","identifier":"P62310","identifierLink":"https://www.uniprot.org/uniprotkb/P62310/entry","name":"LSM3","description":"U6 snRNA-associated Sm-like protein LSm3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13110","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348372","identifier":"Q9UK45","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK45/entry","name":"LSM7","description":"U6 snRNA-associated Sm-like protein LSm7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372521","identifier":"Q9Y4Z0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4Z0/entry","name":"LSM4","description":"U6 snRNA-associated Sm-like protein LSm4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373007","identifier":"Q9Y4Y9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4Y9/entry","name":"LSM5","description":"U6 snRNA-associated Sm-like protein LSm5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373310","identifier":"P62312","identifierLink":"https://www.uniprot.org/uniprotkb/P62312/entry","name":"LSM6","description":"U6 snRNA-associated Sm-like protein LSm6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26559","complexName":"Classical MHC Ia complex, HLA-A-B2M","organismName":"Homo sapiens; 9606","description":"Antigen-presenting major histocompatibility complex which presents the bound peptide antigen to CD8+ cytotoxic T-lymphocytes. The complex assembles in the endoplasmic reticulum  and is transported to the cell surface. Presents primarily viral and tumor-derived peptides","predictedComplex":false,"interactors":[{"ac":"EBI-1042870","identifier":"P04439","identifierLink":"https://www.uniprot.org/uniprotkb/P04439/entry","name":"HLA-A","description":"HLA class I histocompatibility antigen, A alpha chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16675","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64073190","identifier":"CHEBI:166824","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:166824","name":"peptide antigen","description":"peptide antigen","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-714718","identifier":"P61769","identifierLink":"https://www.uniprot.org/uniprotkb/P61769/entry","name":"B2M","description":"Beta-2-microglobulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19944","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26560","complexName":"Classical MHC Ia complex, HLA-B-B2M","organismName":"Homo sapiens; 9606","description":"Antigen-presenting major histocompatibility complex which presents the bound peptide antigen to CD8+ cytotoxic T-lymphocytes. The complex assembles in the endoplasmic reticulum  and is transported to the cell surface. Presents primarily viral and tumor-derived peptides. SpecificHLA-B alleles with protection against infection severity or susceptibility to autoimmunity and hypersensitivity.","predictedComplex":false,"interactors":[{"ac":"EBI-1046513","identifier":"P01889","identifierLink":"https://www.uniprot.org/uniprotkb/P01889/entry","name":"HLA-B","description":"HLA class I histocompatibility antigen, B alpha chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16675","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64073190","identifier":"CHEBI:166824","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:166824","name":"peptide antigen","description":"peptide antigen","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-714718","identifier":"P61769","identifierLink":"https://www.uniprot.org/uniprotkb/P61769/entry","name":"B2M","description":"Beta-2-microglobulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19944","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26561","complexName":"Classical MHC Ia complex, HLA-C-B2M","organismName":"Homo sapiens; 9606","description":"Antigen-presenting major histocompatibility complex which presents the bound peptide antigen to CD8+ cytotoxic T-lymphocytes. The complex assembles in the endoplasmic reticulum and is transported to the cell surface. Presents primarily viral and tumor-derived peptides. HLA-C is expressed at relatively low levels on the cell surface and presents antigens less efficiently than HLA-A and -B. Its primary function may be in natural killer cell recognition.","predictedComplex":false,"interactors":[{"ac":"EBI-1051396","identifier":"P10321","identifierLink":"https://www.uniprot.org/uniprotkb/P10321/entry","name":"HLA-C","description":"HLA class I histocompatibility antigen, C alpha chain","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16675","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64073190","identifier":"CHEBI:166824","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:166824","name":"peptide antigen","description":"peptide antigen","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-714718","identifier":"P61769","identifierLink":"https://www.uniprot.org/uniprotkb/P61769/entry","name":"B2M","description":"Beta-2-microglobulin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19944","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26562","complexName":"Anamorsin-NDOR1 complex","organismName":"Homo sapiens; 9606","description":"Iron-sulfur (Fe-S) complex required for the maturation of extramitochondrial Fe-S proteins. Protein complex that supplies reducing equivalents to the early steps of the cytosolic Fe-S assembly (CIA) pathway and also functions in ribonucleotide reductase cluster assembly, potentially also supplying reducing equivalents to the di-iron cluster. Electrons from NADPH are transferred via FAD and FMN, the two flavin cofactors in NDOR1, to the Fe-S cluster(s) in CIAPIN1, which subsequently deliver the electrons to proteins in the CIA pathway.","predictedComplex":false,"interactors":[{"ac":"EBI-10249760","identifier":"Q9UHB4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UHB4/entry","name":"NDOR1","description":"NADPH-dependent diflavin oxidoreductase 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19384","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11172266","identifier":"CHEBI:49601","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49601","name":"fe2s2 iron-sulfur cluster","description":"Fe2S2 iron-sulfur cluster","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1802358","identifier":"CHEBI:49883","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49883","name":"tetra-mu3-sulfido-tetrairon","description":"tetra-mu(3)-sulfido-tetrairon (IRON/SULFUR CLUSTER)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-750511","identifier":"Q6FI81","identifierLink":"https://www.uniprot.org/uniprotkb/Q6FI81/entry","name":"CIAPIN1","description":"Anamorsin","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13273","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9663515","identifier":"CHEBI:58210","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58210","name":"fmn(3-)","description":"FMN(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26563","complexName":"Phosphopantothenoylcysteine decarboxylase complex","organismName":"Homo sapiens; 9606","description":"Catalyzes decarboxylation of 4'-phosphopantothenoylcysteine to yield 4'-phosphopantetheine; the third step in the biosynthesis of Coenzyme A (CoA). \r\n\r\nThe synthesis of CoA involves the phosphorylation of pantothenate (vitamin B5) to 4'-phosphopantothenate, to which a cysteine is then added to form 4'-phospho-N-pantothenoylcysteine (PCC). PPC is decarboxylated to 4'-phosphopantetheine by phosphopantothenoylcysteine decarboxylase (this complex). 4'-phosphopantetheine is adenylylated to form dephospho-CoA which is then phosphorylated to form coenzyme A.","predictedComplex":false,"interactors":[{"ac":"EBI-724333","identifier":"Q96CD2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96CD2/entry","name":"PPCDC","description":"Phosphopantothenoylcysteine decarboxylase","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14359","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8786278","identifier":"CHEBI:17621","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:17621","name":"fmn","description":"FMN","stochiometry":"minValue: 3, maxValue: 3","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26564","complexName":"Serine/threonine-protein phosphatase 2A complex, B56 delta variant","organismName":"Homo sapiens; 9606","description":"Serine/threonine protein phosphatase complex with a central rle in maintaining cellular homeostasis. PP2A-B56 has been associated with maintenance of sister chromatid cohesion, regulation of kinetochore-microtubule attachment and with chromosome biorientation.","predictedComplex":false,"interactors":[{"ac":"EBI-302388","identifier":"P30153","identifierLink":"https://www.uniprot.org/uniprotkb/P30153/entry","name":"PPP2R1A","description":"Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-396563","identifier":"Q14738","identifierLink":"https://www.uniprot.org/uniprotkb/Q14738/entry","name":"PPP2R5D","description":"Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10257","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712311","identifier":"P67775","identifierLink":"https://www.uniprot.org/uniprotkb/P67775/entry","name":"PPP2CA","description":"Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26565","complexName":"Serine/threonine-protein phosphatase 2A complex, B56 epsilon variant","organismName":"Homo sapiens; 9606","description":"Serine/threonine protein phosphatase complex with a central rle in maintaining cellular homeostasis. PP2A-B56 has been associated with maintenance of sister chromatid cohesion, regulation of kinetochore-microtubule attachment and with chromosome biorientation.","predictedComplex":false,"interactors":[{"ac":"EBI-302388","identifier":"P30153","identifierLink":"https://www.uniprot.org/uniprotkb/P30153/entry","name":"PPP2R1A","description":"Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712311","identifier":"P67775","identifierLink":"https://www.uniprot.org/uniprotkb/P67775/entry","name":"PPP2CA","description":"Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-968374","identifier":"Q16537","identifierLink":"https://www.uniprot.org/uniprotkb/Q16537/entry","name":"PPP2R5E","description":"Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10257","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26566","complexName":"MIM mitochondrial import complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Major translocase complex which orchestrates the insertion of precursors of multi-spanning alpha-helical proteins, both N-terminal (signal-anchored) or C-terminal (tail-anchored) anchored, into the mitochondrial outer membrane. Accept precursor proteins from the TOM70 receptor in the TOM40 mitochondrial outer membrane translocase core complex and also inserts single-spanning proteins that are imported in a Tom70-independent manner. Facilitates mitophagy through the loading of Atg43 (O13709) to the mitochondrial outer membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-64092832","identifier":"G2TRP0","identifierLink":"https://www.uniprot.org/uniprotkb/G2TRP0/entry","name":"mim2","description":"Mitochondrial import protein 2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28230","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64092866","identifier":"Q9C1W7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9C1W7/entry","name":"mim1","description":"Mitochondrial import protein 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]}]},{"complexAC":"CPX-26567","complexName":"HIR histone chaperone complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Histone chaperone complex which promotes nucleosome assembly. Cooperates with the cia1 (O74515) co-chaperone to deposit histone (H3/H4)2 tetramers on DNA for replication-independent chromatin assembly","predictedComplex":false,"interactors":[{"ac":"EBI-1556094","identifier":"P87314","identifierLink":"https://www.uniprot.org/uniprotkb/P87314/entry","name":"hip1","description":"Protein hir1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13831","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1556117","identifier":"O74309","identifierLink":"https://www.uniprot.org/uniprotkb/O74309/entry","name":"slm9","description":"Histone transcription regulator slm9","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13831","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1556159","identifier":"P87315","identifierLink":"https://www.uniprot.org/uniprotkb/P87315/entry","name":"hip3","description":"Histone transcription regulator 3 homolog","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15502","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64092883","identifier":"O43083","identifierLink":"https://www.uniprot.org/uniprotkb/O43083/entry","name":"hpc2","description":"Histone promoter control protein 2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]}]},{"complexAC":"CPX-26568","complexName":"Translation elongation factor 1, eEF1B complex","organismName":"Homo sapiens; 9606","description":"Plays a key role in protein biosynthesis through the delivery of aminoacylated-tRNA (aa-tRNA) to а corresponding codon of the mRNA-programmed ribosome. \r\n\r\nThe eEF1 family of translation elongation factors is comprised of the two variants of eEF1A (EEF1A1 and EEF1A2 (Q05639)), and the eEF1B complex (this complex). EEF1A1 (CPX-26572) and EEF1A2 (CPX-26573) transfer aa-tRNA from aa-tRNA synthetase to the ribosome, and then a deacylated tRNA back to aa-tRNA synthetase. EEF1B2 and EEF1D stimulate the exchange of GDP bound to eEF1A to GTP.","predictedComplex":false,"interactors":[{"ac":"EBI-26968288","identifier":"P29692-1","identifierLink":"https://www.uniprot.org/uniprotkb/P29692-1/entry","name":"EEF1D","description":"Elongation factor 1-delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-351467","identifier":"P26641","identifierLink":"https://www.uniprot.org/uniprotkb/P26641/entry","name":"EEF1G","description":"Elongation factor 1-gamma","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43986","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-354334","identifier":"P24534","identifierLink":"https://www.uniprot.org/uniprotkb/P24534/entry","name":"EEF1B2","description":"Elongation factor 1-beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11595","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26569","complexName":"HIR histone chaperone complex, UBN1 variant","organismName":"Homo sapiens; 9606","description":"Histone chaperone complex which promotes nucleosome assembly. Cooperates with the ASF1A (Q9Y294) co-chaperone to deposit histone (H3/H4)2 tetramers on DNA for replication-independent chromatin assembly. It is currently believed that ASF1A delivers histone H3.3/H4 dimers to a HIRA/UBN1 complex, H3.3/H4 tetramerization drives the association of two HIRA/UBN1 subunits, and histone binding to DNA drives release of ASF1A and subsequent histone deposition. The complex regulates H3.3 deposition within transcriptionally active chromatin at genes, promoters, and enhancer elements.","predictedComplex":false,"interactors":[{"ac":"EBI-2795712","identifier":"Q9Y6J0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6J0/entry","name":"CABIN1","description":"Calcineurin-binding protein cabin-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15502","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2880187","identifier":"Q9NPG3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NPG3/entry","name":"UBN1","description":"Ubinuclein-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372342","identifier":"P54198","identifierLink":"https://www.uniprot.org/uniprotkb/P54198/entry","name":"HIRA","description":"Protein HIRA","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13831","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26572","complexName":"Translation elongation factor 1, EEF1A1 variant complex","organismName":"Homo sapiens; 9606","description":"Complex catalyzes the GTP-dependent binding of aminoacyl-tRNA (aa-tRNA) to ribosomes's A-site during the elongation phase of protein biosynthesis. EEF1A1 belongs to the eEF1A family and is highly homologous to EEF1A2 (Q05639).\r\n\r\nUpon elongation initiation, GTP-bound eEF1A1 forms a ternary complex with aa-tRNA of any amino acid specificity. eEF1A1-GTP-aa-tRNA subsequently delivers aa-tRNA to the ribosomal pre-A site. aa-tRNA anticodon base-pairing to the mRNA codon in the A-site, promotes GTP hydrolysis, allowing aa-tRNA to be accommodated in the A-site. Eventually, the GDP-bound eEF1A leaves the ribosome. Ribosome-catalyzed peptide bond formation extends the protein chain, transferring it from the P-site peptidyl tRNA to the A-site aa-tRNA, extending it by one amino acid.\r\n\r\nWith the exception of the hippocampus, the expression of EEF1A1 and EEF1A2 is thought to be mutually exclusive. EEF1A2 is generally restricted to muscle and brain tissue, whilst EEF1A1 is expressed in all other cell types. The tissue-specific suppression of EEF1A2 is thought to be mediated by miRNA, with loss of miRNA control an explanation for the increase in EEF1A2 expression in cancerous tissue.","predictedComplex":false,"interactors":[{"ac":"EBI-352162","identifier":"P68104","identifierLink":"https://www.uniprot.org/uniprotkb/P68104/entry","name":"EEF1A1","description":"Elongation factor 1-alpha 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64096897","identifier":"CHEBI:2651","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:2651","name":"alpha-aminoacyl-trna","description":"alpha-aminoacyl-tRNA","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26573","complexName":"Translation elongation factor 1, EEF1A2 variant complex","organismName":"Homo sapiens; 9606","description":"Complex catalyzes the GTP-dependent binding of aminoacyl-tRNA (aa-tRNA) to the ribosomes's A-site during the elongation phase of protein biosynthesis. EEF1A2 belongs to the eEF1A family and is highly homologous to EEF1A1 (P68104).\r\n\r\nUpon elongation initiation, GTP-bound eEF1A2 forms a ternary complex with aa-tRNA of any amino acid specificity. eEF1A2-GTP-aa-tRNA subsequently delivers aa-tRNA to the ribosomal pre-A site. aa-tRNA anticodon base-pairing to the mRNA codon in the A-site, promotes GTP hydrolysis, allowing aa-tRNA to be accommodated in the A-site. Eventually, the GDP-bound eEF1A2 leaves the ribosome. Ribosome-catalyzed peptide bond formation extends the protein chain, transferring it from the P-site peptidyl tRNA to the A-site aa-tRNA, extending it by one amino acid.\r\n\r\nWith the exception of the hippocampus, the expression of EEF1A2 and EEF1A1 is thought to be mutually exclusive. EEF1A2 is generally restricted to muscle and brain tissue, whilst EEF1A1 is expressed in all other cell types. The tissue-specific suppression of EEF1A2 is thought to be mediated by miRNA, with loss of miRNA control an explanation for the increase in EEF1A2 expression in cancerous tissue.","predictedComplex":false,"interactors":[{"ac":"EBI-354943","identifier":"Q05639","identifierLink":"https://www.uniprot.org/uniprotkb/Q05639/entry","name":"EEF1A2","description":"Elongation factor 1-alpha 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64096897","identifier":"CHEBI:2651","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:2651","name":"alpha-aminoacyl-trna","description":"alpha-aminoacyl-tRNA","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26574","complexName":"HIR histone chaperone complex, UBN2 variant","organismName":"Homo sapiens; 9606","description":"Histone chaperone complex which promotes nucleosome assembly. Cooperates with the ASF1A (Q9Y294) co-chaperone to deposit histone (H3/H4)2 tetramers on DNA for replication-independent chromatin assembly. It is currently believed that ASF1A delivers histone H3.3/H4 dimers to a HIRA/UBN complex, H3.3/H4 tetramerization drives the association of two HIRA/UBN subunits, and histone binding to DNA drives release of ASF1A and subsequent histone deposition. The complex regulates H3.3 deposition within transcriptionally active chromatin at genes, promoters, and enhancer elements.","predictedComplex":false,"interactors":[{"ac":"EBI-2795712","identifier":"Q9Y6J0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6J0/entry","name":"CABIN1","description":"Calcineurin-binding protein cabin-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15502","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372342","identifier":"P54198","identifierLink":"https://www.uniprot.org/uniprotkb/P54198/entry","name":"HIRA","description":"Protein HIRA","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13831","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9661773","identifier":"Q6ZU65","identifierLink":"https://www.uniprot.org/uniprotkb/Q6ZU65/entry","name":"UBN2","description":"Ubinuclein-2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26575","complexName":"ATG13-ATG14-BECN1-PIK3C3-PIK3R4-RB1CC1, autophagy initiation complex","organismName":"Homo sapiens; 9606","description":"Serine/threonine-protein kinase complex required to initiate autophagy to drive the disposal of molecular aggregates as well as damaged or superfluous organelles.\r\n\r\nComplex formed between the scaffolding subunit RB1CC1 (CPX-373) and endosomal sorting and late stage of autophagy components PIK3C3 and PIK3R4, regulatory subunit BECN1 (CPX-73) and the autophagy-specific subunit ATG14, which is responsible for autophagy-initiation and autophagy-specific functions.\r\n\r\nAutophagic dysfunction has been linked Parkinson's disease, as well several other major neurodegenerative diseases.","predictedComplex":false,"interactors":[{"ac":"EBI-1047793","identifier":"Q8TDY2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TDY2/entry","name":"RB1CC1","description":"RB1-inducible coiled-coil protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10687239","identifier":"CPX-73","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-73","name":"Phosphatidylinositol 3-kinase complex, class III, ATG14 variant","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2798775","identifier":"O75143","identifierLink":"https://www.uniprot.org/uniprotkb/O75143/entry","name":"ATG13","description":"Autophagy-related protein 13","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13430","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-908831","identifier":"O75385","identifierLink":"https://www.uniprot.org/uniprotkb/O75385/entry","name":"ULK1","description":"Serine/threonine-protein kinase ULK1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24348","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26577","complexName":"Translation elongation factor 1, EEF1A2 variant complex","organismName":"Oryctolagus cuniculus; 9986","description":"Complex catalyzes the GTP-dependent binding of aminoacyl-tRNA (aa-tRNA) to the ribosomes's A-site during the elongation phase of protein biosynthesis. EEF1A2 belongs to the eEF1A family and is highly homologous to EEF1A1 (P68105).\r\n\r\nUpon elongation initiation, GTP-bound eEF1A2 forms a ternary complex with aa-tRNA of any amino acid specificity. eEF1A2-GTP-aa-tRNA subsequently delivers aa-tRNA to the ribosomal pre-A site. aa-tRNA anticodon base-pairing to the mRNA codon in the A-site, promotes GTP hydrolysis, allowing aa-tRNA to be accommodated in the A-site. Eventually, the GDP-bound eEF1A2 leaves the ribosome. Ribosome-catalyzed peptide bond formation extends the protein chain, transferring it from the P-site peptidyl tRNA to the A-site aa-tRNA, extending it by one amino acid.\r\n\r\nThe expression of EEF1A2 and EEF1A1 is thought to be mutually exclusive.","predictedComplex":false,"interactors":[{"ac":"EBI-64096897","identifier":"CHEBI:2651","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:2651","name":"alpha-aminoacyl-trna","description":"alpha-aminoacyl-tRNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-7645815","identifier":"Q71V39","identifierLink":"https://www.uniprot.org/uniprotkb/Q71V39/entry","name":"EEF1A2","description":"Elongation factor 1-alpha 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Oryctolagus cuniculus; 9986","xrefs":[]}]},{"complexAC":"CPX-26578","complexName":"Translation elongation factor 1, EEF1A1 variant complex","organismName":"Oryctolagus cuniculus; 9986","description":"Complex catalyzes the GTP-dependent binding of aminoacyl-tRNA (aa-tRNA) to the ribosomes's A-site during the elongation phase of protein biosynthesis. EEF1A1 belongs to the eEF1A family and is highly homologous to EEF1A2 (Q71V39).\r\n\r\nUpon elongation initiation, GTP-bound eEF1A1 forms a ternary complex with aa-tRNA of any amino acid specificity. eEF1A1-GTP-aa-tRNA subsequently delivers aa-tRNA to the ribosomal pre-A site. aa-tRNA anticodon base-pairing to the mRNA codon in the A-site, promotes GTP hydrolysis, allowing aa-tRNA to be accommodated in the A-site. Eventually, the GDP-bound eEF1A1 leaves the ribosome. Ribosome-catalyzed peptide bond formation extends the protein chain, transferring it from the P-site peptidyl tRNA to the A-site aa-tRNA, extending it by one amino acid.\r\n\r\nThe expression of EEF1A1 and EEF1A2 is thought to be mutually exclusive.","predictedComplex":false,"interactors":[{"ac":"EBI-64096897","identifier":"CHEBI:2651","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:2651","name":"alpha-aminoacyl-trna","description":"alpha-aminoacyl-tRNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-7645934","identifier":"P68105","identifierLink":"https://www.uniprot.org/uniprotkb/P68105/entry","name":"EEF1A1","description":"Elongation factor 1-alpha 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Oryctolagus cuniculus; 9986","xrefs":[]}]},{"complexAC":"CPX-26579","complexName":"Pelota-HBS1L ribosome dissociation complex","organismName":"Homo sapiens; 9606","description":"Mediates dissociation of inactive 80S ribosomes associated in a non-translating, inactive pool, for example following stress-induced global shut-down of translation. Binds to the ribosomal A site. GTP hydrolysis, dissociation of HBS1L and accommodation of PELO in the ribosome, results in the binding of ABCE1 (P61221) followed by ATP-dependent subunit dissociation. Also plays a role in RNA quality control in No-Go decay (NGD) pathway, releasing ribosomes that are stalled at the 3'-end of mRNAs lacking a termination codon.","predictedComplex":false,"interactors":[{"ac":"EBI-1043580","identifier":"Q9BRX2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BRX2/entry","name":"PELO","description":"Protein pelota homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10853","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2868258","identifier":"Q9Y450","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y450/entry","name":"HBS1L","description":"HBS1-like protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-989053","identifier":"CHEBI:15996","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15996","name":"gtp","description":"guanosine triphosphate - GTP","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26580","complexName":"Bub1-Bub3 complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Promotes spindle assembly checkpoint signalling. The spindle checkpoint ensures accurate chromosome segregation by sending a signal from an unattached kinetochore to inhibit anaphase onset. Binds to kinetochores during prometaphase and metaphase. Recruitment of bub1 and bub3 to spc7 (O59757) when phosphorylated on MELT motifs by mph1 kinase (O94235) maintains the spindle checkpoint.","predictedComplex":false,"interactors":[{"ac":"EBI-1002539","identifier":"O94751","identifierLink":"https://www.uniprot.org/uniprotkb/O94751/entry","name":"bub1","description":"Spindle assembly checkpoint serine/threonine-protein kinase bub1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR14030","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1269300","identifier":"O42860","identifierLink":"https://www.uniprot.org/uniprotkb/O42860/entry","name":"bub3","description":"Spindle assembly checkpoint protein bub3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26583","complexName":"Cleavage and polyadenylation specificity factor complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Endonuclease complex required for mRNA 3' end processing to form a defined 3' end of the transcribed RNA. The complex cleaves pre-mRNAs, adds a polyadenylate tail, and triggers transcription termination. The 3' end of mature mRNAs is generated by a site-specific endonucleolytic cleavage of an internal phosphodiester bond of the primary transcript by YSH1. The upstream cleavage product generated is then polyadenylated by PAP1 to form a 50-90 adenosine tail at its 3-prime hydroxyl end, which is required for nuclear export, translation, and stability of mRNA. The downstream cleavage product is rapidly degraded. Cleavage and polyadenylation cycles are regulated by phosphorylation/dephosphorylation.","predictedComplex":false,"interactors":[{"ac":"EBI-4320127","identifier":"P13681","identifierLink":"https://www.uniprot.org/uniprotkb/P13681/entry","name":"dis2","description":"Serine/threonine-protein phosphatase PP1-1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11668","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64100259","identifier":"O43040","identifierLink":"https://www.uniprot.org/uniprotkb/O43040/entry","name":"ctf1","description":"Cleavage and termination factor 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR45735","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64100281","identifier":"O42868","identifierLink":"https://www.uniprot.org/uniprotkb/O42868/entry","name":"ssu72","description":"RNA polymerase II subunit A C-terminal domain phosphatase ssu72","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR20383","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64100303","identifier":"O13794","identifierLink":"https://www.uniprot.org/uniprotkb/O13794/entry","name":"ysh1","description":"Endoribonuclease ysh1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11203","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64100325","identifier":"Q10222","identifierLink":"https://www.uniprot.org/uniprotkb/Q10222/entry","name":"pta1","description":"mRNA cleavage and polyadenylation specificity factor complex subunit pta1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15245","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64100342","identifier":"Q9UTN4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UTN4/entry","name":"pfs2","description":"Polyadenylation factor subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR22836","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64100367","identifier":"O74740","identifierLink":"https://www.uniprot.org/uniprotkb/O74740/entry","name":"cft2","description":"Cleavage factor two protein 2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR45922","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64100389","identifier":"Q9UTD1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UTD1/entry","name":"yth1","description":"mRNA 3'-end-processing protein yth1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64100421","identifier":"Q9UT39","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UT39/entry","name":"yiq4","description":"Uncharacterized WD repeat-containing protein C824.04","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR19861","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7171599","identifier":"O74535","identifierLink":"https://www.uniprot.org/uniprotkb/O74535/entry","name":"cpsfx","description":"Cleavage and polyadenylation factor complex subunit C74.02c","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-7997221","identifier":"Q10295","identifierLink":"https://www.uniprot.org/uniprotkb/Q10295/entry","name":"pla1","description":"Poly(A) polymerase pla1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10682","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8993703","identifier":"O74733","identifierLink":"https://www.uniprot.org/uniprotkb/O74733/entry","name":"cft1","description":"Protein cft1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26584","complexName":"Cytoplasmic histone acetyltransferase type B, HAT1 complex","organismName":"Homo sapiens; 9606","description":"Type B histone acetyltransferase (HAT-B) complex capable of acetylating both free histones and nucleosomes by transferring an acetyl group from acetyl coenzyme A (CHEBI:15351) to acetyllysine (CHEBI:17752). Required for chromatin assembly following DNA replication. Complex primarily acetylates Lys-12 of histone H4 (H4K12). Additionally, HAT1 can also acetylate H4K5 while RBBP7 has been shown to increase the catalytic activity of the HAT complex's activity as well as its specificity for H4K12. \r\n\r\nLocated primarily in the cytoplasm and thought to play more of a house-keeping role, the complex is responsible for acetylating newly synthesized histones H3, H4 prior to their assembly into nucleosome. In addition to the complex's catalytic activity, its association with histones H4 (P62805) and H3 (P68431) is thought to extend to a role in nuclear import of these histones and their subsequent delivery to chromatin assembly factors.","predictedComplex":false,"interactors":[{"ac":"EBI-2339359","identifier":"O14929","identifierLink":"https://www.uniprot.org/uniprotkb/O14929/entry","name":"HAT1","description":"Histone acetyltransferase type B catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12046","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352227","identifier":"Q16576","identifierLink":"https://www.uniprot.org/uniprotkb/Q16576/entry","name":"RBBP7","description":"Histone-binding protein RBBP7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26586","complexName":"Serine/threonine-protein phosphatase 2A complex, B55 beta variant","organismName":"Homo sapiens; 9606","description":"Serine/threonine protein phosphatase complex with a central role in the control of cell cycle progression through mitosis. It also regulates the entry into mitosis at the G2/M checkpoint.","predictedComplex":false,"interactors":[{"ac":"EBI-1052159","identifier":"Q00005","identifierLink":"https://www.uniprot.org/uniprotkb/Q00005/entry","name":"PPP2R2B","description":"Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11871","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302388","identifier":"P30153","identifierLink":"https://www.uniprot.org/uniprotkb/P30153/entry","name":"PPP2R1A","description":"Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712311","identifier":"P67775","identifierLink":"https://www.uniprot.org/uniprotkb/P67775/entry","name":"PPP2CA","description":"Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26587","complexName":"Serine/threonine-protein phosphatase 2A complex, B55 gamma variant","organismName":"Homo sapiens; 9606","description":"Serine/threonine protein phosphatase complex with a central role in the control of cell cycle progression through mitosis. It also regulates the entry into mitosis at the G2/M checkpoint.","predictedComplex":false,"interactors":[{"ac":"EBI-1774058","identifier":"Q9Y2T4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2T4/entry","name":"PPP2R2C","description":"Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B gamma isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11871","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302388","identifier":"P30153","identifierLink":"https://www.uniprot.org/uniprotkb/P30153/entry","name":"PPP2R1A","description":"Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712311","identifier":"P67775","identifierLink":"https://www.uniprot.org/uniprotkb/P67775/entry","name":"PPP2CA","description":"Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26588","complexName":"Palmitoyltransferase complex, GOLGA7-ZDHHC9","organismName":"Homo sapiens; 9606","description":"Cystine palmitoyltransferase complex which catalyzes the addition of palmitate specifically for C-terminal HRAS (P01112) and NRAS (P01111). Palmitoylation of proteins occurs through a two step reaction: the autopalmitoylation of the enzyme to create a palmitoyl-ZDHHC9 intermediate followed by the transfer of the palmitoyl moiety to the RAS substrate. Palmitoyl-CoA serves as the palmitate donor.","predictedComplex":false,"interactors":[{"ac":"EBI-12690113","identifier":"Q9Y397","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y397/entry","name":"ZDHHC9","description":"Palmitoyltransferase ZDHHC9","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22883","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4403685","identifier":"Q7Z5G4","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z5G4/entry","name":"GOLGA7","description":"Golgin subfamily A member 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13254","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26589","complexName":"MUS81-EME1 structure-specific endonuclease complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Structure-specific endonuclease that plays an important role in rescuing stalled replication forks and resolving the mitotic recombination intermediates. Has a substrate preference for branched DNA structures with a 5' end at the branch nick with cleavage probably occurring approximately half a helical turn upstream of the free 5-prime end. Resolves the four-way Holliday junction (HJ) in which the two recombining DNAs are covalently-linked junctions in crossover formation during meiotic recombination.","predictedComplex":false,"interactors":[{"ac":"EBI-7326720","identifier":"P87231","identifierLink":"https://www.uniprot.org/uniprotkb/P87231/entry","name":"mus81","description":"Crossover junction endonuclease mus81","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13451","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7326747","identifier":"Q9C103","identifierLink":"https://www.uniprot.org/uniprotkb/Q9C103/entry","name":"eme1","description":"Crossover junction endonuclease eme1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR21077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-2716","complexName":"Eukaryotic translation initiation factor 2 complex","organismName":"Homo sapiens; 9606","description":"Guides the initiator methionyl-tRNA to the 40S ribosomal subunit (CPX-5223) as a eukaryotic translation initiation factor 2 (eIF2).GTP.Met-tRNAiMet) carrier complex. The resulting 43S complex, which also includes eIF3 (CPX-6036) and eIF1A, binds at or near the 5'-end of capped eukaryotic messenger RNAs. Recognition of the AUG codon translational start site by Met-tRNAi(Met) is accompanied by GTP hydrolysis (stimulated by the eIF5 complex), which subsequently releases Met-tRNA to the ribosomal peptidyl site, and converts eIF2-GTP to eIF2-GDP. Binding of nucleotide exchange factor eIF2B complex (CPX-429) replaces GDP again for GTP. This activity is inhibited when phosphorylated EIF2S1 binds to EIF2S3. \r\n\r\nMutations in EIF2S3 affects complex formation and the development of severe neurological diseases.","predictedComplex":false,"interactors":[{"ac":"EBI-1054228","identifier":"P41091","identifierLink":"https://www.uniprot.org/uniprotkb/P41091/entry","name":"EIF2S3","description":"Eukaryotic translation initiation factor 2 subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR42854","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1056162","identifier":"P05198","identifierLink":"https://www.uniprot.org/uniprotkb/P05198/entry","name":"EIF2S1","description":"Eukaryotic translation initiation factor 2 subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10602","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14022093","identifier":"CHEBI:33699","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:33699","name":"messenger rna","description":"messenger RNA","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-66842664","identifier":"CHEBI:16635","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16635","name":"met-trna(met)","description":"Met-tRNA(Met)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-711977","identifier":"P20042","identifierLink":"https://www.uniprot.org/uniprotkb/P20042/entry","name":"EIF2S2","description":"Eukaryotic translation initiation factor 2 subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23001","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-989053","identifier":"CHEBI:15996","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15996","name":"gtp","description":"guanosine triphosphate - GTP","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26592","complexName":"Box H/ACA ribonucleoprotein complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Pseudouridine synthesis complex that converts uridine into pseudouridine at numerous specific sites within ribosomal RNAs (rRNAs) and spliceosomal small nuclear RNAs (snRNAs), isomerizing the uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine residues may serve to stabilize the conformation of rRNAs.","predictedComplex":false,"interactors":[{"ac":"EBI-16413110","identifier":"CHEBI:133336","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:133336","name":"h/aca box small nucleolar rna","description":"H/ACA box small nucleolar RNA","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-65655881","identifier":"Q9P7H0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P7H0/entry","name":"nhp2","description":"H/ACA ribonucleoprotein complex subunit nhp2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-65659296","identifier":"O14007","identifierLink":"https://www.uniprot.org/uniprotkb/O14007/entry","name":"cbf5","description":"H/ACA ribonucleoprotein complex subunit cbf5","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23127","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-65661770","identifier":"Q9P7M5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P7M5/entry","name":"nop10","description":"H/ACA ribonucleoprotein complex subunit nop10","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-65666586","identifier":"Q06975","identifierLink":"https://www.uniprot.org/uniprotkb/Q06975/entry","name":"gar1","description":"H/ACA ribonucleoprotein complex subunit gar1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23237","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26593","complexName":"tRNA-specific adenosine-34 deaminase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Deaminates adenosine-34 (wobble position) to inosine in double-stranded tRNA. When present at the wobble position, inosine can pair degenerately with uracil, cytosine, or adenosine, enabling a single tRNA to recognize up to three different codons.","predictedComplex":false,"interactors":[{"ac":"EBI-2478877","identifier":"O94642","identifierLink":"https://www.uniprot.org/uniprotkb/O94642/entry","name":"tad2","description":"tRNA-specific adenosine deaminase subunit tad2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11079","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2478895","identifier":"Q9P7N4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P7N4/entry","name":"tad3","description":"tRNA-specific adenosine deaminase subunit tad3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11079","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26594","complexName":"Eukaryotic translation initiation factor 2 complex, Eif2s3x variant","organismName":"Mus musculus; 10090","description":"Guides the initiator methionyl-tRNA to the 40S ribosomal subunit (CPX-5261) as a eukaryotic translation initiation factor 2 (eIF2).GTP.Met-tRNAiMet) carrier complex. The resulting 43S complex, which also includes eIF3 and eIF1A, binds at or near the 5'-end of capped eukaryotic messenger RNAs. Recognition of the AUG codon translational start site by Met-tRNAi(Met) is accompanied by GTP hydrolysis (stimulated by the eIF5 complex), which subsequently releases Met-tRNA to the ribosomal peptidyl site, and converts eIF2-GTP to eIF2-GDP. Binding of nucleotide exchange factor eIF2B complex replaces GDP again for GTP. This activity is inhibited when phosphorylated Eif2s1 binds to Eif2s3x. \r\n\r\nThe gamma subunit in mouse eIF2 complex can be either X-linked (this complex) or Y-linked (CPX-26595). Eif2s3x along with its paralog, Eif2s3y (Q9Z0N2) is suspected to contribute to spermatogenesis up to the round spermatid stage. The two paralogs are functionally interchangeable in spermatogenesis, but differ in expression, with the stronger Eif2s3y expression in spermatogonia thought to be required for subsequent meiotic stages but not for mitotic proliferation.","predictedComplex":false,"interactors":[{"ac":"EBI-1202234","identifier":"Q6ZWX6","identifierLink":"https://www.uniprot.org/uniprotkb/Q6ZWX6/entry","name":"Eif2s1","description":"Eukaryotic translation initiation factor 2 subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10602","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14022093","identifier":"CHEBI:33699","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:33699","name":"messenger rna","description":"messenger RNA","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2527165","identifier":"Q99L45","identifierLink":"https://www.uniprot.org/uniprotkb/Q99L45/entry","name":"Eif2s2","description":"Eukaryotic translation initiation factor 2 subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23001","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2642789","identifier":"Q9Z0N1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0N1/entry","name":"Eif2s3x","description":"Eukaryotic translation initiation factor 2 subunit 3, X-linked","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR42854","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-66842664","identifier":"CHEBI:16635","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16635","name":"met-trna(met)","description":"Met-tRNA(Met)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-989053","identifier":"CHEBI:15996","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15996","name":"gtp","description":"guanosine triphosphate - GTP","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26595","complexName":"Eukaryotic translation initiation factor 2 complex, Eif2s3y variant","organismName":"Mus musculus; 10090","description":"Guides the initiator methionyl-tRNA to the 40S ribosomal subunit (CPX-5261) as a eukaryotic translation initiation factor 2 (eIF2).GTP.Met-tRNAiMet) carrier complex. The resulting 43S complex, which also includes eIF3 and eIF1A, binds at or near the 5'-end of capped eukaryotic messenger RNAs. Recognition of the AUG codon translational start site by Met-tRNAi(Met) is accompanied by GTP hydrolysis (stimulated by the eIF5 complex), which subsequently releases Met-tRNA to the ribosomal peptidyl site, and converts eIF2-GTP to eIF2-GDP. Binding of nucleotide exchange factor eIF2B complex replaces GDP again for GTP. This activity is inhibited when phosphorylated Eif2s1 binds to Eif2s3x. \r\n\r\nThe gamma subunit in mouse eIF2 complex can be either X-linked (CPX-26594) or Y-linked (this complex). Eif2s3x (Q9Z0N1) along with its paralog, Eif2s3y is suspected to contribute to spermatogenesis up to the round spermatid stage. The two paralogs are functionally interchangeable in spermatogenesis, but differ in expression, with the stronger Eif2s3y expression in spermatogonia thought to be required for subsequent meiotic stages but not for mitotic proliferation.","predictedComplex":false,"interactors":[{"ac":"EBI-1202234","identifier":"Q6ZWX6","identifierLink":"https://www.uniprot.org/uniprotkb/Q6ZWX6/entry","name":"Eif2s1","description":"Eukaryotic translation initiation factor 2 subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10602","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14022093","identifier":"CHEBI:33699","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:33699","name":"messenger rna","description":"messenger RNA","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-2527165","identifier":"Q99L45","identifierLink":"https://www.uniprot.org/uniprotkb/Q99L45/entry","name":"Eif2s2","description":"Eukaryotic translation initiation factor 2 subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23001","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30866268","identifier":"Q9Z0N2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0N2/entry","name":"Eif2s3y","description":"Eukaryotic translation initiation factor 2 subunit 3, Y-linked","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR42854","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-66842664","identifier":"CHEBI:16635","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:16635","name":"met-trna(met)","description":"Met-tRNA(Met)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-989053","identifier":"CHEBI:15996","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15996","name":"gtp","description":"guanosine triphosphate - GTP","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26596","complexName":"CYP8-TUP11/12 corepressor complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Corepressor complex with a role in gene regulation,","predictedComplex":false,"interactors":[{"ac":"EBI-66892472","identifier":"Q9UUG8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UUG8/entry","name":"tup12","description":"Transcriptional repressor tup12","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR22847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-66892497","identifier":"Q09715","identifierLink":"https://www.uniprot.org/uniprotkb/Q09715/entry","name":"tup11","description":"Transcriptional repressor tup11","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR22847","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-66892546","identifier":"O60184","identifierLink":"https://www.uniprot.org/uniprotkb/O60184/entry","name":"ssn6","description":"General transcriptional corepressor ssn6","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR14017","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26599","complexName":"Nuclear histone-HAT1-associated multichaperone complex, ASF1B variant","organismName":"Homo sapiens; 9606","description":"Type B histone acetyltransferase (HAT-B)  containing multichaperone complex capable of acetylating both free histones and nucleosomes by transferring an acetyl group from acetyl coenzyme A (CHEBI:15351) to acetyllysine (CHEBI:17752). Required for chromatin assembly following DNA replication. Complex both directly and indirectly influences genome stability and integrity, gene transcription, as well as DNA replication and repair.\r\n\r\nComplex buffers newly formed soluble H3-H4 dimers accumulated during replication stress, possibly also re-actylating evicted H3-H4 dimers. Both splicing variants of NASP (testicular (tNASP, P49321-1 and somatic (sNASP, P49321-2, part of this multi-chaperone complex) are required to maintain a soluble pool of the H3-H4 dimers during the cell cyle and shield them from degradation by chaperone-mediated autophagy.","predictedComplex":false,"interactors":[{"ac":"EBI-1055650","identifier":"Q9NVP2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NVP2/entry","name":"ASF1B","description":"Histone chaperone ASF1B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2339359","identifier":"O14929","identifierLink":"https://www.uniprot.org/uniprotkb/O14929/entry","name":"HAT1","description":"Histone acetyltransferase type B catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12046","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352227","identifier":"Q16576","identifierLink":"https://www.uniprot.org/uniprotkb/Q16576/entry","name":"RBBP7","description":"Histone-binding protein RBBP7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7038920","identifier":"P49321-2","identifierLink":"https://www.uniprot.org/uniprotkb/P49321-2/entry","name":"NASP","description":"Nuclear autoantigenic sperm protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-26600","complexName":"tRNA (cytosine(32)-N(3))-methytransferase complex","organismName":"Homo sapiens; 9606","description":"S-adenosyl-L-methionine (SAM)-dependent methyltransferase responsible for N3-methylcytidine modification of cytosine-32 of the tRNA anticodon loop of cytosolic tRNA(Ser). SARS1 acts as the tRNASer substrate selection factor for METTL6, increasing its methylation activity. The activity of METTL6 does not appears to depend on the serylation activity of SARS1.","predictedComplex":false,"interactors":[{"ac":"EBI-1053431","identifier":"P49591","identifierLink":"https://www.uniprot.org/uniprotkb/P49591/entry","name":"SARS1","description":"Serine--tRNA ligase, cytoplasmic","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11778","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-17861723","identifier":"Q8TCB7","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TCB7/entry","name":"METTL6","description":"tRNA N(3)-cytidine methyltransferase METTL6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22809","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30813205","identifier":"CHEBI:59789","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:59789","name":"s-adenosyl-l-methionine zwitterion","description":"S-adenosyl-L-methionine zwitterion","stochiometry":"minValue: 1, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26601","complexName":"Nuclear histone-HAT1-associated multichaperone complex, ASF1A variant","organismName":"Homo sapiens; 9606","description":"Type B histone acetyltransferase (HAT-B)-containing multichaperone complex capable of acetylating both free histones and nucleosomes by transferring an acetyl group from acetyl coenzyme A (CHEBI:15351) to acetyllysine (CHEBI:17752). Required for chromatin assembly following DNA replication. Complex both directly and indirectly influences genome stability and integrity, gene transcription, as well as DNA replication and repair.\r\n\r\nComplex buffers newly formed soluble H3-H4 dimers accumulated during replication stress, possibly also re-actylating evicted H3-H4 dimers. Both splicing variants of NASP (testicular (tNASP, P49321-1 and somatic (sNASP, P49321-2, part of this multi-chaperone complex) are required to maintain a soluble pool of the H3-H4 dimers during the cell cyle and shield them from degradation by chaperone-mediated autophagy.","predictedComplex":false,"interactors":[{"ac":"EBI-2339359","identifier":"O14929","identifierLink":"https://www.uniprot.org/uniprotkb/O14929/entry","name":"HAT1","description":"Histone acetyltransferase type B catalytic subunit","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12046","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-352227","identifier":"Q16576","identifierLink":"https://www.uniprot.org/uniprotkb/Q16576/entry","name":"RBBP7","description":"Histone-binding protein RBBP7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7038920","identifier":"P49321-2","identifierLink":"https://www.uniprot.org/uniprotkb/P49321-2/entry","name":"NASP","description":"Nuclear autoantigenic sperm protein","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-749553","identifier":"Q9Y294","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y294/entry","name":"ASF1A","description":"Histone chaperone ASF1A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26602","complexName":"DOP1A-MON2, golgi-endosome traffic complex","organismName":"Homo sapiens; 9606","description":"Phosphatidic acid and phosphatidylinositol-4-phoshate (PI4P)-dependent kinesin-1 adaptor complex which regulates membrane trafficking of cargo proteins between the late Golgi and early endosomes and is crucial for the peripheral positioning of organelles. The DOP1A-MON2 complex promotes centrifugally biased bidirectional transport, whilst inhibiting centripetal-membrane-trafficking and organelle positioning.\r\n\r\nMissense mutations in the extreme MON2 C-terminal end which interacts with DOP1A is thought to cause a deficit in golgi-endosome protein movement and has been implicated in congenital neurodevelopmental disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-20838127","identifier":"Q5JWR5","identifierLink":"https://www.uniprot.org/uniprotkb/Q5JWR5/entry","name":"DOP1A","description":"Protein DOP1A","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14042","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358882","identifier":"Q7Z3U7","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z3U7/entry","name":"MON2","description":"Protein MON2 homolog","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10663","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26603","complexName":"ATP9A-DOP1B-MON2, golgi transporter complex","organismName":"Homo sapiens; 9606","description":"Plays a role in endosomal recycling. Enables SNX3 (O60493) retromer-mediated endosomal sorting of WLS (Q5T9L3), which transports WNT morphogens to the cell surface in developing tissues. Complex is involved in the formation of endosomal carriers that direct WLS trafficking from the endoplasmic reticulum back to Golgi, and away from lysosomal degradation.\r\n\r\nMON2 and ATP9A mutations have been implicated in neurodevelopmental disorders, characterized by global developmental delay.","predictedComplex":false,"interactors":[{"ac":"EBI-2878108","identifier":"O75110","identifierLink":"https://www.uniprot.org/uniprotkb/O75110/entry","name":"ATP9A","description":"Probable phospholipid-transporting ATPase IIA","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358882","identifier":"Q7Z3U7","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Z3U7/entry","name":"MON2","description":"Protein MON2 homolog","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10663","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4403087","identifier":"Q9Y3R5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3R5/entry","name":"DOP1B","description":"Protein DOP1B","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14042","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26604","complexName":"bZIP transcription factor complex, atf1-pcr1","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Transcription factor complex which activates the expression of stress response genes.","predictedComplex":false,"interactors":[{"ac":"EBI-3861527","identifier":"P52890","identifierLink":"https://www.uniprot.org/uniprotkb/P52890/entry","name":"atf1","description":"Transcription factor atf1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR19304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-66897566","identifier":"Q09926","identifierLink":"https://www.uniprot.org/uniprotkb/Q09926/entry","name":"pcr1","description":"Transcription factor pcr1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]}]},{"complexAC":"CPX-26605","complexName":"HDA2-SAEG-1-SAEG-2 histone deacetylase complex","organismName":"Caenorhabditis elegans; 6239","description":"Class I histone deacetylase complex specifically recruited by activated nuclear egl-4 (O76360) to regulate gene expression related to behavioral and physiological responses to cGMP, including the regulation of the egg-laying rate and body length.","predictedComplex":false,"interactors":[{"ac":"EBI-314673","identifier":"Q09440","identifierLink":"https://www.uniprot.org/uniprotkb/Q09440/entry","name":"hda-2","description":"Putative histone deacetylase 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-66899780","identifier":"Q03615","identifierLink":"https://www.uniprot.org/uniprotkb/Q03615/entry","name":"saeg-2","description":"Suppressor of activated egl-4 protein 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR23399","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6748186","identifier":"Q20733","identifierLink":"https://www.uniprot.org/uniprotkb/Q20733/entry","name":"saeg-1","description":"Suppressor of activated egl-4 protein 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR16089","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26608","complexName":"ASF1B-NASP, histone H3-H4 co-chaperone complex","organismName":"Homo sapiens; 9606","description":"Histone H3-H4 chaperone complex. Binds and stabilizes unbound histone H3-H4 to maintain a soluble reservoir and modulate degradation by autophagy. Both splicing variants of NASP (testicular (tNASP, P49321-1 and somatic (sNASP, P49321-2, part of this complex) are essential in maintaining a soluble pool of the H3-H4 dimers during the cell cyle and shield them from degradation by chaperone-mediated autophagy.","predictedComplex":false,"interactors":[{"ac":"EBI-1055650","identifier":"Q9NVP2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NVP2/entry","name":"ASF1B","description":"Histone chaperone ASF1B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7038920","identifier":"P49321-2","identifierLink":"https://www.uniprot.org/uniprotkb/P49321-2/entry","name":"NASP","description":"Nuclear autoantigenic sperm protein","stochiometry":"minValue: 1, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-26609","complexName":"ASF1A-NASP, histone H3-H4 co-chaperone complex","organismName":"Homo sapiens; 9606","description":"Histone H3-H4 chaperone complex. Binds and stabilizes unbound histone H3-H4 to maintain a soluble reservoir and modulate degradation by autophagy. Both splicing variants of NASP (testicular (tNASP, P49321-1 and somatic (sNASP, P49321-2, part of this complex) are essential in maintaining a soluble pool of the H3-H4 dimers during the cell cyle and shield them from degradation by chaperone-mediated autophagy.","predictedComplex":false,"interactors":[{"ac":"EBI-7038920","identifier":"P49321-2","identifierLink":"https://www.uniprot.org/uniprotkb/P49321-2/entry","name":"NASP","description":"Nuclear autoantigenic sperm protein","stochiometry":"minValue: 1, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-749553","identifier":"Q9Y294","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y294/entry","name":"ASF1A","description":"Histone chaperone ASF1A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26610","complexName":"slx1-slx4 structure-specific endonuclease complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"A structure-specific DNA endonuclease that cleaves the phosphodiester backbone on the 3'-side of the DNA branchpoint of branched DNA substrates including stem-loops and Y-structures, replication forks, 5'- and 3'-flaps, and nicked or intact Holliday junctions and is therefore involved in DNA recombination and repair. It is involved in rDNA copy number regulation and appears to act at the termination of rDNA replication.","predictedComplex":false,"interactors":[{"ac":"EBI-67092731","identifier":"Q9P6M0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P6M0/entry","name":"slx4","description":"Structure-specific endonuclease subunit slx4","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-67092774","identifier":"Q9P7M3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P7M3/entry","name":"slx1","description":"Structure-specific endonuclease subunit slx1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR20208","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9097897","identifier":"CHEBI:60240","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:60240","name":"divalent metal cation","description":"divalent metal cation","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26611","complexName":"RNA decapping and exonuclease complex","organismName":"Drosophila melanogaster; 7227","description":"Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. The activity of this complex is tightly regulated to prevent premature degradation of the transcript.","predictedComplex":false,"interactors":[{"ac":"EBI-149103","identifier":"Q9W1H5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W1H5/entry","name":"DCP1","description":null,"stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR16290","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-151223","identifier":"Q9VVI2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVI2/entry","name":"Edc3","description":"Enhancer of mRNA-decapping protein 3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13612","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-156384","identifier":"Q9VKK1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VKK1/entry","name":"Ge-1","description":"Enhancer of mRNA-decapping protein 4 homolog","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15598","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2108819","identifier":"Q5U127","identifierLink":"https://www.uniprot.org/uniprotkb/Q5U127/entry","name":"DCP2","description":"m7GpppN-mRNA hydrolase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23114","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-300281","identifier":"P23128","identifierLink":"https://www.uniprot.org/uniprotkb/P23128/entry","name":"me31B","description":"ATP-dependent RNA helicase me31b","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR47960","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67093065","identifier":"E1JJR3","identifierLink":"https://www.uniprot.org/uniprotkb/E1JJR3/entry","name":"pcm","description":"5'-3' exoribonuclease 1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12341","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26612","complexName":"Cytosolic ASF1A-IPO4 histone H3-H4 chaperone-importin complex","organismName":"Homo sapiens; 9606","description":"ASF1A, a histone chaperone, forms a cytosolic complex with Importin-4 (IPO4) and newly synthesized histones H3 and H4, facilitating their transport into the nucleus for chromatin assembly. Complex specifically recognizes histone H3 monomethylated at lysine 9 (H3K9me1) and histone H4 diacetylated at lysines 5 and 12 (H4K5ac, H4K12ac), modifications characteristic of newly made histones. These post-translational marks are acquired in a stepwise fashion during histone maturation, beginning shortly after synthesis, and help guide the histones through their processing and transport stages. ASF1A not only shields the H3-H4 dimer to prevent premature tetramer formation but also facilitates its binding to IPO4, ensuring proper nuclear import. This sequential, modification-dependent process ensures that only properly processed histones are delivered into the nucleus for incorporation into chromatin.","predictedComplex":false,"interactors":[{"ac":"EBI-395967","identifier":"Q8TEX9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TEX9/entry","name":"IPO4","description":"Importin-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67104822","identifier":"CHEBI:234587","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:234587","name":"histone h3","description":"Histone H3","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-67104825","identifier":"CHEBI:234588","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:234588","name":"histone h4","description":"Histone H4","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-749553","identifier":"Q9Y294","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y294/entry","name":"ASF1A","description":"Histone chaperone ASF1A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26613","complexName":"Cytosolic ASF1B-IPO4 histone H3-H4 chaperone-importin complex","organismName":"Homo sapiens; 9606","description":"ASF1B, a histone chaperone, forms a cytosolic complex with Importin-4 (IPO4) and newly synthesized histones H3 and H4, facilitating their transport into the nucleus for chromatin assembly. Complex components specifically recognize histone H3 monomethylated at lysine 9 (H3K9me1) and histone H4 diacetylated at lysines 5 and 12 (H4K5ac, H4K12ac), modifications characteristic of newly made histones. These post-translational marks are acquired in a stepwise fashion during histone maturation, beginning shortly after synthesis, and help guide the histones through their processing and transport stages. ASF1B not only shields the H3-H4 dimer to prevent premature tetramer formation but also facilitates its binding to IPO4, ensuring proper nuclear import. This sequential, modification-dependent process ensures that only properly processed histones are delivered into the nucleus for incorporation into chromatin.","predictedComplex":false,"interactors":[{"ac":"EBI-1055650","identifier":"Q9NVP2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NVP2/entry","name":"ASF1B","description":"Histone chaperone ASF1B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12040","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395967","identifier":"Q8TEX9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TEX9/entry","name":"IPO4","description":"Importin-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10527","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67104822","identifier":"CHEBI:234587","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:234587","name":"histone h3","description":"Histone H3","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-67104825","identifier":"CHEBI:234588","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:234588","name":"histone h4","description":"Histone H4","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26614","complexName":"NDC80 complex","organismName":"Drosophila melanogaster; 7227","description":"Crucial for the stable kinetochore-microtubule attachments that are needed to sustain the centromere tensions involved in achieving proper chromosome alignment in eukaryotic cells, with a role in chromosome alignment and microtubule-dependent control of MAD1-MAD2 and dynein complexes at kinetochores.","predictedComplex":false,"interactors":[{"ac":"EBI-168789","identifier":"Q9VM45","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VM45/entry","name":"Nuf2","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-179943","identifier":"Q9VYB1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VYB1/entry","name":"Ndc80","description":"Kinetochore protein NDC80","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10643","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67093163","identifier":"Q6IKI1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6IKI1/entry","name":"Kmn2","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-97707","identifier":"Q9V3V7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9V3V7/entry","name":"Spc25","description":"Kinetochore protein Spc25","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]}]},{"complexAC":"CPX-26617","complexName":"SEC62-SEC63 complex","organismName":"Drosophila melanogaster; 7227","description":"Required for post-translational translocation of nascent proteins into the endoplasmic reticulum. Plays a crucial role in targeting of the signal recognition particle-independent protein substrate to the protein-conducting channel and also in the assembly of the post-translocon complex.","predictedComplex":false,"interactors":[{"ac":"EBI-118768","identifier":"Q9VJW1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VJW1/entry","name":"Sec71","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10663","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-119289","identifier":"Q9VS57","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VS57/entry","name":"Sec63","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR24075","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67104306","identifier":"Q9VL49","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VL49/entry","name":"Trp1","description":"Translocation protein SEC62","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12443","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26618","complexName":"SEC62-SEC63 complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Required for post-translational translocation of nascent proteins into the endoplasmic reticulum. Plays a crucial role in targeting of the signal recognition particle-independent protein substrate to the protein-conducting channel and also in the assembly of the post-translocon complex.","predictedComplex":false,"interactors":[{"ac":"EBI-21242328","identifier":"O13787","identifierLink":"https://www.uniprot.org/uniprotkb/O13787/entry","name":"sec62","description":"Translocation protein sec62","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12443","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67104378","identifier":"Q9UUA4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UUA4/entry","name":"sec66","description":"Translocation protein sec66","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR28229","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67104388","identifier":"O14085","identifierLink":"https://www.uniprot.org/uniprotkb/O14085/entry","name":"sec67","description":"ER protein translocation subcomplex subunit sec67","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR46035","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67126442","identifier":"Q9HGN7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HGN7/entry","name":"sec63","description":"Translocation protein sec63","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR24075","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26621","complexName":"ATP citrate synthase complex","organismName":"Homo sapiens; 9606","description":"Catalyzes the synthesis of cytosolic acetyl coenzyme A (acetyl-CoA), a fundamental cellular building block. Complex cleaves citrate into oxaloacetate and acetyl-acetyl-CoA, the latter serving as common substrate in multiple biochemical reactions in protein, carbohydrate and lipid metabolism.\r\n\r\nAberrant activity of ACLY has been linked to cardiovascular diseases, metabolic disorders and many cancers.","predictedComplex":false,"interactors":[{"ac":"EBI-1042794","identifier":"P53396","identifierLink":"https://www.uniprot.org/uniprotkb/P53396/entry","name":"ACLY","description":"ATP-citrate synthase","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23118","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-967760","identifier":"CHEBI:18420","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:18420","name":"magnesium(2+)","description":"Magnesium(2+)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26622","complexName":"tat-5-mon-2-pad-1, golgi transporter complex","organismName":"Caenorhabditis elegans; 6239","description":"Plays a role in endosomal recycling, as well as an important role in\r\nregulating lipid asymmetry and inhibiting extracellular vesicle formation. Enables snx-3 (Q9XW41) retromer-mediated endosomal sorting of mig-14 (Q7YWX7), which transports WNT morphogens to the cell surface in developing tissues. Complex is involved in the formation of endosomal carriers that direct mig-14 trafficking from the endoplasmic reticulum back to Golgi, and away from lysosomal degradation.\r\n\r\nDepletion of pad-1 results in embryonic lethality, whilst depleted tat-5 results in gastrulation defects and embryonic lethality.","predictedComplex":false,"interactors":[{"ac":"EBI-67105069","identifier":"Q9XW10","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XW10/entry","name":"pad-1","description":"Protein pad-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR14042","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67105089","identifier":"Q19338","identifierLink":"https://www.uniprot.org/uniprotkb/Q19338/entry","name":"mon-2","description":"Monensin-resistant homolog 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR10663","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-67105109","identifier":"G5EBH1","identifierLink":"https://www.uniprot.org/uniprotkb/G5EBH1/entry","name":"tat-5","description":"Probable phospholipid-transporting ATPase tat-5","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1028","complexName":"NEO1-DOP1-MON2 golgi transporter complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Functions in vesicle trafficking within the Golgi/endosomal system to regulate retrograde recycling of cargoes from endosomes back to and within the Golgi. In contrast to the DOP1-MON2 interaction in humans, DOP1 weakly interacts with MON2 in yeast, and therefore the complex's role in membrane remodelling at the tubular endosomal network and the trans-Golgi network interface is unclear.","predictedComplex":false,"interactors":[{"ac":"EBI-28333","identifier":"P48563","identifierLink":"https://www.uniprot.org/uniprotkb/P48563/entry","name":"MON2","description":"Protein MON2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10663","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3137","identifier":"P40527","identifierLink":"https://www.uniprot.org/uniprotkb/P40527/entry","name":"NEO1","description":"Phospholipid-transporting ATPase NEO1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR24092","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34442","identifier":"Q03921","identifierLink":"https://www.uniprot.org/uniprotkb/Q03921/entry","name":"DOP1","description":"Protein DOP1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR14042","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26623","complexName":"TDRD3-TOP3B type IA topoisomerase complex","organismName":"Drosophila melanogaster; 7227","description":"DNA/RNA type IA topoisomerase family, which transiently cleaves and rejoins one strand of the DNA duplex, relaxing  supercoiled DNA and torsional tension of DNA introduced during DNA replication and transcription, resolving recombination intermediates during meiosis and DNA repair. Transiently traps the 5' end of the cleaved DNA by covalent bonding via catalytic tyrosine residues.","predictedComplex":false,"interactors":[{"ac":"EBI-3411133","identifier":"Q9VUH8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VUH8/entry","name":"Tdrd3","description":"Survival of motor neuron-related-splicing factor 30","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13681","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8283672","identifier":"O96651","identifierLink":"https://www.uniprot.org/uniprotkb/O96651/entry","name":"Top3beta","description":"DNA topoisomerase 3-beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11390","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8187","complexName":"Y+LAT1-4F2 heteromeric amino acid transporter complex","organismName":"Homo sapiens; 9606","description":"L-type amino acid transporter which catalyses the transmembrane electroneutral antiport  of cationic and neutral amino acids, such as phenylalanine, tyrosine, leucine, histidine, methionine, tryptophan, valine, isoleucine and alanine, and also cysteine in a sodium-dependent manner. Asymmetric antiporter, causing the basolateral efflux of cationic amino acids and influx of neutral amino acids together with sodium ions.","predictedComplex":false,"interactors":[{"ac":"EBI-2849880","identifier":"Q9UM01","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UM01/entry","name":"SLC7A7","description":"Y+L amino acid transporter 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11785","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-702356","identifier":"P08195","identifierLink":"https://www.uniprot.org/uniprotkb/P08195/entry","name":"SLC3A2","description":"Amino acid transporter heavy chain SLC3A2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8188","complexName":"Y+LAT2-4F2 heteromeric amino acid transporter complex","organismName":"Homo sapiens; 9606","description":"L-type amino acid transporter which catalyses the transmembrane electroneutral antiport  of cationic and neutral amino acids, such as phenylalanine, tyrosine, leucine, histidine, methionine, tryptophan, valine, isoleucine and alanine, and also cysteine in a sodium-dependent manner. Asymmetric antiporter, causing the basolateral efflux of cationic amino acids and influx of neutral amino acids together with sodium ions.","predictedComplex":false,"interactors":[{"ac":"EBI-2880595","identifier":"Q92536","identifierLink":"https://www.uniprot.org/uniprotkb/Q92536/entry","name":"SLC7A6","description":"Y+L amino acid transporter 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11785","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-702356","identifier":"P08195","identifierLink":"https://www.uniprot.org/uniprotkb/P08195/entry","name":"SLC3A2","description":"Amino acid transporter heavy chain SLC3A2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2210","complexName":"Subcortical maternal complex","organismName":"Homo sapiens; 9606","description":"Essential role in zygote progression beyond the first embryonic cell divisions potentially by controlling spindle positioning through regulation of subcortical F-actin. It is present in the subcortex of eggs and preimplantation embryos and is excluded from regions of cell-cell contact in the cleavage-stage embryo. It segregates to the outer cells of morulae and blastocysts, and is absent in the embryo inner cell mass.","predictedComplex":false,"interactors":[{"ac":"EBI-10892722","identifier":"Q6TGC4","identifierLink":"https://www.uniprot.org/uniprotkb/Q6TGC4/entry","name":"PADI6","description":"Inactive protein-arginine deiminase type-6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10837","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11071382","identifier":"P59047","identifierLink":"https://www.uniprot.org/uniprotkb/P59047/entry","name":"NLRP5","description":"NACHT, LRR and PYD domains-containing protein 5","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45690","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18583589","identifier":"A6NGQ2","identifierLink":"https://www.uniprot.org/uniprotkb/A6NGQ2/entry","name":"OOEP","description":"Oocyte-expressed protein homolog","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19447","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22049227","identifier":"Q8WX94","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WX94/entry","name":"NLRP7","description":"NACHT, LRR and PYD domains-containing protein 7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45690","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22731520","identifier":"Q587J8","identifierLink":"https://www.uniprot.org/uniprotkb/Q587J8/entry","name":"KHDC3L","description":"KH domain-containing protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19447","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32711753","identifier":"Q9H808-1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H808-1/entry","name":"TLE6","description":"Transducin-like enhancer protein 6","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-6374482","identifier":"Q9NX02","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NX02/entry","name":"NLRP2","description":"NACHT, LRR and PYD domains-containing protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45690","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8189","complexName":"ASC1-4F2 heteromeric amino acid transporter complex","organismName":"Homo sapiens; 9606","description":"Amino acid transporter which catalyses the transmembrane electroneutral antiport  of small neutral L- and D-amino acids across the plasma membrane in a sodium-independent manner. Important for the transport of D-amino acids involved in neural signalling and adipocyte differentiation.","predictedComplex":false,"interactors":[{"ac":"EBI-12068238","identifier":"Q9NS82","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NS82/entry","name":"SLC7A10","description":"Asc-type amino acid transporter 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11785","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-702356","identifier":"P08195","identifierLink":"https://www.uniprot.org/uniprotkb/P08195/entry","name":"SLC3A2","description":"Amino acid transporter heavy chain SLC3A2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8190","complexName":"XCT-4F2 heteromeric amino acid transporter complex","organismName":"Homo sapiens; 9606","description":"Amino acid transporter which catalyses the transmembrane electroneutral exchange of intracellular glutamate for extracellular cysteine thus playing an important role in the maintenance of the redox balance in cells by providing cysteine for glutathione biosynthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-3843348","identifier":"Q9UPY5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UPY5/entry","name":"SLC7A11","description":"Cystine/glutamate transporter","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11785","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-702356","identifier":"P08195","identifierLink":"https://www.uniprot.org/uniprotkb/P08195/entry","name":"SLC3A2","description":"Amino acid transporter heavy chain SLC3A2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46673","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8191","complexName":"B(0)AT1-Collectrin heteromeric amino acid transporter complex","organismName":"Homo sapiens; 9606","description":"Amino acid transporter which catalyses the transmembrane electroneutral exchange of neutral amino acids across the apical membrane of renal and intestinal epithelial cells .","predictedComplex":false,"interactors":[{"ac":"EBI-25475705","identifier":"Q695T7","identifierLink":"https://www.uniprot.org/uniprotkb/Q695T7/entry","name":"SLC6A19","description":"Sodium-dependent neutral amino acid transporter B(0)AT1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11616","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3924906","identifier":"Q9HBJ8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HBJ8/entry","name":"CLTRN","description":"Collectrin","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46884","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8192","complexName":"B(0)AT1-ACE2 heteromeric amino acid transporter complex","organismName":"Homo sapiens; 9606","description":"Amino acid transporter which catalyses the transmembrane electroneutral which mediates uptake of neutral amino acids into intestinal cells in a sodium-dependent manner.","predictedComplex":false,"interactors":[{"ac":"EBI-25475705","identifier":"Q695T7","identifierLink":"https://www.uniprot.org/uniprotkb/Q695T7/entry","name":"SLC6A19","description":"Sodium-dependent neutral amino acid transporter B(0)AT1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11616","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7730807","identifier":"Q9BYF1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BYF1/entry","name":"ACE2","description":"Angiotensin-converting enzyme 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10514","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8201","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL32 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6426390","identifier":"Q96NJ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96NJ5/entry","name":"KLHL32","description":"Kelch-like protein 32","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45632","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8202","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL34 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6426410","identifier":"Q8N239","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N239/entry","name":"KLHL34","description":"Kelch-like protein 34","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45632","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8221","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL35 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9477654","identifier":"Q6PF15","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PF15/entry","name":"KLHL35","description":"Kelch-like protein 35","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8222","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL36 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6426427","identifier":"Q8N4N3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8N4N3/entry","name":"KLHL36","description":"Kelch-like protein 36","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45632","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8241","complexName":"CRL3 E3 ubiquitin ligase complex, ENC1 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate. CRL3-ENC1 target proteins include the serine/threonine-protein kinases LATS1 (O95835) and LATS2 (Q9NRM7) which control the  Hippo signaling pathway and thus cell proliferation and apoptosis.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6425462","identifier":"O14682","identifierLink":"https://www.uniprot.org/uniprotkb/O14682/entry","name":"ENC1","description":"Ectoderm-neural cortex protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24410","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8242","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL38 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.  CRL3-KLHL38 target proteins include BECN1 (Q14457) a component of the phosphatidylinositol 3-kinase complex, class III (CPX-73/CPX-74) which plays a key role in initiation and maturation of autophagosomes.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6426443","identifier":"Q2WGJ6","identifierLink":"https://www.uniprot.org/uniprotkb/Q2WGJ6/entry","name":"KLHL38","description":"Kelch-like protein 38","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8261","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL40 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.  CRL3-KLHL40 target proteins include the transcription factor TFDP1 (Q14186) thus playing a role in skeletal muscle myogenesis. It may also ubiquitinate the GTP-binding protein SAR1A (Q9NR31), regulating membrane tubulation and the trafficking of collagen.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7851314","identifier":"Q2TBA0","identifierLink":"https://www.uniprot.org/uniprotkb/Q2TBA0/entry","name":"KLHL40","description":"Kelch-like protein 40","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8262","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL41 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.  CRL3-KLHL41 target proteins include the thin filament chaperone, NRAP (Q86VF7) which regulates the dynamics of myofibril formation.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5353084","identifier":"O60662","identifierLink":"https://www.uniprot.org/uniprotkb/O60662/entry","name":"KLHL41","description":"Kelch-like protein 41","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24412","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8263","complexName":"CRL3 E3 ubiquitin ligase complex, KLHL42 variant","organismName":"Homo sapiens; 9606","description":"E3 ubiquitin ligase which catalyzes the transfer of ubiquitin from an E2 enzyme to a substrate bound to a substrate receptor by promoting the formation of an isopeptide bond between the Ub carboxy-terminus and specific lysine side chains on the substrate.  CRL3-KLHL42 target proteins include the PPP2R5E serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon (Q16537) thus mediating TGFB signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-398523","identifier":"P62877","identifierLink":"https://www.uniprot.org/uniprotkb/P62877/entry","name":"RBX1","description":"E3 ubiquitin-protein ligase RBX1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-456129","identifier":"Q13618","identifierLink":"https://www.uniprot.org/uniprotkb/Q13618/entry","name":"CUL3","description":"Cullin-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11932","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-739890","identifier":"Q9P2K6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P2K6/entry","name":"KLHL42","description":"Kelch-like protein 42","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45972","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8282","complexName":"MalT-MalY transcriptional regulator complex","organismName":"Escherichia coli (strain K12); 83333","description":"Complex formation represses the activity of MALT (CPX-8283) as a signal transduction ATPase which transcriptionally activates the maltose system responsible for the uptake and metabolism of maltodextrins. MALY represses MALT activity by blocking its oligomerization and strengthening ADP-mediated MALT autoinhibition. Maltotriose binding results in complex disassociation.","predictedComplex":false,"interactors":[{"ac":"EBI-1124666","identifier":"P23256","identifierLink":"https://www.uniprot.org/uniprotkb/P23256/entry","name":"malY","description":"Protein MalY","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[]},{"ac":"EBI-542934","identifier":"P06993","identifierLink":"https://www.uniprot.org/uniprotkb/P06993/entry","name":"malT","description":"HTH-type transcriptional regulator MalT","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR44688","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8852014","identifier":"CHEBI:597326","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:597326","name":"pyridoxal 5'-phosphate(2-)","description":"pyridoxal 5'-phosphate(2-)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-8283","complexName":"MalT transcriptional activator complex","organismName":"Escherichia coli (strain K12); 83333","description":"Signal transduction ATPase which transcriptionally activates the maltose system responsible for the uptake and metabolism of maltodextrins. Maltotriose binding drives oligomerization and together these stabilize the C-terminal domains of MALT, allowing cooperative binding of MalT to promoter region of its target genes, via a short DNA motif, the MalT box (5'-GGA[TG]GA-3')  and enable RNA polymerase recruitment for subsequent transcription initiation. Oligomerization requires ATP binding but the ATPase activity of the protein does not appear to be required for activity.","predictedComplex":false,"interactors":[{"ac":"EBI-46447033","identifier":"CHEBI:30616","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:30616","name":"atp(4-)","description":"ATP(4-)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-542934","identifier":"P06993","identifierLink":"https://www.uniprot.org/uniprotkb/P06993/entry","name":"malT","description":"HTH-type transcriptional regulator MalT","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Escherichia coli (strain K12); 83333","xrefs":[{"identifier":"PTHR44688","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8302","complexName":"ABCB10-ABCB7-FECH ABC transporter","organismName":"Homo sapiens; 9606","description":"Required for heme biosynthesis, incorporating iron into protoporphyrin IX and may also act as a mitochondrial matrix heme exporter. Also plays a role in cellular iron homeostasis.","predictedComplex":false,"interactors":[{"ac":"EBI-1236950","identifier":"O75027","identifierLink":"https://www.uniprot.org/uniprotkb/O75027/entry","name":"ABCB7","description":"Iron-sulfur clusters transporter ABCB7, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24221","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1390356","identifier":"P22830","identifierLink":"https://www.uniprot.org/uniprotkb/P22830/entry","name":"FECH","description":"Ferrochelatase, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11108","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-46449825","identifier":"CHEBI:190135","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:190135","name":"di-mu-sulfido-diiron","description":"di-mu-sulfido-diiron","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-6164528","identifier":"Q9NRK6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NRK6/entry","name":"ABCB10","description":"ATP-binding cassette sub-family B member 10, mitochondrial","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24221","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8304","complexName":"UFM1 ribosome E3 ligase complex","organismName":"Homo sapiens; 9606","description":"E3 ligase which covalently attaches the ubiquitin-like modifier UFM1 (P61960) to lysine residues on substrates. Ufmylation is involved in processes such as endoplasmic reticulum-associated protein degradation, ribosome-associated protein quality control at the endoplasmic reticulum (ER), and ER-phagy that drives the removal of damaged ER. Required for the release and recycling of stalled or terminated ribosomes from the ER membrane. The presence of the substrate adapter CDK5RAP3 alters the specificity of the E3 complex from autoUFMylation of DDRGK1 to that of RPL26 (P61254), thus switching cellular processes from ER-phagy to ER-ribosome-associated protein quality control.","predictedComplex":false,"interactors":[{"ac":"EBI-1048088","identifier":"O94874","identifierLink":"https://www.uniprot.org/uniprotkb/O94874/entry","name":"UFL1","description":"E3 UFM1-protein ligase 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1054024","identifier":"Q96HY6","identifierLink":"https://www.uniprot.org/uniprotkb/Q96HY6/entry","name":"DDRGK1","description":"DDRGK domain-containing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48176","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-718818","identifier":"Q96JB5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96JB5/entry","name":"CDK5RAP3","description":"CDK5 regulatory subunit-associated protein 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8305","complexName":"FMR1 RNA-binding homodimer","organismName":"Homo sapiens; 9606","description":"mRNA binding complex that plays a critical role in mRNA metabolism, regulating alternative mRNA splicing, mRNA stability, mRNA dendritic transport and postsynaptic local protein synthesis of target mRNAs. Undergoes liquid-liquid phase separation on binding to target mRNAs leading to their assembly into cytoplasmic membrane‐less ribonucleoprotein stress granules that both concentrates mRNAs with associated regulatory factors and also sequesters them in the cytoplasm preventing nuclear functions such as alternative splicing, transcriptional regulation or mRNA processing. Formation of  membraneless foci is driven by the C-terminal 188-residue low-complexity region of the protein and is enhanced by phosphorylation of this region. The complex plays a central role in neuronal development and synaptic plasticity.","predictedComplex":false,"interactors":[{"ac":"EBI-366305","identifier":"Q06787","identifierLink":"https://www.uniprot.org/uniprotkb/Q06787/entry","name":"FMR1","description":"Fragile X messenger ribonucleoprotein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10603","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8306","complexName":"FMR1-FXR1 RNA-binding complex","organismName":"Homo sapiens; 9606","description":"mRNA binding complex that play a critical role in mRNA metabolism, regulating alternative mRNA splicing, mRNA stability, mRNA dendritic transport and postsynaptic local protein synthesis of target mRNAs.Undergoes liquid-liquid phase separation on binding to target mRNAs leading to their assembly into cytoplasmic membrane‐less ribonucleoprotein stress granules that both concentrates mRNAs with associated regulatory factors and also sequesters them in the cytoplasm preventing nuclear functions such as alternative splicing, transcriptional regulation or mRNA processing.","predictedComplex":false,"interactors":[{"ac":"EBI-366305","identifier":"Q06787","identifierLink":"https://www.uniprot.org/uniprotkb/Q06787/entry","name":"FMR1","description":"Fragile X messenger ribonucleoprotein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10603","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-713291","identifier":"P51114","identifierLink":"https://www.uniprot.org/uniprotkb/P51114/entry","name":"FXR1","description":"RNA-binding protein FXR1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10603","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8307","complexName":"EXT1-EXT2 heparan sulfate biosynthesis complex","organismName":"Homo sapiens; 9606","description":"Glycosyltransferase required for the elongation of heparin sulfate chains, long complex polysaccharides which are attached to a serine residue of a large number of cell surface proteins to form a proteoglycan. Heparin sulfate backbone extension involves the alternating transfer of UDP-alpha-D-glucuronate(3-) (CHEBI:58052) in beta 1-3 linkage to N-acetylglucosamine and UDP-N-acetyl-alpha-D-glucosamine(2-) (CHEBI:57705) in beta 1-4 linkage to glucuronic acid by the enzyme complex.","predictedComplex":false,"interactors":[{"ac":"EBI-1046007","identifier":"Q16394","identifierLink":"https://www.uniprot.org/uniprotkb/Q16394/entry","name":"EXT1","description":"Exostosin-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11062","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1047761","identifier":"Q93063","identifierLink":"https://www.uniprot.org/uniprotkb/Q93063/entry","name":"EXT2","description":"Exostosin-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11062","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8322","complexName":"FMR1-FXR2 RNA-binding complex","organismName":"Homo sapiens; 9606","description":"mRNA binding complex that play a critical role in mRNA metabolism, regulating alternative mRNA splicing, mRNA stability, mRNA dendritic transport and postsynaptic local protein synthesis of target mRNAs. Undergoes liquid-liquid phase separation on binding to target mRNAs leading to their assembly into cytoplasmic membrane‐less ribonucleoprotein stress granules that both concentrates mRNAs with associated regulatory factors and also sequesters them in the cytoplasm preventing nuclear functions such as alternative splicing, transcriptional regulation or mRNA processing.","predictedComplex":false,"interactors":[{"ac":"EBI-366305","identifier":"Q06787","identifierLink":"https://www.uniprot.org/uniprotkb/Q06787/entry","name":"FMR1","description":"Fragile X messenger ribonucleoprotein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10603","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-740459","identifier":"P51116","identifierLink":"https://www.uniprot.org/uniprotkb/P51116/entry","name":"FXR2","description":"RNA-binding protein FXR2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10603","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8323","complexName":"FXR1 RNA-binding homodimer","organismName":"Homo sapiens; 9606","description":"mRNA binding complex that play a critical role in mRNA metabolism, regulating alternative mRNA splicing, mRNA stability, mRNA dendritic transport and postsynaptic local protein synthesis of target mRNAs. Undergoes liquid-liquid phase separation on binding to target mRNAs leading to their assembly into cytoplasmic membrane‐less ribonucleoprotein stress granules that both concentrates mRNAs with associated regulatory factors and also sequesters them in the cytoplasm preventing nuclear functions such as alternative splicing, transcriptional regulation or mRNA processing.","predictedComplex":false,"interactors":[{"ac":"EBI-713291","identifier":"P51114","identifierLink":"https://www.uniprot.org/uniprotkb/P51114/entry","name":"FXR1","description":"RNA-binding protein FXR1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10603","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8341","complexName":"FXR2 RNA-binding homodimer","organismName":"Homo sapiens; 9606","description":"mRNA binding complex that play a critical role in mRNA metabolism, regulating alternative mRNA splicing, mRNA stability, mRNA dendritic transport and postsynaptic local protein synthesis of target mRNAs. Undergoes liquid-liquid phase separation on binding to target mRNAs leading to their assembly into cytoplasmic membrane‐less ribonucleoprotein stress granules that both concentrates mRNAs with associated regulatory factors and also sequesters them in the cytoplasm preventing nuclear functions such as alternative splicing, transcriptional regulation or mRNA processing.","predictedComplex":false,"interactors":[{"ac":"EBI-740459","identifier":"P51116","identifierLink":"https://www.uniprot.org/uniprotkb/P51116/entry","name":"FXR2","description":"RNA-binding protein FXR2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10603","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8342","complexName":"FXR1-FXR2 RNA-binding complex","organismName":"Homo sapiens; 9606","description":"mRNA binding complex that play a critical role in mRNA metabolism, regulating alternative mRNA splicing, mRNA stability, mRNA dendritic transport and postsynaptic local protein synthesis of target mRNAs. Undergoes liquid-liquid phase separation on binding to target mRNAs leading to their assembly into cytoplasmic membrane‐less ribonucleoprotein stress granules that both concentrates mRNAs with associated regulatory factors and also sequesters them in the cytoplasm preventing nuclear functions such as alternative splicing, transcriptional regulation or mRNA processing.","predictedComplex":false,"interactors":[{"ac":"EBI-713291","identifier":"P51114","identifierLink":"https://www.uniprot.org/uniprotkb/P51114/entry","name":"FXR1","description":"RNA-binding protein FXR1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10603","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-740459","identifier":"P51116","identifierLink":"https://www.uniprot.org/uniprotkb/P51116/entry","name":"FXR2","description":"RNA-binding protein FXR2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10603","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8343","complexName":"Eukaryotic translation initiation factor 2B complex","organismName":"Homo sapiens; 9606","description":"A dedicated guanine nucleotide exchange factor for the eukaryotic initiation factor 2 (CPX-2716), catalyzing the exchange of GDP to GTP.","predictedComplex":false,"interactors":[{"ac":"EBI-2340132","identifier":"Q9UI10","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UI10/entry","name":"EIF2B4","description":"Translation initiation factor eIF2B subunit delta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10233","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4401110","identifier":"Q13144","identifierLink":"https://www.uniprot.org/uniprotkb/Q13144/entry","name":"EIF2B5","description":"Translation initiation factor eIF2B subunit epsilon","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45887","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-491065","identifier":"Q14232","identifierLink":"https://www.uniprot.org/uniprotkb/Q14232/entry","name":"EIF2B1","description":"Translation initiation factor eIF2B subunit alpha","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45860","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-702257","identifier":"Q9NR50","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NR50/entry","name":"EIF2B3","description":"Translation initiation factor eIF2B subunit gamma","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45989","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-718773","identifier":"P49770","identifierLink":"https://www.uniprot.org/uniprotkb/P49770/entry","name":"EIF2B2","description":"Translation initiation factor eIF2B subunit beta","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45859","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8344","complexName":"BRE1 E3 ubiquitin ligase complex","organismName":"Homo sapiens; 9606","description":"E3 ubiqitin ligase complex which ubiquitinates Lys-120 of histone H2B. This then acts as a epigenetic tag for both transcriptional activation and repression of specific genes potentially, in some cases via recruitment by TP53 (P04637). Interacts with the PAF1 (CPX-2381) complex, which plays a role in transcriptional elongation and also with RNA polymerase II (CPX-2387/CPX-7481) via the WAC adapter protein (Q9BTA9).","predictedComplex":false,"interactors":[{"ac":"EBI-2372238","identifier":"Q5VTR2","identifierLink":"https://www.uniprot.org/uniprotkb/Q5VTR2/entry","name":"RNF20","description":"E3 ubiquitin-protein ligase BRE1A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23163","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744408","identifier":"O75150","identifierLink":"https://www.uniprot.org/uniprotkb/O75150/entry","name":"RNF40","description":"E3 ubiquitin-protein ligase BRE1B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23163","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8361","complexName":"ZNT5-ZNT6 proton-coupled zinc antiporter complex","organismName":"Homo sapiens; 9606","description":"Proton-coupled zinc ion antiporter required for the entry of zinc into the lumen of organelles associated with the secretory pathway, thus regulating the folding and activation of a number of ecto-enzymes including alkaline phosphatases, such as  ALPL (P05186) and ALPL (P05187), and enzymes involved in phosphatidylinositol glycan anchor biosynthesis. Also plays a role in the storage and secretion of insulin via the transport of zinc into secretory granules of pancreatic beta-cells.","predictedComplex":false,"interactors":[{"ac":"EBI-11337878","identifier":"Q8TAD4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAD4/entry","name":"SLC30A5","description":"Proton-coupled zinc antiporter SLC30A5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45755","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2849005","identifier":"Q6NXT4","identifierLink":"https://www.uniprot.org/uniprotkb/Q6NXT4/entry","name":"SLC30A6","description":"Zinc transporter 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46531","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8381","complexName":"ZNT1 proton-coupled zinc antiporter homodimer","organismName":"Homo sapiens; 9606","description":"Proton-coupled zinc ion antiporter present in the plasma membrane and required for exporting cytosolic zinc into the extracellular space thus protecting cells from zinc toxicity","predictedComplex":false,"interactors":[{"ac":"EBI-10982148","identifier":"Q9Y6M5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6M5/entry","name":"SLC30A1","description":"Proton-coupled zinc antiporter SLC30A1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45820","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8382","complexName":"ZNT8 proton-coupled zinc antiporter homodimer","organismName":"Homo sapiens; 9606","description":"Proton-coupled zinc ion antiporter which plays an essential role in regulating Zn2+ accumulation in the insulin secretory granules of pancreatic beta-cells. ZNT8 is responsible for transporting zinc from the cytoplasm into insulin granules, stabilizing insulin hexamer formation.","predictedComplex":false,"interactors":[{"ac":"EBI-10262251","identifier":"Q8IWU4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IWU4/entry","name":"SLC30A8","description":"Proton-coupled zinc antiporter SLC30A8","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11562","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8406","complexName":"ZNT2 proton-coupled zinc antiporter homodimer","organismName":"Homo sapiens; 9606","description":"Proton-coupled zinc ion antiporter which is expressed in specialized secretory tissues, including the mammary gland where it imports Zn2+ into vesicles for secretion into milk during lactation. Relocates to the lysosomes and activates lysosomal-mediated cell death during early mammary gland involution. Associated with the inner mitochondrial membrane and acts as an auxiliary Zn2+ importer into mitochondria in mammary cells.","predictedComplex":false,"interactors":[{"ac":"EBI-8644112","identifier":"Q9BRI3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BRI3/entry","name":"SLC30A2","description":"Proton-coupled zinc antiporter SLC30A2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11562","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8407","complexName":"ZNT1-ZNT2 proton-coupled zinc antiporter complex","organismName":"Homo sapiens; 9606","description":"Proton-coupled zinc ion antiporter present in the plasma membrane and required for exporting cytosolic zinc into the extracellular space thus protecting cells from zinc toxicity","predictedComplex":false,"interactors":[{"ac":"EBI-10982148","identifier":"Q9Y6M5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6M5/entry","name":"SLC30A1","description":"Proton-coupled zinc antiporter SLC30A1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45820","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8644112","identifier":"Q9BRI3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BRI3/entry","name":"SLC30A2","description":"Proton-coupled zinc antiporter SLC30A2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11562","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8410","complexName":"HAS1-HAS3 hyaluronan biosynthesis complex","organismName":"Homo sapiens; 9606","description":"Glycosyltransferase required for the elongation of hyaluronan, a glycosaminoglycan present in the pericellular and extracellular matrix. Has enzyme complex catalyze the alternating transfer of UDP-alpha-D-glucuronate(3-) (CHEBI:58052) in beta 1-3 linkage to N-acetylglucosamine and UDP-N-acetyl-alpha-D-glucosamine(2-) (CHEBI:57705) in beta 1-4 linkage to glucuronic acid.\r\n\r\nThe combination of HAS enzymes and the cellular environment have specific effects on Hyaluronan biosynthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-1052423","identifier":"Q92839","identifierLink":"https://www.uniprot.org/uniprotkb/Q92839/entry","name":"HAS1","description":"Hyaluronan synthase 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22913","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16628799","identifier":"O00219","identifierLink":"https://www.uniprot.org/uniprotkb/O00219/entry","name":"HAS3","description":"Hyaluronan synthase 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22913","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8422","complexName":"HAS1-HAS2 hyaluronan biosynthesis complex","organismName":"Homo sapiens; 9606","description":"Glycosyltransferase required for the elongation of hyaluronan, a glycosaminoglycan present in the pericellular and extracellular matrix. HAS enzyme complex catalyze the alternating transfer of UDP-alpha-D-glucuronate(3-) (CHEBI:58052) in beta 1-3 linkage to N-acetylglucosamine and UDP-N-acetyl-alpha-D-glucosamine(2-) (CHEBI:57705) in beta 1-4 linkage to glucuronic acid.\r\n\r\n\r\nThe combination of HAS enzymes and the cellular environment have specific effects on Hyaluronan biosynthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-1052423","identifier":"Q92839","identifierLink":"https://www.uniprot.org/uniprotkb/Q92839/entry","name":"HAS1","description":"Hyaluronan synthase 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22913","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16628852","identifier":"Q92819","identifierLink":"https://www.uniprot.org/uniprotkb/Q92819/entry","name":"HAS2","description":"Hyaluronan synthase 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22913","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8423","complexName":"HAS3 hyaluronan biosynthesis complex","organismName":"Homo sapiens; 9606","description":"Glycosyltransferase required for the elongation of hyaluronan, a glycosaminoglycan present in the pericellular and extracellular matrix. Has enzyme complex catalyze the alternating transfer of UDP-alpha-D-glucuronate(3-) (CHEBI:58052) in beta 1-3 linkage to N-acetylglucosamine and UDP-N-acetyl-alpha-D-glucosamine(2-) (CHEBI:57705) in beta 1-4 linkage to glucuronic acid.\r\n\r\nThe combination of HAS enzymes and the cellular environment have specific effects on Hyaluronan biosynthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-16628799","identifier":"O00219","identifierLink":"https://www.uniprot.org/uniprotkb/O00219/entry","name":"HAS3","description":"Hyaluronan synthase 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22913","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8424","complexName":"HAS2-HAS3 hyaluronan biosynthesis complex","organismName":"Homo sapiens; 9606","description":"Glycosyltransferase required for the elongation of hyaluronan, a glycosaminoglycan present in the pericellular and extracellular matrix. Has enzyme complex catalyze the alternating transfer of UDP-alpha-D-glucuronate(3-) (CHEBI:58052) in beta 1-3 linkage to N-acetylglucosamine and UDP-N-acetyl-alpha-D-glucosamine(2-) (CHEBI:57705) in beta 1-4 linkage to glucuronic acid.\r\n\r\nThe combination of HAS enzymes and the cellular environment have specific effects on Hyaluronan biosynthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-16628799","identifier":"O00219","identifierLink":"https://www.uniprot.org/uniprotkb/O00219/entry","name":"HAS3","description":"Hyaluronan synthase 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22913","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16628852","identifier":"Q92819","identifierLink":"https://www.uniprot.org/uniprotkb/Q92819/entry","name":"HAS2","description":"Hyaluronan synthase 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22913","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8426","complexName":"ZNT3 proton-coupled zinc antiporter homodimer","organismName":"Homo sapiens; 9606","description":"Proton-coupled zinc ion antiporter present in synaptic-like microvesicles, regulating vesicular zinc concentrations in presynaptic cells. May play a role in maintaining cellular zinc ion homeostasis in the brain.","predictedComplex":false,"interactors":[{"ac":"EBI-10294651","identifier":"Q99726","identifierLink":"https://www.uniprot.org/uniprotkb/Q99726/entry","name":"SLC30A3","description":"Probable proton-coupled zinc antiporter SLC30A3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11562","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8427","complexName":"ZNT1-ZNT3 proton-coupled zinc antiporter complex","organismName":"Homo sapiens; 9606","description":"Proton-coupled zinc ion antiporter present in synaptic-like microvesicles, regulating vesicular zinc concentrations in presynaptic cells. May play a role in maintaining cellular zinc ion homeostasis in the brain.","predictedComplex":false,"interactors":[{"ac":"EBI-10294651","identifier":"Q99726","identifierLink":"https://www.uniprot.org/uniprotkb/Q99726/entry","name":"SLC30A3","description":"Probable proton-coupled zinc antiporter SLC30A3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11562","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-10982148","identifier":"Q9Y6M5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6M5/entry","name":"SLC30A1","description":"Proton-coupled zinc antiporter SLC30A1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45820","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8428","complexName":"ZNT2-ZNT3 proton-coupled zinc antiporter complex","organismName":"Homo sapiens; 9606","description":"Proton-coupled zinc ion antiporter present in vesicles, regulating vesicular zinc concentrations in cells.","predictedComplex":false,"interactors":[{"ac":"EBI-10294651","identifier":"Q99726","identifierLink":"https://www.uniprot.org/uniprotkb/Q99726/entry","name":"SLC30A3","description":"Probable proton-coupled zinc antiporter SLC30A3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11562","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8644112","identifier":"Q9BRI3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BRI3/entry","name":"SLC30A2","description":"Proton-coupled zinc antiporter SLC30A2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11562","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8429","complexName":"ZNT4 proton-coupled zinc antiporter homodimer","organismName":"Homo sapiens; 9606","description":"Proton-coupled zinc ion antiporter which is expressed in the lysosome where it imports Zn2+ from the the cytoplasm into the lysosmal lumen. Expressed in  specialized secretory tissues, including the mammary gland where it imports Zn2+ into vesicles for secretion into milk during lactation.","predictedComplex":false,"interactors":[{"ac":"EBI-13918058","identifier":"O14863","identifierLink":"https://www.uniprot.org/uniprotkb/O14863/entry","name":"SLC30A4","description":"Probable proton-coupled zinc antiporter SLC30A4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11562","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8432","complexName":"GPR88-Gi1 signaling complex","organismName":"Homo sapiens; 9606","description":"A transmembrane signaling complex which couples an orphan receptor, GPR88, to guanine nucleotide-binding proteins.  Ligand binding induces a conformation change that facilitates the exchange of GDP for GTP on GNAI2. This exchange leads to the dissociation of the complex and both GTP-bound GNAI2 and the GNB1-GNG1 stimulate a number of downstream effectors, modulating GABAergic and glutamatergic signaling. May also affect the activity of several other G-protein-coupled receptors such as dopamine receptors and opioid receptors. May play a role in regulating brain and behavioral functions.","predictedComplex":false,"interactors":[{"ac":"EBI-10220715","identifier":"P63211","identifierLink":"https://www.uniprot.org/uniprotkb/P63211/entry","name":"GNGT1","description":"Guanine nucleotide-binding protein G(T) subunit gamma-T1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13809","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357130","identifier":"P62873","identifierLink":"https://www.uniprot.org/uniprotkb/P62873/entry","name":"GNB1","description":"Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48416338","identifier":"Q9GZN0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9GZN0/entry","name":"GPR88","description":"G protein-coupled receptor 88","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24240","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-618639","identifier":"P63096","identifierLink":"https://www.uniprot.org/uniprotkb/P63096/entry","name":"GNAI1","description":"Guanine nucleotide-binding protein G(i) subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10218","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8441","complexName":"ZNT1-ZNT4 proton-coupled zinc antiporter complex","organismName":"Homo sapiens; 9606","description":"Proton-coupled zinc ion antiporter present in the plasma membrane and required for exporting cytosolic zinc into the extracellular space thus protecting cells from zinc toxicity","predictedComplex":false,"interactors":[{"ac":"EBI-10982148","identifier":"Q9Y6M5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6M5/entry","name":"SLC30A1","description":"Proton-coupled zinc antiporter SLC30A1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45820","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13918058","identifier":"O14863","identifierLink":"https://www.uniprot.org/uniprotkb/O14863/entry","name":"SLC30A4","description":"Probable proton-coupled zinc antiporter SLC30A4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11562","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8442","complexName":"ZNT2-ZNT4 proton-coupled zinc antiporter complex","organismName":"Homo sapiens; 9606","description":"Proton-coupled zinc ion antiporter which is expressed in specialized secretory tissues, including the mammary gland where it imports Zn2+ into vesicles for secretion into milk during lactation. Relocates to the lysosomes and activates lysosomal-mediated cell death during early mammary gland involution. Associated with the inner mitochondrial membrane and acts as an auxiliary Zn2+ importer into mitochondria in mammary cells.","predictedComplex":false,"interactors":[{"ac":"EBI-13918058","identifier":"O14863","identifierLink":"https://www.uniprot.org/uniprotkb/O14863/entry","name":"SLC30A4","description":"Probable proton-coupled zinc antiporter SLC30A4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11562","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8644112","identifier":"Q9BRI3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BRI3/entry","name":"SLC30A2","description":"Proton-coupled zinc antiporter SLC30A2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11562","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8443","complexName":"ZNT3-ZNT4 proton-coupled zinc antiporter complex","organismName":"Homo sapiens; 9606","description":"Proton-coupled zinc ion antiporter which regulates vesicular zinc concentrations","predictedComplex":false,"interactors":[{"ac":"EBI-10294651","identifier":"Q99726","identifierLink":"https://www.uniprot.org/uniprotkb/Q99726/entry","name":"SLC30A3","description":"Probable proton-coupled zinc antiporter SLC30A3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11562","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13918058","identifier":"O14863","identifierLink":"https://www.uniprot.org/uniprotkb/O14863/entry","name":"SLC30A4","description":"Probable proton-coupled zinc antiporter SLC30A4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11562","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8444","complexName":"ZNT7 proton-coupled zinc antiporter complex","organismName":"Homo sapiens; 9606","description":"Proton-coupled zinc ion antiporter which mediates zinc entry from the cytosol into the lumen of the endoplasmic reticulum. Supply zinc to nascent ectoenzymes in the early secretory pathway including alkaline phosphatases, ecto-5'-nucleotidase NT5E (P21589) and ENPP2 (Q13822).","predictedComplex":false,"interactors":[{"ac":"EBI-1043569","identifier":"Q8NEW0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NEW0/entry","name":"SLC30A7","description":"Zinc transporter 7","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45755","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8462","complexName":"ZNT10 calcium-coupled manganese antiporter homodimer","organismName":"Homo sapiens; 9606","description":"Calcium-coupled manganese ion antiporter which mediates the active removal of Mn2+ from the cell, utilizing the steep transmembrane Ca2+ gradient, thus preventing the generation of harmful oxygen radicals caused by the redox activity of Mn2+.","predictedComplex":false,"interactors":[{"ac":"EBI-13917996","identifier":"Q6XR72","identifierLink":"https://www.uniprot.org/uniprotkb/Q6XR72/entry","name":"SLC30A10","description":"Calcium/manganese antiporter SLC30A10","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45820","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8463","complexName":"ZNT2-ZNT10 proton-coupled zinc antiporter complex","organismName":"Homo sapiens; 9606","description":"Proton-coupled zinc ion antiporter which is expressed in the endosome and lysosome where it imports Zn2+ into the lumen of these organelles.","predictedComplex":false,"interactors":[{"ac":"EBI-13917996","identifier":"Q6XR72","identifierLink":"https://www.uniprot.org/uniprotkb/Q6XR72/entry","name":"SLC30A10","description":"Calcium/manganese antiporter SLC30A10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45820","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8644112","identifier":"Q9BRI3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BRI3/entry","name":"SLC30A2","description":"Proton-coupled zinc antiporter SLC30A2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11562","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8464","complexName":"ZNT3-ZNT10 proton-coupled zinc antiporter complex","organismName":"Homo sapiens; 9606","description":"Proton-coupled zinc ion antiporter which is expressed in the endosome and lysosome where it imports Zn2+ into the lumen of these organelles.","predictedComplex":false,"interactors":[{"ac":"EBI-10294651","identifier":"Q99726","identifierLink":"https://www.uniprot.org/uniprotkb/Q99726/entry","name":"SLC30A3","description":"Probable proton-coupled zinc antiporter SLC30A3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11562","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13917996","identifier":"Q6XR72","identifierLink":"https://www.uniprot.org/uniprotkb/Q6XR72/entry","name":"SLC30A10","description":"Calcium/manganese antiporter SLC30A10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45820","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8465","complexName":"ZNT4-ZNT10 proton-coupled zinc antiporter complex","organismName":"Homo sapiens; 9606","description":"Proton-coupled zinc ion antiporter which is expressed in the endosome and lysosome where it imports Zn2+ into the lumen of these organelles.","predictedComplex":false,"interactors":[{"ac":"EBI-13917996","identifier":"Q6XR72","identifierLink":"https://www.uniprot.org/uniprotkb/Q6XR72/entry","name":"SLC30A10","description":"Calcium/manganese antiporter SLC30A10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45820","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-13918058","identifier":"O14863","identifierLink":"https://www.uniprot.org/uniprotkb/O14863/entry","name":"SLC30A4","description":"Probable proton-coupled zinc antiporter SLC30A4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11562","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8467","complexName":"HAS2 hyaluronan biosynthesis complex","organismName":"Homo sapiens; 9606","description":"Glycosyltransferase required for the elongation of hyaluronan, a glycosaminoglycan present in the pericellular and extracellular matrix. Has enzyme complex catalyze the alternating transfer of UDP-alpha-D-glucuronate(3-) (CHEBI:58052) in beta 1-3 linkage to N-acetylglucosamine and UDP-N-acetyl-alpha-D-glucosamine(2-) (CHEBI:57705) in beta 1-4 linkage to glucuronic acid.\r\n\r\nThe combination of HAS enzymes and the cellular environment have specific effects on Hyaluronan biosynthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-16628852","identifier":"Q92819","identifierLink":"https://www.uniprot.org/uniprotkb/Q92819/entry","name":"HAS2","description":"Hyaluronan synthase 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22913","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8468","complexName":"GluK2 glutamate ionotropic kainate-type receptor complex","organismName":"Homo sapiens; 9606","description":"An ionotropic glutamate receptor which localizes either post-synaptically to drive synaptic depolarization or pre-synaptically to regulate neurotransmitter release. Belonging to the kainate-type glutamate receptors (KARs) sub-family, GluKs are ligand-gated cation channels activated by the neurotransmitter L-glutamate. GluKs play complex roles in neural development and CNS function.\r\n\r\nImplicated in neurodevelopmental disorders leading to intellectural disability as well as, nervous system disorders including epilepsy, neuropathic pain, austism, bipolar disorder and schizophrenia.","predictedComplex":false,"interactors":[{"ac":"EBI-3909911","identifier":"Q13002","identifierLink":"https://www.uniprot.org/uniprotkb/Q13002/entry","name":"GRIK2","description":"Glutamate receptor ionotropic, kainate 2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8481","complexName":"HAS1 hyaluronan biosynthesis complex","organismName":"Homo sapiens; 9606","description":"Glycosyltransferases required for the elongation of hyaluronan, a glycosaminoglycan present in the pericellular and extracellular matrix. HAS enzyme complex catalyze the alternating transfer of UDP-alpha-D-glucuronate(3-) (CHEBI:58052) in beta 1-3 linkage to N-acetylglucosamine and UDP-N-acetyl-alpha-D-glucosamine(2-) (CHEBI:57705) in beta 1-4 linkage to glucuronic acid.\r\n\r\n\r\nThe combination of HAS enzymes and the cellular environment have specific effects on Hyaluronan biosynthesis.","predictedComplex":false,"interactors":[{"ac":"EBI-1052423","identifier":"Q92839","identifierLink":"https://www.uniprot.org/uniprotkb/Q92839/entry","name":"HAS1","description":"Hyaluronan synthase 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22913","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8502","complexName":"UDP-glucuronosyltransferase 1A1 complex, UGT1A1-1 variant","organismName":"Homo sapiens; 9606","description":"Membrane-bound UDP-glucuronosyltransferase present in the endoplasmic reticulum that catalyzes the transfer of glucuronic acid to hydroxyl, carboxyl, or amine group compounds. Required for the biotransformation of lipophilic xenobiotics, increasing the conjugated metabolite's water solubility and facilitating excretion into either the urine or bile. UGT1A1 glucuronidates relatively bulky molecules such as bilirubin and planar or smaller molecules such as estradiol.","predictedComplex":false,"interactors":[{"ac":"EBI-9482608","identifier":"P22309-1","identifierLink":"https://www.uniprot.org/uniprotkb/P22309-1/entry","name":"UGT1A1","description":"UDP-glucuronosyltransferase 1A1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-8503","complexName":"GLUK2-GLUK5 glutamate ionotropic kainate-type receptor complex","organismName":"Homo sapiens; 9606","description":"An ionotropic glutamate receptor which localizes either post-synaptically to drive synaptic depolarization or pre-synaptically to regulate neurotransmitter release. Belonging to the kainate-type glutamate receptors (KARs) sub-family, GluKs are ligand-gated cation channels activated by the neurotransmitter l-glutamate. 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Methylation of mRNA by this complex suppresses pseudohyphal development.","predictedComplex":false,"interactors":[{"ac":"EBI-11537","identifier":"P53185","identifierLink":"https://www.uniprot.org/uniprotkb/P53185/entry","name":"VIR1","description":"Protein virilizer","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-11619","identifier":"P38236","identifierLink":"https://www.uniprot.org/uniprotkb/P38236/entry","name":"MUM2","description":"Protein MUM2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-29095","identifier":"P40167","identifierLink":"https://www.uniprot.org/uniprotkb/P40167/entry","name":"SLZ1","description":"Sporulation-specific with a leucine zipper motif protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-9210","identifier":"P41833","identifierLink":"https://www.uniprot.org/uniprotkb/P41833/entry","name":"IME4","description":"N(6)-adenosine-methyltransferase IME4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9509","identifier":"P25583","identifierLink":"https://www.uniprot.org/uniprotkb/P25583/entry","name":"KAR4","description":"Karyogamy protein KAR4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13107","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8560","complexName":"UDP-glucuronosyltransferase 1A1 complex, UGT1A1-2-UTG1A9-1 variant","organismName":"Homo sapiens; 9606","description":"Membrane-bound UDP-glucuronosyltransferase present in the endoplasmic reticulum that catalyzes the transfer of glucuronic acid to hydroxyl, carboxyl, or amine group compounds. Required for the biotransformation of lipophilic xenobiotics, increasing the conjugated metabolite's water solubility and facilitating excretion into either the urine or bile. The UGT1A1-2-UGT1A9-1 heteromer has a lower activity than the UGT1A1-1-UGT1A9-1 heteromer (CPX-8552) due to a dominant negative effect of the inactive UGT1A1-2 isoform.","predictedComplex":false,"interactors":[{"ac":"EBI-9486373","identifier":"O60656-1","identifierLink":"https://www.uniprot.org/uniprotkb/O60656-1/entry","name":"UGT1A9","description":"UDP-glucuronosyltransferase 1A9","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-9490970","identifier":"P22309-2","identifierLink":"https://www.uniprot.org/uniprotkb/P22309-2/entry","name":"UGT1A1","description":"UDP-glucuronosyltransferase 1A1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-8562","complexName":"UDP-glucuronosyltransferase 1A1 complex, UGT1A9-UTG2B7 variant","organismName":"Homo sapiens; 9606","description":"Membrane-bound UDP-glucuronosyltransferase present in the endoplasmic reticulum that catalyzes the transfer of glucuronic acid to hydroxyl, carboxyl, or amine group compounds. Required for the biotransformation of lipophilic xenobiotics, increasing the conjugated metabolite's water solubility and facilitating excretion into either the urine or bile.","predictedComplex":false,"interactors":[{"ac":"EBI-3909213","identifier":"P16662","identifierLink":"https://www.uniprot.org/uniprotkb/P16662/entry","name":"UGT2B7","description":"UDP-glucuronosyltransferase 2B7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48043","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9486373","identifier":"O60656-1","identifierLink":"https://www.uniprot.org/uniprotkb/O60656-1/entry","name":"UGT1A9","description":"UDP-glucuronosyltransferase 1A9","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-8563","complexName":"UDP-glucuronosyltransferase 1A1 complex, UGT1A1-2-UGT2B7 variant","organismName":"Homo sapiens; 9606","description":"Membrane-bound UDP-glucuronosyltransferase present in the endoplasmic reticulum that catalyzes the transfer of glucuronic acid to hydroxyl, carboxyl, or amine group compounds. Required for the biotransformation of lipophilic xenobiotics, increasing the conjugated metabolite's water solubility and facilitating excretion into either the urine or bile.  The UGT1A1-2-UGT2B7-1 heteromer has a lower activity than the UGT1A1-1-UGT2B7-1 heteromer (CPX-8557) due to a dominant negative effect of the inactive UGT1A1-2 isoform.","predictedComplex":false,"interactors":[{"ac":"EBI-3909213","identifier":"P16662","identifierLink":"https://www.uniprot.org/uniprotkb/P16662/entry","name":"UGT2B7","description":"UDP-glucuronosyltransferase 2B7","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48043","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9490970","identifier":"P22309-2","identifierLink":"https://www.uniprot.org/uniprotkb/P22309-2/entry","name":"UGT1A1","description":"UDP-glucuronosyltransferase 1A1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-8565","complexName":"PUCH ribonuclease complex, slfl-3 variant","organismName":"Caenorhabditis elegans; 6239","description":"piRNA precursor endonuclease which processes single-stranded piRNA precursor molecules to define the 5'-end of a new piRNA. This is then bound by a PIWI protein, such as ergo-1 (O61931). PUCH-mediated processing absolutely requires requires a 7-methyl-G cap (m7 G-cap) and an uracil at position three and exhibits a strong preference for an adenine or guanine residue at position 1. The complex interacts with PETISCO (CPX-4306/CPX-4307), a complex that binds to and stabilizes piRNA precursors. This enhances piRNA processing.","predictedComplex":false,"interactors":[{"ac":"EBI-322405","identifier":"O61766","identifierLink":"https://www.uniprot.org/uniprotkb/O61766/entry","name":"slfl-3","description":"Schlafen-like protein 3","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-331502","identifier":"O17608","identifierLink":"https://www.uniprot.org/uniprotkb/O17608/entry","name":"tofu-1","description":"Schlafen-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-48423238","identifier":"Q19614","identifierLink":"https://www.uniprot.org/uniprotkb/Q19614/entry","name":"tofu-2","description":"Schlafen-like protein 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12381","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-784","complexName":"Vacuolar transporter chaperone complex, VTC3 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Polyphosphate (polyP) polymerase that synthesizes polyP from ATP and translocates polyP across the vacuolar membrane to maintain an intracellular phosphate (Pi) homeostasis. Integral membrane complex enriched at the vacuolar membrane, but also localizes to other cellular compartments. VTC proteins have been implicated in several membrane-related processes, such as sorting of H+-translocating ATPases, endocytosis, ER-Golgi trafficking, vacuole fusion, and the microautophagic scission of vesicles into the vacuolar lumen. May bind calmodulin during some, or all, of these processes. This VTC3 variant is located mostly in the vacuole. VTC5 (P38966) can associate with the VTC complex and may act as an optional regulatory subunit.","predictedComplex":false,"interactors":[{"ac":"EBI-20513","identifier":"P40046","identifierLink":"https://www.uniprot.org/uniprotkb/P40046/entry","name":"VTC1","description":"Vacuolar transporter chaperone complex subunit 1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-25789","identifier":"P47075","identifierLink":"https://www.uniprot.org/uniprotkb/P47075/entry","name":"VTC4","description":"Vacuolar transporter chaperone complex subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46140","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-36919","identifier":"Q02725","identifierLink":"https://www.uniprot.org/uniprotkb/Q02725/entry","name":"VTC3","description":"Vacuolar transporter chaperone 3 complex subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46140","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8568","complexName":"Vacuolar transporter chaperone complex, VTC2 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"High-molecular-weight integral membrane complex enriched at the vacuolar membrane, but also localizes to other cellular compartments. VTC proteins have been implicated in several membrane-related processes, such as sorting of H+-translocating ATPases, endocytosis, ER-Golgi trafficking, vacuole fusion, vacuolar polyphosphate homeostasis and the microautophagic scission of vesicles into the vacuolar lumen. May bind calmodulin during some, or all, of these processes. This VTC2 variant is mostly located at the ER and nuclear envelope. VTC5 (P38966) can associate with the VTC complex and may act as an optional regulatory subunit.","predictedComplex":false,"interactors":[{"ac":"EBI-20513","identifier":"P40046","identifierLink":"https://www.uniprot.org/uniprotkb/P40046/entry","name":"VTC1","description":"Vacuolar transporter chaperone complex subunit 1","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-22750","identifier":"P43585","identifierLink":"https://www.uniprot.org/uniprotkb/P43585/entry","name":"VTC2","description":"Vacuolar transporter chaperone complex subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46140","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-25789","identifier":"P47075","identifierLink":"https://www.uniprot.org/uniprotkb/P47075/entry","name":"VTC4","description":"Vacuolar transporter chaperone complex subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46140","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8569","complexName":"PUCH ribonuclease complex, slfl-4 variant","organismName":"Caenorhabditis elegans; 6239","description":"piRNA precursor endonuclease which processes single-stranded piRNA precursor molecules to define the 5'-end of a new piRNA. This is then bound by a PIWI protein, such as ergo-1 (O61931). PUCH-mediated processing absolutely requires requires a 7-methyl-G cap (m7 G-cap) and an uracil at position three and exhibits a strong preference for an adenine or guanine residue at position 1. The complex interacts with PETISCO (CPX-4306/CPX-4307), a complex that binds to and stabilizes piRNA precursors. This enhances piRNA processing.","predictedComplex":false,"interactors":[{"ac":"EBI-331502","identifier":"O17608","identifierLink":"https://www.uniprot.org/uniprotkb/O17608/entry","name":"tofu-1","description":"Schlafen-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-48423238","identifier":"Q19614","identifierLink":"https://www.uniprot.org/uniprotkb/Q19614/entry","name":"tofu-2","description":"Schlafen-like protein 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12381","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48423288","identifier":"O76720","identifierLink":"https://www.uniprot.org/uniprotkb/O76720/entry","name":"slfl-4","description":"Schlafen-like protein 4","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]}]},{"complexAC":"CPX-8570","complexName":"VCP-DERL1 AAA ATPase complex","organismName":"Homo sapiens; 9606","description":"A type II AAA ATPase that is involved in the dislocation/extraction step of its substrate proteins from cellular structures or multiprotein complexes into the cytosol where they are largely degraded by the proteasome. Part of the endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins A transmembrane channel formed by tetrameric DERL1 provides a pathway for large ERAD substrates to exit the endoplasmic reticulum membrane driven by coordinated movement in both DERL1 and VCP.","predictedComplex":false,"interactors":[{"ac":"EBI-355164","identifier":"P55072","identifierLink":"https://www.uniprot.org/uniprotkb/P55072/entry","name":"VCP","description":"Transitional endoplasmic reticulum ATPase","stochiometry":"minValue: 6, maxValue: 6","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23077","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-398977","identifier":"Q9BUN8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BUN8/entry","name":"DERL1","description":"Derlin-1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11009","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8571","complexName":"GABA-A receptor, alpha4-beta3-gamma2","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-3909227","identifier":"P48169","identifierLink":"https://www.uniprot.org/uniprotkb/P48169/entry","name":"GABRA4","description":"Gamma-aminobutyric acid receptor subunit alpha-4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6258252","identifier":"P28472","identifierLink":"https://www.uniprot.org/uniprotkb/P28472/entry","name":"GABRB3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 3, maxValue: 3","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008430","identifier":"P18507","identifierLink":"https://www.uniprot.org/uniprotkb/P18507/entry","name":"GABRG2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8572","complexName":"Integrin alpha3-beta3 complex","organismName":"Homo sapiens; 9606","description":"Class 1 transmembrane receptors involved in bi-directional signaling to mediate cell-cell and cell-extracellular matrix (ECM) adhesion. Inside-out signaling mainly acts to bring the integrin into their active conformations whereas outside-in signalling involving integrins are associated with protein kinase activities.\r\n\r\nThe 24 functional receptors are obligate heterodimers derived from a family of 18 alpha subunits and 8 beta subunits. Grouping into subgroups is based on ligand-binding properties or the subunit composition.\r\n\r\nLigands for integrin alpha-3/beta-3 include laminin and RGD-sequence containing proteins like fibronectin, vitronectin and fibrinogen.","predictedComplex":false,"interactors":[{"ac":"EBI-2550768","identifier":"P26006","identifierLink":"https://www.uniprot.org/uniprotkb/P26006/entry","name":"ITGA3","description":"Integrin alpha-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23220","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-702847","identifier":"P05106","identifierLink":"https://www.uniprot.org/uniprotkb/P05106/entry","name":"ITGB3","description":"Integrin beta-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10082","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8573","complexName":"GABA-A receptor, alpha3-beta3-theta","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states.\r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-12820585","identifier":"Q9UN88","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UN88/entry","name":"GABRQ","description":"Gamma-aminobutyric acid receptor subunit theta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1763805","identifier":"P34903","identifierLink":"https://www.uniprot.org/uniprotkb/P34903/entry","name":"GABRA3","description":"Gamma-aminobutyric acid receptor subunit alpha-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6258252","identifier":"P28472","identifierLink":"https://www.uniprot.org/uniprotkb/P28472/entry","name":"GABRB3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8574","complexName":"GABA-A receptor, alpha4-beta2-gamma2","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptor assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-3909227","identifier":"P48169","identifierLink":"https://www.uniprot.org/uniprotkb/P48169/entry","name":"GABRA4","description":"Gamma-aminobutyric acid receptor subunit alpha-4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6949072","identifier":"P47870","identifierLink":"https://www.uniprot.org/uniprotkb/P47870/entry","name":"GABRB2","description":"Gamma-aminobutyric acid receptor subunit beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008430","identifier":"P18507","identifierLink":"https://www.uniprot.org/uniprotkb/P18507/entry","name":"GABRG2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8575","complexName":"GABA-A receptor, alpha5-beta3-gamma3","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptor assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nPredominantly expressed in the cerebral cortex, the GABA-A, alpha-5 receptor subtypes constitute less than 5% of the entire receptor population but up to 25% of the receptor subtype are located in the crucial learning and memory-associated area of the brain; the hippocampus.\r\n \r\nLargely absent at GABAergic synapses, exhibit little synaptic phasic inhibition, but abundant in the dendritic regions of extrasynaptic sites, and mediate tonic inhibition with continuously occurring smaller amplitude.\r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets:\r\n\r\n1) Positive allosteric modulation of GABA-A alpha-5 receptor subtypes can selectively decrease hippocampal activity and reverse psychosis-like physiological and behavioural changes in rats; may potentially help treat patients with post-traumatic stress disorder (PTSD) and comorbid psychosis; allopregnanolone (CHEBI:50169), a naturally occurring progesterone derivative, is a PAM referred to as brexanolone when used for the medical treatment of moderate to severe postpartum depression.\r\n\r\n2) Negative-allosteric modulators for reducing their tonic inhibition have been shown to enhance learning and memory in neurological disorders such as schizophrenia, Down syndrome, and autism with a possible alternative benzodiazepine binding site.","predictedComplex":false,"interactors":[{"ac":"EBI-48429392","identifier":"Q99928","identifierLink":"https://www.uniprot.org/uniprotkb/Q99928/entry","name":"GABRG3","description":"Gamma-aminobutyric acid receptor subunit gamma-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6258252","identifier":"P28472","identifierLink":"https://www.uniprot.org/uniprotkb/P28472/entry","name":"GABRB3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008566","identifier":"P31644","identifierLink":"https://www.uniprot.org/uniprotkb/P31644/entry","name":"GABRA5","description":"Gamma-aminobutyric acid receptor subunit alpha-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8576","complexName":"GABA-A receptor, alpha5-beta2-gamma2","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptor assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nPredominantly expressed in the cerebral cortex, the GABA-A, alpha-5 receptor subtypes constitute less than 5% of the entire receptor population but up to 25% of the receptor subtype are located in the crucial learning and memory-associated area of the brain; the hippocampus.\r\n \r\nLargely absent at GABAergic synapses, exhibit little synaptic phasic inhibition, but abundant in the dendritic regions of extrasynaptic sites, and mediate tonic inhibition with continuously occurring smaller amplitude.\r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets:\r\n\r\n1) Positive allosteric modulation of GABA-A alpha-5 receptor subtypes can selectively decrease hippocampal activity and reverse psychosis-like physiological and behavioural changes in rats; may potentially help treat patients with post-traumatic stress disorder (PTSD) and comorbid psychosis; allopregnanolone (CHEBI:50169), a naturally occurring progesterone derivative, is a PAM referred to as brexanolone when used for the medical treatment of moderate to severe postpartum depression.\r\n\r\n2) Negative-allosteric modulators for reducing their tonic inhibition have been shown to enhance learning and memory in neurological disorders such as schizophrenia, Down syndrome, and autism with a possible alternative benzodiazepine binding site.","predictedComplex":false,"interactors":[{"ac":"EBI-6949072","identifier":"P47870","identifierLink":"https://www.uniprot.org/uniprotkb/P47870/entry","name":"GABRB2","description":"Gamma-aminobutyric acid receptor subunit beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008430","identifier":"P18507","identifierLink":"https://www.uniprot.org/uniprotkb/P18507/entry","name":"GABRG2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008566","identifier":"P31644","identifierLink":"https://www.uniprot.org/uniprotkb/P31644/entry","name":"GABRA5","description":"Gamma-aminobutyric acid receptor subunit alpha-5","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8577","complexName":"GABA-A receptor, alpha2-beta2-gamma2","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states.\r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-2685723","identifier":"P47869","identifierLink":"https://www.uniprot.org/uniprotkb/P47869/entry","name":"GABRA2","description":"Gamma-aminobutyric acid receptor subunit alpha-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6949072","identifier":"P47870","identifierLink":"https://www.uniprot.org/uniprotkb/P47870/entry","name":"GABRB2","description":"Gamma-aminobutyric acid receptor subunit beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008430","identifier":"P18507","identifierLink":"https://www.uniprot.org/uniprotkb/P18507/entry","name":"GABRG2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8578","complexName":"GABA-A receptor, alpha1-beta2-delta","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA receptors containing alpha/beta/delta subunits are localized to extra- and peri-synaptic membranes where a low concentration of ambient of GABA enables them to be one of the primary mediators of tonic inhibition. Associated with extrasynaptic activity and known to be involved in the ventral tegmental area (VTA) pathway in the brain's hippocampus. \r\n\r\nAssemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. Their many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.\r\n\r\nBenzodiazepine-insensitive, but high sensitivity to low GABA concentrations and ethanol, an indirect GABA agonist; acohol mimics GABA, binds to GABA receptors and inhibits neuronal signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-6258308","identifier":"P14867","identifierLink":"https://www.uniprot.org/uniprotkb/P14867/entry","name":"GABRA1","description":"Gamma-aminobutyric acid receptor subunit alpha-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6949072","identifier":"P47870","identifierLink":"https://www.uniprot.org/uniprotkb/P47870/entry","name":"GABRB2","description":"Gamma-aminobutyric acid receptor subunit beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744352","identifier":"O14764","identifierLink":"https://www.uniprot.org/uniprotkb/O14764/entry","name":"GABRD","description":"Gamma-aminobutyric acid receptor subunit delta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8579","complexName":"GABA-A receptor, alpha3-beta3-gamma3","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states.\r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-1763805","identifier":"P34903","identifierLink":"https://www.uniprot.org/uniprotkb/P34903/entry","name":"GABRA3","description":"Gamma-aminobutyric acid receptor subunit alpha-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48429392","identifier":"Q99928","identifierLink":"https://www.uniprot.org/uniprotkb/Q99928/entry","name":"GABRG3","description":"Gamma-aminobutyric acid receptor subunit gamma-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6258252","identifier":"P28472","identifierLink":"https://www.uniprot.org/uniprotkb/P28472/entry","name":"GABRB3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8580","complexName":"GABA-A receptor, alpha3-beta2-gamma2","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states.\r\n\r\nGABA-A alpha-3 receptor subtypes undergo pre-mRNA editing by adenosine desaminase (ADAR) resulting in reduced cell surface expression and the total number of alpha-3 subunits, suggesting that editing plays a role in receptor trafficking.\r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-1763805","identifier":"P34903","identifierLink":"https://www.uniprot.org/uniprotkb/P34903/entry","name":"GABRA3","description":"Gamma-aminobutyric acid receptor subunit alpha-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6949072","identifier":"P47870","identifierLink":"https://www.uniprot.org/uniprotkb/P47870/entry","name":"GABRB2","description":"Gamma-aminobutyric acid receptor subunit beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008430","identifier":"P18507","identifierLink":"https://www.uniprot.org/uniprotkb/P18507/entry","name":"GABRG2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8581","complexName":"GABA-A receptor alpha6-beta2-gamma2","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptor assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets.","predictedComplex":false,"interactors":[{"ac":"EBI-6949072","identifier":"P47870","identifierLink":"https://www.uniprot.org/uniprotkb/P47870/entry","name":"GABRB2","description":"Gamma-aminobutyric acid receptor subunit beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008430","identifier":"P18507","identifierLink":"https://www.uniprot.org/uniprotkb/P18507/entry","name":"GABRG2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008507","identifier":"Q16445","identifierLink":"https://www.uniprot.org/uniprotkb/Q16445/entry","name":"GABRA6","description":"Gamma-aminobutyric acid receptor subunit alpha-6","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8601","complexName":"STRIPAK complex, STRIP2-STRN3 variant","organismName":"Homo sapiens; 9606","description":"Multisubunit protein phosphatase complex which acts as a signaling hub to recruit multiple catalytic and regulatory binding partners  Key negative regulator of the Hippo pathway that controls tissue homeostasis and suppresses tumorigenesis. Recruited to auto-activated STK3/4 (Q13188/Q13043)  via the adaptor protein SLMAP (Q14BN4) to reverse T-loop phosphorylation of these Hippo kinases, limiting their activation through feedback inhibition. Inositol hexakisphosphate acts to sense the cellular phosphate balance and may regulate phosphatase activity by stabilizing STRIP2, enabling STRIPAK assembly.","predictedComplex":false,"interactors":[{"ac":"EBI-1053857","identifier":"Q13033","identifierLink":"https://www.uniprot.org/uniprotkb/Q13033/entry","name":"STRN3","description":"Striatin-3","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15653","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1251377","identifier":"CHEBI:17401","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:17401","name":"myo-inositol hexakisphosphate","description":"myo-inositol hexakisphosphate","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1774281","identifier":"Q9ULQ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ULQ0/entry","name":"STRIP2","description":"Striatin-interacting protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302388","identifier":"P30153","identifierLink":"https://www.uniprot.org/uniprotkb/P30153/entry","name":"PPP2R1A","description":"Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712311","identifier":"P67775","identifierLink":"https://www.uniprot.org/uniprotkb/P67775/entry","name":"PPP2CA","description":"Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-713935","identifier":"Q9Y3A3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3A3/entry","name":"MOB4","description":"MOB-like protein phocein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8602","complexName":"GluK1-GluK2 glutamate ionotropic kainate-type receptor complex","organismName":"Rattus norvegicus; 10116","description":"An ionotropic glutamate receptor which localizes either post-synaptically to drive synaptic depolarization or pre-synaptically to regulate neurotransmitter release. Belonging to the kainate-type glutamate receptors (KARs) sub-family, GluKs are ligand-gated cation channels activated by the neurotransmitter l-glutamate. GluKs play complex roles in neural development and CNS function.","predictedComplex":false,"interactors":[{"ac":"EBI-15612757","identifier":"P22756","identifierLink":"https://www.uniprot.org/uniprotkb/P22756/entry","name":"Grik1","description":"Glutamate receptor ionotropic, kainate 1","stochiometry":"minValue: 1, maxValue: 3","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7809795","identifier":"P42260","identifierLink":"https://www.uniprot.org/uniprotkb/P42260/entry","name":"Grik2","description":"Glutamate receptor ionotropic, kainate 2","stochiometry":"minValue: 1, maxValue: 3","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8603","complexName":"GluK2-GluK5 glutamate ionotropic kainate-type receptor complex","organismName":"Rattus norvegicus; 10116","description":"An ionotropic glutamate receptor which localizes either post-synaptically to drive synaptic depolarization or pre-synaptically to regulate neurotransmitter release. Belonging to the kainate-type glutamate receptors (KARs) sub-family, GluKs are ligand-gated cation channels activated by the neurotransmitter l-glutamate. GluKs play complex roles in neural development and CNS function.","predictedComplex":false,"interactors":[{"ac":"EBI-48421334","identifier":"Q63273","identifierLink":"https://www.uniprot.org/uniprotkb/Q63273/entry","name":"Grik5","description":"Glutamate receptor ionotropic, kainate 5","stochiometry":"minValue: 1, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7809795","identifier":"P42260","identifierLink":"https://www.uniprot.org/uniprotkb/P42260/entry","name":"Grik2","description":"Glutamate receptor ionotropic, kainate 2","stochiometry":"minValue: 2, maxValue: 3","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8604","complexName":"STRIPAK complex, STRIP1-STRN variant","organismName":"Homo sapiens; 9606","description":"Multisubunit protein phosphatase complex which acts as a signaling hub to recruit multiple catalytic and regulatory binding partners  Key negative regulator of the Hippo pathway that controls tissue homeostasis and suppresses tumorigenesis. Recruited to auto-activated STK3/4 (Q13188/Q13043)  via the adaptor protein SLMAP (Q14BN4) to reverse T-loop phosphorylation of these Hippo kinases, limiting their activation through feedback inhibition. Inositol hexakisphosphate acts to sense the cellular phosphate balance and may regulate phosphatase activity by stabilizing STRIP1, enabling STRIPAK assembly.","predictedComplex":false,"interactors":[{"ac":"EBI-1046642","identifier":"O43815","identifierLink":"https://www.uniprot.org/uniprotkb/O43815/entry","name":"STRN","description":"Striatin","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15653","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1251377","identifier":"CHEBI:17401","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:17401","name":"myo-inositol hexakisphosphate","description":"myo-inositol hexakisphosphate","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1773588","identifier":"Q5VSL9","identifierLink":"https://www.uniprot.org/uniprotkb/Q5VSL9/entry","name":"STRIP1","description":"Striatin-interacting protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302388","identifier":"P30153","identifierLink":"https://www.uniprot.org/uniprotkb/P30153/entry","name":"PPP2R1A","description":"Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712311","identifier":"P67775","identifierLink":"https://www.uniprot.org/uniprotkb/P67775/entry","name":"PPP2CA","description":"Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-713935","identifier":"Q9Y3A3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3A3/entry","name":"MOB4","description":"MOB-like protein phocein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8605","complexName":"STRIPAK complex, STRIP2-STRN variant","organismName":"Homo sapiens; 9606","description":"Multisubunit protein phosphatase complex which acts as a signaling hub to recruit multiple catalytic and regulatory binding partners  Key negative regulator of the Hippo pathway that controls tissue homeostasis and suppresses tumorigenesis. Recruited to auto-activated STK3/4 (Q13188/Q13043)  via the adaptor protein SLMAP (Q14BN4) to reverse T-loop phosphorylation of these Hippo kinases, limiting their activation through feedback inhibition. Inositol hexakisphosphate acts to sense the cellular phosphate balance and may regulate phosphatase activity by stabilizing STRIP2, enabling STRIPAK assembly.","predictedComplex":false,"interactors":[{"ac":"EBI-1046642","identifier":"O43815","identifierLink":"https://www.uniprot.org/uniprotkb/O43815/entry","name":"STRN","description":"Striatin","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15653","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1251377","identifier":"CHEBI:17401","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:17401","name":"myo-inositol hexakisphosphate","description":"myo-inositol hexakisphosphate","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1774281","identifier":"Q9ULQ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ULQ0/entry","name":"STRIP2","description":"Striatin-interacting protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302388","identifier":"P30153","identifierLink":"https://www.uniprot.org/uniprotkb/P30153/entry","name":"PPP2R1A","description":"Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712311","identifier":"P67775","identifierLink":"https://www.uniprot.org/uniprotkb/P67775/entry","name":"PPP2CA","description":"Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-713935","identifier":"Q9Y3A3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3A3/entry","name":"MOB4","description":"MOB-like protein phocein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8606","complexName":"STRIPAK complex, STRIP1-STRN4 variant","organismName":"Homo sapiens; 9606","description":"Multisubunit protein phosphatase complex which acts as a signaling hub to recruit multiple catalytic and regulatory binding partners  Key negative regulator of the Hippo pathway that controls tissue homeostasis and suppresses tumorigenesis. Recruited to auto-activated STK3/4 (Q13188/Q13043)  via the adaptor protein SLMAP (Q14BN4) to reverse T-loop phosphorylation of these Hippo kinases, limiting their activation through feedback inhibition. Inositol hexakisphosphate acts to sense the cellular phosphate balance and may regulate phosphatase activity by stabilizing STRIP1, enabling STRIPAK assembly.","predictedComplex":false,"interactors":[{"ac":"EBI-1251377","identifier":"CHEBI:17401","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:17401","name":"myo-inositol hexakisphosphate","description":"myo-inositol hexakisphosphate","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1773588","identifier":"Q5VSL9","identifierLink":"https://www.uniprot.org/uniprotkb/Q5VSL9/entry","name":"STRIP1","description":"Striatin-interacting protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302388","identifier":"P30153","identifierLink":"https://www.uniprot.org/uniprotkb/P30153/entry","name":"PPP2R1A","description":"Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712311","identifier":"P67775","identifierLink":"https://www.uniprot.org/uniprotkb/P67775/entry","name":"PPP2CA","description":"Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-713935","identifier":"Q9Y3A3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3A3/entry","name":"MOB4","description":"MOB-like protein phocein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-717245","identifier":"Q9NRL3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NRL3/entry","name":"STRN4","description":"Striatin-4","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15653","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8607","complexName":"STRIPAK complex, STRIP2-STRN4 variant","organismName":"Homo sapiens; 9606","description":"Multisubunit protein phosphatase complex which acts as a signaling hub to recruit multiple catalytic and regulatory binding partners  Key negative regulator of the Hippo pathway that controls tissue homeostasis and suppresses tumorigenesis. Recruited to auto-activated STK3/4 (Q13188/Q13043)  via the adaptor protein SLMAP (Q14BN4) to reverse T-loop phosphorylation of these Hippo kinases, limiting their activation through feedback inhibition. Inositol hexakisphosphate acts to sense the cellular phosphate balance and may regulate phosphatase activity by stabilizing STRIP2, enabling STRIPAK assembly.","predictedComplex":false,"interactors":[{"ac":"EBI-1251377","identifier":"CHEBI:17401","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:17401","name":"myo-inositol hexakisphosphate","description":"myo-inositol hexakisphosphate","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-1774281","identifier":"Q9ULQ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9ULQ0/entry","name":"STRIP2","description":"Striatin-interacting protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13239","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302388","identifier":"P30153","identifierLink":"https://www.uniprot.org/uniprotkb/P30153/entry","name":"PPP2R1A","description":"Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10648","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712311","identifier":"P67775","identifierLink":"https://www.uniprot.org/uniprotkb/P67775/entry","name":"PPP2CA","description":"Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-713935","identifier":"Q9Y3A3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3A3/entry","name":"MOB4","description":"MOB-like protein phocein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR22599","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-717245","identifier":"Q9NRL3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NRL3/entry","name":"STRN4","description":"Striatin-4","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15653","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-8608","complexName":"GluK1-GluK3-GluK5 glutamate ionotropic kainate-type receptor complex","organismName":"Rattus norvegicus; 10116","description":"An ionotropic glutamate receptor which localizes either post-synaptically to drive synaptic depolarization or pre-synaptically to regulate neurotransmitter release. Belonging to the kainate-type glutamate receptors (KARs) sub-family, GluKs are ligand-gated cation channels activated by the neurotransmitter l-glutamate. GluKs play complex roles in neural development and CNS function.","predictedComplex":false,"interactors":[{"ac":"EBI-15612757","identifier":"P22756","identifierLink":"https://www.uniprot.org/uniprotkb/P22756/entry","name":"Grik1","description":"Glutamate receptor ionotropic, kainate 1","stochiometry":"minValue: 1, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48420651","identifier":"P42264","identifierLink":"https://www.uniprot.org/uniprotkb/P42264/entry","name":"Grik3","description":"Glutamate receptor ionotropic, kainate 3","stochiometry":"minValue: 1, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-48421334","identifier":"Q63273","identifierLink":"https://www.uniprot.org/uniprotkb/Q63273/entry","name":"Grik5","description":"Glutamate receptor ionotropic, kainate 5","stochiometry":"minValue: 1, maxValue: 2","interactorType":"protein","organismName":"Rattus norvegicus; 10116","xrefs":[{"identifier":"PTHR18966","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1219","complexName":"Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nRegulates cell differentiation specifically in post-mitotic brain tissue. In this variant of the complex transcriptional repression is probably driven by the presence of the ARID1A subunit. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, SMARCA2/BRM (CPX-1203) and SMARCA4/BRG1 (this complex) do not co-occur in the same complex. In contrast to the neuron-specific SWI/SNF complex the brain-specific SWI/SNF complex misses core subunit SMARCC1 (Q92922) and alternative subunits ACTL6A (O96019), SMARCD1 (Q96GM5) or SMARCD3 (Q6STE5). May contain pBAF-specific subunit PBRM1 (BAF180, Q86U86).  \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-302489","identifier":"P51532","identifierLink":"https://www.uniprot.org/uniprotkb/P51532/entry","name":"SMARCA4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358441","identifier":"Q92925","identifierLink":"https://www.uniprot.org/uniprotkb/Q92925/entry","name":"SMARCD2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-637887","identifier":"O14497","identifierLink":"https://www.uniprot.org/uniprotkb/O14497/entry","name":"ARID1A","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724528","identifier":"O94805","identifierLink":"https://www.uniprot.org/uniprotkb/O94805/entry","name":"ACTL6B","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1220","complexName":"Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nRegulates cell differentiation specifically in post-mitotic brain tissue. In this variant of the complex transcriptional activation is probably driven by the presence of the ARID1B subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 &  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, SMARCA2/BRM (this complex) and SMARCA4/BRG1 (CPX-1221) do not co-occur in the same complex. In contrast to the neuron-specific SWI/SNF complex the brain-specific SWI/SNF complex misses core subunit SMARCC1 (Q92922) and alternative subunits ACTL6A (O96019), SMARCD1 (Q96GM5) or SMARCD3 (Q6STE5). May contain pBAF-specific subunit PBRM1 (BAF180, Q86U86).  \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358441","identifier":"Q92925","identifierLink":"https://www.uniprot.org/uniprotkb/Q92925/entry","name":"SMARCD2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679562","identifier":"P51531","identifierLink":"https://www.uniprot.org/uniprotkb/P51531/entry","name":"SMARCA2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679921","identifier":"Q8NFD5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NFD5/entry","name":"ARID1B","description":"AT-rich interactive domain-containing protein 1B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724528","identifier":"O94805","identifierLink":"https://www.uniprot.org/uniprotkb/O94805/entry","name":"ACTL6B","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1221","complexName":"Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nRegulates cell differentiation specifically in post-mitotic brain tissue. In this variant of the complex transcriptional activation is probably driven by the presence of the ARID1B subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 &  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, SMARCA2/BRM (CPX-1220) and SMARCA4/BRG1 (this complex) do not co-occur in the same complex. In contrast to the neuron-specific SWI/SNF complex the brain-specific SWI/SNF complex misses core subunit SMARCC1 (Q92922) and alternative subunits ACTL6A (O96019), SMARCD1 (Q96GM5) or SMARCD3 (Q6STE5). May contain pBAF-specific subunit PBRM1 (BAF180, Q86U86).  \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-302489","identifier":"P51532","identifierLink":"https://www.uniprot.org/uniprotkb/P51532/entry","name":"SMARCA4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358441","identifier":"Q92925","identifierLink":"https://www.uniprot.org/uniprotkb/Q92925/entry","name":"SMARCD2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679921","identifier":"Q8NFD5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NFD5/entry","name":"ARID1B","description":"AT-rich interactive domain-containing protein 1B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724528","identifier":"O94805","identifierLink":"https://www.uniprot.org/uniprotkb/O94805/entry","name":"ACTL6B","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1222","complexName":"Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to promoters and enhancers of target genes in muscle cells and alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nSWI/SNF complexes containing DPF3 are specific to muscle cells where they play an essential role in the development of heart and skeletal muscle cells. Also found in brown adipocytes where they regulate gene-expression of brown fat-selective genes. \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional repression is probably driven by the presence of the ARID1A subunit. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, SMARCA2/BRM (CPX-1194) and SMARCA4/BRG1 (this complex) do not co-occur in the same complex. SMARCD1 (BAF60A) and SMARCD2 (BAF60B) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: DPF2/BAF45D (Q92785), BRD9 (Q9H8M2), SS18 (Q15532), BCL11A (Q9H165), BCL11B (Q9C0K0), BCL7A (Q4VC05), BCL7B (Q9BQE9), BCL7C (Q8WUZ0). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-16355309","identifier":"Q92784","identifierLink":"https://www.uniprot.org/uniprotkb/Q92784/entry","name":"DPF3","description":"Zinc finger protein DPF3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302489","identifier":"P51532","identifierLink":"https://www.uniprot.org/uniprotkb/P51532/entry","name":"SMARCA4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355018","identifier":"O96019","identifierLink":"https://www.uniprot.org/uniprotkb/O96019/entry","name":"ACTL6A","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358441","identifier":"Q92925","identifierLink":"https://www.uniprot.org/uniprotkb/Q92925/entry","name":"SMARCD2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465496","identifier":"Q6STE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6STE5/entry","name":"SMARCD3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-637887","identifier":"O14497","identifierLink":"https://www.uniprot.org/uniprotkb/O14497/entry","name":"ARID1A","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1223","complexName":"Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to promoters and enhancers of target genes in muscle cells and alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nSWI/SNF complexes containing DPF3 are specific to muscle cells where they play an essential role in the development of heart and skeletal muscle cells. Also found in brown adipocytes where they regulate gene-expression of brown fat-selective genes. \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional activation is probably driven by the presence of the ARID1B subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 &  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, SMARCA2/BRM (this complex) and SMARCA4/BRG1 (CPX-1224) do not co-occur in the same complex. SMARCD1 (BAF60A) and SMARCD2 (BAF60B) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: DPF2/BAF45D (Q92785), BRD9 (Q9H8M2), SS18 (Q15532), BCL11A (Q9H165), BCL11B (Q9C0K0), BCL7A (Q4VC05), BCL7B (Q9BQE9), BCL7C (Q8WUZ0). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-16355309","identifier":"Q92784","identifierLink":"https://www.uniprot.org/uniprotkb/Q92784/entry","name":"DPF3","description":"Zinc finger protein DPF3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355018","identifier":"O96019","identifierLink":"https://www.uniprot.org/uniprotkb/O96019/entry","name":"ACTL6A","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358441","identifier":"Q92925","identifierLink":"https://www.uniprot.org/uniprotkb/Q92925/entry","name":"SMARCD2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465496","identifier":"Q6STE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6STE5/entry","name":"SMARCD3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679562","identifier":"P51531","identifierLink":"https://www.uniprot.org/uniprotkb/P51531/entry","name":"SMARCA2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679921","identifier":"Q8NFD5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NFD5/entry","name":"ARID1B","description":"AT-rich interactive domain-containing protein 1B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1224","complexName":"Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to promoters and enhancers of target genes in muscle cells and alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nSWI/SNF complexes containing DPF3 are specific to muscle cells where they play an essential role in the development of heart and skeletal muscle cells. Also found in brown adipocytes where they regulate gene-expression of brown fat-selective genes. \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional activation is probably driven by the presence of the ARID1B subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 &  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, SMARCA2/BRM (CPX-1223) and SMARCA4/BRG1 (this complex) do not co-occur in the same complex. SMARCD1 (BAF60A) and SMARCD2 (BAF60B) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: DPF2/BAF45D (Q92785), BRD9 (Q9H8M2), SS18 (Q15532), BCL11A (Q9H165), BCL11B (Q9C0K0), BCL7A (Q4VC05), BCL7B (Q9BQE9), BCL7C (Q8WUZ0). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-16355309","identifier":"Q92784","identifierLink":"https://www.uniprot.org/uniprotkb/Q92784/entry","name":"DPF3","description":"Zinc finger protein DPF3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302489","identifier":"P51532","identifierLink":"https://www.uniprot.org/uniprotkb/P51532/entry","name":"SMARCA4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355018","identifier":"O96019","identifierLink":"https://www.uniprot.org/uniprotkb/O96019/entry","name":"ACTL6A","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358441","identifier":"Q92925","identifierLink":"https://www.uniprot.org/uniprotkb/Q92925/entry","name":"SMARCD2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465496","identifier":"Q6STE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6STE5/entry","name":"SMARCD3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679921","identifier":"Q8NFD5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NFD5/entry","name":"ARID1B","description":"AT-rich interactive domain-containing protein 1B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1225","complexName":"Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to promoters and enhancers of target genes in muscle cells and alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nSWI/SNF complexes containing DPF3 are specific to muscle cells where they play an essential role in the development of heart and skeletal muscle cells. Also found in brown adipocytes where they regulate gene-expression of brown fat-selective genes. \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional repression is probably driven by the presence of the ARID1A subunit. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, SMARCA2/BRM (this complex) and SMARCA4/BRG1 (CPX-1226) do not co-occur in the same complex. SMARCD1 (BAF60A) and SMARCD2 (BAF60B) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: DPF2/BAF45D (Q92785), BRD9 (Q9H8M2), SS18 (Q15532), BCL11A (Q9H165), BCL11B (Q9C0K0), BCL7A (Q4VC05), BCL7B (Q9BQE9), BCL7C (Q8WUZ0). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-16355309","identifier":"Q92784","identifierLink":"https://www.uniprot.org/uniprotkb/Q92784/entry","name":"DPF3","description":"Zinc finger protein DPF3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358441","identifier":"Q92925","identifierLink":"https://www.uniprot.org/uniprotkb/Q92925/entry","name":"SMARCD2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465496","identifier":"Q6STE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6STE5/entry","name":"SMARCD3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-637887","identifier":"O14497","identifierLink":"https://www.uniprot.org/uniprotkb/O14497/entry","name":"ARID1A","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679562","identifier":"P51531","identifierLink":"https://www.uniprot.org/uniprotkb/P51531/entry","name":"SMARCA2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724528","identifier":"O94805","identifierLink":"https://www.uniprot.org/uniprotkb/O94805/entry","name":"ACTL6B","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1226","complexName":"Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to promoters and enhancers of target genes in muscle cells and alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nSWI/SNF complexes containing DPF3 are specific to muscle cells where they play an essential role in the development of heart and skeletal muscle cells. Also found in brown adipocytes where they regulate gene-expression of brown fat-selective genes. \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional repression is probably driven by the presence of the ARID1A subunit. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, SMARCA2/BRM (CPX-1225) and SMARCA4/BRG1 (this complex) do not co-occur in the same complex. SMARCD1 (BAF60A) and SMARCD2 (BAF60B) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: DPF2/BAF45D (Q92785), BRD9 (Q9H8M2), SS18 (Q15532), BCL11A (Q9H165), BCL11B (Q9C0K0), BCL7A (Q4VC05), BCL7B (Q9BQE9), BCL7C (Q8WUZ0). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-16355309","identifier":"Q92784","identifierLink":"https://www.uniprot.org/uniprotkb/Q92784/entry","name":"DPF3","description":"Zinc finger protein DPF3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302489","identifier":"P51532","identifierLink":"https://www.uniprot.org/uniprotkb/P51532/entry","name":"SMARCA4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358441","identifier":"Q92925","identifierLink":"https://www.uniprot.org/uniprotkb/Q92925/entry","name":"SMARCD2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465496","identifier":"Q6STE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6STE5/entry","name":"SMARCD3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-637887","identifier":"O14497","identifierLink":"https://www.uniprot.org/uniprotkb/O14497/entry","name":"ARID1A","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724528","identifier":"O94805","identifierLink":"https://www.uniprot.org/uniprotkb/O94805/entry","name":"ACTL6B","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1227","complexName":"Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to promoters and enhancers of target genes in muscle cells and alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nSWI/SNF complexes containing DPF3 are specific to muscle cells where they play an essential role in the development of heart and skeletal muscle cells. Also found in brown adipocytes where they regulate gene-expression of brown fat-selective genes. \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional activation is probably driven by the presence of the ARID1B subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 &  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, SMARCA2/BRM (this complex) and SMARCA4/BRG1 (CPX-1228) do not co-occur in the same complex. SMARCD1 (BAF60A) and SMARCD2 (BAF60B) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: DPF2/BAF45D (Q92785), BRD9 (Q9H8M2), SS18 (Q15532), BCL11A (Q9H165), BCL11B (Q9C0K0), BCL7A (Q4VC05), BCL7B (Q9BQE9), BCL7C (Q8WUZ0). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-16355309","identifier":"Q92784","identifierLink":"https://www.uniprot.org/uniprotkb/Q92784/entry","name":"DPF3","description":"Zinc finger protein DPF3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358441","identifier":"Q92925","identifierLink":"https://www.uniprot.org/uniprotkb/Q92925/entry","name":"SMARCD2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465496","identifier":"Q6STE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6STE5/entry","name":"SMARCD3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679562","identifier":"P51531","identifierLink":"https://www.uniprot.org/uniprotkb/P51531/entry","name":"SMARCA2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679921","identifier":"Q8NFD5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NFD5/entry","name":"ARID1B","description":"AT-rich interactive domain-containing protein 1B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724528","identifier":"O94805","identifierLink":"https://www.uniprot.org/uniprotkb/O94805/entry","name":"ACTL6B","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1228","complexName":"Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant","organismName":"Homo sapiens; 9606","description":"An ATP-dependent chromatin remodeling complex which is recruited to promoters and enhancers of target genes in muscle cells and alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P11473) via SMARCD subunits. \r\n\r\nSWI/SNF complexes containing DPF3 are specific to muscle cells where they play an essential role in the development of heart and skeletal muscle cells. Also found in brown adipocytes where they regulate gene-expression of brown fat-selective genes. \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional activation is probably driven by the presence of the ARID1B subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 &  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, SMARCA2/BRM (CPX-1227) and SMARCA4/BRG1 (this complex) do not co-occur in the same complex. SMARCD1 (BAF60A) and SMARCD2 (BAF60B) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: DPF2/BAF45D (Q92785), BRD9 (Q9H8M2), SS18 (Q15532), BCL11A (Q9H165), BCL11B (Q9C0K0), BCL7A (Q4VC05), BCL7B (Q9BQE9), BCL7C (Q8WUZ0). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-16355309","identifier":"Q92784","identifierLink":"https://www.uniprot.org/uniprotkb/Q92784/entry","name":"DPF3","description":"Zinc finger protein DPF3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302489","identifier":"P51532","identifierLink":"https://www.uniprot.org/uniprotkb/P51532/entry","name":"SMARCA4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-355653","identifier":"Q92922","identifierLink":"https://www.uniprot.org/uniprotkb/Q92922/entry","name":"SMARCC1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357418","identifier":"Q8TAQ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAQ2/entry","name":"SMARCC2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358419","identifier":"Q12824","identifierLink":"https://www.uniprot.org/uniprotkb/Q12824/entry","name":"SMARCB1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358441","identifier":"Q92925","identifierLink":"https://www.uniprot.org/uniprotkb/Q92925/entry","name":"SMARCD2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-358489","identifier":"Q96GM5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96GM5/entry","name":"SMARCD1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-455078","identifier":"Q969G3","identifierLink":"https://www.uniprot.org/uniprotkb/Q969G3/entry","name":"SMARCE1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-465496","identifier":"Q6STE5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6STE5/entry","name":"SMARCD3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-679921","identifier":"Q8NFD5","identifierLink":"https://www.uniprot.org/uniprotkb/Q8NFD5/entry","name":"ARID1B","description":"AT-rich interactive domain-containing protein 1B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-724528","identifier":"O94805","identifierLink":"https://www.uniprot.org/uniprotkb/O94805/entry","name":"ACTL6B","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1229","complexName":"RAP1-GCR1-GCR2 transcription activation complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Transcription factor required for the transcription of glycolytic genes. Appears to simultaneously bind to two adjacent DNA elements (UAS(RPG) and the CT box, bound specifically by RAP1 and GCR1, respectively). The complex can activate transcription through isolated UAS(RPG) ((upstream activating sequence in ribosomal protein genes)) but not CT elements. CT box-dependent transcriptional activation requires GCR2. GCR2 is essential only for the expression of CT box-containing glycolytic genes, but not for ribosomal genes, which do not have a CT box. GCR2 tappears  to  induce a  conformation change in GCR1  and/or stimulate \r\nits hyperphosphorylation.","predictedComplex":false,"interactors":[{"ac":"EBI-14821","identifier":"P11938","identifierLink":"https://www.uniprot.org/uniprotkb/P11938/entry","name":"RAP1","description":"DNA-binding protein RAP1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR16466","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7463","identifier":"P07261","identifierLink":"https://www.uniprot.org/uniprotkb/P07261/entry","name":"GCR1","description":"Glycolytic genes transcriptional activator GCR1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR37784","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7469","identifier":"Q01722","identifierLink":"https://www.uniprot.org/uniprotkb/Q01722/entry","name":"GCR2","description":"Glycolytic genes transcriptional activator GCR2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1230","complexName":"BNI4-GLC7 phosphatase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Protein phosphatase complex which is important for the regulation of bud site emergence. The asymmetric localization of BNI4-GLC7 is essential for proper morphological development and correct deposition of the chitin ring as the complex  recruits chitin synthase III to the cell cortex on the mother-side of the septin collar.","predictedComplex":false,"interactors":[{"ac":"EBI-13715","identifier":"P32598","identifierLink":"https://www.uniprot.org/uniprotkb/P32598/entry","name":"GLC7","description":"Serine/threonine-protein phosphatase PP1-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11668","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-3704","identifier":"P53858","identifierLink":"https://www.uniprot.org/uniprotkb/P53858/entry","name":"BNI4","description":"Protein BNI4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12751","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1231","complexName":"GAC1-GLC7 phosphatase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Protein phosphatase complex that potentially controls glycogen synthesis by regulating the phosphorylation state of glycogen synthase, GSY2.","predictedComplex":false,"interactors":[{"ac":"EBI-13715","identifier":"P32598","identifierLink":"https://www.uniprot.org/uniprotkb/P32598/entry","name":"GLC7","description":"Serine/threonine-protein phosphatase PP1-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11668","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-7259","identifier":"P28006","identifierLink":"https://www.uniprot.org/uniprotkb/P28006/entry","name":"GAC1","description":"Serine/threonine-protein phosphatase 1 regulatory subunit GAC1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12307","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1232","complexName":"SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nSWI/SNF complexes containing Dpf3 are specific to muscle cells where they play an essential role in the development of heart and skeletal muscle cells. Also found in brown adipocytes where they regulate gene-expression of brown fat-selective genes. \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional repression is probably driven by the presence of the Arid1a subunit. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, Smarca2/Brm (this complex) and Smarca4/Brg1 (CPX-1233) do not co-occur in the same complex. Smarcd1 (Baf60a) and Smarcd2 (Baf60b) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: Dpf2/Baf45d (Q61103), Brd9 (Q3UQU0), Ss18 (Q62280), Bcl11a (Q9QYE3), Bcl11b (Q99PV8), Bcl7a (Q9CXE2), Bcl7b (Q921K9), BCL7C (O08664). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-10765904","identifier":"Q6DIC0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6DIC0/entry","name":"Smarca2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942759","identifier":"Q9Z2N8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z2N8/entry","name":"Actl6a","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371499","identifier":"A2BH40","identifierLink":"https://www.uniprot.org/uniprotkb/A2BH40/entry","name":"Arid1a","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371529","identifier":"Q61466","identifierLink":"https://www.uniprot.org/uniprotkb/Q61466/entry","name":"Smarcd1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3870565","identifier":"Q6PDG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDG5/entry","name":"Smarcc2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5736813","identifier":"Q99JR8","identifierLink":"https://www.uniprot.org/uniprotkb/Q99JR8/entry","name":"Smarcd2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642789","identifier":"O54941","identifierLink":"https://www.uniprot.org/uniprotkb/O54941/entry","name":"Smarce1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-648047","identifier":"P97496","identifierLink":"https://www.uniprot.org/uniprotkb/P97496/entry","name":"Smarcc1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-689365","identifier":"Q9Z0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0H3/entry","name":"Smarcb1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7525857","identifier":"Q6P9Z1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P9Z1/entry","name":"Smarcd3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1233","complexName":"SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nRegulates cell differentiation in several lineages, such as T cells and myocytes, and specific variants exist in embryonic stem cells (esBAF) and neuronal progenitor cells (npBAF). \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional repression is probably driven by the presence of the Arid1a subunit. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, Smarca2/Brm (CPX-1232) and Smarca4/Brg1 (this complex) do not co-occur in the same complex. Smarcd1 (Baf60a) and Smarcd2 (Baf60b) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: Dpf2/Baf45d (Q61103), Brd9 (Q3UQU0), Ss18 (Q62280), Bcl11a (Q9QYE3), Bcl11b (Q99PV8), Bcl7a (Q9CXE2), Bcl7b (Q921K9), Bcl7c (O08664). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-1210244","identifier":"Q3TKT4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TKT4/entry","name":"Smarca4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942759","identifier":"Q9Z2N8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z2N8/entry","name":"Actl6a","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371499","identifier":"A2BH40","identifierLink":"https://www.uniprot.org/uniprotkb/A2BH40/entry","name":"Arid1a","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371529","identifier":"Q61466","identifierLink":"https://www.uniprot.org/uniprotkb/Q61466/entry","name":"Smarcd1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3870565","identifier":"Q6PDG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDG5/entry","name":"Smarcc2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5736813","identifier":"Q99JR8","identifierLink":"https://www.uniprot.org/uniprotkb/Q99JR8/entry","name":"Smarcd2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642789","identifier":"O54941","identifierLink":"https://www.uniprot.org/uniprotkb/O54941/entry","name":"Smarce1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-648047","identifier":"P97496","identifierLink":"https://www.uniprot.org/uniprotkb/P97496/entry","name":"Smarcc1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-689365","identifier":"Q9Z0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0H3/entry","name":"Smarcb1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7525857","identifier":"Q6P9Z1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P9Z1/entry","name":"Smarcd3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1234","complexName":"SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nRegulates cell differentiation in several lineages, such as T cells and myocytes, and specific variants exist in embryonic stem cells (esBAF) and neuronal progenitor cells (npBAF). \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional activation is probably driven by the presence of the Arid1b subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 &  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, Smarca2/Brm (this complex) and Smarca4/Brg1 (CPX-1235) do not co-occur in the same complex. Smarcd1 (Baf60a) and Smarcd2 (Baf60b) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: Dpf2/Baf45d (Q61103), Brd9 (Q3UQU0), Ss18 (Q62280), Bcl11a (Q9QYE3), Bcl11b (Q99PV8), Bcl7a (Q9CXE2), Bcl7b (Q921K9), BCL7C (O08664). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-10765904","identifier":"Q6DIC0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6DIC0/entry","name":"Smarca2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16368402","identifier":"E9Q6R4","identifierLink":"https://www.uniprot.org/uniprotkb/E9Q6R4/entry","name":"Arid1b","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-2942759","identifier":"Q9Z2N8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z2N8/entry","name":"Actl6a","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371529","identifier":"Q61466","identifierLink":"https://www.uniprot.org/uniprotkb/Q61466/entry","name":"Smarcd1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3870565","identifier":"Q6PDG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDG5/entry","name":"Smarcc2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5736813","identifier":"Q99JR8","identifierLink":"https://www.uniprot.org/uniprotkb/Q99JR8/entry","name":"Smarcd2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642789","identifier":"O54941","identifierLink":"https://www.uniprot.org/uniprotkb/O54941/entry","name":"Smarce1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-648047","identifier":"P97496","identifierLink":"https://www.uniprot.org/uniprotkb/P97496/entry","name":"Smarcc1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-689365","identifier":"Q9Z0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0H3/entry","name":"Smarcb1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7525857","identifier":"Q6P9Z1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P9Z1/entry","name":"Smarcd3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1235","complexName":"SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nRegulates cell differentiation in several lineages, such as T cells and myocytes, and specific variants exist in embryonic stem cells (esBAF) and neuronal progenitor cells (npBAF). \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional activation is probably driven by the presence of the Arid1b subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 &  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, Smarca2/Brm (CPX-1234) and Smarca4/Brg1 (this complex) do not co-occur in the same complex. Smarcd1 (Baf60a) and Smarcd2 (Baf60b) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: Dpf2/Baf45d (Q61103), Brd9 (Q3UQU0), Ss18 (Q62280), Bcl11a (Q9QYE3), Bcl11b (Q99PV8), Bcl7a (Q9CXE2), Bcl7b (Q921K9), BCL7C (O08664). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-1210244","identifier":"Q3TKT4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TKT4/entry","name":"Smarca4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16368402","identifier":"E9Q6R4","identifierLink":"https://www.uniprot.org/uniprotkb/E9Q6R4/entry","name":"Arid1b","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-2942759","identifier":"Q9Z2N8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z2N8/entry","name":"Actl6a","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371529","identifier":"Q61466","identifierLink":"https://www.uniprot.org/uniprotkb/Q61466/entry","name":"Smarcd1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3870565","identifier":"Q6PDG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDG5/entry","name":"Smarcc2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5736813","identifier":"Q99JR8","identifierLink":"https://www.uniprot.org/uniprotkb/Q99JR8/entry","name":"Smarcd2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642789","identifier":"O54941","identifierLink":"https://www.uniprot.org/uniprotkb/O54941/entry","name":"Smarce1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-648047","identifier":"P97496","identifierLink":"https://www.uniprot.org/uniprotkb/P97496/entry","name":"Smarcc1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-689365","identifier":"Q9Z0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0H3/entry","name":"Smarcb1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7525857","identifier":"Q6P9Z1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P9Z1/entry","name":"Smarcd3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1236","complexName":"SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nRegulates cell differentiation in several lineages, such as T cells and myocytes, and specific variants exist in embryonic stem cells (esBAF) and neuronal progenitor cells (npBAF). \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional repression is probably driven by the presence of the Arid1a subunit. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, Smarca2/Brm (this complex) and Smarca4/Brg1 (CPX-1237) do not co-occur in the same complex. Smarcd1 (Baf60a) and Smarcd2 (Baf60b) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: Dpf2/Baf45d (Q61103), Brd9 (Q3UQU0), Ss18 (Q62280), Bcl11a (Q9QYE3), Bcl11b (Q99PV8), Bcl7a (Q9CXE2), Bcl7b (Q921K9), BCL7C (O08664). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-10765904","identifier":"Q6DIC0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6DIC0/entry","name":"Smarca2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371499","identifier":"A2BH40","identifierLink":"https://www.uniprot.org/uniprotkb/A2BH40/entry","name":"Arid1a","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371529","identifier":"Q61466","identifierLink":"https://www.uniprot.org/uniprotkb/Q61466/entry","name":"Smarcd1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371554","identifier":"Q99MR0","identifierLink":"https://www.uniprot.org/uniprotkb/Q99MR0/entry","name":"Actl6b","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3870565","identifier":"Q6PDG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDG5/entry","name":"Smarcc2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5736813","identifier":"Q99JR8","identifierLink":"https://www.uniprot.org/uniprotkb/Q99JR8/entry","name":"Smarcd2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642789","identifier":"O54941","identifierLink":"https://www.uniprot.org/uniprotkb/O54941/entry","name":"Smarce1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-648047","identifier":"P97496","identifierLink":"https://www.uniprot.org/uniprotkb/P97496/entry","name":"Smarcc1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-689365","identifier":"Q9Z0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0H3/entry","name":"Smarcb1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7525857","identifier":"Q6P9Z1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P9Z1/entry","name":"Smarcd3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1237","complexName":"SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nRegulates cell differentiation in several lineages, such as T cells and myocytes, and specific variants exist in embryonic stem cells (esBAF) and neuronal progenitor cells (npBAF). \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional repression is probably driven by the presence of the Arid1a subunit. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, Smarca2/Brm (CPX-1236this complex) and Smarca4/Brg1 (this complex) do not co-occur in the same complex. Smarcd1 (Baf60a) and Smarcd2 (Baf60b) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: Dpf2/Baf45d (Q61103), Brd9 (Q3UQU0), Ss18 (Q62280), Bcl11a (Q9QYE3), Bcl11b (Q99PV8), Bcl7a (Q9CXE2), Bcl7b (Q921K9), Bcl7c (O08664). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-1210244","identifier":"Q3TKT4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TKT4/entry","name":"Smarca4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371499","identifier":"A2BH40","identifierLink":"https://www.uniprot.org/uniprotkb/A2BH40/entry","name":"Arid1a","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371529","identifier":"Q61466","identifierLink":"https://www.uniprot.org/uniprotkb/Q61466/entry","name":"Smarcd1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371554","identifier":"Q99MR0","identifierLink":"https://www.uniprot.org/uniprotkb/Q99MR0/entry","name":"Actl6b","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3870565","identifier":"Q6PDG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDG5/entry","name":"Smarcc2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5736813","identifier":"Q99JR8","identifierLink":"https://www.uniprot.org/uniprotkb/Q99JR8/entry","name":"Smarcd2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642789","identifier":"O54941","identifierLink":"https://www.uniprot.org/uniprotkb/O54941/entry","name":"Smarce1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-648047","identifier":"P97496","identifierLink":"https://www.uniprot.org/uniprotkb/P97496/entry","name":"Smarcc1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-689365","identifier":"Q9Z0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0H3/entry","name":"Smarcb1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7525857","identifier":"Q6P9Z1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P9Z1/entry","name":"Smarcd3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1238","complexName":"SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nRegulates cell differentiation in several lineages, such as T cells and myocytes, and specific variants exist in embryonic stem cells (esBAF) and neuronal progenitor cells (npBAF). \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional activation is probably driven by the presence of the Arid1b subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 &  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, Smarca2/Brm (this complex) and Smarca4/Brg1 (CPX-1239) do not co-occur in the same complex. Smarcd1 (Baf60a) and Smarcd2 (Baf60b) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: Dpf2/Baf45d (Q61103), Brd9 (Q3UQU0), Ss18 (Q62280), Bcl11a (Q9QYE3), Bcl11b (Q99PV8), Bcl7a (Q9CXE2), Bcl7b (Q921K9), Bcl7c (O08664). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-10765904","identifier":"Q6DIC0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6DIC0/entry","name":"Smarca2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16368402","identifier":"E9Q6R4","identifierLink":"https://www.uniprot.org/uniprotkb/E9Q6R4/entry","name":"Arid1b","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371529","identifier":"Q61466","identifierLink":"https://www.uniprot.org/uniprotkb/Q61466/entry","name":"Smarcd1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371554","identifier":"Q99MR0","identifierLink":"https://www.uniprot.org/uniprotkb/Q99MR0/entry","name":"Actl6b","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3870565","identifier":"Q6PDG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDG5/entry","name":"Smarcc2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5736813","identifier":"Q99JR8","identifierLink":"https://www.uniprot.org/uniprotkb/Q99JR8/entry","name":"Smarcd2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642789","identifier":"O54941","identifierLink":"https://www.uniprot.org/uniprotkb/O54941/entry","name":"Smarce1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-648047","identifier":"P97496","identifierLink":"https://www.uniprot.org/uniprotkb/P97496/entry","name":"Smarcc1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-689365","identifier":"Q9Z0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0H3/entry","name":"Smarcb1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7525857","identifier":"Q6P9Z1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P9Z1/entry","name":"Smarcd3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1239","complexName":"SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nRegulates cell differentiation in several lineages, such as T cells and myocytes, and specific variants exist in embryonic stem cells (esBAF) and neuronal progenitor cells (npBAF). \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional activation is probably driven by the presence of the Arid1b subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 &  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, Smarca2/Brm (CPX-1238) and Smarca4/Brg1 (this complex) do not co-occur in the same complex. Smarcd1 (Baf60a) and Smarcd2 (Baf60b) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: Dpf2/Baf45d (Q61103), Brd9 (Q3UQU0), Ss18 (Q62280), Bcl11a (Q9QYE3), Bcl11b (Q99PV8), Bcl7a (Q9CXE2), Bcl7b (Q921K9), BCL7C (O08664). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-1210244","identifier":"Q3TKT4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TKT4/entry","name":"Smarca4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16368402","identifier":"E9Q6R4","identifierLink":"https://www.uniprot.org/uniprotkb/E9Q6R4/entry","name":"Arid1b","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371529","identifier":"Q61466","identifierLink":"https://www.uniprot.org/uniprotkb/Q61466/entry","name":"Smarcd1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371554","identifier":"Q99MR0","identifierLink":"https://www.uniprot.org/uniprotkb/Q99MR0/entry","name":"Actl6b","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3870565","identifier":"Q6PDG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDG5/entry","name":"Smarcc2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5736813","identifier":"Q99JR8","identifierLink":"https://www.uniprot.org/uniprotkb/Q99JR8/entry","name":"Smarcd2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642789","identifier":"O54941","identifierLink":"https://www.uniprot.org/uniprotkb/O54941/entry","name":"Smarce1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-648047","identifier":"P97496","identifierLink":"https://www.uniprot.org/uniprotkb/P97496/entry","name":"Smarcc1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-689365","identifier":"Q9Z0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0H3/entry","name":"Smarcb1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7525857","identifier":"Q6P9Z1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P9Z1/entry","name":"Smarcd3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1240","complexName":"Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex which is recruited to promoters and enhancers of target genes in muscle cells and alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nSWI/SNF complexes containing DPF3 are specific to muscle cells where they play an essential role in the development of heart and skeletal muscle cells. Also found in brown adipocytes where they regulate gene-expression of brown fat-selective genes. \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional repression is probably driven by the presence of the Arid1a subunit. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, Smarca2/Brm (this complex) and Smarca4/Brg1 (CPX-1241) do not co-occur in the same complex. Smarcd1 (Baf60a) and Smarcd2 (Baf60b) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: Dpf2/Baf45d (Q61103), Brd9 (Q3UQU0), Ss18 (Q62280), Bcl11a (Q9QYE3), Bcl11b (Q99PV8), Bcl7a (Q9CXE2), Bcl7b (Q921K9), Bcl7c (O08664). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-10765904","identifier":"Q6DIC0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6DIC0/entry","name":"Smarca2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16368943","identifier":"P58269","identifierLink":"https://www.uniprot.org/uniprotkb/P58269/entry","name":"Dpf3","description":"Zinc finger protein DPF3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942759","identifier":"Q9Z2N8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z2N8/entry","name":"Actl6a","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371499","identifier":"A2BH40","identifierLink":"https://www.uniprot.org/uniprotkb/A2BH40/entry","name":"Arid1a","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371529","identifier":"Q61466","identifierLink":"https://www.uniprot.org/uniprotkb/Q61466/entry","name":"Smarcd1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3870565","identifier":"Q6PDG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDG5/entry","name":"Smarcc2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5736813","identifier":"Q99JR8","identifierLink":"https://www.uniprot.org/uniprotkb/Q99JR8/entry","name":"Smarcd2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 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The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nSWI/SNF complexes containing DPF3 are specific to muscle cells where they play an essential role in the development of heart and skeletal muscle cells. Also found in brown adipocytes where they regulate gene-expression of brown fat-selective genes. \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional repression is probably driven by the presence of the Arid1a subunit. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, Smarca2/Brm (CPX-1240) and Smarca4/Brg1 (this complex) do not co-occur in the same complex. Smarcd1 (Baf60a) and Smarcd2 (Baf60b) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: Dpf2/Baf45d (Q61103), Brd9 (Q3UQU0), Ss18 (Q62280), Bcl11a (Q9QYE3), Bcl11b (Q99PV8), Bcl7a (Q9CXE2), Bcl7b (Q921K9), Bcl7c (O08664). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-1210244","identifier":"Q3TKT4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TKT4/entry","name":"Smarca4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16368943","identifier":"P58269","identifierLink":"https://www.uniprot.org/uniprotkb/P58269/entry","name":"Dpf3","description":"Zinc finger protein DPF3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 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The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nSWI/SNF complexes containing DPF3 are specific to muscle cells where they play an essential role in the development of heart and skeletal muscle cells. Also found in brown adipocytes where they regulate gene-expression of brown fat-selective genes. \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional activation is probably driven by the presence of the Arid1b subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 &  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, Smarca2/Brm (this complex) and Smarca4/Brg1 (CPX-1243) do not co-occur in the same complex. Smarcd1 (Baf60a) and Smarcd2 (Baf60b) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: Dpf2/Baf45d (Q61103), Brd9 (Q3UQU0), Ss18 (Q62280), Bcl11a (Q9QYE3), Bcl11b (Q99PV8), Bcl7a (Q9CXE2), Bcl7b (Q921K9), Bcl7c (O08664). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-10765904","identifier":"Q6DIC0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6DIC0/entry","name":"Smarca2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16368402","identifier":"E9Q6R4","identifierLink":"https://www.uniprot.org/uniprotkb/E9Q6R4/entry","name":"Arid1b","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 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The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nSWI/SNF complexes containing DPF3 are specific to muscle cells where they play an essential role in the development of heart and skeletal muscle cells. Also found in brown adipocytes where they regulate gene-expression of brown fat-selective genes. \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional activation is probably driven by the presence of the Arid1b subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 &  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, Smarca2/Brm (CPX-1242) and Smarca4/Brg1 (this complex) do not co-occur in the same complex. Smarcd1 (Baf60a) and Smarcd2 (Baf60b) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: Dpf2/Baf45d (Q61103), Brd9 (Q3UQU0), Ss18 (Q62280), Bcl11a (Q9QYE3), Bcl11b (Q99PV8), Bcl7a (Q9CXE2), Bcl7b (Q921K9), Bcl7c (O08664). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-1210244","identifier":"Q3TKT4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TKT4/entry","name":"Smarca4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16368402","identifier":"E9Q6R4","identifierLink":"https://www.uniprot.org/uniprotkb/E9Q6R4/entry","name":"Arid1b","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 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The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nSWI/SNF complexes containing DPF3 are specific to muscle cells where they play an essential role in the development of heart and skeletal muscle cells. Also found in brown adipocytes where they regulate gene-expression of brown fat-selective genes. \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional repression is probably driven by the presence of the Arid1a subunit. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, Smarca2/Brm (this complex) and Smarca4/Brg1 (CPX-1245) do not co-occur in the same complex. Smarcd1 (Baf60a) and Smarcd2 (Baf60b) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: Dpf2/Baf45d (Q61103), Brd9 (Q3UQU0), Ss18 (Q62280), Bcl11a (Q9QYE3), Bcl11b (Q99PV8), Bcl7a (Q9CXE2), Bcl7b (Q921K9), BCL7C (O08664). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-10765904","identifier":"Q6DIC0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6DIC0/entry","name":"Smarca2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16368943","identifier":"P58269","identifierLink":"https://www.uniprot.org/uniprotkb/P58269/entry","name":"Dpf3","description":"Zinc finger protein DPF3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371499","identifier":"A2BH40","identifierLink":"https://www.uniprot.org/uniprotkb/A2BH40/entry","name":"Arid1a","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371529","identifier":"Q61466","identifierLink":"https://www.uniprot.org/uniprotkb/Q61466/entry","name":"Smarcd1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371554","identifier":"Q99MR0","identifierLink":"https://www.uniprot.org/uniprotkb/Q99MR0/entry","name":"Actl6b","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3870565","identifier":"Q6PDG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDG5/entry","name":"Smarcc2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5736813","identifier":"Q99JR8","identifierLink":"https://www.uniprot.org/uniprotkb/Q99JR8/entry","name":"Smarcd2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642789","identifier":"O54941","identifierLink":"https://www.uniprot.org/uniprotkb/O54941/entry","name":"Smarce1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-648047","identifier":"P97496","identifierLink":"https://www.uniprot.org/uniprotkb/P97496/entry","name":"Smarcc1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-689365","identifier":"Q9Z0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0H3/entry","name":"Smarcb1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7525857","identifier":"Q6P9Z1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P9Z1/entry","name":"Smarcd3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1245","complexName":"Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex which is recruited to promoters and enhancers of target genes in muscle cells and alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nSWI/SNF complexes containing DPF3 are specific to muscle cells where they play an essential role in the development of heart and skeletal muscle cells. Also found in brown adipocytes where they regulate gene-expression of brown fat-selective genes. \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional repression is probably driven by the presence of the Arid1a subunit. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, Smarca2/Brm (CPX-1244) and Smarca4/Brg1 (this complex) do not co-occur in the same complex. Smarcd1 (Baf60a) and Smarcd2 (Baf60b) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: Dpf2/Baf45d (Q61103), Brd9 (Q3UQU0), Ss18 (Q62280), Bcl11a (Q9QYE3), Bcl11b (Q99PV8), Bcl7a (Q9CXE2), Bcl7b (Q921K9), Bcl7c (O08664). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-1210244","identifier":"Q3TKT4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TKT4/entry","name":"Smarca4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16368943","identifier":"P58269","identifierLink":"https://www.uniprot.org/uniprotkb/P58269/entry","name":"Dpf3","description":"Zinc finger protein DPF3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371499","identifier":"A2BH40","identifierLink":"https://www.uniprot.org/uniprotkb/A2BH40/entry","name":"Arid1a","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371529","identifier":"Q61466","identifierLink":"https://www.uniprot.org/uniprotkb/Q61466/entry","name":"Smarcd1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371554","identifier":"Q99MR0","identifierLink":"https://www.uniprot.org/uniprotkb/Q99MR0/entry","name":"Actl6b","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3870565","identifier":"Q6PDG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDG5/entry","name":"Smarcc2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5736813","identifier":"Q99JR8","identifierLink":"https://www.uniprot.org/uniprotkb/Q99JR8/entry","name":"Smarcd2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642789","identifier":"O54941","identifierLink":"https://www.uniprot.org/uniprotkb/O54941/entry","name":"Smarce1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-648047","identifier":"P97496","identifierLink":"https://www.uniprot.org/uniprotkb/P97496/entry","name":"Smarcc1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-689365","identifier":"Q9Z0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0H3/entry","name":"Smarcb1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7525857","identifier":"Q6P9Z1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P9Z1/entry","name":"Smarcd3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1246","complexName":"Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex which is recruited to promoters and enhancers of target genes in muscle cells and alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nSWI/SNF complexes containing DPF3 are specific to muscle cells where they play an essential role in the development of heart and skeletal muscle cells. Also found in brown adipocytes where they regulate gene-expression of brown fat-selective genes. \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional activation is probably driven by the presence of the Arid1b subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 &  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, Smarca2/Brm (this complex) and Smarca4/Brg1 (CPX-1247) do not co-occur in the same complex. Smarcd1 (Baf60a) and Smarcd2 (Baf60b) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: Dpf2/Baf45d (Q61103), Brd9 (Q3UQU0), Ss18 (Q62280), Bcl11a (Q9QYE3), Bcl11b (Q99PV8), Bcl7a (Q9CXE2), Bcl7b (Q921K9), Bcl7c (O08664). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-10765904","identifier":"Q6DIC0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6DIC0/entry","name":"Smarca2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16368402","identifier":"E9Q6R4","identifierLink":"https://www.uniprot.org/uniprotkb/E9Q6R4/entry","name":"Arid1b","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-16368943","identifier":"P58269","identifierLink":"https://www.uniprot.org/uniprotkb/P58269/entry","name":"Dpf3","description":"Zinc finger protein DPF3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371529","identifier":"Q61466","identifierLink":"https://www.uniprot.org/uniprotkb/Q61466/entry","name":"Smarcd1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371554","identifier":"Q99MR0","identifierLink":"https://www.uniprot.org/uniprotkb/Q99MR0/entry","name":"Actl6b","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3870565","identifier":"Q6PDG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDG5/entry","name":"Smarcc2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5736813","identifier":"Q99JR8","identifierLink":"https://www.uniprot.org/uniprotkb/Q99JR8/entry","name":"Smarcd2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642789","identifier":"O54941","identifierLink":"https://www.uniprot.org/uniprotkb/O54941/entry","name":"Smarce1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-648047","identifier":"P97496","identifierLink":"https://www.uniprot.org/uniprotkb/P97496/entry","name":"Smarcc1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-689365","identifier":"Q9Z0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0H3/entry","name":"Smarcb1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 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The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nSWI/SNF complexes containing DPF3 are specific to muscle cells where they play an essential role in the development of heart and skeletal muscle cells. Also found in brown adipocytes where they regulate gene-expression of brown fat-selective genes. \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nIn this variant of the complex transcriptional activation is probably driven by the presence of the Arid1b subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 &  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, Smarca2/Brm (CPX-1246) and Smarca4/Brg1 (this complex) do not co-occur in the same complex. Smarcd1 (Baf60a) and Smarcd2 (Baf60b) also may not co-occur. The following proteins may be associated with SWI/SNF (BAF) complex variants, with one or more from each family present in any given complex: Dpf2/Baf45d (Q61103), Brd9 (Q3UQU0), Ss18 (Q62280), Bcl11a (Q9QYE3), Bcl11b (Q99PV8), Bcl7a (Q9CXE2), Bcl7b (Q921K9), Bcl7c (O08664). \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-1210244","identifier":"Q3TKT4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TKT4/entry","name":"Smarca4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16368402","identifier":"E9Q6R4","identifierLink":"https://www.uniprot.org/uniprotkb/E9Q6R4/entry","name":"Arid1b","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-16368943","identifier":"P58269","identifierLink":"https://www.uniprot.org/uniprotkb/P58269/entry","name":"Dpf3","description":"Zinc finger protein DPF3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371529","identifier":"Q61466","identifierLink":"https://www.uniprot.org/uniprotkb/Q61466/entry","name":"Smarcd1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371554","identifier":"Q99MR0","identifierLink":"https://www.uniprot.org/uniprotkb/Q99MR0/entry","name":"Actl6b","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3870565","identifier":"Q6PDG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDG5/entry","name":"Smarcc2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5736813","identifier":"Q99JR8","identifierLink":"https://www.uniprot.org/uniprotkb/Q99JR8/entry","name":"Smarcd2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642789","identifier":"O54941","identifierLink":"https://www.uniprot.org/uniprotkb/O54941/entry","name":"Smarce1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-648047","identifier":"P97496","identifierLink":"https://www.uniprot.org/uniprotkb/P97496/entry","name":"Smarcc1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-689365","identifier":"Q9Z0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0H3/entry","name":"Smarcb1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7525857","identifier":"Q6P9Z1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P9Z1/entry","name":"Smarcd3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1248","complexName":"Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\npBAF complexes facilitate the ligand-dependant transcriptional activation of target genes by nuclear hormone receptors and regulates cell differentiation, esp. in cardiac development. \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. pBAF exists in two variants, containing either Actl6a (this complex) or Actl6b (CPX-1250) subunit. Subunit Brd7 may be restricted to pBAF complexes in embryonic stem cells and not present in differentiated cells. The alternative ATPase, Smarca2/Brm (Q6DIC0), does not occur in the pBAF complexes. Smarcd1 (Baf60a) and Smarcd2 (Baf60b) may not co-occur. It is not clear if Bcl7a (Q9CXE2), Bcl7b (Q921K9), Bcl7c (O08664) or Smarcd3 (Q6P9Z1) are part of any pBAF variants.\r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-11516816","identifier":"E9Q7E2","identifierLink":"https://www.uniprot.org/uniprotkb/E9Q7E2/entry","name":"Arid2","description":"AT-rich interactive domain-containing protein 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22970","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1210244","identifier":"Q3TKT4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TKT4/entry","name":"Smarca4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942759","identifier":"Q9Z2N8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z2N8/entry","name":"Actl6a","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371529","identifier":"Q61466","identifierLink":"https://www.uniprot.org/uniprotkb/Q61466/entry","name":"Smarcd1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3870565","identifier":"Q6PDG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDG5/entry","name":"Smarcc2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5736813","identifier":"Q99JR8","identifierLink":"https://www.uniprot.org/uniprotkb/Q99JR8/entry","name":"Smarcd2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5744069","identifier":"Q8BSQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BSQ9/entry","name":"Pbrm1","description":"Protein polybromo-1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16062","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642789","identifier":"O54941","identifierLink":"https://www.uniprot.org/uniprotkb/O54941/entry","name":"Smarce1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-643930","identifier":"O88665","identifierLink":"https://www.uniprot.org/uniprotkb/O88665/entry","name":"Brd7","description":"Bromodomain-containing protein 7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22881","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-648047","identifier":"P97496","identifierLink":"https://www.uniprot.org/uniprotkb/P97496/entry","name":"Smarcc1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-689365","identifier":"Q9Z0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0H3/entry","name":"Smarcb1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8339310","identifier":"Q9D8M7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D8M7/entry","name":"Phf10","description":"PHD finger protein 10","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1249","complexName":"SDS22-GLC7 phosphatase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Protein phosphatase complex implicated in acting in opposition to the Chromosomal Passenger complex (CPX-1900) at the kinetochore. Glc7 dephosphorylation of kinetochore proteins promotes mitotic spindle attachment. The opposing Chromosomal Passenger complex and Glc7 activities ensure that chromosomes achieve a bipolar attachment to the spindle. SDS22 appears to both act as a targeting subunit for the enzyme and also to regulate phosphatase activity.","predictedComplex":false,"interactors":[{"ac":"EBI-13715","identifier":"P32598","identifierLink":"https://www.uniprot.org/uniprotkb/P32598/entry","name":"GLC7","description":"Serine/threonine-protein phosphatase PP1-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11668","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-16783","identifier":"P36047","identifierLink":"https://www.uniprot.org/uniprotkb/P36047/entry","name":"SDS22","description":"Protein phosphatase 1 regulatory subunit SDS22","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45973","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1250","complexName":"Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (VDR, P48281) via Smarcd subunits. \r\n\r\npBAF complexes facilitate the ligand-dependant transcriptional activation of target genes by nuclear hormone receptors and regulates cell differentiation, esp. in cardiac development. \r\n\r\nActs as transcriptional repressor of neuronal genes in non-neuronal cells by interacting with the REST repressor complex and histone deacetylases (HDACs). \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. pBAF exists in two variants, containing either Actl6a (CPX-1248) or Actl6b (this complex) subunit. Subunit Brd7 may be restricted to pBAF complexes in embryonic stem cells and not present in differentiated cells. The alternative ATPase, Smarca2/Brm (Q6DIC0), does not occur in the pBAF complexes. Smarcd1 (Baf60a) and Smarcd2 (Baf60b) may not co-occur. It is not clear if Bcl7a (Q9CXE2), Bcl7b (Q921K9), Bcl7c (O08664) or Smarcd3 (Q6P9Z1) are part of any pBAF variants.\r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-11516816","identifier":"E9Q7E2","identifierLink":"https://www.uniprot.org/uniprotkb/E9Q7E2/entry","name":"Arid2","description":"AT-rich interactive domain-containing protein 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22970","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1210244","identifier":"Q3TKT4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TKT4/entry","name":"Smarca4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371529","identifier":"Q61466","identifierLink":"https://www.uniprot.org/uniprotkb/Q61466/entry","name":"Smarcd1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371554","identifier":"Q99MR0","identifierLink":"https://www.uniprot.org/uniprotkb/Q99MR0/entry","name":"Actl6b","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3870565","identifier":"Q6PDG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDG5/entry","name":"Smarcc2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5736813","identifier":"Q99JR8","identifierLink":"https://www.uniprot.org/uniprotkb/Q99JR8/entry","name":"Smarcd2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5744069","identifier":"Q8BSQ9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8BSQ9/entry","name":"Pbrm1","description":"Protein polybromo-1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16062","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642789","identifier":"O54941","identifierLink":"https://www.uniprot.org/uniprotkb/O54941/entry","name":"Smarce1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-643930","identifier":"O88665","identifierLink":"https://www.uniprot.org/uniprotkb/O88665/entry","name":"Brd7","description":"Bromodomain-containing protein 7","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR22881","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-648047","identifier":"P97496","identifierLink":"https://www.uniprot.org/uniprotkb/P97496/entry","name":"Smarcc1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-689365","identifier":"Q9Z0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0H3/entry","name":"Smarcb1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8339310","identifier":"Q9D8M7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D8M7/entry","name":"Phf10","description":"PHD finger protein 10","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1251","complexName":"Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nThe embryonic stem cell-specific SWI/SNF complex is critical for self-renewal, maintenance and pluripotency of embryonic stem cells. The lack of subunit Arid1b suggests it primarily acts as a transcriptional repressor but also has the ability to activate some genes. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. The embryonic stem cell-specific (esc-)SWI/SNF complex specifically lacks subunits Actl6b (Q99MR0), ARID1B (E9Q6R4), SMARCA2 (Q6DIC0), SMARCC2 (Q6PDG5) and SMARCD3 (Q6P9Z1). SMARCD2 (Q99JR8) may be present in esc-SWI/SNF complexes in which case it probably forms a variant, replacing SMARCD1. BCL7A, BCL7B and BCL7C have been shown to be part of the esc-SWI/SNF complex but may be mutually exclusive and therefore probably forms further variants.\r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-1210244","identifier":"Q3TKT4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TKT4/entry","name":"Smarca4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16371163","identifier":"Q9CXE2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9CXE2/entry","name":"Bcl7a","description":"B-cell CLL/lymphoma 7 protein family member A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2552901","identifier":"Q921K9","identifierLink":"https://www.uniprot.org/uniprotkb/Q921K9/entry","name":"Bcl7b","description":"B-cell CLL/lymphoma 7 protein family member B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12767","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942759","identifier":"Q9Z2N8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z2N8/entry","name":"Actl6a","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371499","identifier":"A2BH40","identifierLink":"https://www.uniprot.org/uniprotkb/A2BH40/entry","name":"Arid1a","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371529","identifier":"Q61466","identifierLink":"https://www.uniprot.org/uniprotkb/Q61466/entry","name":"Smarcd1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5691800","identifier":"Q61103","identifierLink":"https://www.uniprot.org/uniprotkb/Q61103/entry","name":"Dpf2","description":"Zinc finger protein ubi-d4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642789","identifier":"O54941","identifierLink":"https://www.uniprot.org/uniprotkb/O54941/entry","name":"Smarce1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-648047","identifier":"P97496","identifierLink":"https://www.uniprot.org/uniprotkb/P97496/entry","name":"Smarcc1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-689365","identifier":"Q9Z0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0H3/entry","name":"Smarcb1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 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The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nThe neural progenitor-specific SWI/SNF complex is critical for self-renewal, maintenance and pluripotency of neural progenitor stem cells by selectively activating or repressing its target genes. In this variant of the complex transcriptional repression is probably driven by the presence of the Arid1a subunit. \r\n\r\nDuring neural development a switch from a progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. This process requires a switch of two subunits: Actl6a is replaced by Actl6b (Q99MR0) and PHF10 replaced by Dpf1 (Q9QX66) or Dpf3 (P58269) in neuron-specific SWI/SNF complexes. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. Although similar in function to the embryonic stem cell-specific SWI/SNF complex the composition of the neural progenitor-specific SWI/SNF complexes is more similar to the standard SWI/SNF complexes. It is likely that the two ATPases, Smarca2/Brm (this complex) and Smarca4/Brg1 (CPX-1253) do not co-occur in the same complex. Smarcd1 (Baf60a) and Smarcd3 (Baf60c) also may not co-occur. It is not clear yet if Dpf2/Baf45d (Q61103) is a member of the neural progenitor-specific SWI/SNF complex. \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-10765904","identifier":"Q6DIC0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6DIC0/entry","name":"Smarca2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942759","identifier":"Q9Z2N8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z2N8/entry","name":"Actl6a","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 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The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nThe neural progenitor-specific SWI/SNF complex is critical for self-renewal, maintenance and pluripotency of neural progenitor stem cells by selectively activating or repressing its target genes. In this variant of the complex transcriptional repression is probably driven by the presence of the Arid1a subunit. \r\n\r\nDuring neural development a switch from a progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. This process requires a switch of two subunits: Actl6a is replaced by Actl6b (Q99MR0) and PHF10 replaced by Dpf1 (Q9QX66) or Dpf3 (P58269) in neuron-specific SWI/SNF complexes. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. Although similar in function to the embryonic stem cell-specific SWI/SNF complex the composition of the neural progenitor-specific SWI/SNF complexes is more similar to the standard SWI/SNF complexes. It is likely that the two ATPases, Smarca2/Brm (CPX-1252) and Smarca4/Brg1 (this complex) do not co-occur in the same complex. Smarcd1 (Baf60a) and Smarcd3 (Baf60c) also may not co-occur. It is not clear yet if Dpf2/Baf45d (Q61103) is a member of the neural progenitor-specific SWI/SNF complex. \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-1210244","identifier":"Q3TKT4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TKT4/entry","name":"Smarca4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2942759","identifier":"Q9Z2N8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z2N8/entry","name":"Actl6a","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 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The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nThe neural progenitor-specific SWI/SNF complex is critical for self-renewal, maintenance and pluripotency of neural progenitor stem cells by selectively activating or repressing its target genes. In this variant of the complex transcriptional activation is probably driven by the presence of the Arid1b subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 &  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nThe neural progenitor-specific SWI/SNF complex is critical for self-renewal, maintenance and pluripotency of neural progenitor stem cells by selectively activating or repressing its target genes. In this variant of the complex transcriptional activation is probably driven by the presence of the ARID1B subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 &  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nDuring neural development a switch from a progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. This process requires a switch of two subunits: Actl6a is replaced by Actl6b (Q99MR0) and PHF10 replaced by Dpf1 (Q9QX66) or Dpf3 (P58269) in neuron-specific SWI/SNF complexes. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. Although similar in function to the embryonic stem cell-specific SWI/SNF complex the composition of the neural progenitor-specific SWI/SNF complexes is more similar to the standard SWI/SNF complexes. It is likely that the two ATPases, Smarca2/Brm (this complex) and Smarca4/Brg1 (CPX-1255) do not co-occur in the same complex. Smarcd1 (Baf60a) and Smarcd3 (Baf60c) also may not co-occur. It is not clear yet if Dpf2/Baf45d (Q61103) is a member of the neural progenitor-specific SWI/SNF complex. \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-10765904","identifier":"Q6DIC0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6DIC0/entry","name":"Smarca2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16368402","identifier":"E9Q6R4","identifierLink":"https://www.uniprot.org/uniprotkb/E9Q6R4/entry","name":"Arid1b","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-2942759","identifier":"Q9Z2N8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z2N8/entry","name":"Actl6a","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371529","identifier":"Q61466","identifierLink":"https://www.uniprot.org/uniprotkb/Q61466/entry","name":"Smarcd1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3870565","identifier":"Q6PDG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDG5/entry","name":"Smarcc2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642789","identifier":"O54941","identifierLink":"https://www.uniprot.org/uniprotkb/O54941/entry","name":"Smarce1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-648047","identifier":"P97496","identifierLink":"https://www.uniprot.org/uniprotkb/P97496/entry","name":"Smarcc1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-689365","identifier":"Q9Z0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0H3/entry","name":"Smarcb1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7525857","identifier":"Q6P9Z1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P9Z1/entry","name":"Smarcd3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8339310","identifier":"Q9D8M7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D8M7/entry","name":"Phf10","description":"PHD finger protein 10","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1255","complexName":"Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. 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The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nThe neural progenitor-specific SWI/SNF complex is critical for self-renewal, maintenance and pluripotency of neural progenitor stem cells by selectively activating or repressing its target genes. In this variant of the complex transcriptional activation is probably driven by the presence of the Arid1b subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 &  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nThe neural progenitor-specific SWI/SNF complex is critical for self-renewal, maintenance and pluripotency of neural progenitor stem cells by selectively activating or repressing its target genes. In this variant of the complex transcriptional activation is probably driven by the presence of the ARID1B subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 &  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\nDuring neural development a switch from a progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. This process requires a switch of two subunits: Actl6a is replaced by Actl6b (Q99MR0) and PHF10 replaced by Dpf1 (Q9QX66) or Dpf3 (P58269) in neuron-specific SWI/SNF complexes. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. Although similar in function to the embryonic stem cell-specific SWI/SNF complex the composition of the neural progenitor-specific SWI/SNF complexes is more similar to the standard SWI/SNF complexes. It is likely that the two ATPases, Smarca2/Brm (CPX-1254) and Smarca4/Brg1 (this complex) do not co-occur in the same complex. Smarcd1 (Baf60a) and Smarcd3 (Baf60c) also may not co-occur. It is not clear yet if Dpf2/Baf45d (Q61103) is a member of the neural progenitor-specific SWI/SNF complex. \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-1210244","identifier":"Q3TKT4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TKT4/entry","name":"Smarca4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16368402","identifier":"E9Q6R4","identifierLink":"https://www.uniprot.org/uniprotkb/E9Q6R4/entry","name":"Arid1b","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-2942759","identifier":"Q9Z2N8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z2N8/entry","name":"Actl6a","description":"Actin-like protein 6A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371529","identifier":"Q61466","identifierLink":"https://www.uniprot.org/uniprotkb/Q61466/entry","name":"Smarcd1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3870565","identifier":"Q6PDG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDG5/entry","name":"Smarcc2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642789","identifier":"O54941","identifierLink":"https://www.uniprot.org/uniprotkb/O54941/entry","name":"Smarce1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-648047","identifier":"P97496","identifierLink":"https://www.uniprot.org/uniprotkb/P97496/entry","name":"Smarcc1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-689365","identifier":"Q9Z0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0H3/entry","name":"Smarcb1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7525857","identifier":"Q6P9Z1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P9Z1/entry","name":"Smarcd3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8339310","identifier":"Q9D8M7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9D8M7/entry","name":"Phf10","description":"PHD finger protein 10","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10615","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1256","complexName":"Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nThe neuron-specific SWI/SNF complex is critical for the proliferation of post-mitotic neurons and regulates genes specific for dendritic growth by binding tightly with Crest (Q8BW22). In this variant of the complex transcriptional repression is probably driven by the presence of the Arid1a subunit. \r\n\r\nDuring neural development a switch from a progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. This process requires a switch of two subunits: Actl6a (Q9Z2N8) is replaced by Actl6b and Phf10 (Q9D8M7) replaced by Dpf1 or Dpf3 in neuron-specific SWI/SNF complexes. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, Smarca2/Brm (this complex) and Smarca4/Brg1 (CPX-1257) do not co-occur in the same complex. Smarcd1 (Baf60a) and Smarcd3 (Baf60c) as well as Dpf1 and Dpf3 also may not co-occur.  \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-10765904","identifier":"Q6DIC0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6DIC0/entry","name":"Smarca2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16368943","identifier":"P58269","identifierLink":"https://www.uniprot.org/uniprotkb/P58269/entry","name":"Dpf3","description":"Zinc finger protein DPF3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16371715","identifier":"Q9QX66","identifierLink":"https://www.uniprot.org/uniprotkb/Q9QX66/entry","name":"Dpf1","description":"Zinc finger protein neuro-d4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371499","identifier":"A2BH40","identifierLink":"https://www.uniprot.org/uniprotkb/A2BH40/entry","name":"Arid1a","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371529","identifier":"Q61466","identifierLink":"https://www.uniprot.org/uniprotkb/Q61466/entry","name":"Smarcd1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371554","identifier":"Q99MR0","identifierLink":"https://www.uniprot.org/uniprotkb/Q99MR0/entry","name":"Actl6b","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3870565","identifier":"Q6PDG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDG5/entry","name":"Smarcc2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642789","identifier":"O54941","identifierLink":"https://www.uniprot.org/uniprotkb/O54941/entry","name":"Smarce1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-648047","identifier":"P97496","identifierLink":"https://www.uniprot.org/uniprotkb/P97496/entry","name":"Smarcc1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-689365","identifier":"Q9Z0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0H3/entry","name":"Smarcb1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7525857","identifier":"Q6P9Z1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P9Z1/entry","name":"Smarcd3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1257","complexName":"Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nThe neuron-specific SWI/SNF complex is critical for the proliferation of post-mitotic neurons and regulates genes specific for dendritic growth by binding tightly with Crest (Q8BW22). In this variant of the complex transcriptional repression is probably driven by the presence of the Arid1a subunit. \r\n\r\nDuring neural development a switch from a progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. This process requires a switch of two subunits: Actl6a (Q9Z2N8) is replaced by Actl6b and Phf10 (Q9D8M7) replaced by Dpf1 or Dpf3 in neuron-specific SWI/SNF complexes. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, Smarca2/Brm (CPX-1256) and Smarca4/Brg1 (this complex) do not co-occur in the same complex. Smarcd1 (Baf60a) and Smarcd3 (Baf60c) as well as Dpf1 and Dpf3 also may not co-occur.  \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-1210244","identifier":"Q3TKT4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TKT4/entry","name":"Smarca4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16368943","identifier":"P58269","identifierLink":"https://www.uniprot.org/uniprotkb/P58269/entry","name":"Dpf3","description":"Zinc finger protein DPF3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16371715","identifier":"Q9QX66","identifierLink":"https://www.uniprot.org/uniprotkb/Q9QX66/entry","name":"Dpf1","description":"Zinc finger protein neuro-d4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371499","identifier":"A2BH40","identifierLink":"https://www.uniprot.org/uniprotkb/A2BH40/entry","name":"Arid1a","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371529","identifier":"Q61466","identifierLink":"https://www.uniprot.org/uniprotkb/Q61466/entry","name":"Smarcd1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371554","identifier":"Q99MR0","identifierLink":"https://www.uniprot.org/uniprotkb/Q99MR0/entry","name":"Actl6b","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3870565","identifier":"Q6PDG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDG5/entry","name":"Smarcc2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642789","identifier":"O54941","identifierLink":"https://www.uniprot.org/uniprotkb/O54941/entry","name":"Smarce1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-648047","identifier":"P97496","identifierLink":"https://www.uniprot.org/uniprotkb/P97496/entry","name":"Smarcc1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-689365","identifier":"Q9Z0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0H3/entry","name":"Smarcb1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7525857","identifier":"Q6P9Z1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P9Z1/entry","name":"Smarcd3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1258","complexName":"Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nThe neuron-specific SWI/SNF complex is critical for the proliferation of post-mitotic neurons and regulates genes specific for dendritic growth by binding tightly with Crest (Q8BW22). In this variant of the complex transcriptional activation is probably driven by the presence of the Arid1b subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 and  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\n\r\nDuring neural development a switch from a progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. This process requires a switch of two subunits: Actl6a (Q9Z2N8) is replaced by Actl6b and Phf10 (Q9D8M7) replaced by Dpf1 or Dpf3 in neuron-specific SWI/SNF complexes. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, Smarca2/Brm (this complex) and Smarca4/Brg1 (CPX-1259) do not co-occur in the same complex. Smarcd1 (Baf60a) and Smarcd3 (Baf60c) as well as Dpf1 and Dpf3 also may not co-occur.  \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-10765904","identifier":"Q6DIC0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6DIC0/entry","name":"Smarca2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16368402","identifier":"E9Q6R4","identifierLink":"https://www.uniprot.org/uniprotkb/E9Q6R4/entry","name":"Arid1b","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-16368943","identifier":"P58269","identifierLink":"https://www.uniprot.org/uniprotkb/P58269/entry","name":"Dpf3","description":"Zinc finger protein DPF3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16371715","identifier":"Q9QX66","identifierLink":"https://www.uniprot.org/uniprotkb/Q9QX66/entry","name":"Dpf1","description":"Zinc finger protein neuro-d4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371529","identifier":"Q61466","identifierLink":"https://www.uniprot.org/uniprotkb/Q61466/entry","name":"Smarcd1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 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10090","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-648047","identifier":"P97496","identifierLink":"https://www.uniprot.org/uniprotkb/P97496/entry","name":"Smarcc1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-689365","identifier":"Q9Z0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0H3/entry","name":"Smarcb1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7525857","identifier":"Q6P9Z1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P9Z1/entry","name":"Smarcd3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1259","complexName":"Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nThe neuron-specific SWI/SNF complex is critical for the proliferation of post-mitotic neurons and regulates genes specific for dendritic growth by binding tightly with Crest (Q8BW22). In this variant of the complex transcriptional activation is probably driven by the presence of the Arid1b subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 and  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27. Activates, among others, transcription of oestrogen-responsive genes, glucocorticoid receptor-dependent genes and genes activating the Notch-signalling pathway. \r\n\r\n\r\nDuring neural development a switch from a progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. This process requires a switch of two subunits: Actl6a (Q9Z2N8) is replaced by Actl6b and Phf10 (Q9D8M7) replaced by Dpf1 or Dpf3 in neuron-specific SWI/SNF complexes. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, Smarca2/Brm (CPX-1258) and Smarca4/Brg1 (this complex) do not co-occur in the same complex. Smarcd1 (Baf60a) and Smarcd3 (Baf60c) as well as Dpf1 and Dpf3 also may not co-occur.  \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-1210244","identifier":"Q3TKT4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TKT4/entry","name":"Smarca4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16368402","identifier":"E9Q6R4","identifierLink":"https://www.uniprot.org/uniprotkb/E9Q6R4/entry","name":"Arid1b","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-16368943","identifier":"P58269","identifierLink":"https://www.uniprot.org/uniprotkb/P58269/entry","name":"Dpf3","description":"Zinc finger protein DPF3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23057","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16371715","identifier":"Q9QX66","identifierLink":"https://www.uniprot.org/uniprotkb/Q9QX66/entry","name":"Dpf1","description":"Zinc finger protein neuro-d4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR45888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371529","identifier":"Q61466","identifierLink":"https://www.uniprot.org/uniprotkb/Q61466/entry","name":"Smarcd1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371554","identifier":"Q99MR0","identifierLink":"https://www.uniprot.org/uniprotkb/Q99MR0/entry","name":"Actl6b","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3870565","identifier":"Q6PDG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDG5/entry","name":"Smarcc2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642789","identifier":"O54941","identifierLink":"https://www.uniprot.org/uniprotkb/O54941/entry","name":"Smarce1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-648047","identifier":"P97496","identifierLink":"https://www.uniprot.org/uniprotkb/P97496/entry","name":"Smarcc1","description":"SWI/SNF complex subunit SMARCC1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-689365","identifier":"Q9Z0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0H3/entry","name":"Smarcb1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7525857","identifier":"Q6P9Z1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P9Z1/entry","name":"Smarcd3","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1260","complexName":"SDS22-GLC7-YPI1 phosphatase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Protein phosphatase complex implicated in acting in opposition to the Chromosomal Passenger complex (CPX-1900) at the kinetochore. GLC7 dephosphorylation of kinetochore proteins promotes mitotic spindle attachment. The opposing Chromosomal Passenger complex and GLC7 activities ensure that chromosomes achieve a bipolar attachment to the spindle. SDS22 appears to both act as a targeting subunit for the enzyme and also to regulate phosphatase activity. YPI1 may target the complex to the nucleus and also act to maintain the complex in a largely inactive state, preventing inactivation of the spindle checkpoint.","predictedComplex":false,"interactors":[{"ac":"EBI-13715","identifier":"P32598","identifierLink":"https://www.uniprot.org/uniprotkb/P32598/entry","name":"GLC7","description":"Serine/threonine-protein phosphatase PP1-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11668","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-16783","identifier":"P36047","identifierLink":"https://www.uniprot.org/uniprotkb/P36047/entry","name":"SDS22","description":"Protein phosphatase 1 regulatory subunit SDS22","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45973","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-22913","identifier":"P43587","identifierLink":"https://www.uniprot.org/uniprotkb/P43587/entry","name":"YPI1","description":"Type 1 phosphatases regulator YPI1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR20835","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1261","complexName":"Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nRegulates cell differentiation specifically in post-mitotic brain tissue. In this variant of the complex transcriptional repression is probably driven by the presence of the Arid1a subunit. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, Smarca2/Brm (this complex) and Smarca4/Brg1 (CPX-1262) do not co-occur in the same complex. In contrast to the neuron-specific SWI/SNF complex the brain-specific SWI/SNF complex misses core subunit Smarcc1 (P97496) and alternative subunits Actl6a (Q9Z2N8), Smarcd1 (Q61466) or Smarcd3 (Q6P9Z1). May contain pBAF-specific subunit Pbrm1 (Baf180, Q8BSQ9).  \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-10765904","identifier":"Q6DIC0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6DIC0/entry","name":"Smarca2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371499","identifier":"A2BH40","identifierLink":"https://www.uniprot.org/uniprotkb/A2BH40/entry","name":"Arid1a","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371554","identifier":"Q99MR0","identifierLink":"https://www.uniprot.org/uniprotkb/Q99MR0/entry","name":"Actl6b","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3870565","identifier":"Q6PDG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDG5/entry","name":"Smarcc2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5736813","identifier":"Q99JR8","identifierLink":"https://www.uniprot.org/uniprotkb/Q99JR8/entry","name":"Smarcd2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642789","identifier":"O54941","identifierLink":"https://www.uniprot.org/uniprotkb/O54941/entry","name":"Smarce1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-689365","identifier":"Q9Z0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0H3/entry","name":"Smarcb1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1262","complexName":"Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nRegulates cell differentiation specifically in post-mitotic brain tissue. In this variant of the complex transcriptional repression is probably driven by the presence of the Arid1a subunit. \r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, Smarca2/Brm (CPX-1261) and Smarca4/Brg1 (this complex) do not co-occur in the same complex. In contrast to the neuron-specific SWI/SNF complex the brain-specific SWI/SNF complex misses core subunit Smarcc1 (P97496) and alternative subunits Actl6a (Q9Z2N8), Smarcd1 (Q61466) or Smarcd3 (Q6P9Z1). May contain pBAF-specific subunit Pbrm1 (Baf180, Q8BSQ9).  \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-1210244","identifier":"Q3TKT4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TKT4/entry","name":"Smarca4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371499","identifier":"A2BH40","identifierLink":"https://www.uniprot.org/uniprotkb/A2BH40/entry","name":"Arid1a","description":"AT-rich interactive domain-containing protein 1A","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12656","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371554","identifier":"Q99MR0","identifierLink":"https://www.uniprot.org/uniprotkb/Q99MR0/entry","name":"Actl6b","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3870565","identifier":"Q6PDG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDG5/entry","name":"Smarcc2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5736813","identifier":"Q99JR8","identifierLink":"https://www.uniprot.org/uniprotkb/Q99JR8/entry","name":"Smarcd2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642789","identifier":"O54941","identifierLink":"https://www.uniprot.org/uniprotkb/O54941/entry","name":"Smarce1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-689365","identifier":"Q9Z0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0H3/entry","name":"Smarcb1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1263","complexName":"Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nRegulates cell differentiation specifically in post-mitotic brain tissue. In this variant of the complex transcriptional activation is probably driven by the presence of the Arid1b subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 and  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27.\r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, Smarca2/Brm (this complex) and Smarca4/Brg1 (CPX-1262) do not co-occur in the same complex. In contrast to the neuron-specific SWI/SNF complex the brain-specific SWI/SNF complex misses core subunit Smarcc1 (P97496) and alternative subunits Actl6a (Q9Z2N8), Smarcd1 (Q61466) or Smarcd3 (Q6P9Z1). May contain pBAF-specific subunit Pbrm1 (Baf180, Q8BSQ9).  \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-10765904","identifier":"Q6DIC0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6DIC0/entry","name":"Smarca2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16368402","identifier":"E9Q6R4","identifierLink":"https://www.uniprot.org/uniprotkb/E9Q6R4/entry","name":"Arid1b","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371554","identifier":"Q99MR0","identifierLink":"https://www.uniprot.org/uniprotkb/Q99MR0/entry","name":"Actl6b","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3870565","identifier":"Q6PDG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDG5/entry","name":"Smarcc2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5736813","identifier":"Q99JR8","identifierLink":"https://www.uniprot.org/uniprotkb/Q99JR8/entry","name":"Smarcd2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642789","identifier":"O54941","identifierLink":"https://www.uniprot.org/uniprotkb/O54941/entry","name":"Smarce1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-689365","identifier":"Q9Z0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0H3/entry","name":"Smarcb1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1264","complexName":"Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant","organismName":"Mus musculus; 10090","description":"An ATP-dependent chromatin remodeling complex which is recruited to tissue- and lineage-specific promoters and enhancers of target genes and then alters chromatin structure. The precise process is undefined but the complex appears to reduce the superhelicity of the promoter region DNA around nucleosomes and may produce short DNA loops that are detached from the the nucleosomes, enabling access to the promoter region for a range of transcription factors and the pre-initiation complex (PIC). \r\n\r\nThe complex also plays a role in double-strand break and nucleotide excision repair mechanisms and in the decatenation of newly replicated sister chromatids, a requirement for proper chromosome segregation during mitosis. Also targeted to chromatin by phosphatidylinositol-4,5-bisphosphate which promotes the complex binding to actin filaments. The complex additionally interacts with a range of nuclear receptors and the vitamin D receptor (Vdr, P48281) via Smarcd subunits. \r\n\r\nRegulates cell differentiation specifically in post-mitotic brain tissue. In this variant of the complex transcriptional activation is probably driven by the presence of the Arid1b subunit. Removes Polycomb repressive complex 1 and 2 (PRC1 and  PRC2) resulting in promoter activation via deubiquitination of H2AK119 and demethylation of H3K27.\r\n\r\nThe SWI/SNF complexes have been reported as consisting of 8 to 14 subunits. It is likely that the two ATPases, Smarca2/Brm (this complex) and Smarca4/Brg1 (CPX-1262) do not co-occur in the same complex. In contrast to the neuron-specific SWI/SNF complex the brain-specific SWI/SNF complex misses core subunit Smarcc1 (P97496) and alternative subunits Actl6a (Q9Z2N8), Smarcd1 (Q61466) or Smarcd3 (Q6P9Z1). May contain pBAF-specific subunit Pbrm1 (Baf180, Q8BSQ9).  \r\n\r\nMutations in several subunits affect tissue and developmental processes such as nervous system and cardiac development and maintenance of pluripotency resulting in tumorigenesis or the development of intellectual disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-1210244","identifier":"Q3TKT4","identifierLink":"https://www.uniprot.org/uniprotkb/Q3TKT4/entry","name":"Smarca4","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10799","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16368402","identifier":"E9Q6R4","identifierLink":"https://www.uniprot.org/uniprotkb/E9Q6R4/entry","name":"Arid1b","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[]},{"ac":"EBI-353957","identifier":"P60710","identifierLink":"https://www.uniprot.org/uniprotkb/P60710/entry","name":"Actb","description":"Actin, cytoplasmic 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-371554","identifier":"Q99MR0","identifierLink":"https://www.uniprot.org/uniprotkb/Q99MR0/entry","name":"Actl6b","description":"Actin-like protein 6B","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3870565","identifier":"Q6PDG5","identifierLink":"https://www.uniprot.org/uniprotkb/Q6PDG5/entry","name":"Smarcc2","description":"SWI/SNF complex subunit SMARCC2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR12802","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5736813","identifier":"Q99JR8","identifierLink":"https://www.uniprot.org/uniprotkb/Q99JR8/entry","name":"Smarcd2","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR13844","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-642789","identifier":"O54941","identifierLink":"https://www.uniprot.org/uniprotkb/O54941/entry","name":"Smarce1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46232","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-689365","identifier":"Q9Z0H3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Z0H3/entry","name":"Smarcb1","description":"SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10019","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1265","complexName":"Laminin111-nidogen complex","organismName":"Homo sapiens; 9606","description":"An extracellular matrix complex responsible for basement membrane stabilization and cell-matrix adhesion. Crosslinking of the nidogen subunit from one complex to a laminin arm of a second by tissue transglutaminases forms large assemblies. Facilitates cell adhesion by binding collagens (e.g. collagen type I, CPX-1650 or collagen type IV, CPX-1723) and integrins (e.g. alpha3beta1, CPX-1797 or alphavbeta3, CPX-1795). May modify type I collagen scaffolds and thereby enhance myotube formation.","predictedComplex":false,"interactors":[{"ac":"EBI-2529702","identifier":"CPX-1770","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-1770","name":"Laminin-111 complex","description":"Laminin-111","stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2828729","identifier":"P14543","identifierLink":"https://www.uniprot.org/uniprotkb/P14543/entry","name":"NID1","description":"Nidogen-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46513","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1266","complexName":"REG1-GLC7 phosphatase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Protein phosphatase complex with a role in glucose repression. REG1-GLC7 binds to SNF1 when the SNF1 kinase complex (CPX-232/CPX-2800/CPX-231) is activated by phosphorylation, which occurs at a much higher rate in glucose-limited cells than in glucose-grown cells. REG1-GLC7 facilitates the transition of the kinase complex back to an autoinhibited state, presumably by dephosphorylating SNF1.","predictedComplex":false,"interactors":[{"ac":"EBI-13715","identifier":"P32598","identifierLink":"https://www.uniprot.org/uniprotkb/P32598/entry","name":"GLC7","description":"Serine/threonine-protein phosphatase PP1-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11668","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-8270","identifier":"Q00816","identifierLink":"https://www.uniprot.org/uniprotkb/Q00816/entry","name":"REG1","description":"Resistance to glucose repression protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28051","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1267","complexName":"REG2-GLC7 phosphatase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Protein phosphatase complex with a role in theresponse to glucose levels. During steady-state growth in high glucose, the SNF1 kinase complex (CPX-232/CPX-2800/CPX-231) is inactive and REG2 is not expressed. Prolonged glucose starvation leads to SNF1-dependent accumulation of REG2. Once glucose becomes abundant, REG2-GLC7 contributes to the rapid dephosphorylation and inactivation of SNF1 which acts as a central regulator of cellular energy homeostasis.","predictedComplex":false,"interactors":[{"ac":"EBI-13715","identifier":"P32598","identifierLink":"https://www.uniprot.org/uniprotkb/P32598/entry","name":"GLC7","description":"Serine/threonine-protein phosphatase PP1-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11668","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-14921","identifier":"P38232","identifierLink":"https://www.uniprot.org/uniprotkb/P38232/entry","name":"REG2","description":"Protein REG2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-1554638","identifier":"CHEBI:29035","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29035","name":"manganese(2+)","description":"Manganese (2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1268","complexName":"Glycine decarboxylase multienzyme complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the oxidative cleavage of glycine into CO2 and NH3, utimately playing a role in the conversion of  glycine to serine. The concomitant transfer of a methylene carbon unit to THF1 generates the C1 donor 5,10-methylene tetrahydrofolate. Located in the mitochondrion. The P protein (GCV2, P49095) binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO2 is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (GV3, P39726).","predictedComplex":false,"interactors":[{"ac":"EBI-5940","identifier":"P09624","identifierLink":"https://www.uniprot.org/uniprotkb/P09624/entry","name":"LPD1","description":"Dihydrolipoyl dehydrogenase, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22912","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7486","identifier":"P39726","identifierLink":"https://www.uniprot.org/uniprotkb/P39726/entry","name":"GCV3","description":"Glycine cleavage system H protein, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11715","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7492","identifier":"P49095","identifierLink":"https://www.uniprot.org/uniprotkb/P49095/entry","name":"GCV2","description":"Glycine dehydrogenase (decarboxylating), mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11773","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7499","identifier":"P48015","identifierLink":"https://www.uniprot.org/uniprotkb/P48015/entry","name":"GCV1","description":"Aminomethyltransferase, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43757","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1269","complexName":"Glycosylphosphatidylinositol-mannosyltransferase II complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Mannosyltransferase complex responsible for the transfer of the second mannose to the glycosylphosphatidylinositol (GPI) during GPI precursor assembly. GPI is a complex glycolipid with a core structure, phosphoethanolamine-6-mannose-alpha1,2-mannose-alpha1,6-mannose-alpha1,4-glucosamine-alpha1,6-inositol-phospholipid that functions as a membrane anchor for many cell surface proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-21377","identifier":"P38211","identifierLink":"https://www.uniprot.org/uniprotkb/P38211/entry","name":"GPI18","description":"GPI mannosyltransferase 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12468","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-28971","identifier":"P53896","identifierLink":"https://www.uniprot.org/uniprotkb/P53896/entry","name":"PGA1","description":"GPI mannosyltransferase 2 subunit PGA1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28022","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1270","complexName":"Glycosylphosphatidylinositol-mannosyltransferase I complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Mannosyltransferase complex responsible for the transfer of the first alpha-1,4-mannose to the glycosylphosphatidylinositol (GPI) during GPI precursor assembly. GPI is a complex glycolipid with a core structure, phosphoethanolamine-6-mannose-alpha1,2-mannose-alpha1,6-mannose-alpha1,4-glucosamine-alpha1,6-inositol-phospholipid that functions as a membrane anchor for many cell surface proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-26307","identifier":"P47088","identifierLink":"https://www.uniprot.org/uniprotkb/P47088/entry","name":"GPI14","description":"GPI mannosyltransferase 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3781903","identifier":"P25580","identifierLink":"https://www.uniprot.org/uniprotkb/P25580/entry","name":"PBN1","description":"Protein PBN1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28533","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1271","complexName":"Condensin I complex","organismName":"Caenorhabditis elegans; 6239","description":"Involved in chromosome segregation, both in meiosis and mitosis. Binds to autosomes of both sexes to promote chromosome segregation. Initially located in cytoplasm and associates with chromosomes after nuclear breakdown. \r\n\r\nAssembles in alternating pattern with Condensin II complex (CPX-1272) along metaphase chromosomes with fully resolved sister chromatids. Specifically, the complex is required for conversion of interphase chromatin into mitotic-like condense chromosomes.\r\n\r\nDuring meiosis, localizes to the region between paired homologs at meiosis I and between sister chromatids at meiosis II.\r\n\r\nIn addition, the complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases","predictedComplex":false,"interactors":[{"ac":"EBI-1152127","identifier":"Q20060","identifierLink":"https://www.uniprot.org/uniprotkb/Q20060/entry","name":"smc-4","description":"Structural maintenance of chromosomes protein 4","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR18937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1152136","identifier":"Q09591","identifierLink":"https://www.uniprot.org/uniprotkb/Q09591/entry","name":"mix-1","description":"Mitotic chromosome and X-chromosome-associated protein mix-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR43941","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16399356","identifier":"G5EFJ4","identifierLink":"https://www.uniprot.org/uniprotkb/G5EFJ4/entry","name":"capg-1","description":"Condensin complex subunit capg-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR14418","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16399373","identifier":"G5EGE9","identifierLink":"https://www.uniprot.org/uniprotkb/G5EGE9/entry","name":"dpy-26","description":"Condensin complex subunit dpy-26","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-16399388","identifier":"Q9U2M1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9U2M1/entry","name":"dpy-28","description":"Condensin complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR14222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1272","complexName":"Condensin II complex","organismName":"Caenorhabditis elegans; 6239","description":"Involved in chromosome condensation and segregation, both in meiosis and mitosis. \r\n\r\nSpecifically, plays a role in prophase chromosome condensation and organization, where the complex concentrates on chromosomes when condensation initiates at prophase, and anaphase segregation. Almost exclusively found in the nucleus where it assembles in alternating pattern with Condensin I complex (CPX-1271) along metaphase chromosomes with fully resolved sister chromatids.\r\n\r\nDuring meiosis, localizes within the core of meiotic sister chromatids.","predictedComplex":false,"interactors":[{"ac":"EBI-1152127","identifier":"Q20060","identifierLink":"https://www.uniprot.org/uniprotkb/Q20060/entry","name":"smc-4","description":"Structural maintenance of chromosomes protein 4","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR18937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1152136","identifier":"Q09591","identifierLink":"https://www.uniprot.org/uniprotkb/Q09591/entry","name":"mix-1","description":"Mitotic chromosome and X-chromosome-associated protein mix-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR43941","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2002861","identifier":"P34341","identifierLink":"https://www.uniprot.org/uniprotkb/P34341/entry","name":"kle-2","description":"Condensin-2 complex subunit kle-2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR14324","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6458495","identifier":"Q20818","identifierLink":"https://www.uniprot.org/uniprotkb/Q20818/entry","name":"capg-2","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR16199","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6460139","identifier":"Q95Y84","identifierLink":"https://www.uniprot.org/uniprotkb/Q95Y84/entry","name":"hcp-6","description":"Condensin-2 complex subunit hcp-6","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR14222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1273","complexName":"Condensin I-like dosage compensation complex","organismName":"Caenorhabditis elegans; 6239","description":"Modulates chromosome and sex-specific gene expression. Binds to the two X chromosomes of hermaphrodites to negatively regulate transcription during interphase, and thus ensures that X-linked gene dosage from the X chromosome is equal to the single X in the XO males.\r\n\r\nIn C.elegans, this complex does not appear to have mitotic function.","predictedComplex":false,"interactors":[{"ac":"EBI-1152136","identifier":"Q09591","identifierLink":"https://www.uniprot.org/uniprotkb/Q09591/entry","name":"mix-1","description":"Mitotic chromosome and X-chromosome-associated protein mix-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR43941","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1152153","identifier":"P48996","identifierLink":"https://www.uniprot.org/uniprotkb/P48996/entry","name":"dpy-27","description":"Chromosome condensation protein dpy-27","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR18937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16399356","identifier":"G5EFJ4","identifierLink":"https://www.uniprot.org/uniprotkb/G5EFJ4/entry","name":"capg-1","description":"Condensin complex subunit capg-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR14418","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16399373","identifier":"G5EGE9","identifierLink":"https://www.uniprot.org/uniprotkb/G5EGE9/entry","name":"dpy-26","description":"Condensin complex subunit dpy-26","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-16399388","identifier":"Q9U2M1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9U2M1/entry","name":"dpy-28","description":"Condensin complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR14222","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1274","complexName":"Glycosylphosphatidylinositol-N-acetylglucosaminyltransferase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Monoglycosyltransferase complex that catalyses the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to the 6-position of phosphatidylinositol, the first, and committed, step of glycosylphosphatidylinositol (GPI) biosynthesis. GPI is a complex glycolipid with a core structure, phosphoethanolamine-6-mannose-alpha1,2-mannose-alpha1,6-mannose-alpha1,4-glucosamine-alpha1,6-inositol-phospholipid that functions as a membrane anchor for many cell surface proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-28685","identifier":"P53961","identifierLink":"https://www.uniprot.org/uniprotkb/P53961/entry","name":"GPI15","description":"Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI15","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15231","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-36611","identifier":"Q04082","identifierLink":"https://www.uniprot.org/uniprotkb/Q04082/entry","name":"GPI19","description":"Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI19","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR46346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7804","identifier":"P53306","identifierLink":"https://www.uniprot.org/uniprotkb/P53306/entry","name":"GPI1","description":"Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21329","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7809","identifier":"P46961","identifierLink":"https://www.uniprot.org/uniprotkb/P46961/entry","name":"GPI2","description":"Phosphatidylinositol N-acetylglucosaminyltransferase GPI2 subunit","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12982","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7815","identifier":"P32363","identifierLink":"https://www.uniprot.org/uniprotkb/P32363/entry","name":"SPT14","description":"Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45871","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-975247","identifier":"P62651","identifierLink":"https://www.uniprot.org/uniprotkb/P62651/entry","name":"ERI1","description":"Phosphatidylinositol N-acetylglucosaminyltransferase ERI1 subunit","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1275","complexName":"GPI-anchor transamidase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Transamidase enzyme complex that transfers the glycosylphosphatidylinositol (GPI) lipid to the newly made GPI protein in the endoplasmic reticulum, replacing the C-terminal GPI attachment signal peptide of a protein with the lipid. GPI is a complex glycolipid with a core structure, phosphoethanolamine-6-mannose-alpha1,2-mannose-alpha1,6-mannose-alpha1,4-glucosamine-alpha1,6-inositol-phospholipid that functions as a membrane anchor for many cell surface proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-24869","identifier":"P38875","identifierLink":"https://www.uniprot.org/uniprotkb/P38875/entry","name":"GPI16","description":"GPI transamidase component GPI16","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12959","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4343","identifier":"P41733","identifierLink":"https://www.uniprot.org/uniprotkb/P41733/entry","name":"GAB1","description":"GPI transamidase component GAB1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13121","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7252","identifier":"P39012","identifierLink":"https://www.uniprot.org/uniprotkb/P39012/entry","name":"GAA1","description":"GPI transamidase component GAA1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13304","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7777","identifier":"Q04080","identifierLink":"https://www.uniprot.org/uniprotkb/Q04080/entry","name":"GPI17","description":"GPI transamidase component GPI17","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21072","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7822","identifier":"P49018","identifierLink":"https://www.uniprot.org/uniprotkb/P49018/entry","name":"GPI8","description":"GPI-anchor transamidase","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR48067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1276","complexName":"HMC complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Represses HAP1 activity in the absence of heme, thus modulating oxygen dependent gene expression. The HMC complex  is associated with low DNA-binding and transcriptional activities. Heme disrupts the HMC and allows HAP1 to form a dimer, with higher DNA-binding and transcription rate properties.","predictedComplex":false,"interactors":[{"ac":"EBI-10420","identifier":"P25491","identifierLink":"https://www.uniprot.org/uniprotkb/P25491/entry","name":"YDJ1","description":"Mitochondrial protein import protein MAS5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43888","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16401534","identifier":"P0CE41","identifierLink":"https://www.uniprot.org/uniprotkb/P0CE41/entry","name":"HAP1","description":"Heme-responsive zinc finger transcription factor HAP1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31944","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18084","identifier":"P25567","identifierLink":"https://www.uniprot.org/uniprotkb/P25567/entry","name":"SRO9","description":"RNA-binding protein SRO9","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22792","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8591","identifier":"P10591","identifierLink":"https://www.uniprot.org/uniprotkb/P10591/entry","name":"SSA1","description":"Heat shock protein SSA1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8603","identifier":"P10592","identifierLink":"https://www.uniprot.org/uniprotkb/P10592/entry","name":"SSA2","description":"Heat shock protein SSA2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8659","identifier":"P02829","identifierLink":"https://www.uniprot.org/uniprotkb/P02829/entry","name":"HSP82","description":"ATP-dependent molecular chaperone HSP82","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11528","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8666","identifier":"P15108","identifierLink":"https://www.uniprot.org/uniprotkb/P15108/entry","name":"HSC82","description":"ATP-dependent molecular chaperone HSC82","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11528","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1277","complexName":"INO2-INO4 transcription activation complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Binds to a cis-acting promoter element, designated ICRE (inositol/choline-responsive element, consensus sequence WYTTCAYRTGS). Induces expression of CHO1, the enzyme responsible for the synthesis of phosphatidylethanolamine from CDP-diacylglycerol, under growth conditions when the level of phosphatidate is elevated and tethers the OPI1 repressor to the nuclear/endoplasmic reticulum membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-9262","identifier":"P26798","identifierLink":"https://www.uniprot.org/uniprotkb/P26798/entry","name":"INO2","description":"Protein INO2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-9270","identifier":"P13902","identifierLink":"https://www.uniprot.org/uniprotkb/P13902/entry","name":"INO4","description":"Protein INO4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1278","complexName":"LMA1 complex, TRX1 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for the trafficking of yeast vacuoles, such as homotypic vacuole and ER-derived COPII vesicle fusion with the Golgi. Acts synergistically with SEC18 to support vacuole fusion and acts in an early stage of the vacuole inheritance reaction. The reduction-oxidation activity of thioredoxin does not appear to be required for this function.","predictedComplex":false,"interactors":[{"ac":"EBI-19607","identifier":"P22217","identifierLink":"https://www.uniprot.org/uniprotkb/P22217/entry","name":"TRX1","description":"Thioredoxin-1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10438","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9311","identifier":"P0CT04","identifierLink":"https://www.uniprot.org/uniprotkb/P0CT04/entry","name":"PBI2","description":"Protease B inhibitor 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28288","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1279","complexName":"LMA1 complex, TRX2 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for the trafficking of yeast vacuoles, such as homotypic vacuole and ER-derived COPII vesicle fusion with the Golgi. Acts synergistically with SEC18 to support vacuole fusion and acts in an early stage of the vacuole inheritance reaction. The reduction-oxidation activity of thioredoxin does not appear to be required for this function.","predictedComplex":false,"interactors":[{"ac":"EBI-19598","identifier":"P22803","identifierLink":"https://www.uniprot.org/uniprotkb/P22803/entry","name":"TRX2","description":"Thioredoxin-2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10438","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9311","identifier":"P0CT04","identifierLink":"https://www.uniprot.org/uniprotkb/P0CT04/entry","name":"PBI2","description":"Protease B inhibitor 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR28288","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1280","complexName":"Luminal surveillance complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Recognizes the protein determinant required for ER-associated degradation (ERAD) of mis-folded proteins, recruiting substrates to HRD1-associated machinery, and activating downstream events that commit substrates for degradation. The complex recognizes misfolded glycoproteins independent of their glycosylation status and brings them to the downstream ubiquitination/extraction machinery, however the commitment step to destruction requires the lectin YOS9, which recognizes the glycan species found on terminally misfolded proteins.","predictedComplex":false,"interactors":[{"ac":"EBI-31647","identifier":"Q05787","identifierLink":"https://www.uniprot.org/uniprotkb/Q05787/entry","name":"HRD3","description":"ERAD-associated E3 ubiquitin-protein ligase component HRD3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11102","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-34938","identifier":"Q99220","identifierLink":"https://www.uniprot.org/uniprotkb/Q99220/entry","name":"YOS9","description":"Protein OS-9 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR15414","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7876","identifier":"P16474","identifierLink":"https://www.uniprot.org/uniprotkb/P16474/entry","name":"KAR2","description":"Endoplasmic reticulum chaperone BiP","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1281","complexName":"Laminin111-nidogen complex","organismName":"Mus musculus; 10090","description":"An extracellular matrix complex responsible for basement membrane stabilization and cell-matrix adhesion. Crosslinking of the nidogen subunit from one complex to a laminin arm of a second by tissue transglutaminases forms large assemblies. Facilitates cell adhesion by binding collagens (e.g. collagen type I, CPX-2956 or collagen type IV, CPX-2959) and integrins (e.g. alpha3beta1, CPX-3117 or alphavbeta3, CPX-3035). May modify type I collagen scaffolds and thereby enhance myotube formation.","predictedComplex":false,"interactors":[{"ac":"EBI-1032117","identifier":"P10493","identifierLink":"https://www.uniprot.org/uniprotkb/P10493/entry","name":"Nid1","description":"Nidogen-1","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46513","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9249158","identifier":"CPX-3008","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-3008","name":"Laminin-111 complex","description":"Laminin-111","stochiometry":null,"interactorType":"stable complex","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-1282","complexName":"Laminin211-nidogen complex","organismName":"Homo sapiens; 9606","description":"An extracellular matrix complex responsible for basement membrane stabilization and cell-matrix adhesion. Crosslinking of the nidogen subunit from one complex to a laminin arm of a second by tissue transglutaminases forms large assemblies. Facilitates cell adhesion by binding collagens (e.g. collagen type I, CPX-1650 or collagen type IV, CPX-1723) and integrins (e.g. alpha3beta1, CPX-1797 or alphavbeta3, CPX-1795). May modify type I collagen scaffolds and thereby enhance myotube formation.","predictedComplex":false,"interactors":[{"ac":"EBI-2529716","identifier":"CPX-1771","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-1771","name":"Laminin-211 complex","description":"Laminin-211","stochiometry":null,"interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2828729","identifier":"P14543","identifierLink":"https://www.uniprot.org/uniprotkb/P14543/entry","name":"NID1","description":"Nidogen-1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46513","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1284","complexName":"Laminin211-nidogen complex","organismName":"Mus musculus; 10090","description":"An extracellular matrix complex responsible for basement membrane stabilization and cell-matrix adhesion. Crosslinking of the nidogen subunit from one complex to a laminin arm of a second by tissue transglutaminases forms large assemblies. Facilitates cell adhesion by binding collagens (e.g. collagen type I, CPX-2956 or collagen type IV, CPX-2959) and integrins (e.g. alpha3beta1, CPX-3117 or alphavbeta3, CPX-3035). May modify type I collagen scaffolds and thereby enhance myotube formation.","predictedComplex":false,"interactors":[{"ac":"EBI-1032117","identifier":"P10493","identifierLink":"https://www.uniprot.org/uniprotkb/P10493/entry","name":"Nid1","description":"Nidogen-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46513","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9249180","identifier":"CPX-3009","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-3009","name":"Laminin-211 complex","description":"Laminin-211","stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-1283","complexName":"HTM1-PDI1 exomannosidase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Exomannosidase complex which initiates breakdown of unfolded glycoproteins by trimming the Man8GlcNAc2 glycan to produce Man7GlcNAc2, thus initiating the clearance of these proteins from the endoplasmic reticulum. N-linked Man7GlcNAc2 oligosaccharides serve as a signal for degradation by the Hrd1 ubiquitin ligase complex (CPX-3070).","predictedComplex":false,"interactors":[{"ac":"EBI-1169353","identifier":"CHEBI:29108","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:29108","name":"calcium(2+)","description":null,"stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-13012","identifier":"P17967","identifierLink":"https://www.uniprot.org/uniprotkb/P17967/entry","name":"PDI1","description":"Protein disulfide-isomerase","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR18929","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-24256","identifier":"P38888","identifierLink":"https://www.uniprot.org/uniprotkb/P38888/entry","name":"MNL1","description":"ER degradation-enhancing alpha-mannosidase-like protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45679","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1285","complexName":"Laminin221-nidogen complex","organismName":"Homo sapiens; 9606","description":"An extracellular matrix complex responsible for basement membrane stabilization and cell-matrix adhesion. Crosslinking of the nidogen subunit from one complex to a laminin arm of a second by tissue transglutaminases forms large assemblies. Facilitates cell adhesion by binding collagens (e.g. collagen type I, CPX-1650 or collagen type IV, CPX-1723) and integrins (e.g. alpha3beta1, CPX-1797 or alphavbeta3, CPX-1795). May modify type I collagen scaffolds and thereby enhance myotube formation.","predictedComplex":false,"interactors":[{"ac":"EBI-2529805","identifier":"CPX-1773","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-1773","name":"Laminin-221 complex","description":"Laminin-221","stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-2828729","identifier":"P14543","identifierLink":"https://www.uniprot.org/uniprotkb/P14543/entry","name":"NID1","description":"Nidogen-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46513","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1286","complexName":"Laminin221-nidogen complex","organismName":"Mus musculus; 10090","description":"An extracellular matrix complex responsible for basement membrane stabilization and cell-matrix adhesion. Crosslinking of the nidogen subunit from one complex to a laminin arm of a second by tissue transglutaminases forms large assemblies. Facilitates cell adhesion by binding collagens (e.g. collagen type I, CPX-2956 or collagen type IV, CPX-2959) and integrins (e.g. alpha3beta1, CPX-3117 or alphavbeta3, CPX-3035). May modify type I collagen scaffolds and thereby enhance myotube formation.","predictedComplex":false,"interactors":[{"ac":"EBI-1032117","identifier":"P10493","identifierLink":"https://www.uniprot.org/uniprotkb/P10493/entry","name":"Nid1","description":"Nidogen-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR46513","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9249280","identifier":"CPX-3011","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-3011","name":"Laminin-221 complex","description":"Laminin-221","stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Mus musculus; 10090","xrefs":[]}]},{"complexAC":"CPX-1287","complexName":"MPS2-BBP1 spindle pole body anchor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Key mediator of the link between the nuclear envelope and the spindle pole body (SPB), anchoring the SPB to fusion sites of the inner nuclear membrane and outer nuclear membrane. Forms higher molecular weight assemblies with other SPB proteins (MPS3/P47069, SPC29/P33419) which hold the SPB in the nuclear envelope.","predictedComplex":false,"interactors":[{"ac":"EBI-23834","identifier":"P53159","identifierLink":"https://www.uniprot.org/uniprotkb/P53159/entry","name":"MPS2","description":"Monopolar spindle protein 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-3448","identifier":"Q12365","identifierLink":"https://www.uniprot.org/uniprotkb/Q12365/entry","name":"BBP1","description":"Spindle pole component BBP1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1288","complexName":"MEI5-SAE3 recombination assembly factor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Regulates homologous recombination repair by binding to, and stimulating, the homologous DNA 3-stranded exchange activity of  meiosis-specific DMC1 (P25453). Enhances DMC1 loading onto RPA-coated single-stranded DNA, at a RAD51 foci and that it enhances DMC1-mediated D-loop formation.  The coordinated actions of RAD51 and DMC1 are considered to play a critical role in homology searches and strand exchange during recombination.","predictedComplex":false,"interactors":[{"ac":"EBI-10685","identifier":"P32489","identifierLink":"https://www.uniprot.org/uniprotkb/P32489/entry","name":"MEI5","description":"Meiosis protein 5","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-16412526","identifier":"P89114","identifierLink":"https://www.uniprot.org/uniprotkb/P89114/entry","name":"SAE3","description":"Pachytene arrest protein SAE3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1289","complexName":"Intraflagellar transport complex A","organismName":"Caenorhabditis elegans; 6239","description":"IFT particles, composed of the IFT-A and IFT-B (CPX-1290) complexes, enable bidirectional motility along axoneme microtubules essential for the formation (ciliogenesis) and maintenance of cilia that assemble within a membrane projection from the cell surface. Outward or anterograde movement from the cell body to the ciliary tip  is powered by kinesin-2 while the inward or retrograde movement back to the cell body is powered by cytoplasmic Dynein-2 motor. \r\n\r\nMay be required for ciliary entrance and transport of specific ciliary cargo proteins such as che-3 (Q19542) which are related to motility.","predictedComplex":false,"interactors":[{"ac":"EBI-16011301","identifier":"P90757","identifierLink":"https://www.uniprot.org/uniprotkb/P90757/entry","name":"che-11","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR15722","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16011450","identifier":"G5ECZ4","identifierLink":"https://www.uniprot.org/uniprotkb/G5ECZ4/entry","name":"dyf-2","description":"WD repeat-containing protein dyf-2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR14920","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16413371","identifier":"G5EFW7","identifierLink":"https://www.uniprot.org/uniprotkb/G5EFW7/entry","name":"daf-10","description":"Intraflagellar transport protein 122 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12764","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16413396","identifier":"Q9BIA4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BIA4/entry","name":"ift-43","description":"Intraflagellar transport protein 43 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[]},{"ac":"EBI-2421225","identifier":"Q20255","identifierLink":"https://www.uniprot.org/uniprotkb/Q20255/entry","name":"ift-139","description":"Tetratricopeptide repeat protein 21 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR14699","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-326183","identifier":"Q18859","identifierLink":"https://www.uniprot.org/uniprotkb/Q18859/entry","name":"ifta-1","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12764","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1290","complexName":"Intraflagellar transport complex B","organismName":"Caenorhabditis elegans; 6239","description":"IFT particles, composed of the IFT-A (CPX-1289) and IFT-B complexes, enable bidirectional motility along axoneme microtubules essential for the formation (ciliogenesis) and maintenance of cilia that assemble within a membrane projection from the cell surface. Outward or anterograde movement from the cell body to the ciliary tip  is powered by kinesin-2 while the inward or retrograde movement back to the cell body is powered by cytoplasmic Dynein-2 motor. May be required for ciliary entrance and transport of specific ciliary cargo proteins such as che-3 (Q19542) which are related to motility.","predictedComplex":false,"interactors":[{"ac":"EBI-16011330","identifier":"Q8TA52","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TA52/entry","name":"ift-20","description":"Intraflagellar transport protein 20 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR31978","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16413527","identifier":"A8DYR7","identifierLink":"https://www.uniprot.org/uniprotkb/A8DYR7/entry","name":"ift-81","description":"Intraflagellar transport protein 81 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR15614","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16413547","identifier":"G5ED37","identifierLink":"https://www.uniprot.org/uniprotkb/G5ED37/entry","name":"osm-5","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR44117","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16413569","identifier":"Q8I7G4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8I7G4/entry","name":"dyf-1","description":"Tetratricopeptide repeat protein 30 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR20931","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16413591","identifier":"Q9XUC2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XUC2/entry","name":"ifta-2","description":"Intraflagellar transport associated protein 2","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24073","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16413611","identifier":"Q95QT8","identifierLink":"https://www.uniprot.org/uniprotkb/Q95QT8/entry","name":"dyf-13","description":"Intraflagellar transport protein 56 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR14781","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16413627","identifier":"Q22830","identifierLink":"https://www.uniprot.org/uniprotkb/Q22830/entry","name":"osm-1","description":"Intraflagellar transport protein osm-1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR15722","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16413650","identifier":"Q93833","identifierLink":"https://www.uniprot.org/uniprotkb/Q93833/entry","name":"che-13","description":"Intraflagellar transport protein che-13","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR16011","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16413674","identifier":"Q0G838","identifierLink":"https://www.uniprot.org/uniprotkb/Q0G838/entry","name":"dyf-6","description":"Intraflagellar transport protein 46 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR13376","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16413704","identifier":"G5EGF0","identifierLink":"https://www.uniprot.org/uniprotkb/G5EGF0/entry","name":"che-2","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR24098","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16413732","identifier":"Q17595","identifierLink":"https://www.uniprot.org/uniprotkb/Q17595/entry","name":"dyf-11","description":"TRAF3-interacting protein 1","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR31363","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20726618","identifier":"A0A2C9C2L6","identifierLink":"https://www.uniprot.org/uniprotkb/A0A2C9C2L6/entry","name":"ift-74","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR31432","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-327358","identifier":"Q6I6D4","identifierLink":"https://www.uniprot.org/uniprotkb/Q6I6D4/entry","name":"dyf-3","description":"Clusterin-associated protein 1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR21547","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-329470","identifier":"G5EDF6","identifierLink":"https://www.uniprot.org/uniprotkb/G5EDF6/entry","name":"osm-6","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Caenorhabditis elegans; 6239","xrefs":[{"identifier":"PTHR12969","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1291","complexName":"Evening Complex","organismName":"Arabidopsis thaliana; 3702","description":"A transcription factor complex that is regulated by the circadian clock and negatively regulates hypocotyl growth. Represses the expression of the hypocotyl growth proteins PIF4 (Q8W2F3) and PIF5 (Q84LH8)  in the early evening by directly binding to their promoter regions. \r\n\r\nSignals from both the clock and light pathways converge on PIF4 and PIF5 which permits maximal hypocotyl growth at dawn in diurnal conditions.","predictedComplex":false,"interactors":[{"ac":"EBI-15406721","identifier":"Q9SNB4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9SNB4/entry","name":"LUX","description":"Transcription factor LUX","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR31442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16415004","identifier":"O04211","identifierLink":"https://www.uniprot.org/uniprotkb/O04211/entry","name":"ELF4","description":"Protein EARLY FLOWERING 4","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR33469","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16415030","identifier":"O82804","identifierLink":"https://www.uniprot.org/uniprotkb/O82804/entry","name":"ELF3","description":"Protein EARLY FLOWERING 3","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR34281","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1292","complexName":"REC102-REC104 meiotic recombination initiation complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Required for the formation and repair of programmed DNA double-strand breaks (DSBs) catalyzed by SPO11 (Q22236) during meiotic recombination. May act to bridge the MER2-MEI4-REC114 complex (CPX-1809) with SPO11 and SKI8 (Q02793).  Required for SPO11 nuclear localization, chromatin association, and binding to hot spots. Preferentially localizes to sites on the structural axis, where the series of loops (10-20kb) that pairs of sister chromatids organise into are anchored.","predictedComplex":false,"interactors":[{"ac":"EBI-14432","identifier":"Q02721","identifierLink":"https://www.uniprot.org/uniprotkb/Q02721/entry","name":"REC102","description":"Meiotic recombination protein REC102","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-16412992","identifier":"P33323","identifierLink":"https://www.uniprot.org/uniprotkb/P33323/entry","name":"REC104","description":"Meiotic recombination protein REC104","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1293","complexName":"Mitochondrial 2-oxoglutarate dehydrogenase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Catalyzes the oxidative decarboxylation of alpha-ketoglutarate to succinyl-CoA,  NADH and CO2. Succinyl-CoA is then converted to succinate by succinyl-CoA synthetase or used as a substrate in heme biosynthesis. Acts as a major site of reactive oxygen species generation.","predictedComplex":false,"interactors":[{"ac":"EBI-12459","identifier":"P20967","identifierLink":"https://www.uniprot.org/uniprotkb/P20967/entry","name":"KGD1","description":"2-oxoglutarate dehydrogenase, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23152","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12464","identifier":"P19262","identifierLink":"https://www.uniprot.org/uniprotkb/P19262/entry","name":"KGD2","description":"Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43416","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16295","identifier":"P19955","identifierLink":"https://www.uniprot.org/uniprotkb/P19955/entry","name":"YMR31","description":"Alpha-ketoglutarate dehydrogenase subunit 4, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR31601","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16416616","identifier":"CHEBI:83088","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:83088","name":"(r)-lipoate","description":"(R)-lipoate","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-5940","identifier":"P09624","identifierLink":"https://www.uniprot.org/uniprotkb/P09624/entry","name":"LPD1","description":"Dihydrolipoyl dehydrogenase, mitochondrial","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR22912","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9663508","identifier":"CHEBI:57692","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:57692","name":"fad(3-)","description":"FAD(3-)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-9691551","identifier":"CHEBI:58937","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:58937","name":"thiamine(1+) diphosphate(3-)","description":"thiamine(1+) diphosphate(3-)","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-1294","complexName":"Mitochondrial ribonuclease P complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Responsible for the 5' endonucleolytic cleavage of precursor tRNAs (pre-tRNAs) to remove approximately 12 leader nucleotides to yield mature tRNAs.  The RNA subunit of the mitochondrial RNase P is most  probably a catalytically active ribozyme that is capable of both recognizing and cleaving substrates efficiently and accurately. The protein component serves as an absolutely required cofactor.","predictedComplex":false,"interactors":[{"ac":"EBI-11302071","identifier":"URS00007E9EB6_559292","identifierLink":"http://rnacentral.org/rna/URS00007E9EB6_559292","name":"mt-p rna yeast","description":"mitochondrial RNAsi P RNA RPM1 yeast","stochiometry":null,"interactorType":"ribonucleic acid","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-15903","identifier":"Q02773","identifierLink":"https://www.uniprot.org/uniprotkb/Q02773/entry","name":"RPM2","description":"Ribonuclease P protein component, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47934","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1295","complexName":"MKT1-PBP1 translation regulation complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Translational regulation complex which modulates levels of the HO endonucease in the mother cells of budding yeast, enabling the cells to switch mating types. The mechanism is unclear but the nuclease activity activity of MKT1 appears to be equired for the function.","predictedComplex":false,"interactors":[{"ac":"EBI-10983","identifier":"P40850","identifierLink":"https://www.uniprot.org/uniprotkb/P40850/entry","name":"MKT1","description":"Post-transcriptional regulator MKT1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR11081","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12961","identifier":"P53297","identifierLink":"https://www.uniprot.org/uniprotkb/P53297/entry","name":"PBP1","description":"PAB1-binding protein 1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12854","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1296","complexName":"Urease activation complex","organismName":"Arabidopsis thaliana; 3702","description":"Facilitates the activation of urease. Involves the channeling of two nickel ions into the active site of urease. UREG is crucial for nickel delivery during urease activation.","predictedComplex":false,"interactors":[{"ac":"EBI-16417779","identifier":"Q9SR52","identifierLink":"https://www.uniprot.org/uniprotkb/Q9SR52/entry","name":"URE","description":"Urease","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR43440","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16417810","identifier":"Q7Y0S0","identifierLink":"https://www.uniprot.org/uniprotkb/Q7Y0S0/entry","name":"URED","description":"Urease accessory protein D","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR33643","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16417823","identifier":"O64700","identifierLink":"https://www.uniprot.org/uniprotkb/O64700/entry","name":"UREG","description":"Urease accessory protein G","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR31715","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2296617","identifier":"CHEBI:49786","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:49786","name":"nickel(2+)","description":"Nickel(2+)","stochiometry":"minValue: 2, maxValue: 2","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-4441467","identifier":"Q9XHZ3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9XHZ3/entry","name":"UREF","description":"Urease accessory protein F","stochiometry":null,"interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR33620","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1297","complexName":"CPAP-STIL complex","organismName":"Mus musculus; 10090","description":"A protein complex that is required for centriole biogenesis and duplication. \r\n\r\nDuring procentriole formation during G1/S transition, Plk4 (Q64702) activates STIL by phosphorylating its STAN domain, then activated Stil loads Sass6 and Cenpj (CPAP) to the base of the procentriole to initiate procentriole assembly. Together with Cep135 (Q6P5D4), Cenpj and Sass6 form the central scaffolding of the 9-fold symmetry of the procentriole. \r\n\r\nIn the assembled centriole 9 homodimers of Sass6 form the central waggon wheel while Cep135 and Cenpj connect Sass6 to the microtubules. \r\n\r\nLack of the complex or any of its subunits leads to a loss of centriole formation or spindle formation while overexpression leads to overly long centrioles. Patients with autosomal recessive primary microcephaly often present with aberrant spindle positioning in progenitor cells during brain development and mutations in Cenpj or Stil.","predictedComplex":false,"interactors":[{"ac":"EBI-16417888","identifier":"Q60988","identifierLink":"https://www.uniprot.org/uniprotkb/Q60988/entry","name":"Stil","description":"SCL-interrupting locus protein homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR15128","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16417922","identifier":"Q569L8","identifierLink":"https://www.uniprot.org/uniprotkb/Q569L8/entry","name":"Cpap","description":"Centrosomal P4.1-associated protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR10331","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2552722","identifier":"Q80UK7","identifierLink":"https://www.uniprot.org/uniprotkb/Q80UK7/entry","name":"Sass6","description":"Spindle assembly abnormal protein 6 homolog","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR44281","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1298","complexName":"CEP192-PLK4 complex","organismName":"Mus musculus; 10090","description":"A protein complex essential for centriole biogenesis; temporarily part of the procentriole to which it recruits further proteins involved in procentriole formation. PLK4 is snatched away from CEP192 by CEP152 (A2AUM9) forming CEP152-PLK4 complex (CPX-1160). \r\n\r\nImpairment of centriole duplication eventually leads to impaired spindle formation and mitosis which is linked to tumorigenesis.","predictedComplex":false,"interactors":[{"ac":"EBI-16110918","identifier":"E9Q4Y4","identifierLink":"https://www.uniprot.org/uniprotkb/E9Q4Y4/entry","name":"Cep192","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR16029","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2552433","identifier":"Q64702","identifierLink":"https://www.uniprot.org/uniprotkb/Q64702/entry","name":"Plk4","description":"Serine/threonine-protein kinase PLK4","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR24345","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1299","complexName":"CEP152-PLK4 complex","organismName":"Homo sapiens; 9606","description":"A protein complex essential for centriole biogenesis; temporarily part of the procentriole to which it recruits further proteins involved in procentriole formation. Snatches PLK4 away from CEP192-PLK4 complex (CPX-1161). \r\n\r\nImpairment of centriole duplication eventually leads to impaired spindle formation and mitosis which is linked to tumorigenesis.","predictedComplex":false,"interactors":[{"ac":"EBI-311012","identifier":"O94986","identifierLink":"https://www.uniprot.org/uniprotkb/O94986/entry","name":"CEP152","description":"Centrosomal protein of 152 kDa","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10337","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-746202","identifier":"O00444","identifierLink":"https://www.uniprot.org/uniprotkb/O00444/entry","name":"PLK4","description":"Serine/threonine-protein kinase PLK4","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24345","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1300","complexName":"CEP192-PLK4 complex","organismName":"Danio rerio; 7955","description":"A protein complex essential for centriole biogenesis; temporarily part of the procentriole to which it recruits further proteins involved in procentriole formation. PLK4 is snatched away from CEP192 (A0A0R4IEX1) by CEP152 forming CEP152-PLK4 complex (CPX-1301). \r\n\r\nImpairment of centriole duplication eventually leads to impaired spindle formation and mitosis which is linked to tumorigenesis.","predictedComplex":false,"interactors":[{"ac":"EBI-15188547","identifier":"Q7ZVS3","identifierLink":"https://www.uniprot.org/uniprotkb/Q7ZVS3/entry","name":"plk4","description":"Serine/threonine-protein kinase PLK4","stochiometry":null,"interactorType":"protein","organismName":"Danio rerio; 7955","xrefs":[{"identifier":"PTHR24345","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-42477909","identifier":"A0A8M3AT73","identifierLink":"https://www.uniprot.org/uniprotkb/A0A8M3AT73/entry","name":"cep192","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Danio rerio; 7955","xrefs":[]}]},{"complexAC":"CPX-1301","complexName":"CEP152-PLK4 complex","organismName":"Danio rerio; 7955","description":"A protein complex essential for centriole biogenesis; temporarily part of the procentriole to which it recruits further proteins involved in procentriole formation. Snatches PLK4 away from CEP192-PLK4 complex (CPX-1300). \r\n\r\nImpairment of centriole duplication eventually leads to impaired spindle formation and mitosis which is linked to tumorigenesis.","predictedComplex":false,"interactors":[{"ac":"EBI-15188547","identifier":"Q7ZVS3","identifierLink":"https://www.uniprot.org/uniprotkb/Q7ZVS3/entry","name":"plk4","description":"Serine/threonine-protein kinase PLK4","stochiometry":null,"interactorType":"protein","organismName":"Danio rerio; 7955","xrefs":[{"identifier":"PTHR24345","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-42477921","identifier":"A0A8M3AZU2","identifierLink":"https://www.uniprot.org/uniprotkb/A0A8M3AZU2/entry","name":"cep152","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Danio rerio; 7955","xrefs":[]}]},{"complexAC":"CPX-1302","complexName":"OPY2-MSB2 osmosensory complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Osmosensor that activates the HOG1 mitogen-activated protein kinase (P32485), which regulates diverse osmoadaptive responses. Increased external osmolarity induces conformational changes in the complex formed between the Hkr1-Msb2 homology (HMH) domain of MSB2 and the cysteine-rich region of OPY2. This conformational change is transmitted across the plasma membrane to induce an interaction between the associated STE20 (Q03497) and STE11 (P23561) protein kinases, thus activating a signal cascade which culminates in HOG1 activation.","predictedComplex":false,"interactors":[{"ac":"EBI-11328","identifier":"P32334","identifierLink":"https://www.uniprot.org/uniprotkb/P32334/entry","name":"MSB2","description":"Signaling mucin MSB2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR35778","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2068557","identifier":"Q06810","identifierLink":"https://www.uniprot.org/uniprotkb/Q06810/entry","name":"OPY2","description":"Protein OPY2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1303","complexName":"MST27-MST28 vesicle formation complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Role in promoting vesicle formation. Appears to provide nucleation sites, which recruit and locally concentrate cytosolic coat complexes onto the membranes of the early secretory pathway. The complexes cycles between the endoplasmic reticulum (ER) and Golgi apparatus, however, its steady-state localization is probably in the ER.","predictedComplex":false,"interactors":[{"ac":"EBI-20785","identifier":"P39552","identifierLink":"https://www.uniprot.org/uniprotkb/P39552/entry","name":"MST28","description":"Multicopy suppressor of SEC21 protein 28","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-6205","identifier":"P53176","identifierLink":"https://www.uniprot.org/uniprotkb/P53176/entry","name":"MST27","description":"Multicopy suppressor of SEC21 protein 27","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1304","complexName":"MYO2-VAC17-VAC8 transport complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Transport complex required to move the attached vacuole membrane along actin cables from a mother cell into the bud. Once in the bud, VAC17 is degraded, releasing the vacuole from MYO2 and depositing it at the centre of the bud.","predictedComplex":false,"interactors":[{"ac":"EBI-11659","identifier":"P19524","identifierLink":"https://www.uniprot.org/uniprotkb/P19524/entry","name":"MYO2","description":"Myosin-2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13140","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20212","identifier":"P39968","identifierLink":"https://www.uniprot.org/uniprotkb/P39968/entry","name":"VAC8","description":"Vacuolar protein 8","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR47249","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-21800","identifier":"P25591","identifierLink":"https://www.uniprot.org/uniprotkb/P25591/entry","name":"VAC17","description":"vacuole-related protein 17","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]}]},{"complexAC":"CPX-1305","complexName":"SLBP-SLIP1 complex","organismName":"Danio rerio; 7955","description":"As part of the histone translation initiation machinery SLBP-SLIP1 complex binds the 3-prime-stem-loop structure of histone mRNA (hmRNA), facilitates its translation initiation and may also be involved in its processing and nuclear export. \r\n\r\nRemodels the mRNA ribonucleoprotein complexes (RNPs) from nuclear to cytoplasmic specificity. mif4gd subunit interacts with the eIF4F complex, the cytoplasmic cap-binding complex that binds the 5-prime histone mRNA cap. eIF4F complex binding facilitates the circularisation of hmRNA that is required for its translation. \r\n\r\nActs exclusively during G1/S transition when histones are in greatest demand. Both the complex and hmRNA are degraded at the end of S phase when Thr-80 and Thr-81 of slbp are phosphorylated (as shown in human ortholog). Translation of histones during other cell phases cause defects and can be toxic to the cell.","predictedComplex":false,"interactors":[{"ac":"EBI-16419713","identifier":"Q5EAQ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q5EAQ1/entry","name":"mif4gdb","description":"MIF4G domain-containing protein B","stochiometry":null,"interactorType":"protein","organismName":"Danio rerio; 7955","xrefs":[{"identifier":"PTHR23254","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16419731","identifier":"Q7SXI8","identifierLink":"https://www.uniprot.org/uniprotkb/Q7SXI8/entry","name":"slbp","description":null,"stochiometry":null,"interactorType":"protein","organismName":"Danio rerio; 7955","xrefs":[]}]},{"complexAC":"CPX-1306","complexName":"Nascent polypeptide-associated complex, EGD1-EGD2 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Reversibly binds to cytoplasmic ribosomes and interacts with nascent polypeptides emerging from the ribosome to prevent them from incorrect interactions, thus controlling the early protein folding processes and preventing aggregation or degradation of newly synthesized proteins. The EGD1-EGD2 variant appears to be the dominant form of the complex formed in vivo and has a preference for ribosomes translating metabolic enzymes as well as secretory and membrane proteins. By binding to the first 30-50 amino acids to be translated, the complex prevents mitochondrial precursor proteins synthesized in the cytosol from forming a basic, amphipathic helix. This enables this targeting sequence to first bind to chaperones and mitochondrial import stimulating factors and then to the outer membrane translocase complex (CPX-474) on the mitochondrial surface.","predictedComplex":false,"interactors":[{"ac":"EBI-6371","identifier":"Q02642","identifierLink":"https://www.uniprot.org/uniprotkb/Q02642/entry","name":"EGD1","description":"Nascent polypeptide-associated complex subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6379","identifier":"P38879","identifierLink":"https://www.uniprot.org/uniprotkb/P38879/entry","name":"EGD2","description":"Nascent polypeptide-associated complex subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21713","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1307","complexName":"Nascent polypeptide-associated complex, BTT1-EGD2 variant","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Reversibly binds to cytoplasmic ribosomes and interacts with nascent polypeptides emerging from the ribosome to prevent them from incorrect interactions, thus controlling the early protein folding processes and preventing aggregation or degradation of newly synthesized proteins. The BTT1-EGD2 variant appears to be the less dominant form of the complex formed in vivo and has a preference for ribosomes translating mitochondrial or ribosomal proteins. By binding to the first 30-50 amino acids to be translated, the complex prevents mitochondrial precursor proteins synthesized in the cytosol from forming a basic, amphipathic helix. This enables this targeting sequence to first bind to chaperones and mitochondrial import stimulating factors and then to the outer membrane translocase complex (CPX-474) on the mitochondrial surface.","predictedComplex":false,"interactors":[{"ac":"EBI-3802","identifier":"P40314","identifierLink":"https://www.uniprot.org/uniprotkb/P40314/entry","name":"BTT1","description":"Nascent polypeptide-associated complex subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10351","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6379","identifier":"P38879","identifierLink":"https://www.uniprot.org/uniprotkb/P38879/entry","name":"EGD2","description":"Nascent polypeptide-associated complex subunit alpha","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR21713","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1308","complexName":"LSM1-7-PAT1 complex, variant LSM1A-LSM3A-LSM6A-PAT1","organismName":"Arabidopsis thaliana; 3702","description":"A cytoplasmic complex essential for P-body formation and deadenylation-dependent decapping of mRNA thereby regulating mRNA decay and subsequent degradation by the 5-to-3-prime pathway. Loss of LMS1 subunits leads to a range of severe developmental abnormalities.","predictedComplex":false,"interactors":[{"ac":"EBI-16419347","identifier":"Q945P8","identifierLink":"https://www.uniprot.org/uniprotkb/Q945P8/entry","name":"LSM1A","description":"Sm-like protein LSM1A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR15588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16419382","identifier":"Q9FKB0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9FKB0/entry","name":"LSM5","description":"Sm-like protein LSM5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR20971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16419411","identifier":"F4K4E3","identifierLink":"https://www.uniprot.org/uniprotkb/F4K4E3/entry","name":"LSM4","description":"Sm-like protein LSM4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16585848","identifier":"Q0WPK4","identifierLink":"https://www.uniprot.org/uniprotkb/Q0WPK4/entry","name":"PAT1","description":"Protein PAT1 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR21551","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4431531","identifier":"Q9M1Z3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9M1Z3/entry","name":"LSM6A","description":"Sm-like protein LSM6A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4433669","identifier":"Q9SI54","identifierLink":"https://www.uniprot.org/uniprotkb/Q9SI54/entry","name":"LSM7","description":"Sm-like protein LSM7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9347247","identifier":"Q9LMN4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9LMN4/entry","name":"LSM3A","description":"Sm-like protein LSM3A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR13110","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9347308","identifier":"Q1H595","identifierLink":"https://www.uniprot.org/uniprotkb/Q1H595/entry","name":"LSM2","description":"Sm-like protein LSM2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR13829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1309","complexName":"LSM2-8 complex, variant LSM3A-LSM6A","organismName":"Arabidopsis thaliana; 3702","description":"A ringshaped protein complex that selectively binds to snRNAs and to unspliced transcripts localized within the nucleus. In the U6 snRNP spliceosome machinery stabilises U6 small nuclear RNA (U6 snRNA) to ensure the efficiency and accuracy of constitutive and alternative splicing of selected pre-mRNAs depending on the environmental conditions. Loss of LMS8 leads to a range of severe developmental abnormalities.","predictedComplex":false,"interactors":[{"ac":"EBI-16419382","identifier":"Q9FKB0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9FKB0/entry","name":"LSM5","description":"Sm-like protein LSM5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR20971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16419411","identifier":"F4K4E3","identifierLink":"https://www.uniprot.org/uniprotkb/F4K4E3/entry","name":"LSM4","description":"Sm-like protein LSM4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16419650","identifier":"Q8VYI0","identifierLink":"https://www.uniprot.org/uniprotkb/Q8VYI0/entry","name":"LSM8","description":"Sm-like protein LSM8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR15588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4431531","identifier":"Q9M1Z3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9M1Z3/entry","name":"LSM6A","description":"Sm-like protein LSM6A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4433669","identifier":"Q9SI54","identifierLink":"https://www.uniprot.org/uniprotkb/Q9SI54/entry","name":"LSM7","description":"Sm-like protein LSM7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9347247","identifier":"Q9LMN4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9LMN4/entry","name":"LSM3A","description":"Sm-like protein LSM3A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR13110","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9347308","identifier":"Q1H595","identifierLink":"https://www.uniprot.org/uniprotkb/Q1H595/entry","name":"LSM2","description":"Sm-like protein LSM2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Arabidopsis thaliana; 3702","xrefs":[{"identifier":"PTHR13829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1311","complexName":"SLBP1-SLIP1 complex","organismName":"Xenopus laevis; 8355","description":"As part of the histone translation initiation machinery SLBP-SLIP1 complex binds the 3-prime-stem-loop structure of histone mRNA (hmRNA), facilitates its translation initiation and may also be involved in its processing and nuclear export. \r\n\r\nRemodels the mRNA ribonucleoprotein complexes (RNPs) from nuclear to cytoplasmic specificity. mif4gd-b subunit interacts with the eIF4F complex, the cytoplasmic cap-binding complex that binds the 5-prime histone mRNA cap. eIF4F complex binding facilitates the circularisation of hmRNA that is required for its translation. \r\n\r\nActs exclusively during G1/S transition when histones are in greatest demand. Both the complex and hmRNA are degraded at the end of S phase when Thr-80 and Thr-81 of slbp1 are phosphorylated (as shown in human). Translation of histones during other cell phases cause defects and can be toxic to the cell.","predictedComplex":false,"interactors":[{"ac":"EBI-16419970","identifier":"Q801N6","identifierLink":"https://www.uniprot.org/uniprotkb/Q801N6/entry","name":"mif4gd-b","description":"MIF4G domain-containing protein B","stochiometry":null,"interactorType":"protein","organismName":"Xenopus laevis; 8355","xrefs":[{"identifier":"PTHR23254","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2696430","identifier":"P79943","identifierLink":"https://www.uniprot.org/uniprotkb/P79943/entry","name":"slbp1","description":"Histone RNA hairpin-binding protein","stochiometry":null,"interactorType":"protein","organismName":"Xenopus laevis; 8355","xrefs":[{"identifier":"PTHR17408","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1312","complexName":"SLBP-SLIP1 complex","organismName":"Mus musculus; 10090","description":"As part of the histone translation initiation machinery SLBP-SLIP1 complex binds the 3-prime-stem-loop structure of histone mRNA (hmRNA), facilitates its translation initiation and may also be involved in its processing and nuclear export. \r\n\r\nRemodels the mRNA ribonucleoprotein complexes (RNPs) from nuclear to cytoplasmic specificity. Mif4gd subunit interacts with Eif4g1 (Q6NZJ6) and Eif4g2 (Q62448), components of eIF4F complex, the cytoplasmic cap-binding complex that binds the 5-prime histone mRNA cap. Eif4g1/2 binding facilitates the circularisation of hmRNA that is required for its translation. \r\n\r\nActs exclusively during G1/S transition when histones are in greatest demand. Both the complex and hmRNA are degraded at the end of S phase when Thr-61 and Thr-62 of Slbp are phosphorylated. Translation of histones during other cell phases cause defects and can be toxic to the cell.","predictedComplex":false,"interactors":[{"ac":"EBI-11600284","identifier":"Q3UBZ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q3UBZ5/entry","name":"Mif4gd","description":"MIF4G domain-containing protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR23254","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7770423","identifier":"P97440","identifierLink":"https://www.uniprot.org/uniprotkb/P97440/entry","name":"Slbp","description":"Histone RNA hairpin-binding protein","stochiometry":null,"interactorType":"protein","organismName":"Mus musculus; 10090","xrefs":[{"identifier":"PTHR17408","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1313","complexName":"SLBP-SLIP1 complex","organismName":"Homo sapiens; 9606","description":"As part of the histone translation initiation machinery SLBP-SLIP1 complex binds the 3-prime-stem-loop structure of histone mRNA (hmRNA), facilitates its translation initiation and may also be involved in its processing and nuclear export. \r\n\r\nRemodels the mRNA ribonucleoprotein complexes (RNPs) from nuclear to cytoplasmic specificity. MIF4GD subunit interacts with EIF4G1 (Q04637) and EIF4G2 (P78344), components of eIF4F complex, the cytoplasmic cap-binding complex that binds the 5-prime histone mRNA cap. EIF4G1/2 binding facilitates the circularisation of hmRNA that is required for its translation. \r\n\r\nActs exclusively during G1/S transition when histones are in greatest demand. Both, the complex and hmRNA are degraded at the end of S phase when Thr-61 and Thr-62 of SLBP are phosphorylated. Translation of histones during other cell phases cause defects and can be toxic to the cell.","predictedComplex":false,"interactors":[{"ac":"EBI-2696402","identifier":"Q14493","identifierLink":"https://www.uniprot.org/uniprotkb/Q14493/entry","name":"SLBP","description":"Histone RNA hairpin-binding protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR17408","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373498","identifier":"A9UHW6","identifierLink":"https://www.uniprot.org/uniprotkb/A9UHW6/entry","name":"MIF4GD","description":"MIF4G domain-containing protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23254","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1314","complexName":"bI4 intron splicing factor complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Self-splicing ribozymal RNA Group I intron splicing factor for mitochondrial introns. A guanosine cofactor docks onto an active G-binding site and hydrolyses the phosphodiester bond at the splice site located in P1, resulting in a free hydroxyl group at the upstream exon and the guanosine cofactor being attached to the 5-prime end of the intron. Then the terminal guanosine of the intron occupies the G-binding site to organize the second ester-transfer reaction leading to the ligation of the adjacent upstream and downstream exons and release of the catalytic intron.","predictedComplex":false,"interactors":[{"ac":"EBI-16420196","identifier":null,"identifierLink":null,"name":"bi4_intron_yeast_mrna","description":"bI4 intron RNA","stochiometry":null,"interactorType":"messenger rna","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[]},{"ac":"EBI-16420207","identifier":"P03879","identifierLink":"https://www.uniprot.org/uniprotkb/P03879/entry","name":"BI4","description":"Intron-encoded RNA maturase bI4","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR19271","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-18753","identifier":"P11325","identifierLink":"https://www.uniprot.org/uniprotkb/P11325/entry","name":"NAM2","description":"Leucine--tRNA ligase, mitochondrial","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR43740","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1315","complexName":"Nonsense-mediated decay complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Recognizes and elicits the rapid degradation of mRNAs that prematurely terminate translation and also regulates the expression of specific genes by degrading natural mRNAs. Nonsence-mediated decay (NMD) is triggered by the messenger ribonucleoprotein (mRNP) context surrounding the translation termination event. NMD targets can be recognized as targets due to the lack of factors bound downstream from the termination codon. A ribosome terminating translation at a termination codon substantially upstream from the poly(A) tail terminates translation inefficiently. NMD may occur because the PAB1 (P04147) or other factor bound to the poly(A) tail is not in close enough proximity to the terminating ribosome to enable interaction of the PAB1 with SUP35 (P05453), which is bound to the terminating ribosome and thus establishes the correct mRNP context for a normal translation termination event. In the absence of correct translation termination, the nonsense-mediated decay complex interacts with the translation release factor ERF1-ERF3 complex (CPX-435), resulting in an aberrant translation termination event and NMD activation. NMD activation leads to the decapping of the mRNA by the decapping complex, DCP1-DCP2 (CPX-1628), followed by 5-prime to 3-prime degradation of the mRNA by the exoribonuclease XRN1 (P22147).","predictedComplex":false,"interactors":[{"ac":"EBI-11831","identifier":"P30771","identifierLink":"https://www.uniprot.org/uniprotkb/P30771/entry","name":"NAM7","description":"ATP-dependent helicase NAM7","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10887","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12071","identifier":"P38798","identifierLink":"https://www.uniprot.org/uniprotkb/P38798/entry","name":"NMD2","description":"Nonsense-mediated mRNA decay protein 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12839","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-20117","identifier":"P48412","identifierLink":"https://www.uniprot.org/uniprotkb/P48412/entry","name":"UPF3","description":"Nonsense-mediated mRNA decay protein 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13112","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1316","complexName":"NRD1 snoRNA termination complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"ATP-dependent 5-prime->3-prime DNA/RNA helicase complex required for transcription termination at genes encoding snRNAs and snoRNAs30 and at cryptic unstable transcripts, which are an important class of transcription units that code for ncRNA. May also include some mRNAs as substrates. NRD1 and NAB3 recognize and bind to specific motifs on the nascent RNA (GUAA/G and UCUUG respectively)  NRD1 additionally interacts with phosphoryated Ser-5 of the C-terminal domain of the largest subunit of RNAPII  (CPX-2662). This positions SEN1 onto the nascent RNA in close proximity to RNAPII and  the complex translocates along the RNA causing dismantling of the elongation complex (ternary complexes composed of the transcribing RNA polymerase, the DNA template and the nascent RNA) in a reaction that requires the action of the helicase domain of SEN1.","predictedComplex":false,"interactors":[{"ac":"EBI-11776","identifier":"P38996","identifierLink":"https://www.uniprot.org/uniprotkb/P38996/entry","name":"NAB3","description":"Nuclear polyadenylated RNA-binding protein 3","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13968","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-12228","identifier":"P53617","identifierLink":"https://www.uniprot.org/uniprotkb/P53617/entry","name":"NRD1","description":"Protein NRD1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR23189","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16945","identifier":"Q00416","identifierLink":"https://www.uniprot.org/uniprotkb/Q00416/entry","name":"SEN1","description":"Helicase SEN1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10887","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1317","complexName":"WHI2-PSR1 phosphatase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Protein phosphatase complex required for full activation of the general stress response, possibly through the dephosphorylation of MSN2 (P33748). MSN2 is a transcription factor which binds to cis-acting STREs (stress response elements) in the promoter regions of many stress-responsive genes, and activates their transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-20530","identifier":"P12611","identifierLink":"https://www.uniprot.org/uniprotkb/P12611/entry","name":"WHI2","description":"Growth regulation protein","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13384","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-31129","identifier":"Q07800","identifierLink":"https://www.uniprot.org/uniprotkb/Q07800/entry","name":"PSR1","description":"Phosphatase PSR1","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1318","complexName":"WHI2-PSR2 phosphatase complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Protein phosphatase complex required for full activation of the general stress response, possibly through the dephosphorylation of MSN2 (P33748). MSN2 is a transcription factor which binds to cis-acting STREs (stress response elements) in the promoter regions of many stress-responsive genes, and activate their transcription.","predictedComplex":false,"interactors":[{"ac":"EBI-20530","identifier":"P12611","identifierLink":"https://www.uniprot.org/uniprotkb/P12611/entry","name":"WHI2","description":"Growth regulation protein","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR13384","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-32049","identifier":"Q07949","identifierLink":"https://www.uniprot.org/uniprotkb/Q07949/entry","name":"PSR2","description":"Probable phosphatase PSR2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR12210","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-1319","complexName":"PSTB lipid transfer acceptor membrane complex","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","description":"Lipid transfer complex that is responsible for interorganelle transport of phospholipids, specifically for the non-vesicular transport of phospholipids such as phosphatidylserine from the endoplasmic reticulum to the endosome. Resides in the acceptor (endosomal) membrane and binds to specific lipids on the donor membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-14018","identifier":"P53037","identifierLink":"https://www.uniprot.org/uniprotkb/P53037/entry","name":"PSD2","description":"Phosphatidylserine decarboxylase proenzyme 2","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR10067","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2076838","identifier":"P53844","identifierLink":"https://www.uniprot.org/uniprotkb/P53844/entry","name":"PDR17","description":"Phosphatidylinositol transfer protein PDR17","stochiometry":null,"interactorType":"protein","organismName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c); 559292","xrefs":[{"identifier":"PTHR45824","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26385","complexName":"Dynein-1 complex, variant 16","organismName":"Homo sapiens; 9606","description":"Multi-protein molecular motor. Dynein-1 is one of three major classes of dynein, which share a conserved motor domain that couples ATP hydrolysis with conformational changes to power intracellular retrograde movement of cargoes including vesicles and organelles along microtubules within the cytoplasm. Depletion of DYNC1LI1 present in this complex is thought to reduce dynein-1 binding to spindle assembly checkpoint proteins which ensure correct orientation of sister chromatids needed for the proper segregation during anaphase.\r\n\r\nMutations in DYNC1H1 have been implicated in neurological disorders including an axonal form of Charcot-Marie-Tooth disease.","predictedComplex":false,"interactors":[{"ac":"EBI-2556107","identifier":"Q9Y6G9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y6G9/entry","name":"DYNC1LI1","description":"Cytoplasmic dynein 1 light intermediate chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12688","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356015","identifier":"Q14204","identifierLink":"https://www.uniprot.org/uniprotkb/Q14204/entry","name":"DYNC1H1","description":"Cytoplasmic dynein 1 heavy chain 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10676","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372128","identifier":"Q9NP97","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NP97/entry","name":"DYNLRB1","description":"Dynein light chain roadblock-type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10779","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742371","identifier":"Q96FJ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q96FJ2/entry","name":"DYNLL2","description":"Dynein light chain 2, cytoplasmic","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11886","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-742998","identifier":"Q13409","identifierLink":"https://www.uniprot.org/uniprotkb/Q13409/entry","name":"DYNC1I2","description":"Cytoplasmic dynein 1 intermediate chain 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12442","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-743027","identifier":"P51808","identifierLink":"https://www.uniprot.org/uniprotkb/P51808/entry","name":"DYNLT3","description":"Dynein light chain Tctex-type 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21255","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26386","complexName":"F-actin capping protein complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Caps the barbed end of the actin filament thereby blocking the exchange of subunits at these ends. The complex is an essential component for the reconstitution of movement powered by actin polymerization and is important for actin assembly and cell motility.","predictedComplex":false,"interactors":[{"ac":"EBI-61219249","identifier":"Q9HGP5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HGP5/entry","name":"acp2","description":"F-actin-capping protein subunit beta","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-697254","identifier":"Q10434","identifierLink":"https://www.uniprot.org/uniprotkb/Q10434/entry","name":"acp1","description":"F-actin-capping protein subunit alpha","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10653","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26387","complexName":"Dynactin complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Recruited to autoinhibited dynein, a retrograde microtubule motor complex to  activate the processive, unidirectional movement of dynein. Required for intracellular transport by dynein by localizing cytoplasmic dynein to its proper intracellular cargo and modulating dynein motor activity. Dynactin increases the run length of single dynein motors, but does not alter the directionality of dynein movement.","predictedComplex":false,"interactors":[{"ac":"EBI-1556587","identifier":"O42667","identifierLink":"https://www.uniprot.org/uniprotkb/O42667/entry","name":"ssm4","description":"Microtubule-associated protein ssm4","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR18916","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61220550","identifier":"O94630","identifierLink":"https://www.uniprot.org/uniprotkb/O94630/entry","name":"arp1","description":"Centractin","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61220565","identifier":"Q9USP4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9USP4/entry","name":"mug1","description":"Meiotically up-regulated gene 1 protein","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61220579","identifier":"O13715","identifierLink":"https://www.uniprot.org/uniprotkb/O13715/entry","name":"mug5","description":"Meiotically up-regulated gene 5 protein","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]}]},{"complexAC":"CPX-26388","complexName":"DAXX-ATRX histone H3-specific chaperone complex","organismName":"Homo sapiens; 9606","description":"ATP-dependent chromatin remodeling complex which promotes the replication-independent incorporation of H3.3 into telomeric, pericentromeric, and other repetitive DNA regions. DAXX acts as the targeting subunit recognising a combination of the methylation states of H3K9 and H3K4 and associating with CBX5.","predictedComplex":false,"interactors":[{"ac":"EBI-396461","identifier":"P46100","identifierLink":"https://www.uniprot.org/uniprotkb/P46100/entry","name":"ATRX","description":"Transcriptional regulator ATRX","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46357","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-77321","identifier":"Q9UER7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UER7/entry","name":"DAXX","description":"Death domain-associated protein 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12766","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26389","complexName":"IZUMO1-JUNO fertilization complex","organismName":"Homo sapiens; 9606","description":"Complex formation provides the first known physical link between egg (IZUMO1R/JUNO) and sperm (IZUMO1) as part of the fertilization process, initiating recognition and adhesion of the two gametes and possibly triggering their fusion.","predictedComplex":false,"interactors":[{"ac":"EBI-16357190","identifier":"Q8IYV9","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IYV9/entry","name":"IZUMO1","description":"Izumo sperm-egg fusion protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR35540","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16357235","identifier":"A6ND01","identifierLink":"https://www.uniprot.org/uniprotkb/A6ND01/entry","name":"IZUMO1R","description":"Sperm-egg fusion protein Juno","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10517","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26390","complexName":"Dynactin complex","organismName":"Sus scrofa; 9823","description":"Recruited to autoinhibited dynein, a retrograde microtubule motor complex, by a coiled-coil-containing adaptor (Bicaudal-D or Hook family) protein to form the tripartite dynein-dynactin-adaptor assembly which activates the processive, unidirectional movement of dynein. Dynactin and dynein contribute to a number of motility associated events including endomembrane movement, nuclear envelope breakdown, and mitotic spindle assembly.","predictedComplex":false,"interactors":[{"ac":"EBI-12513903","identifier":"Q6QAQ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q6QAQ1/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Sus scrofa; 9823","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61223560","identifier":"F2Z5G5","identifierLink":"https://www.uniprot.org/uniprotkb/F2Z5G5/entry","name":"ACTR1A","description":"Alpha-centractin","stochiometry":"minValue: 8, maxValue: 8","interactorType":"protein","organismName":"Sus scrofa; 9823","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61223636","identifier":"CPX-26391","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-26391","name":"F-actin capping protein complex, CAPZA1 variant","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Sus scrofa; 9823","xrefs":[]},{"ac":"EBI-61223731","identifier":"I3LHK5","identifierLink":"https://www.uniprot.org/uniprotkb/I3LHK5/entry","name":"ACTR10","description":"Actin-related protein 10","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Sus scrofa; 9823","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61223800","identifier":"A0A4X1TB62","identifierLink":"https://www.uniprot.org/uniprotkb/A0A4X1TB62/entry","name":"DCTN4","description":"Dynactin subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Sus scrofa; 9823","xrefs":[{"identifier":"PTHR13034","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61223844","identifier":"A0A286ZK88","identifierLink":"https://www.uniprot.org/uniprotkb/A0A286ZK88/entry","name":"DCTN5","description":"Dynactin subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Sus scrofa; 9823","xrefs":[{"identifier":"PTHR46126","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61223911","identifier":"D0G6S1","identifierLink":"https://www.uniprot.org/uniprotkb/D0G6S1/entry","name":"DCTN6","description":"Dynactin subunit 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Sus scrofa; 9823","xrefs":[{"identifier":"PTHR13072","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61223994","identifier":"A0A5G2QD80","identifierLink":"https://www.uniprot.org/uniprotkb/A0A5G2QD80/entry","name":"DCTN2","description":"Dynactin subunit 2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Sus scrofa; 9823","xrefs":[{"identifier":"PTHR15346","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61224087","identifier":"A0A287B8J2","identifierLink":"https://www.uniprot.org/uniprotkb/A0A287B8J2/entry","name":"DCTN1","description":"Dynactin subunit 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Sus scrofa; 9823","xrefs":[{"identifier":"PTHR18916","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61224147","identifier":"F1SEC0","identifierLink":"https://www.uniprot.org/uniprotkb/F1SEC0/entry","name":"DCTN3","description":"Dynactin subunit 3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Sus scrofa; 9823","xrefs":[{"identifier":"PTHR28360","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26391","complexName":"F-actin capping protein complex, CAPZA1 variant","organismName":"Sus scrofa; 9823","description":"Caps the barbed end of the actin filament  in a Ca(2+)-independent manner thereby blocking the exchange of subunits at these ends. The complex is an essential component for the reconstitution of movement powered by actin polymerization and is important for actin assembly and cell motility.","predictedComplex":false,"interactors":[{"ac":"EBI-61223644","identifier":"A0PFK7","identifierLink":"https://www.uniprot.org/uniprotkb/A0PFK7/entry","name":"CAPZB","description":"F-actin-capping protein subunit beta","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Sus scrofa; 9823","xrefs":[{"identifier":"PTHR10619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61223686","identifier":"A0PFK5","identifierLink":"https://www.uniprot.org/uniprotkb/A0PFK5/entry","name":"CAPZA1","description":"F-actin-capping protein subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Sus scrofa; 9823","xrefs":[{"identifier":"PTHR10653","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-6441","complexName":"Integrator core complex","organismName":"Homo sapiens; 9606","description":"Plays a role the regulation of gene expression by targeting RNA polymerase II (CPX-2387/CPX-7481) to cause the premature transcription termination of coding and non-coding RNAs,  inducing promoter-proximal termination at promoters and attenuating nonproductive transcription at enhancers.. The Integrator positions its cleavage module (INTS4, INTS9 and INTS11) at the RNA exit tunnel of RNA polymerase II ensuring that the exiting nascent RNA moves directly into the endonuclease active site for cleavage.","predictedComplex":false,"interactors":[{"ac":"EBI-1049156","identifier":"Q96CB8","identifierLink":"https://www.uniprot.org/uniprotkb/Q96CB8/entry","name":"INTS12","description":"Integrator complex subunit 12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13415","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11276282","identifier":"Q9NVH2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NVH2/entry","name":"INTS7","description":"Integrator complex subunit 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13322","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1381827","identifier":"Q9UL03","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UL03/entry","name":"INTS6","description":"Integrator complex subunit 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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The Integrator positions its cleavage module (INTS4, INTS9 and INTS11) at the RNA exit tunnel of RNA polymerase II ensuring that the exiting nascent RNA moves directly into the endonuclease active site for cleavage. INTS2, INTS5, INTS6 and INTS8 bind to and position PP2A to dephosphorylate the C-terminal domain of RNA polymerase II subunit POLR2A (P24928) at serine-2, -5, and -7 preventing the release of paused Pol II and limiting transcriptional activation.","predictedComplex":false,"interactors":[{"ac":"EBI-1049156","identifier":"Q96CB8","identifierLink":"https://www.uniprot.org/uniprotkb/Q96CB8/entry","name":"INTS12","description":"Integrator complex subunit 12","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13415","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11276282","identifier":"Q9NVH2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NVH2/entry","name":"INTS7","description":"Integrator complex subunit 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13322","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1381827","identifier":"Q9UL03","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UL03/entry","name":"INTS6","description":"Integrator complex subunit 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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9606","xrefs":[{"identifier":"PTHR16055","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5663129","identifier":"Q96HW7","identifierLink":"https://www.uniprot.org/uniprotkb/Q96HW7/entry","name":"INTS4","description":"Integrator complex subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20938","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712311","identifier":"P67775","identifierLink":"https://www.uniprot.org/uniprotkb/P67775/entry","name":"PPP2CA","description":"Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45619","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-718667","identifier":"Q96N11","identifierLink":"https://www.uniprot.org/uniprotkb/Q96N11/entry","name":"INTS15","description":"Integrator complex subunit 15","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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9606","xrefs":[{"identifier":"PTHR11203","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7600112","identifier":"Q6P9B9","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P9B9/entry","name":"INTS5","description":"Integrator complex subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31697","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-8471507","identifier":"Q9H0H0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9H0H0/entry","name":"INTS2","description":"Integrator complex subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28608","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26395","complexName":"SNARE complex STX1A-SNAP25-VAMP2","organismName":"Homo sapiens; 9606","description":"SNARE complex required for fusion of synaptic vesicles enabling Ca2+-dependent neurotransmitter release at presynaptic terminals, specifically regulation of monoamine release. Mediates membrane fusion through the spontaneous assembly of four complementary SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) motifs. SNAREs bind to each other in-trans, that is, with SNAREs anchored in each apposed tethered membrane. The assembly process leads to a tight connection between the fusing membranes and initiates membrane fusion. STX1A and SNAP25 are anchored to the presynaptic membrane, whereas VAMP2 is located on the synaptic vesicle membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-520113","identifier":"P63027","identifierLink":"https://www.uniprot.org/uniprotkb/P63027/entry","name":"VAMP2","description":"Vesicle-associated membrane protein 2","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-524785","identifier":"P60880","identifierLink":"https://www.uniprot.org/uniprotkb/P60880/entry","name":"SNAP25","description":"Synaptosomal-associated protein 25","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712466","identifier":"Q16623","identifierLink":"https://www.uniprot.org/uniprotkb/Q16623/entry","name":"STX1A","description":"Syntaxin-1A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26396","complexName":"PtdIns(3,5)P2 regulatory complex","organismName":"Homo sapiens; 9606","description":"Regulates both the synthesis, from phosphatidylinositol 3-phosphate (PI3P), and turnover of the low abundance, signaling lipid phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2; CHEBI:16851). Primarily localized at endosomal membranes with PtdIns(3,5)P2 regulating the activity of ion channels. FIG4 is active as both a lipid phosphatase and also as a serine phosphatase that acts on PIKFYVE to increase its lipid kinase activity. PIKFYVE autophosphorylation represses its lipid kinase activity and stimulates FIG4 lipid phosphatase activity.","predictedComplex":false,"interactors":[{"ac":"EBI-2107455","identifier":"Q08AM6","identifierLink":"https://www.uniprot.org/uniprotkb/Q08AM6/entry","name":"VAC14","description":"Protein VAC14 homolog","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR16023","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4290773","identifier":"Q92562","identifierLink":"https://www.uniprot.org/uniprotkb/Q92562/entry","name":"FIG4","description":"Polyphosphoinositide phosphatase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45738","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6138650","identifier":"Q9Y2I7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2I7/entry","name":"PIKFYVE","description":"1-phosphatidylinositol 3-phosphate 5-kinase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR46715","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26397","complexName":"SNARE complex STX1B-SNAP25-VAMP2","organismName":"Homo sapiens; 9606","description":"SNARE complex required for fusion of synaptic vesicles enabling Ca2+-dependent neurotransmitter release at presynaptic terminals, specifically regulation of  basal extracellular dopamine levels. Mediates membrane fusion through the spontaneous assembly of four complementary SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) motifs. SNAREs bind to each other in-trans, that is, with SNAREs anchored in each apposed tethered membrane. The assembly process leads to a tight connection between the fusing membranes and initiates membrane fusion. STX1B and SNAP25 are anchored to the presynaptic membrane, whereas VAMP2 is located on the synaptic vesicle membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-520113","identifier":"P63027","identifierLink":"https://www.uniprot.org/uniprotkb/P63027/entry","name":"VAMP2","description":"Vesicle-associated membrane protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-524785","identifier":"P60880","identifierLink":"https://www.uniprot.org/uniprotkb/P60880/entry","name":"SNAP25","description":"Synaptosomal-associated protein 25","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9071709","identifier":"P61266","identifierLink":"https://www.uniprot.org/uniprotkb/P61266/entry","name":"STX1B","description":"Syntaxin-1B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26398","complexName":"SNARE complex STX1A-SNAP25-VAMP1","organismName":"Homo sapiens; 9606","description":"SNARE complex required for fusion of synaptic vesicles enabling Ca2+-dependent neurotransmitter release at presynaptic terminals, specifically regulation of monoamine release. 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STX1A and SNAP25 are anchored to the presynaptic membrane, whereas VAMP1 is located on the synaptic vesicle membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-10201335","identifier":"P23763","identifierLink":"https://www.uniprot.org/uniprotkb/P23763/entry","name":"VAMP1","description":"Vesicle-associated membrane protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-524785","identifier":"P60880","identifierLink":"https://www.uniprot.org/uniprotkb/P60880/entry","name":"SNAP25","description":"Synaptosomal-associated protein 25","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712466","identifier":"Q16623","identifierLink":"https://www.uniprot.org/uniprotkb/Q16623/entry","name":"STX1A","description":"Syntaxin-1A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26399","complexName":"SNARE complex STX1B-SNAP25-VAMP1","organismName":"Homo sapiens; 9606","description":"SNARE complex required for fusion of synaptic vesicles enabling Ca2+-dependent neurotransmitter release at presynaptic terminals, specifically regulation of  basal extracellular dopamine levels. 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STX1B and SNAP25 are anchored to the presynaptic membrane, whereas VAMP1 is located on the synaptic vesicle membrane.","predictedComplex":false,"interactors":[{"ac":"EBI-10201335","identifier":"P23763","identifierLink":"https://www.uniprot.org/uniprotkb/P23763/entry","name":"VAMP1","description":"Vesicle-associated membrane protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-524785","identifier":"P60880","identifierLink":"https://www.uniprot.org/uniprotkb/P60880/entry","name":"SNAP25","description":"Synaptosomal-associated protein 25","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9071709","identifier":"P61266","identifierLink":"https://www.uniprot.org/uniprotkb/P61266/entry","name":"STX1B","description":"Syntaxin-1B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26400","complexName":"SNARE complex STX17-SNAP47-VAMP7","organismName":"Homo sapiens; 9606","description":"SNARE complex required for the fusion of the double-membraned autophagosome with the single-membraned lysosome during both selective autophagy under non-starvation conditions and starvation-induced autophagy. Mediates membrane fusion through the spontaneous assembly of four complementary SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) motifs. SNAREs bind to each other in-trans, that is, with SNAREs anchored in each apposed tethered membrane. The assembly process leads to a tight connection between the fusing membranes and initiates membrane fusion..","predictedComplex":false,"interactors":[{"ac":"EBI-10244848","identifier":"Q5SQN1","identifierLink":"https://www.uniprot.org/uniprotkb/Q5SQN1/entry","name":"SNAP47","description":"Synaptosomal-associated protein 47","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1052205","identifier":"P51809","identifierLink":"https://www.uniprot.org/uniprotkb/P51809/entry","name":"VAMP7","description":"Vesicle-associated membrane protein 7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21136","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2797775","identifier":"P56962","identifierLink":"https://www.uniprot.org/uniprotkb/P56962/entry","name":"STX17","description":"Syntaxin-17","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26401","complexName":"SNARE complex STX17-SNAP47-VAMP8","organismName":"Homo sapiens; 9606","description":"SNARE complex required for the fusion of the double-membraned autophagosome with the single-membraned lysosome during both selective autophagy under non-starvation conditions and starvation-induced autophagy. Mediates membrane fusion through the spontaneous assembly of four complementary SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) motifs. SNAREs bind to each other in-trans, that is, with SNAREs anchored in each apposed tethered membrane. The assembly process leads to a tight connection between the fusing membranes and initiates membrane fusion..","predictedComplex":false,"interactors":[{"ac":"EBI-10244848","identifier":"Q5SQN1","identifierLink":"https://www.uniprot.org/uniprotkb/Q5SQN1/entry","name":"SNAP47","description":"Synaptosomal-associated protein 47","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19305","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2797775","identifier":"P56962","identifierLink":"https://www.uniprot.org/uniprotkb/P56962/entry","name":"STX17","description":"Syntaxin-17","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19957","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-727028","identifier":"Q9BV40","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BV40/entry","name":"VAMP8","description":"Vesicle-associated membrane protein 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26402","complexName":"GABA-A receptor, alpha1-alpha2-beta2-gamma2","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. 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GABA-A receptors are also found in liver, smooth airways muscle and immune cells.","predictedComplex":false,"interactors":[{"ac":"EBI-2685723","identifier":"P47869","identifierLink":"https://www.uniprot.org/uniprotkb/P47869/entry","name":"GABRA2","description":"Gamma-aminobutyric acid receptor subunit alpha-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6258308","identifier":"P14867","identifierLink":"https://www.uniprot.org/uniprotkb/P14867/entry","name":"GABRA1","description":"Gamma-aminobutyric acid receptor subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6949072","identifier":"P47870","identifierLink":"https://www.uniprot.org/uniprotkb/P47870/entry","name":"GABRB2","description":"Gamma-aminobutyric acid receptor subunit beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008430","identifier":"P18507","identifierLink":"https://www.uniprot.org/uniprotkb/P18507/entry","name":"GABRG2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26403","complexName":"GABA-A receptor, alpha1-alpha2-beta1-beta2-gamma2","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. 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GABA-A receptors are also found in liver, smooth airways muscle and immune cells.","predictedComplex":false,"interactors":[{"ac":"EBI-2685723","identifier":"P47869","identifierLink":"https://www.uniprot.org/uniprotkb/P47869/entry","name":"GABRA2","description":"Gamma-aminobutyric acid receptor subunit alpha-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3914848","identifier":"P18505","identifierLink":"https://www.uniprot.org/uniprotkb/P18505/entry","name":"GABRB1","description":"Gamma-aminobutyric acid receptor subunit beta-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6258308","identifier":"P14867","identifierLink":"https://www.uniprot.org/uniprotkb/P14867/entry","name":"GABRA1","description":"Gamma-aminobutyric acid receptor subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6949072","identifier":"P47870","identifierLink":"https://www.uniprot.org/uniprotkb/P47870/entry","name":"GABRB2","description":"Gamma-aminobutyric acid receptor subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008430","identifier":"P18507","identifierLink":"https://www.uniprot.org/uniprotkb/P18507/entry","name":"GABRG2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26404","complexName":"GABA-A receptor, alpha1-alpha2-beta2-beta3-gamma2","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. 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GABA-A receptors are also found in liver, smooth airways muscle and immune cells.","predictedComplex":false,"interactors":[{"ac":"EBI-2685723","identifier":"P47869","identifierLink":"https://www.uniprot.org/uniprotkb/P47869/entry","name":"GABRA2","description":"Gamma-aminobutyric acid receptor subunit alpha-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6258252","identifier":"P28472","identifierLink":"https://www.uniprot.org/uniprotkb/P28472/entry","name":"GABRB3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6258308","identifier":"P14867","identifierLink":"https://www.uniprot.org/uniprotkb/P14867/entry","name":"GABRA1","description":"Gamma-aminobutyric acid receptor subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6949072","identifier":"P47870","identifierLink":"https://www.uniprot.org/uniprotkb/P47870/entry","name":"GABRB2","description":"Gamma-aminobutyric acid receptor subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008430","identifier":"P18507","identifierLink":"https://www.uniprot.org/uniprotkb/P18507/entry","name":"GABRG2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26405","complexName":"GABA-A receptor, alpha1-alpha3-beta2-gamma2","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. 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GABA-A receptors are also found in liver, smooth airways muscle and immune cells.","predictedComplex":false,"interactors":[{"ac":"EBI-1763805","identifier":"P34903","identifierLink":"https://www.uniprot.org/uniprotkb/P34903/entry","name":"GABRA3","description":"Gamma-aminobutyric acid receptor subunit alpha-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6258308","identifier":"P14867","identifierLink":"https://www.uniprot.org/uniprotkb/P14867/entry","name":"GABRA1","description":"Gamma-aminobutyric acid receptor subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6949072","identifier":"P47870","identifierLink":"https://www.uniprot.org/uniprotkb/P47870/entry","name":"GABRB2","description":"Gamma-aminobutyric acid receptor subunit beta-2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008430","identifier":"P18507","identifierLink":"https://www.uniprot.org/uniprotkb/P18507/entry","name":"GABRG2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26406","complexName":"SPT4-SPT5 transcription elongation factor complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"An essential RNA polymerase II elongation factor which functions in the control of RNAP II processivity. Mediates both activation and inhibition of transcription elongation, and plays a role in pre-mRNA processing.","predictedComplex":false,"interactors":[{"ac":"EBI-61252586","identifier":"O13936","identifierLink":"https://www.uniprot.org/uniprotkb/O13936/entry","name":"spt5","description":"Transcription elongation factor spt5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11125","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61252655","identifier":"Q9P7K8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P7K8/entry","name":"spt4","description":"Transcription elongation factor spt4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12882","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26407","complexName":"GABA-A receptor, alpha1-beta2-beta3-gamma2","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. 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GABA-A receptors are also found in liver, smooth airways muscle and immune cells.","predictedComplex":false,"interactors":[{"ac":"EBI-6258252","identifier":"P28472","identifierLink":"https://www.uniprot.org/uniprotkb/P28472/entry","name":"GABRB3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6258308","identifier":"P14867","identifierLink":"https://www.uniprot.org/uniprotkb/P14867/entry","name":"GABRA1","description":"Gamma-aminobutyric acid receptor subunit alpha-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6949072","identifier":"P47870","identifierLink":"https://www.uniprot.org/uniprotkb/P47870/entry","name":"GABRB2","description":"Gamma-aminobutyric acid receptor subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008430","identifier":"P18507","identifierLink":"https://www.uniprot.org/uniprotkb/P18507/entry","name":"GABRG2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26408","complexName":"GABA-A receptor, alpha1-alpha2-beta3-gamma2","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets. GABA-A receptors are also found in liver, smooth airways muscle and immune cells.","predictedComplex":false,"interactors":[{"ac":"EBI-2685723","identifier":"P47869","identifierLink":"https://www.uniprot.org/uniprotkb/P47869/entry","name":"GABRA2","description":"Gamma-aminobutyric acid receptor subunit alpha-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6258252","identifier":"P28472","identifierLink":"https://www.uniprot.org/uniprotkb/P28472/entry","name":"GABRB3","description":"Gamma-aminobutyric acid receptor subunit beta-3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6258308","identifier":"P14867","identifierLink":"https://www.uniprot.org/uniprotkb/P14867/entry","name":"GABRA1","description":"Gamma-aminobutyric acid receptor subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008430","identifier":"P18507","identifierLink":"https://www.uniprot.org/uniprotkb/P18507/entry","name":"GABRG2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26409","complexName":"GABA-A receptor, alpha1-beta1-beta2-gamma2","organismName":"Homo sapiens; 9606","description":"Ligand-gated chloride channel which acts as the main driver of fast inhibitory neurotransmission in the nervous system. GABA (CHEBI:16865), the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening a chloride ion-selective pore.\r\n\r\nGABA-A receptors assemble in specific combinations of receptor subunits from a pool of nineteen in a cell-type specific manner, giving rise to receptors with distinct distributions and functions in both physiological and disease states. \r\n\r\nTheir many allosteric sites, which bind compounds with anticonvulsant, anti-anxiety, analgesic, sedative and anaesthetic properties make GABA-A receptors attractive drug targets. GABA-A receptors are also found in liver, smooth airways muscle and immune cells.","predictedComplex":false,"interactors":[{"ac":"EBI-3914848","identifier":"P18505","identifierLink":"https://www.uniprot.org/uniprotkb/P18505/entry","name":"GABRB1","description":"Gamma-aminobutyric acid receptor subunit beta-1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6258308","identifier":"P14867","identifierLink":"https://www.uniprot.org/uniprotkb/P14867/entry","name":"GABRA1","description":"Gamma-aminobutyric acid receptor subunit alpha-1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-6949072","identifier":"P47870","identifierLink":"https://www.uniprot.org/uniprotkb/P47870/entry","name":"GABRB2","description":"Gamma-aminobutyric acid receptor subunit beta-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9008430","identifier":"P18507","identifierLink":"https://www.uniprot.org/uniprotkb/P18507/entry","name":"GABRG2","description":"Gamma-aminobutyric acid receptor subunit gamma-2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18945","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26411","complexName":"U6 small nuclear ribonucleoprotein complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Non-coding RNA containing complex, part of the pre-B complex that acts as a chaperone for U6 spliceosomal-RNA. The spliceosome is a highly dynamic structure, assembled by sequential binding and release of the small nuclear RNAs (snRNA) and protein factors which removes intronic sequence from pre-mRNA. U6 is part of the activated spliceosome and is involved in the first trans-estherification step of splicing. After splicing is complete, the spliceosome disassembles and free U6 snRNP forms. It then reassociates with U4 to form U4/U6 snRNP.","predictedComplex":false,"interactors":[{"ac":"EBI-1560482","identifier":"Q9Y7M4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y7M4/entry","name":"lsm3","description":"LSM complex subunit lsm3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13110","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-539326","identifier":"O74483","identifierLink":"https://www.uniprot.org/uniprotkb/O74483/entry","name":"lsm8","description":"LSM2-LSM8 complex subunit lsm8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61254278","identifier":"O14352","identifierLink":"https://www.uniprot.org/uniprotkb/O14352/entry","name":"lsm4","description":"LSM complex subunit lsm4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61254315","identifier":"O42978","identifierLink":"https://www.uniprot.org/uniprotkb/O42978/entry","name":"lsm5","description":"LSM complex subunit lsm5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR20971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61254349","identifier":"Q9UUI1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UUI1/entry","name":"lsm6","description":"LSM complex subunit lsm6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61254385","identifier":"O74499","identifierLink":"https://www.uniprot.org/uniprotkb/O74499/entry","name":"lsm7","description":"LSM complex subunit lsm7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61254428","identifier":"URS000234A4A1_4896","identifierLink":"http://rnacentral.org/rna/URS000234A4A1_4896","name":"small nuclear rna u6","description":"Schizosaccharomyces pombe (fission yeast) small nuclear RNA U6","stochiometry":null,"interactorType":"small nuclear rna","organismName":"Schizosaccharomyces pombe; 4896","xrefs":[]},{"ac":"EBI-61254434","identifier":"O94408","identifierLink":"https://www.uniprot.org/uniprotkb/O94408/entry","name":"lsm2","description":"LSM complex subunit lsm2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61254480","identifier":"Q9USY2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9USY2/entry","name":"prp24","description":"U4/U6 snRNA-associated-splicing factor prp24","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23147","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26412","complexName":"ATR-ATRIP DNA damage-sensing kinase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Master regulator of the DNA damage response controlling a signaling cascade required for the maintenance of genomic integrity. Activated by RPA complex -coated single-stranded DNA at the site of DNA double-strand breaks and stalled replication forks. Appears to control the production of an adequate and balanced pool of deoxyribonucleotides and maintain replication fork stability.","predictedComplex":false,"interactors":[{"ac":"EBI-768555","identifier":"Q02099","identifierLink":"https://www.uniprot.org/uniprotkb/Q02099/entry","name":"rad3","description":"Protein kinase rad3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-768575","identifier":"P36632","identifierLink":"https://www.uniprot.org/uniprotkb/P36632/entry","name":"rad26","description":"DNA repair protein rad26","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]}]},{"complexAC":"CPX-26413","complexName":"CENP-A recruiting complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Ensures the integrity of mitotic spindles by playing a role in the loading of kinetochore factors mis6/CENP-I (P87227) and cnp1/CENP-A (Q9Y812). CENP-A-containing nucleosomes have the ability to bind inner kinetochore proteins, such as cnp3/ CENP-C (Q9USR9) and mis15/CENP-N (Q9C0W0), initiating kinetochore formation.","predictedComplex":false,"interactors":[{"ac":"EBI-1148703","identifier":"O94244","identifierLink":"https://www.uniprot.org/uniprotkb/O94244/entry","name":"mis16","description":"Histone acetyltransferase type B subunit 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR22850","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1148763","identifier":"Q9P802","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P802/entry","name":"mis18","description":"Kinetochore protein mis18","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR16431","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61254955","identifier":"O94682","identifierLink":"https://www.uniprot.org/uniprotkb/O94682/entry","name":"mis20","description":"CENP-A recruiting complex protein mis20","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-61254972","identifier":"O42995","identifierLink":"https://www.uniprot.org/uniprotkb/O42995/entry","name":"mis19","description":"CENP-A recruiting complex protein mis19","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]}]},{"complexAC":"CPX-26415","complexName":"U6 small nuclear ribonucleoprotein complex","organismName":"Homo sapiens; 9606","description":"Non-coding RNA containing complex, part of the pre-B complex that acts as a chaperone for U6 spliceosomal-RNA. The spliceosome executes pre-mRNA splicing through a highly dynamic series of compositional and conformational transitions encompassing assembly, activation, catalysis and disassembly of a highly dynamic structure, involving the binding and release of the small nuclear RNAs (snRNA) and protein factors which remove intronic sequence from pre-mRNA. Spliceosome stages are characterized as E, A, B and remodelling of the pre-catalytic spliceosome (B complex) into the activated spliceosome (Bact complex) and subsequently, the catalytically activated spliceosome (B* complex) to carry out two RNA-catalysed transesterification reactions that lead to intron removal and splicing together of the flanking exon sequences.\r\n\r\nU6 is part of the activated spliceosome and is involved in the first trans-estherification step of splicing. After splicing is complete, the spliceosome disassembles and free U6 snRNP forms. It then reassociates with U4 to form U4/U6 snRNP.\r\n\r\nPRP24 (P49960) functions as a snRNP recycling factor to re-anneal U4 and U6 snRNAs in Saccharomyces cerevisiae (CPX-24). SART3 (Q15020) the PRP24 orthologue in humans, is thought to associate with U6 and U4/U6 snRNP during the recycling phase of the spliceosome cycle but it dissociates during the formation of the U4/U6.U5 tri-complex.","predictedComplex":false,"interactors":[{"ac":"EBI-27124795","identifier":"URS00006767A8_9606","identifierLink":"http://rnacentral.org/rna/URS00006767A8_9606","name":"u6_human_snrna","description":"Homo sapiens U6 spliceosomal RNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small nuclear rna","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-308619","identifier":"Q15020","identifierLink":"https://www.uniprot.org/uniprotkb/Q15020/entry","name":"SART3","description":"Spliceosome associated factor 3, U4/U6 recycling protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15481","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347416","identifier":"Q9Y333","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y333/entry","name":"LSM2","description":"U6 snRNA-associated Sm-like protein LSm2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347779","identifier":"O95777","identifierLink":"https://www.uniprot.org/uniprotkb/O95777/entry","name":"LSM8","description":"U6 snRNA-associated Sm-like protein LSm8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348239","identifier":"P62310","identifierLink":"https://www.uniprot.org/uniprotkb/P62310/entry","name":"LSM3","description":"U6 snRNA-associated Sm-like protein LSm3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13110","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348372","identifier":"Q9UK45","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK45/entry","name":"LSM7","description":"U6 snRNA-associated Sm-like protein LSm7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372521","identifier":"Q9Y4Z0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4Z0/entry","name":"LSM4","description":"U6 snRNA-associated Sm-like protein LSm4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373007","identifier":"Q9Y4Y9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4Y9/entry","name":"LSM5","description":"U6 snRNA-associated Sm-like protein LSm5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373310","identifier":"P62312","identifierLink":"https://www.uniprot.org/uniprotkb/P62312/entry","name":"LSM6","description":"U6 snRNA-associated Sm-like protein LSm6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26416","complexName":"Gamma tubulin ring complex","organismName":"Homo sapiens; 9606","description":"Templates the formation of microtubules, determining the position and direction of microtubule growth from alpha/beta-tubulin dimers that join head-to-tail to form protofilaments.","predictedComplex":false,"interactors":[{"ac":"EBI-1046278","identifier":"Q96CW5","identifierLink":"https://www.uniprot.org/uniprotkb/Q96CW5/entry","name":"TUBGCP3","description":"Gamma-tubulin complex component 3","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19302","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1052544","identifier":"Q9UGJ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UGJ1/entry","name":"TUBGCP4","description":"Gamma-tubulin complex component 4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19302","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1052566","identifier":"Q6NZ67","identifierLink":"https://www.uniprot.org/uniprotkb/Q6NZ67/entry","name":"MZT2B","description":"Mitotic-spindle organizing protein 2B","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28578","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2555061","identifier":"Q96RT8","identifierLink":"https://www.uniprot.org/uniprotkb/Q96RT8/entry","name":"TUBGCP5","description":"Gamma-tubulin complex component 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19302","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2555074","identifier":"Q96RT7","identifierLink":"https://www.uniprot.org/uniprotkb/Q96RT7/entry","name":"TUBGCP6","description":"Gamma-tubulin complex component 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19302","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2558548","identifier":"Q6P582","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P582/entry","name":"MZT2A","description":"Mitotic-spindle organizing protein 2A","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28578","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2637198","identifier":"Q08AG7","identifierLink":"https://www.uniprot.org/uniprotkb/Q08AG7/entry","name":"MZT1","description":"Mitotic-spindle organizing protein 1","stochiometry":null,"interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR28520","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302589","identifier":"P23258","identifierLink":"https://www.uniprot.org/uniprotkb/P23258/entry","name":"TUBG1","description":"Tubulin gamma-1 chain","stochiometry":"minValue: 14, maxValue: 14","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-353944","identifier":"P60709","identifierLink":"https://www.uniprot.org/uniprotkb/P60709/entry","name":"ACTB","description":"Actin, cytoplasmic 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11937","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357881","identifier":"Q9BSJ2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BSJ2/entry","name":"TUBGCP2","description":"Gamma-tubulin complex component 2","stochiometry":"minValue: 5, maxValue: 5","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19302","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26417","complexName":"U4 small nuclear ribonucleoprotein complex","organismName":"Homo sapiens; 9606","description":"Small nuclear RNA (snRNA) containing complex that is involved in mRNA splicing as part of the spliceosome. The spliceosome executes pre-mRNA splicing through a highly dynamic series of compositional and conformational transitions encompassing assembly, activation, catalysis and disassembly of a highly dynamic structure, involving the binding and release of the small nuclear RNAs (snRNA) and protein factors which remove intronic sequence from pre-mRNA. Spliceosome stages are characterized as E, A, B and remodelling of the pre-catalytic spliceosome (B complex) into the activated spliceosome (Bact complex) and subsequently, the catalytically activated spliceosome (B* complex) to carry out two RNA-catalysed transesterification reactions that lead to intron removal and splicing together of the flanking exon sequences.\r\n\r\nU4 snRNP is present only in the pre-B and B complexes. The splicing active site is only formed in the B-act complex, allowing clear differentiation between the B-like and B-act-like complexes. U4 dissociates from the spliceosome during the activation step, but the U4 snRNP is also found in a complex with the U6 snRNP (the U4/6 snRNP complex), an intermediate in the assembly of the spliceosome.  The U4/6 complex is then re-assembled in each cycle. Its function is thought to be to deliver U6 to the spliceosome.","predictedComplex":false,"interactors":[{"ac":"EBI-297993","identifier":"P62316","identifierLink":"https://www.uniprot.org/uniprotkb/P62316/entry","name":"SNRPD2","description":"Small nuclear ribonucleoprotein Sm D2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12777","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348082","identifier":"P62304","identifierLink":"https://www.uniprot.org/uniprotkb/P62304/entry","name":"SNRPE","description":"Small nuclear ribonucleoprotein E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11193","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356900","identifier":"P62306","identifierLink":"https://www.uniprot.org/uniprotkb/P62306/entry","name":"SNRPF","description":"Small nuclear ribonucleoprotein F","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372177","identifier":"P62314","identifierLink":"https://www.uniprot.org/uniprotkb/P62314/entry","name":"SNRPD1","description":"Small nuclear ribonucleoprotein Sm D1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372458","identifier":"P14678","identifierLink":"https://www.uniprot.org/uniprotkb/P14678/entry","name":"SNRPB","description":"Small nuclear ribonucleoprotein-associated proteins B and B'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372789","identifier":"P62318","identifierLink":"https://www.uniprot.org/uniprotkb/P62318/entry","name":"SNRPD3","description":"Small nuclear ribonucleoprotein Sm D3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-4325816","identifier":"URS0000715A86_9606","identifierLink":"http://rnacentral.org/rna/URS0000715A86_9606","name":"u4_human_snrna","description":"Human U4 spliceosomal RNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small nuclear rna","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-624585","identifier":"P62308","identifierLink":"https://www.uniprot.org/uniprotkb/P62308/entry","name":"SNRPG","description":"Small nuclear ribonucleoprotein G","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712228","identifier":"P55769","identifierLink":"https://www.uniprot.org/uniprotkb/P55769/entry","name":"SNU13","description":"NHP2-like protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-718395","identifier":"O43172","identifierLink":"https://www.uniprot.org/uniprotkb/O43172/entry","name":"PRPF4","description":"U4/U6 small nuclear ribonucleoprotein Prp4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19846","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744322","identifier":"O43395","identifierLink":"https://www.uniprot.org/uniprotkb/O43395/entry","name":"PRPF3","description":"U4/U6 small nuclear ribonucleoprotein Prp3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14212","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26418","complexName":"U4/U6 small nuclear ribonucleoprotein complex","organismName":"Homo sapiens; 9606","description":"Small RNA (snRNA) containing complex that is involved in mRNA splicing as part of the spliceosome. U4/6 snRNP complex, an intermediate in the assembly of the spliceosome.The spliceosome executes pre-mRNA splicing through a highly dynamic series of compositional and conformational transitions encompassing assembly, activation, catalysis and disassembly. Spliceosome stages are characterized as E, A, B and remodelling of the pre-catalytic spliceosome (B complex) into the activated spliceosome (Bact complex) and subsequently, the catalytically activated spliceosome (B* complex) to carry out two RNA-catalysed transesterification reactions that lead to intron removal and splicing together of the flanking exon sequences.\r\n\r\nPRP24 (P49960) functions as a snRNP recycling factor to re-anneal U4 and U6 snRNAs in Saccharomyces cerevisiae (CPX-24). SART3 (Q15020) the PRP24 orthologue in humans, is thought to associate with U6 and U4/U6 snRN during the recycling phase of the spliceosome cycle but it dissociates during the formation of the U4/U6.U5 tri-complex.","predictedComplex":false,"interactors":[{"ac":"EBI-1567797","identifier":"Q8WWY3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WWY3/entry","name":"PRPF31","description":"U4/U6 small nuclear ribonucleoprotein Prp31","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13904","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61255726","identifier":"CPX-26415","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-26415","name":"U6 small nuclear ribonucleoprotein complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-61258696","identifier":"CPX-26417","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-26417","name":"U4 small nuclear ribonucleoprotein complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-26421","complexName":"U5 small nuclear ribonucleoprotein complete complex","organismName":"Homo sapiens; 9606","description":"Small nuclear RNA (snRNA) containing complex, involved in mRNA splicing. This complex and the U6 snRNP, CPX-26415 are the two components of the catalytic core part of the pre-B spliceosomal complex. \r\n\r\nThe spliceosome executes pre-mRNA splicing through a highly dynamic series of compositional and conformational transitions encompassing assembly, activation, catalysis and disassembly of a highly dynamic structure, involving the binding and release of the small nuclear RNAs (snRNA) and protein factors which remove intronic sequence from pre-mRNA. Spliceosome stages are characterized as E, A, B and remodelling of the pre-catalytic spliceosome (B complex) into the activated spliceosome (Bact complex) and subsequently, the catalytically activated spliceosome (B* complex) to carry out two RNA-catalysed transesterification reactions that lead to intron removal and splicing together of the flanking exon sequences.","predictedComplex":false,"interactors":[{"ac":"EBI-1045395","identifier":"O75643","identifierLink":"https://www.uniprot.org/uniprotkb/O75643/entry","name":"SNRNP200","description":"U5 small nuclear ribonucleoprotein 200 kDa helicase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24075","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-297993","identifier":"P62316","identifierLink":"https://www.uniprot.org/uniprotkb/P62316/entry","name":"SNRPD2","description":"Small nuclear ribonucleoprotein Sm D2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12777","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348082","identifier":"P62304","identifierLink":"https://www.uniprot.org/uniprotkb/P62304/entry","name":"SNRPE","description":"Small nuclear ribonucleoprotein E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11193","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356900","identifier":"P62306","identifierLink":"https://www.uniprot.org/uniprotkb/P62306/entry","name":"SNRPF","description":"Small nuclear ribonucleoprotein F","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357897","identifier":"Q15029","identifierLink":"https://www.uniprot.org/uniprotkb/Q15029/entry","name":"EFTUD2","description":"116 kDa U5 small nuclear ribonucleoprotein component","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR42908","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372177","identifier":"P62314","identifierLink":"https://www.uniprot.org/uniprotkb/P62314/entry","name":"SNRPD1","description":"Small nuclear ribonucleoprotein Sm D1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372458","identifier":"P14678","identifierLink":"https://www.uniprot.org/uniprotkb/P14678/entry","name":"SNRPB","description":"Small nuclear ribonucleoprotein-associated proteins B and B'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372789","identifier":"P62318","identifierLink":"https://www.uniprot.org/uniprotkb/P62318/entry","name":"SNRPD3","description":"Small nuclear ribonucleoprotein Sm D3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-536755","identifier":"O94906","identifierLink":"https://www.uniprot.org/uniprotkb/O94906/entry","name":"PRPF6","description":"Pre-mRNA-processing factor 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11246","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-538479","identifier":"Q6P2Q9","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P2Q9/entry","name":"PRPF8","description":"Pre-mRNA-processing-splicing factor 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11140","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-538492","identifier":"Q96DI7","identifierLink":"https://www.uniprot.org/uniprotkb/Q96DI7/entry","name":"SNRNP40","description":"U5 small nuclear ribonucleoprotein 40 kDa protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44006","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-540096","identifier":"Q9BUQ8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BUQ8/entry","name":"DDX23","description":"Probable ATP-dependent RNA helicase DDX23","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47958","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61264774","identifier":"URS000075BAAE_9606","identifierLink":"http://rnacentral.org/rna/URS000075BAAE_9606","name":"rna, u5a small nuclear 1 (rnu5a-1)","description":"Homo sapiens (human) RNA, U5A small nuclear 1 (RNU5A-1)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small nuclear rna","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-624585","identifier":"P62308","identifierLink":"https://www.uniprot.org/uniprotkb/P62308/entry","name":"SNRPG","description":"Small nuclear ribonucleoprotein G","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-768015","identifier":"O95400","identifierLink":"https://www.uniprot.org/uniprotkb/O95400/entry","name":"CD2BP2","description":"CD2 antigen cytoplasmic tail-binding protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13138","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26422","complexName":"Checkpoint clamp complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Enables the DNA repair pathways to restore the integrity of the DNA prior to DNA synthesis or separation of the replicated chromosomes. In response to genotoxic damage, the 9-1-1 complex is loaded around DNA by the Rad17-containing clamp loader. The DNA-bound 9-1-1 complex then facilitates ATR-mediated phosphorylation and activation of chk1 (O61661), a protein kinase that regulates S-phase progression, G2/M arrest, and replication fork stabilization.","predictedComplex":false,"interactors":[{"ac":"EBI-767597","identifier":"P78955","identifierLink":"https://www.uniprot.org/uniprotkb/P78955/entry","name":"hus1","description":"Checkpoint protein hus1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12900","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-767637","identifier":"P22193","identifierLink":"https://www.uniprot.org/uniprotkb/P22193/entry","name":"rad1","description":"DNA damage checkpoint control protein rad1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10870","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-768686","identifier":"P26306","identifierLink":"https://www.uniprot.org/uniprotkb/P26306/entry","name":"rad9","description":"DNA repair protein rad9","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15237","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26423","complexName":"Box C/D snoRNA-guided RNP methyltransferase complex, FBL variant","organismName":"Homo sapiens; 9606","description":"Small nucleolar RNA (snoRNA) dependent 2'-O-methyltransferase complex. Upon forming a snoRNP complex with a box C/D snoRNA and other core proteins, FBL transfers a methyl group to the 2'-hydroxyl of the ribose moiety in substrate RNAs. Complex plays a role in pre-rRNA cleavage and in 2'-O-methylation of nucleotides at specific positions in rRNAs, snoRNAs, and other RNAs during maturation. \r\n\r\nFBL is enriched in the nucleolus' dense fibrillar center where it participates in pre-rRNA processing by mediating 2'-O-methylation modifications.","predictedComplex":false,"interactors":[{"ac":"EBI-12520674","identifier":"CHEBI:67040","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:67040","name":"s-adenosyl-l-methioninate","description":"S-adenosyl-L-methioninate","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-12521462","identifier":"CHEBI:133335","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:133335","name":"c/d box small nucleolar rnas","description":"C/D box small nucleolar RNAs","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-358318","identifier":"P22087","identifierLink":"https://www.uniprot.org/uniprotkb/P22087/entry","name":"FBL","description":"rRNA 2'-O-methyltransferase fibrillarin","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10335","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395469","identifier":"Q9Y2X3","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y2X3/entry","name":"NOP58","description":"Nucleolar protein 58","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-396034","identifier":"O00567","identifierLink":"https://www.uniprot.org/uniprotkb/O00567/entry","name":"NOP56","description":"Nucleolar protein 56","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10894","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-712228","identifier":"P55769","identifierLink":"https://www.uniprot.org/uniprotkb/P55769/entry","name":"SNU13","description":"NHP2-like protein 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26424","complexName":"METTL1-WUHO tRNA (guanine-N(7)-)-methyltransferase complex","organismName":"Drosophila melanogaster; 7227","description":"7-Methyltransferase that modifies guanosine-46 in the variable loop of certain tRNAs that contain the 5'-RAGGU-3' motif. m7G46 makes triple-base interactions with cytosine-13 and guanosine-22. The tertiary interactions increase the thermal stability of the tRNAs and thus modulates steady-state tRNA levels. The complex is equired for the formation of elongated spermatids.","predictedComplex":false,"interactors":[{"ac":"EBI-103749","identifier":"O77263","identifierLink":"https://www.uniprot.org/uniprotkb/O77263/entry","name":"Mettl1","description":"tRNA (guanine-N(7)-)-methyltransferase","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23417","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-30813205","identifier":"CHEBI:59789","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:59789","name":"s-adenosyl-l-methionine zwitterion","description":"S-adenosyl-L-methionine zwitterion","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-56883582","identifier":"Q9W415","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W415/entry","name":"wuho","description":"tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit wuho","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR16288","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-2391","complexName":"U4/U6.U5 small nuclear ribonucleoprotein complex","organismName":"Homo sapiens; 9606","description":"Major pre-formed spliceosome building block. The spliceosome executes pre-mRNA splicing through a highly dynamic series of compositional and conformational transitions encompassing assembly, activation, catalysis and disassembly of a highly dynamic structure, involving the binding and release of the small nuclear RNAs (snRNA) and protein factors which remove intronic sequence from pre-mRNA. Spliceosome stages are characterized as E, A, B and remodelling of the pre-catalytic spliceosome (B complex) into the activated spliceosome (Bact complex) and subsequently, the catalytically activated spliceosome (B* complex) to carry out two RNA-catalysed transesterification reactions that lead to intron removal and splicing together of the flanking exon sequences.\r\n\r\nAssociation of the U4/U6.U5 tri-snRNP with the pre-spliceosomes E and A (i.e CPX-2392, CPX-2539 snRNPs bound to the 5' splice site and the branch site of the pre-mRNA intron respectively) leads to the formation of the mature spliceosomes, B and C. The DEAD-box helicase DDX23 releases the 5' splice site from U1 snRNP and transfers it to the ACAGAGA box within U6 snRNA. The RNA helicase SNRNP200 then separates U4 snRNA from U6 snRNA and allows the U6 snRNA sequence adjacent to the 5' splice site-bound ACAGAGA box to fold and associate with part of U2 snRNA to yield the active site harboring two catalytic metal ions. When the branch site adenosine is docked into the active site, the branching reaction produces the cleaved 5' exon and the lariat-intron intermediate. The 5' exon remains in the active site, but the branch site adenosine must leave the active site for the incoming 3′ splice site site for the exon–ligation reaction. Finally, the 5' and 3' exons are ligated, and the resulting mRNA is released from the active site.","predictedComplex":false,"interactors":[{"ac":"EBI-1044822","identifier":"Q53GS9","identifierLink":"https://www.uniprot.org/uniprotkb/Q53GS9/entry","name":"USP39","description":"Ubiquitin carboxyl-terminal hydrolase 39","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21646","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1045395","identifier":"O75643","identifierLink":"https://www.uniprot.org/uniprotkb/O75643/entry","name":"SNRNP200","description":"U5 small nuclear ribonucleoprotein 200 kDa helicase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24075","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1567797","identifier":"Q8WWY3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WWY3/entry","name":"PRPF31","description":"U4/U6 small nuclear ribonucleoprotein Prp31","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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Spliceosome stages are characterized as E, A, B and remodelling of the pre-catalytic spliceosome (B complex) into the activated spliceosome (Bact complex) and subsequently, the catalytically activated C* spliceosome to carry out two RNA-catalysed transesterification reactions that lead to intron removal and splicing together of the flanking exon sequences.","predictedComplex":false,"interactors":[{"ac":"EBI-1044822","identifier":"Q53GS9","identifierLink":"https://www.uniprot.org/uniprotkb/Q53GS9/entry","name":"USP39","description":"Ubiquitin carboxyl-terminal hydrolase 39","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21646","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1045395","identifier":"O75643","identifierLink":"https://www.uniprot.org/uniprotkb/O75643/entry","name":"SNRNP200","description":"U5 small nuclear ribonucleoprotein 200 kDa helicase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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Phosphorylation of Rad9 disrupts its interaction with replication protein A (RPA) and is dependent on  checkpoint clamp complex chromatin loading","predictedComplex":false,"interactors":[{"ac":"EBI-908382","identifier":"O59836","identifierLink":"https://www.uniprot.org/uniprotkb/O59836/entry","name":"him1","description":"Hsk1-interacting molecule 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-908476","identifier":"P50582","identifierLink":"https://www.uniprot.org/uniprotkb/P50582/entry","name":"hsk1","description":"Cell cycle serine/threonine-protein kinase hsk1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11909","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26439","complexName":"DBF4-dependent Cdc7 kinase complex","organismName":"Drosophila melanogaster; 7227","description":"Serine/threonine-protein kinase essential for the initiation of DNA replication during the S phase of mitosis. 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Phosphorylation of Rad9 disrupts its interaction with replication protein A (RPA) and is dependent on  checkpoint clamp complex  chromatin loading","predictedComplex":false,"interactors":[{"ac":"EBI-126864","identifier":"Q9W3Y1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W3Y1/entry","name":"Cdc7","description":"non-specific serine/threonine protein kinase Cdc7","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR44167","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3415429","identifier":"Q9NK54","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NK54/entry","name":"chif","description":"Protein chiffon","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26440","complexName":"Checkpoint clamp complex","organismName":"Drosophila melanogaster; 7227","description":"Enables the DNA repair pathways to restore the integrity of the DNA prior to DNA synthesis or separation of the replicated chromosomes. In response to genotoxic damage, the 9-1-1 complex is loaded around DNA by the Rad17-containing clamp loader. The DNA-bound 9-1-1 complex then facilitates ATR-mediated phosphorylation and activation of chk1 (P34208), a protein kinase that regulates S-phase progression, G2/M arrest, and replication fork stabilization.","predictedComplex":false,"interactors":[{"ac":"EBI-58764254","identifier":"Q9VN60","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VN60/entry","name":"Hus1-like","description":"Checkpoint protein Hus1-like","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR12900","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-93096","identifier":"O96533","identifierLink":"https://www.uniprot.org/uniprotkb/O96533/entry","name":"Rad9","description":"Cell cycle checkpoint control protein Rad9","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-9952246","identifier":"Q9VQD4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VQD4/entry","name":"Rad1","description":"DNA repair protein Rad1","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10870","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26441","complexName":"Major Spliceosomal Pre-B-act complex","organismName":"Homo sapiens; 9606","description":"Early-form of the activated B (B-act) spliceosome. B-act is activated but not catalytically primed; it is functionally blocked prior to the first catalytic step of splicing. The B to B-act to C (B*) transition involves at least six stages, pre-B-act (this complex), B-act-I, B-act-II, B-act-III, B-act-IV and post-B-act.\r\n\r\nThe spliceosome executes pre-mRNA splicing through a highly dynamic series of compositional and conformational transitions encompassing assembly, activation, catalysis and disassembly of a highly dynamic structure, involving the binding and release of the small nuclear RNAs (snRNA) and protein factors which remove intronic sequence from pre-mRNA. Spliceosome stages are characterized as E, A, B and remodelling of the pre-catalytic spliceosome (B complex) into the activated spliceosome (B-act) and subsequently, the catalytically activated spliceosome (C* complex) to carry out two RNA-catalysed transesterification reactions that lead to intron removal and splicing together of the flanking 5' and 3'-exons.\r\n\r\nB-act in humans bears little resemblance to the B complex. The B to B-act to C transitions involve extensive re-shuffling of spliceosome components; the B-act to C transition, propelled by the ATPase helicases is less dramatic compared to the B to B-act transition but involves a flux of considerably more proteins than the C to C* and P (post-catalytic spliceosome) to ILS (intron lariat spliceosome) transitions, which is driven by the ATPase/helicases DHX38 and DHX8, respectively.","predictedComplex":false,"interactors":[{"ac":"EBI-1045395","identifier":"O75643","identifierLink":"https://www.uniprot.org/uniprotkb/O75643/entry","name":"SNRNP200","description":"U5 small nuclear ribonucleoprotein 200 kDa helicase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24075","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1046261","identifier":"Q9Y3B4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3B4/entry","name":"SF3B6","description":"Splicing factor 3B subunit 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-1049701","identifier":"Q9BZJ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BZJ0/entry","name":"CRNKL1","description":"Crooked neck-like protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11246","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1051504","identifier":"O43660","identifierLink":"https://www.uniprot.org/uniprotkb/O43660/entry","name":"PLRG1","description":"Pleiotropic regulator 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19923","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1051880","identifier":"Q12874","identifierLink":"https://www.uniprot.org/uniprotkb/Q12874/entry","name":"SF3A3","description":"Splicing factor 3A subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12786","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1053651","identifier":"P08579","identifierLink":"https://www.uniprot.org/uniprotkb/P08579/entry","name":"SNRPB2","description":"U2 small nuclear ribonucleoprotein B''","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10501","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1054743","identifier":"Q15459","identifierLink":"https://www.uniprot.org/uniprotkb/Q15459/entry","name":"SF3A1","description":"Splicing factor 3A subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15316","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1055880","identifier":"Q8IYB3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IYB3/entry","name":"SRRM1","description":"Serine/arginine repetitive matrix protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23148","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2371709","identifier":"Q9P013","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P013/entry","name":"CWC15","description":"Spliceosome-associated protein CWC15 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12718","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2462271","identifier":"Q15428","identifierLink":"https://www.uniprot.org/uniprotkb/Q15428/entry","name":"SF3A2","description":"Splicing factor 3A subunit 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23205","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2512328","identifier":"O60306","identifierLink":"https://www.uniprot.org/uniprotkb/O60306/entry","name":"AQR","description":"RNA helicase aquarius","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10887","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2555365","identifier":"Q7RTV0","identifierLink":"https://www.uniprot.org/uniprotkb/Q7RTV0/entry","name":"PHF5A","description":"PHD finger-like domain-containing protein 5A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13120","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2555428","identifier":"Q9BWJ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BWJ5/entry","name":"SF3B5","description":"Splicing factor 3B subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20978","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2561225","identifier":"O60870","identifierLink":"https://www.uniprot.org/uniprotkb/O60870/entry","name":"KIN","description":"DNA/RNA-binding protein KIN17","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12805","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2602260","identifier":"Q9NW64","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NW64/entry","name":"RBM22","description":"Pre-mRNA-splicing factor RBM22","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14089","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27124795","identifier":"URS00006767A8_9606","identifierLink":"http://rnacentral.org/rna/URS00006767A8_9606","name":"u6_human_snrna","description":"Homo sapiens U6 spliceosomal RNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small nuclear rna","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-27124798","identifier":"URS00006A1489_9606","identifierLink":"http://rnacentral.org/rna/URS00006A1489_9606","name":"u2_human_snrna","description":"Human U2  spliceosomal RNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small nuclear rna","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-295232","identifier":"Q9HCS7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HCS7/entry","name":"XAB2","description":"Pre-mRNA-splicing factor SYF1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11246","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-297993","identifier":"P62316","identifierLink":"https://www.uniprot.org/uniprotkb/P62316/entry","name":"SNRPD2","description":"Small nuclear ribonucleoprotein Sm D2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12777","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-346977","identifier":"Q15393","identifierLink":"https://www.uniprot.org/uniprotkb/Q15393/entry","name":"SF3B3","description":"Splicing factor 3B subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348082","identifier":"P62304","identifierLink":"https://www.uniprot.org/uniprotkb/P62304/entry","name":"SNRPE","description":"Small nuclear ribonucleoprotein E","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11193","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348469","identifier":"Q15427","identifierLink":"https://www.uniprot.org/uniprotkb/Q15427/entry","name":"SF3B4","description":"Splicing factor 3B subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48030","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356900","identifier":"P62306","identifierLink":"https://www.uniprot.org/uniprotkb/P62306/entry","name":"SNRPF","description":"Small nuclear ribonucleoprotein F","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357897","identifier":"Q15029","identifierLink":"https://www.uniprot.org/uniprotkb/Q15029/entry","name":"EFTUD2","description":"116 kDa U5 small nuclear ribonucleoprotein component","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR42908","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372177","identifier":"P62314","identifierLink":"https://www.uniprot.org/uniprotkb/P62314/entry","name":"SNRPD1","description":"Small nuclear ribonucleoprotein Sm D1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372458","identifier":"P14678","identifierLink":"https://www.uniprot.org/uniprotkb/P14678/entry","name":"SNRPB","description":"Small nuclear ribonucleoprotein-associated proteins B and B'","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372789","identifier":"P62318","identifierLink":"https://www.uniprot.org/uniprotkb/P62318/entry","name":"SNRPD3","description":"Small nuclear ribonucleoprotein Sm D3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-374880","identifier":"Q99459","identifierLink":"https://www.uniprot.org/uniprotkb/Q99459/entry","name":"CDC5L","description":"Cell division cycle 5-like protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45885","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3904603","identifier":"P41223","identifierLink":"https://www.uniprot.org/uniprotkb/P41223/entry","name":"BUD31","description":"Protein BUD31 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-538479","identifier":"Q6P2Q9","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P2Q9/entry","name":"PRPF8","description":"Pre-mRNA-processing-splicing factor 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11140","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-538492","identifier":"Q96DI7","identifierLink":"https://www.uniprot.org/uniprotkb/Q96DI7/entry","name":"SNRNP40","description":"U5 small nuclear ribonucleoprotein 40 kDa protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44006","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-591818","identifier":"Q9UNP9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UNP9/entry","name":"PPIE","description":"Peptidyl-prolyl cis-trans isomerase E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11071","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61264774","identifier":"URS000075BAAE_9606","identifierLink":"http://rnacentral.org/rna/URS000075BAAE_9606","name":"rna, u5a small nuclear 1 (rnu5a-1)","description":"Homo sapiens (human) RNA, U5A small nuclear 1 (RNU5A-1)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small nuclear rna","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-61269451","identifier":"CHEBI:139356","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:139356","name":"precursor messenger rna","description":"precursor messenger RNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-61277930","identifier":"CPX-26447","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-26447","name":"Retention and splicing complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-624585","identifier":"P62308","identifierLink":"https://www.uniprot.org/uniprotkb/P62308/entry","name":"SNRPG","description":"Small nuclear ribonucleoprotein G","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-632715","identifier":"Q13573","identifierLink":"https://www.uniprot.org/uniprotkb/Q13573/entry","name":"SNW1","description":"SNW domain-containing protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12096","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749111","identifier":"Q13435","identifierLink":"https://www.uniprot.org/uniprotkb/Q13435/entry","name":"SF3B2","description":"Splicing factor 3B subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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9606","xrefs":[{"identifier":"PTHR12097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26442","complexName":"spo4-spo6 meiosis-specific protein kinase complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Meiosis-specific protein kinase complex which is required for the initiation and progression of the second meiotic division and regulates the length of anaphase II spindles.","predictedComplex":false,"interactors":[{"ac":"EBI-61271871","identifier":"Q9UQY9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UQY9/entry","name":"spo4","description":"Cell cycle protein kinase spo4","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11909","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61271909","identifier":"Q9Y7J1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y7J1/entry","name":"spo6","description":"Sporulation-specific protein 6","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15375","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26444","complexName":"DNA replication factor C complex, rad17 variant","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"DNA-dependent ATPase clamp-loader complex that uses the energy of ATP binding and hydrolysis to recruit the checkpoint clamp complex (CPX-26422) to the recessed 5' end of a double-stranded DNA-single-stranded DNA junction as part of a DNA damage checkpoint system..","predictedComplex":false,"interactors":[{"ac":"EBI-1208934","identifier":"Q09843","identifierLink":"https://www.uniprot.org/uniprotkb/Q09843/entry","name":"rfc2","description":"Replication factor C subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1208954","identifier":"O14003","identifierLink":"https://www.uniprot.org/uniprotkb/O14003/entry","name":"rfc3","description":"Replication factor C subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 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Binds the leading strand DNA pol2 (P87154) which stimulates the complex to load DNA polymerase processivity factor PCNA (Q03392, CPX-547) onto primed and gapped leading strand DNA in an ATP-dependent manner.","predictedComplex":false,"interactors":[{"ac":"EBI-1208934","identifier":"Q09843","identifierLink":"https://www.uniprot.org/uniprotkb/Q09843/entry","name":"rfc2","description":"Replication factor C subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1208954","identifier":"O14003","identifierLink":"https://www.uniprot.org/uniprotkb/O14003/entry","name":"rfc3","description":"Replication factor C subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1208980","identifier":"O94449","identifierLink":"https://www.uniprot.org/uniprotkb/O94449/entry","name":"rfc4","description":"Replication factor C subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1208995","identifier":"O94697","identifierLink":"https://www.uniprot.org/uniprotkb/O94697/entry","name":"rfc5","description":"Replication factor C subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61272644","identifier":"Q9USQ1","identifierLink":"https://www.uniprot.org/uniprotkb/Q9USQ1/entry","name":"ctf18","description":"Chromosome transmission fidelity protein 18","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23389","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61272738","identifier":"Q65ZA6","identifierLink":"https://www.uniprot.org/uniprotkb/Q65ZA6/entry","name":"ctf8","description":"Chromosome transmission fidelity protein 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR47475","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61272751","identifier":"Q09732","identifierLink":"https://www.uniprot.org/uniprotkb/Q09732/entry","name":"dcc1","description":"Sister chromatid cohesion protein dcc1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13395","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26447","complexName":"Retention and splicing complex","organismName":"Homo sapiens; 9606","description":"The retention and splicing complex (RES) is a splicing factor which interacts with precursor mRNA at the onset of the first trans-esterification reaction, playing a critical role in splicing and retention of precursor mRNA.","predictedComplex":false,"interactors":[{"ac":"EBI-2561235","identifier":"Q9BRD0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BRD0/entry","name":"BUD13","description":"BUD13 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31809","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749336","identifier":"Q8TAD8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TAD8/entry","name":"SNIP1","description":"Smad nuclear-interacting protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23308","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-7704044","identifier":"Q9Y388","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y388/entry","name":"RBMX2","description":"RNA-binding motif protein, X-linked 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45880","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26448","complexName":"Major Spliceosomal B-act-I complex","organismName":"Homo sapiens; 9606","description":"Early-form of the activated B (B-act) spliceosome. B-act is activated but not catalytically primed; it is functionally blocked prior to the first catalytic step of splicing. The B to B-act to post-B-act transition involves at least six stages, pre-B-act, B-act-I (this complex), B-act-II, B-act-III, B-act-IV and post-B-act.\r\n\r\nThe spliceosome executes pre-mRNA splicing through a highly dynamic series of compositional and conformational transitions encompassing assembly, activation, catalysis and disassembly of a highly dynamic structure, involving the binding and release of the small nuclear RNAs (snRNA) and protein factors which remove intronic sequence from pre-mRNA. Spliceosome stages are characterized as E, A, B and remodelling of the pre-catalytic spliceosome (B complex) into the activated spliceosome (B-act) and subsequently, the catalytically activated spliceosome (C* complex) to carry out two RNA-catalysed transesterification reactions that lead to intron removal and splicing together of the flanking 5' and 3'-exons.\r\n\r\nB-act in humans bears little resemblance to the B complex. The B to B-act to C transitions involve extensive re-shuffling of spliceosome components; the B-act to C transition, propelled by the ATPase helicases is less dramatic compared to the B to B-act transition but involves a flux of considerably more proteins than the C to C* and P (post-catalytic spliceosome) to ILS (intron lariat spliceosome) transitions, which is driven by the ATPase/helicases DHX38 and DHX8, respectively.","predictedComplex":false,"interactors":[{"ac":"EBI-1045395","identifier":"O75643","identifierLink":"https://www.uniprot.org/uniprotkb/O75643/entry","name":"SNRNP200","description":"U5 small nuclear ribonucleoprotein 200 kDa helicase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24075","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1046261","identifier":"Q9Y3B4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3B4/entry","name":"SF3B6","description":"Splicing factor 3B subunit 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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9606","xrefs":[{"identifier":"PTHR45625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2371709","identifier":"Q9P013","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P013/entry","name":"CWC15","description":"Spliceosome-associated protein CWC15 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12718","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2462271","identifier":"Q15428","identifierLink":"https://www.uniprot.org/uniprotkb/Q15428/entry","name":"SF3A2","description":"Splicing factor 3A subunit 2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23205","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2512328","identifier":"O60306","identifierLink":"https://www.uniprot.org/uniprotkb/O60306/entry","name":"AQR","description":"RNA helicase aquarius","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10887","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2555365","identifier":"Q7RTV0","identifierLink":"https://www.uniprot.org/uniprotkb/Q7RTV0/entry","name":"PHF5A","description":"PHD finger-like domain-containing protein 5A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13120","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2555428","identifier":"Q9BWJ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BWJ5/entry","name":"SF3B5","description":"Splicing factor 3B subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20978","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2602260","identifier":"Q9NW64","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NW64/entry","name":"RBM22","description":"Pre-mRNA-splicing factor RBM22","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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9606","xrefs":[{"identifier":"PTHR11193","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348469","identifier":"Q15427","identifierLink":"https://www.uniprot.org/uniprotkb/Q15427/entry","name":"SF3B4","description":"Splicing factor 3B subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48030","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356900","identifier":"P62306","identifierLink":"https://www.uniprot.org/uniprotkb/P62306/entry","name":"SNRPF","description":"Small nuclear ribonucleoprotein F","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357897","identifier":"Q15029","identifierLink":"https://www.uniprot.org/uniprotkb/Q15029/entry","name":"EFTUD2","description":"116 kDa U5 small nuclear ribonucleoprotein component","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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Spliceosome stages are characterized as E, A, B and remodelling of the pre-catalytic spliceosome (B complex) into the activated spliceosome (B-act) and subsequently, the catalytically activated spliceosome (C* complex) to carry out two RNA-catalysed transesterification reactions that lead to intron removal and splicing together of the flanking 5' and 3'-exons.\r\n\r\nB-act in humans bears little resemblance to the B complex. 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The complex binds to DNA-loaded PCNA to induce opening of the PCNA ring, leading to the release of ELG1-RFC bound-PCNA.","predictedComplex":false,"interactors":[{"ac":"EBI-1208934","identifier":"Q09843","identifierLink":"https://www.uniprot.org/uniprotkb/Q09843/entry","name":"rfc2","description":"Replication factor C subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1208954","identifier":"O14003","identifierLink":"https://www.uniprot.org/uniprotkb/O14003/entry","name":"rfc3","description":"Replication factor C subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1208980","identifier":"O94449","identifierLink":"https://www.uniprot.org/uniprotkb/O94449/entry","name":"rfc4","description":"Replication factor C subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1208995","identifier":"O94697","identifierLink":"https://www.uniprot.org/uniprotkb/O94697/entry","name":"rfc5","description":"Replication factor C subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR11669","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61303267","identifier":"O43086","identifierLink":"https://www.uniprot.org/uniprotkb/O43086/entry","name":"elg1","description":"Telomere length regulation protein elg1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23389","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26453","complexName":"PAF1 complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"A multifunctional complex involved in  many aspects of RNA polymerase II (Pol II) transcriptional regulation, including transcriptional elongation, 3'-terminal end processing, and histone modification. Role in 3'-end formation of mRNAs, required for the recruitment of cleavage and polyadenylation factors cft1 (O74733) and pcf11 (Q1023) to RNA polymerase II.","predictedComplex":false,"interactors":[{"ac":"EBI-21242917","identifier":"Q9P6R2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P6R2/entry","name":"yoh8","description":"Uncharacterized protein C13E7.08c","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23146","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61303330","identifier":"Q9US06","identifierLink":"https://www.uniprot.org/uniprotkb/Q9US06/entry","name":"paf1","description":"RNA polymerase II-associated protein 1 homolog","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23188","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61303365","identifier":"Q9UUE7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UUE7/entry","name":"cdc73","description":"Cell division control protein 73","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12466","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61303380","identifier":"O94667","identifierLink":"https://www.uniprot.org/uniprotkb/O94667/entry","name":"rtf1","description":"RNA polymerase-associated protein C651.09c","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61303394","identifier":"O42668","identifierLink":"https://www.uniprot.org/uniprotkb/O42668/entry","name":"tpr1","description":"Tetratricopeptide repeat protein 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR14027","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26454","complexName":"Major Spliceosomal B-act-IV complex","organismName":"Homo sapiens; 9606","description":"Late-form of the activated B (B-act) spliceosome. B-act is activated but not catalytically primed; it is functionally blocked prior to the first catalytic step of splicing. The B to B-act to post-B-act transition involves at least six stages, pre-B-act, B-act-I, B-act-II, B-act-III, B-act-IV (this complex) and post-B-act.\r\n\r\nThe spliceosome executes pre-mRNA splicing through a highly dynamic series of compositional and conformational transitions encompassing assembly, activation, catalysis and disassembly of a highly dynamic structure, involving the binding and release of the small nuclear RNAs (snRNA) and protein factors which remove intronic sequence from pre-mRNA. Spliceosome stages are characterized as E, A, B and remodelling of the pre-catalytic spliceosome (B complex) into the activated spliceosome (B-act) and subsequently, the catalytically activated spliceosome (C* complex) to carry out two RNA-catalysed transesterification reactions that lead to intron removal and splicing together of the flanking 5' and 3'-exons.\r\n\r\nB-act in humans bears little resemblance to the B complex. The B to B-act to C transitions involve extensive re-shuffling of spliceosome components; the B-act to C transition, propelled by the ATPase helicases is less dramatic compared to the B to B-act transition but involves a flux of considerably more proteins than the C to C* and P (post-catalytic spliceosome) to ILS (intron lariat spliceosome) transitions, which is driven by the ATPase/helicases DHX38 and DHX8, respectively.","predictedComplex":false,"interactors":[{"ac":"EBI-1049701","identifier":"Q9BZJ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BZJ0/entry","name":"CRNKL1","description":"Crooked neck-like protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11246","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1050106","identifier":"O75934","identifierLink":"https://www.uniprot.org/uniprotkb/O75934/entry","name":"BCAS2","description":"Pre-mRNA-splicing factor SPF27","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13296","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1050142","identifier":"Q9UQ35","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UQ35/entry","name":"SRRM2","description":"Serine/arginine repetitive matrix protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR34755","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1051504","identifier":"O43660","identifierLink":"https://www.uniprot.org/uniprotkb/O43660/entry","name":"PLRG1","description":"Pleiotropic regulator 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19923","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1051880","identifier":"Q12874","identifierLink":"https://www.uniprot.org/uniprotkb/Q12874/entry","name":"SF3A3","description":"Splicing factor 3A subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12786","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1053651","identifier":"P08579","identifierLink":"https://www.uniprot.org/uniprotkb/P08579/entry","name":"SNRPB2","description":"U2 small nuclear ribonucleoprotein B''","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10501","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2130294","identifier":"O15541","identifierLink":"https://www.uniprot.org/uniprotkb/O15541/entry","name":"RNF113A","description":"E3 ubiquitin-protein ligase RNF113A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12930","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2371709","identifier":"Q9P013","identifierLink":"https://www.uniprot.org/uniprotkb/Q9P013/entry","name":"CWC15","description":"Spliceosome-associated protein CWC15 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12718","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2512328","identifier":"O60306","identifierLink":"https://www.uniprot.org/uniprotkb/O60306/entry","name":"AQR","description":"RNA helicase aquarius","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10887","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2513119","identifier":"Q8WUA2","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WUA2/entry","name":"PPIL4","description":"Peptidyl-prolyl cis-trans isomerase-like 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45843","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2555365","identifier":"Q7RTV0","identifierLink":"https://www.uniprot.org/uniprotkb/Q7RTV0/entry","name":"PHF5A","description":"PHD finger-like domain-containing protein 5A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13120","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2555428","identifier":"Q9BWJ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BWJ5/entry","name":"SF3B5","description":"Splicing factor 3B subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20978","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2557644","identifier":"O95926","identifierLink":"https://www.uniprot.org/uniprotkb/O95926/entry","name":"SYF2","description":"Pre-mRNA-splicing factor SYF2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13264","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2557649","identifier":"Q9Y3C6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3C6/entry","name":"PPIL1","description":"Peptidyl-prolyl cis-trans isomerase-like 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45625","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2557812","identifier":"O60508","identifierLink":"https://www.uniprot.org/uniprotkb/O60508/entry","name":"CDC40","description":"Pre-mRNA-processing factor 17","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43979","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2602260","identifier":"Q9NW64","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NW64/entry","name":"RBM22","description":"Pre-mRNA-splicing factor RBM22","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14089","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-27124795","identifier":"URS00006767A8_9606","identifierLink":"http://rnacentral.org/rna/URS00006767A8_9606","name":"u6_human_snrna","description":"Homo sapiens U6 spliceosomal RNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small nuclear rna","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-27124798","identifier":"URS00006A1489_9606","identifierLink":"http://rnacentral.org/rna/URS00006A1489_9606","name":"u2_human_snrna","description":"Human U2  spliceosomal RNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small nuclear rna","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-295232","identifier":"Q9HCS7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HCS7/entry","name":"XAB2","description":"Pre-mRNA-splicing factor SYF1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11246","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-297993","identifier":"P62316","identifierLink":"https://www.uniprot.org/uniprotkb/P62316/entry","name":"SNRPD2","description":"Small nuclear ribonucleoprotein Sm D2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12777","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-311446","identifier":"O60231","identifierLink":"https://www.uniprot.org/uniprotkb/O60231/entry","name":"DHX16","description":"Pre-mRNA-splicing factor ATP-dependent RNA helicase DHX16","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18934","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-346977","identifier":"Q15393","identifierLink":"https://www.uniprot.org/uniprotkb/Q15393/entry","name":"SF3B3","description":"Splicing factor 3B subunit 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10644","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348082","identifier":"P62304","identifierLink":"https://www.uniprot.org/uniprotkb/P62304/entry","name":"SNRPE","description":"Small nuclear ribonucleoprotein E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11193","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348469","identifier":"Q15427","identifierLink":"https://www.uniprot.org/uniprotkb/Q15427/entry","name":"SF3B4","description":"Splicing factor 3B subunit 4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR48030","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356900","identifier":"P62306","identifierLink":"https://www.uniprot.org/uniprotkb/P62306/entry","name":"SNRPF","description":"Small nuclear ribonucleoprotein F","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357897","identifier":"Q15029","identifierLink":"https://www.uniprot.org/uniprotkb/Q15029/entry","name":"EFTUD2","description":"116 kDa U5 small nuclear ribonucleoprotein component","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR42908","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372177","identifier":"P62314","identifierLink":"https://www.uniprot.org/uniprotkb/P62314/entry","name":"SNRPD1","description":"Small nuclear ribonucleoprotein Sm D1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372458","identifier":"P14678","identifierLink":"https://www.uniprot.org/uniprotkb/P14678/entry","name":"SNRPB","description":"Small nuclear ribonucleoprotein-associated proteins B and B'","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372789","identifier":"P62318","identifierLink":"https://www.uniprot.org/uniprotkb/P62318/entry","name":"SNRPD3","description":"Small nuclear ribonucleoprotein Sm D3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373289","identifier":"Q9HCG8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HCG8/entry","name":"CWC22","description":"Pre-mRNA-splicing factor CWC22 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR18034","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-374880","identifier":"Q99459","identifierLink":"https://www.uniprot.org/uniprotkb/Q99459/entry","name":"CDC5L","description":"Cell division cycle 5-like protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR45885","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-3904603","identifier":"P41223","identifierLink":"https://www.uniprot.org/uniprotkb/P41223/entry","name":"BUD31","description":"Protein BUD31 homolog","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19411","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-395746","identifier":"Q9UMS4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UMS4/entry","name":"PRPF19","description":"Pre-mRNA-processing factor 19","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR43995","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-538479","identifier":"Q6P2Q9","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P2Q9/entry","name":"PRPF8","description":"Pre-mRNA-processing-splicing factor 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11140","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-538492","identifier":"Q96DI7","identifierLink":"https://www.uniprot.org/uniprotkb/Q96DI7/entry","name":"SNRNP40","description":"U5 small nuclear ribonucleoprotein 40 kDa protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44006","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-591818","identifier":"Q9UNP9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UNP9/entry","name":"PPIE","description":"Peptidyl-prolyl cis-trans isomerase E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11071","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61264774","identifier":"URS000075BAAE_9606","identifierLink":"http://rnacentral.org/rna/URS000075BAAE_9606","name":"rna, u5a small nuclear 1 (rnu5a-1)","description":"Homo sapiens (human) RNA, U5A small nuclear 1 (RNU5A-1)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small nuclear rna","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-61269451","identifier":"CHEBI:139356","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:139356","name":"precursor messenger rna","description":"precursor messenger RNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-624585","identifier":"P62308","identifierLink":"https://www.uniprot.org/uniprotkb/P62308/entry","name":"SNRPG","description":"Small nuclear ribonucleoprotein G","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-632715","identifier":"Q13573","identifierLink":"https://www.uniprot.org/uniprotkb/Q13573/entry","name":"SNW1","description":"SNW domain-containing protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12096","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-749111","identifier":"Q13435","identifierLink":"https://www.uniprot.org/uniprotkb/Q13435/entry","name":"SF3B2","description":"Splicing factor 3B subunit 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12785","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-876439","identifier":"P09661","identifierLink":"https://www.uniprot.org/uniprotkb/P09661/entry","name":"SNRPA1","description":"U2 small nuclear ribonucleoprotein A'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10552","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-876542","identifier":"O75533","identifierLink":"https://www.uniprot.org/uniprotkb/O75533/entry","name":"SF3B1","description":"Splicing factor 3B subunit 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12097","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26455","complexName":"Nuclear origin recognition complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Protein complex that binds to the autonomously replicating sequence (ARS) origin of DNA replication in an ATP-dependent manner and recruits other proteins, such as the initiation factors cdc18 (P54789),  to form a pre-replicative complex before the initiation of DNA replication that occurs in S phase.","predictedComplex":false,"interactors":[{"ac":"EBI-2028187","identifier":"Q09142","identifierLink":"https://www.uniprot.org/uniprotkb/Q09142/entry","name":"orc2","description":"Origin recognition complex subunit 2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR14052","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61312763","identifier":"P54789","identifierLink":"https://www.uniprot.org/uniprotkb/P54789/entry","name":"orc1","description":"Origin recognition complex subunit 1","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10763","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61312834","identifier":"Q10067","identifierLink":"https://www.uniprot.org/uniprotkb/Q10067/entry","name":"orc3","description":"Origin recognition complex subunit 3","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12748","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61312859","identifier":"Q9Y794","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y794/entry","name":"orc4","description":"Origin recognition complex subunit 4","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12087","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-63977113","identifier":"O43114","identifierLink":"https://www.uniprot.org/uniprotkb/O43114/entry","name":"orc5","description":"Origin recognition complex subunit 5","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12705","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-63977142","identifier":"O74796","identifierLink":"https://www.uniprot.org/uniprotkb/O74796/entry","name":"orc6","description":"Origin recognition complex subunit 6","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13394","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26456","complexName":"ATR-ATRIP DNA damage-sensing kinase complex","organismName":"Drosophila melanogaster; 7227","description":"Master regulator of the DNA damage response controlling a signaling cascade required for the maintenance of genomic integrity. Activated by RPA complex-coated single-stranded DNA at the site of DNA double-strand breaks and stalled replication forks. Appears to control the production of an adequate and balanced pool of deoxyribonucleotides and maintain replication fork stability.","predictedComplex":false,"interactors":[{"ac":"EBI-135793","identifier":"Q9VVN4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VVN4/entry","name":"mus304","description":"ATR-interacting protein mus304","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR28594","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-498133","identifier":"Q9VXG8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VXG8/entry","name":"mei-41","description":"Serine/threonine-protein kinase ATR","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11139","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26457","complexName":"Replication protein A complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Single-stranded DNA binding protein complex involved in all processes that involve single-stranded (ss)DNA by binding to and protecting exposed ssDNA from nucleases. Forms a physical platform to recruit other factors to the DNA including those involved in DNA damage signaling, DNA repair, and DNA replication. RPA protects against inappropriate telomere recombination, and upon telomere uncapping, prevents cell proliferation by a checkpoint-independent pathway. RPA prevents degradation of ssDNA and prevents formation of secondary structures.","predictedComplex":false,"interactors":[{"ac":"EBI-15597497","identifier":"Q92373","identifierLink":"https://www.uniprot.org/uniprotkb/Q92373/entry","name":"ssb2","description":"Replication factor A protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13989","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15597535","identifier":"Q92374","identifierLink":"https://www.uniprot.org/uniprotkb/Q92374/entry","name":"ssb3","description":"Replication factor A protein 3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15114","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-966394","identifier":"Q92372","identifierLink":"https://www.uniprot.org/uniprotkb/Q92372/entry","name":"ssb1","description":"Replication factor A protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23273","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26458","complexName":"Major Spliceosomal Post-B-act complex","organismName":"Homo sapiens; 9606","description":"Step-1 catalytically-activated B (B-act) spliceosome. The B to B-act to post-B-act transition involves at least six stages, pre-B-act, B-act-I, B-act-II, B-act-III, B-act-IV and post-B-act (this complex).\r\n\r\nThe spliceosome executes pre-mRNA splicing through a highly dynamic series of compositional and conformational transitions encompassing assembly, activation, catalysis and disassembly of a highly dynamic structure, involving the binding and release of the small nuclear RNAs (snRNA) and protein factors which remove intronic sequence from pre-mRNA. Spliceosome stages are characterized as E, A, B and remodelling of the pre-catalytic spliceosome (B complex) into the activated spliceosome (B-act) and subsequently, the catalytically activated spliceosome (C complex) to carry out two RNA-catalysed transesterification reactions that lead to intron removal and splicing together of the flanking 5' and 3'-exons.\r\n\r\nB-act in humans bears little resemblance to the B complex. The B to B-act to C transitions involve extensive re-shuffling of spliceosome components; the B-act to C transition, propelled by the ATPase helicases is less dramatic compared to the B to B-act transition but involves a flux of considerably more proteins than the C to C* and P (post-catalytic spliceosome) to ILS (intron lariat spliceosome) transitions, which is driven by the ATPase/helicases DHX38 and DHX8, respectively.","predictedComplex":false,"interactors":[{"ac":"EBI-1049701","identifier":"Q9BZJ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BZJ0/entry","name":"CRNKL1","description":"Crooked neck-like protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11246","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1050106","identifier":"O75934","identifierLink":"https://www.uniprot.org/uniprotkb/O75934/entry","name":"BCAS2","description":"Pre-mRNA-splicing factor SPF27","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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9606","xrefs":[{"identifier":"PTHR45843","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2555365","identifier":"Q7RTV0","identifierLink":"https://www.uniprot.org/uniprotkb/Q7RTV0/entry","name":"PHF5A","description":"PHD finger-like domain-containing protein 5A","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13120","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2555428","identifier":"Q9BWJ5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BWJ5/entry","name":"SF3B5","description":"Splicing factor 3B subunit 5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20978","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-2557644","identifier":"O95926","identifierLink":"https://www.uniprot.org/uniprotkb/O95926/entry","name":"SYF2","description":"Pre-mRNA-splicing factor SYF2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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9606","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357897","identifier":"Q15029","identifierLink":"https://www.uniprot.org/uniprotkb/Q15029/entry","name":"EFTUD2","description":"116 kDa U5 small nuclear ribonucleoprotein component","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR42908","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372177","identifier":"P62314","identifierLink":"https://www.uniprot.org/uniprotkb/P62314/entry","name":"SNRPD1","description":"Small nuclear ribonucleoprotein Sm D1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372458","identifier":"P14678","identifierLink":"https://www.uniprot.org/uniprotkb/P14678/entry","name":"SNRPB","description":"Small nuclear ribonucleoprotein-associated proteins B and B'","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 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Phosphorylates the C-terminal domain (CTD) of RNA polymerase II (CPX-2625). 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Binds to the ribosomal A site. GTP hydrolysis, dissociation of HBS1 and accommodation of DOM34 in the ribosome, results in the binding of RLI1 (O60102) followed by ATP-dependent subunit dissociation.","predictedComplex":false,"interactors":[{"ac":"EBI-15882111","identifier":"O74774","identifierLink":"https://www.uniprot.org/uniprotkb/O74774/entry","name":"hbs1","description":"Elongation factor 1 alpha-like protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR23115","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-15882140","identifier":"Q9USL5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9USL5/entry","name":"dom34","description":"Protein dom34","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10853","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-989053","identifier":"CHEBI:15996","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:15996","name":"gtp","description":"guanosine triphosphate - GTP","stochiometry":null,"interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26479","complexName":"Major Post-catalytic P Spliceosome complex","organismName":"Homo sapiens; 9606","description":"Post-catalytic spliceosomal complex. 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Spliceosome stages are characterized as E, A, B and remodelling of the pre-catalytic spliceosome B complex into the activated spliceosome B-act and subsequently, the catalytically activated spliceosome C* complex to carry out two RNA-catalysed transesterification reactions that lead to intron removal and splicing together of the flanking 5' and 3'-exons.\r\n\r\nThe B-act to C transitions involve extensive re-shuffling of spliceosome components; the B-act to C transition, propelled by the ATPase helicases is less dramatic compared to the B to B-act transition but involves a flux of considerably more proteins than the C to C* and P (post-catalytic spliceosome) to ILS (intron lariat spliceosome) transitions, which is driven by the ATPase/helicases DHX38 (Q92620) and DHX8, respectively.","predictedComplex":false,"interactors":[{"ac":"EBI-1049701","identifier":"Q9BZJ0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BZJ0/entry","name":"CRNKL1","description":"Crooked neck-like protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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9606","xrefs":[{"identifier":"PTHR11140","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-538492","identifier":"Q96DI7","identifierLink":"https://www.uniprot.org/uniprotkb/Q96DI7/entry","name":"SNRNP40","description":"U5 small nuclear ribonucleoprotein 40 kDa protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44006","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-5453285","identifier":"Q2TBE0","identifierLink":"https://www.uniprot.org/uniprotkb/Q2TBE0/entry","name":"CWF19L2","description":"CWF19-like protein 2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12072","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-591818","identifier":"Q9UNP9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UNP9/entry","name":"PPIE","description":"Peptidyl-prolyl cis-trans isomerase E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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9606","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-632715","identifier":"Q13573","identifierLink":"https://www.uniprot.org/uniprotkb/Q13573/entry","name":"SNW1","description":"SNW domain-containing protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12096","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-876439","identifier":"P09661","identifierLink":"https://www.uniprot.org/uniprotkb/P09661/entry","name":"SNRPA1","description":"U2 small nuclear ribonucleoprotein A'","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10552","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26483","complexName":"U6 small nuclear ribonucleoprotein complex","organismName":"Drosophila melanogaster; 7227","description":"Non-coding RNA containing complex, part of the pre-B complex that acts as a chaperone for U6 spliceosomal-RNA. The spliceosome is a highly dynamic structure, assembled by sequential binding and release of the small nuclear RNAs (snRNA) and protein factors which removes intronic sequence from pre-mRNA. U6 is part of the activated spliceosome and is involved in the first trans-estherification step of splicing. After splicing is complete, the spliceosome disassembles and free U6 snRNP forms. It then reassociates with U4 to form U4/U6 snRNP.","predictedComplex":false,"interactors":[{"ac":"EBI-117085","identifier":"Q9VRT7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VRT7/entry","name":"BcDNA:RE60135","description":"U6 snRNA-associated Sm-like protein LSm5","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR20971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-128970","identifier":"Q9W2P5","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W2P5/entry","name":"Dmel\\CG9344","description":"U6 snRNA-associated Sm-like protein LSm6","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-140047","identifier":"Q9W087","identifierLink":"https://www.uniprot.org/uniprotkb/Q9W087/entry","name":"l(3)neo7","description":"U6 snRNA-associated Sm-like protein LSm8","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR15588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-150361","identifier":"Q9VTW6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VTW6/entry","name":"Dmel\\CG10418","description":"U6 snRNA-associated Sm-like protein LSm2","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-166874","identifier":"Q8IMX8","identifierLink":"https://www.uniprot.org/uniprotkb/Q8IMX8/entry","name":"LSm3","description":"U6 snRNA-associated Sm-like protein LSm3","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR13110","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-63974433","identifier":"URS000009C54D_7227","identifierLink":"http://rnacentral.org/rna/URS000009C54D_7227","name":"small nuclear rna u6 at 96a a (dmel_cr31379, dmel_cr31539, dmel_cr32867)","description":"Drosophila melanogaster (fruit fly) small nuclear RNA U6 at 96A a (Dmel_CR31379, Dmel_CR31539, Dmel_CR32867)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small nuclear rna","organismName":"Drosophila melanogaster; 7227","xrefs":[]},{"ac":"EBI-88876","identifier":"Q9VJI7","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VJI7/entry","name":"LSm7","description":"U6 snRNA-associated Sm-like protein LSm7","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-99437","identifier":"Q9VKW8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9VKW8/entry","name":"CG5356","description":"U6 snRNA-associated Sm-like protein LSm4","stochiometry":null,"interactorType":"protein","organismName":"Drosophila melanogaster; 7227","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26484","complexName":"TSC1-TSC2 complex","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","description":"Acts as a GTPase-activating protein (GAP) for the small GTPase rheb (O94363) thus negatively regulating tor1 (O14356) signaling.","predictedComplex":false,"interactors":[{"ac":"EBI-1560709","identifier":"Q09778","identifierLink":"https://www.uniprot.org/uniprotkb/Q09778/entry","name":"tsc1","description":"Tuberous sclerosis 1 protein homolog","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15154","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-63985479","identifier":"Q9UUG9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UUG9/entry","name":"tsc2","description":"Tuberous sclerosis 2 protein homolog","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR10063","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26485","complexName":"U11 small nuclear ribonucleoprotein complex","organismName":"Homo sapiens; 9606","description":"Minor spliceosome building block. The minor spliceosome catalyses the removal of an atypical (U12) class of eukaryotic precursor-mRNA (pre-mRNA) introns and is thought to excise approximately 1 in 300 introns in human pre-mRNA. U12 introns constitute roughly 0.5% of all introns, and are recognizable by their non-consensus AT-AC termini as well as a high degree of conservation at the 5' splice site. U12-dependent introns are thought to be evolutionarily ancient but absent in many species including model organisms such as Caenorhabditis elegans and Saccharomyces cerevisiae. \r\n\r\nThe minor spliceosome contains several specific low-abundance snRNPs, including U11 (this complex), U12, U4atac, U6atac and the common U5 snRNP also present in the major spliceosome. U12-type intron containing genes are mainly related to information processing functions, including DNA replication and repair, transcription, RNA processing, and translation, but can also be found in genes related to cytoskeletal organization, vesicular transport, and voltage-gated ion channel activity.","predictedComplex":false,"interactors":[{"ac":"EBI-2876632","identifier":"Q6IEG0","identifierLink":"https://www.uniprot.org/uniprotkb/Q6IEG0/entry","name":"SNRNP48","description":"U11/U12 small nuclear ribonucleoprotein 48 kDa protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21402","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-297993","identifier":"P62316","identifierLink":"https://www.uniprot.org/uniprotkb/P62316/entry","name":"SNRPD2","description":"Small nuclear ribonucleoprotein Sm D2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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U12-type intron containing genes are mainly related to information processing functions, including DNA replication and repair, transcription, RNA processing, and translation, but can also be found in genes related to cytoskeletal organization, vesicular transport, and voltage-gated ion channel activity.\r\n\r\nU12-dependent introns are thought to be evolutionarily ancient but absent in many species including model organisms such as Caenorhabditis elegans and Saccharomyces cerevisiae.\r\n\r\nMutations in SF3B4 is associated with recessive skeletal dysplasia and eye disorders.","predictedComplex":false,"interactors":[{"ac":"EBI-297993","identifier":"P62316","identifierLink":"https://www.uniprot.org/uniprotkb/P62316/entry","name":"SNRPD2","description":"Small nuclear ribonucleoprotein Sm D2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12777","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348082","identifier":"P62304","identifierLink":"https://www.uniprot.org/uniprotkb/P62304/entry","name":"SNRPE","description":"Small nuclear ribonucleoprotein E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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9606","xrefs":[{"identifier":"PTHR10701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372789","identifier":"P62318","identifierLink":"https://www.uniprot.org/uniprotkb/P62318/entry","name":"SNRPD3","description":"Small nuclear ribonucleoprotein Sm D3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-61269451","identifier":"CHEBI:139356","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:139356","name":"precursor messenger rna","description":"precursor messenger RNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]},{"ac":"EBI-624585","identifier":"P62308","identifierLink":"https://www.uniprot.org/uniprotkb/P62308/entry","name":"SNRPG","description":"Small nuclear ribonucleoprotein G","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-63983305","identifier":"URS00006ECA78_9606","identifierLink":"http://rnacentral.org/rna/URS00006ECA78_9606","name":"rna, u12 small nuclear (rnu12)","description":"Homo sapiens (human) RNA, U12 small nuclear (RNU12)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small nuclear rna","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-748391","identifier":"Q9BWG6","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BWG6/entry","name":"SCNM1","description":"Sodium channel modifier 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR32297","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-9010003","identifier":"CPX-2227","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-2227","name":"SF3B complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-26488","complexName":"Glycodelin complex","organismName":"Homo sapiens; 9606","description":"Regulates critical steps during fertilization and interacts with cell-surface receptors in an immunomodulatory capacity.\r\n\r\nFound in reproductive tiisues, Glycodelin exists in four distinct isoforms, -A, -S, -F and -C which arise from differing N-linked glycosylation at Asn-46 and Asn-81. Glycodelin-A is found in amniotic fluid, the uterine luminal cavity, endometrium decidua and maternal serum, Glycodelin-C in cumulus cells, Glycodelin-F in follicular fluid, luteinized granulosa cells and the oviduct and, Glycodelin-S in seminal plasma and seminal vesicles.\r\n\r\nAll four forms share the same protein core but differ in their glycosylation and in their biological activity. Glycodelin-A's role is attributed to contraceptive and immunosuppressive activities, Glycodelin-C's role to the binding of spermatozoa to the zona pellucida, Glycodelin-F's role to inhibiting spermatozoa-zona pellucida binding, significantly suppressing progesterone-induced acrosome reaction of spermatozoa, and Glycodelin-S's role to binding and maintaining the uncapacitated state of human spermatozoa.","predictedComplex":false,"interactors":[{"ac":"EBI-465167","identifier":"P09466","identifierLink":"https://www.uniprot.org/uniprotkb/P09466/entry","name":"PAEP","description":"Glycodelin","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11430","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26489","complexName":"U11/U12 di-small nuclear ribonucleoprotein complex","organismName":"Homo sapiens; 9606","description":"U11/U12 di-snRNP minor spliceosome intron recognition complex. The minor spliceosome catalyses the removal of an atypical (U12) class of eukaryotic precursor-mRNA introns. U12 introns constitute roughly 0.5% of all introns, and are recognizable by their non-consensus AT-AC termini as well as a high degree of conservation at the 5' splice site. U12-dependent introns are thought to be evolutionarily ancient but absent in many species including model organisms such as Caenorhabditis elegans and Saccharomyces cerevisiae. \r\n\r\nThe minor spliceosome contains several specific low-abundance snRNPs, including U11 (CPX-26485), U12 (CPX-26487), U4atac, U6atac and the common U5 snRNP also present in the major spliceosome. U12-type intron containing genes are mainly related to information processing functions, including DNA replication and repair, transcription, RNA processing, and translation, but can also be found in genes related to cytoskeletal organization, vesicular transport, and voltage-gated ion channel activity.\r\n\r\nSeveral disease-related mutations in RNPC3 implicated in pituitary growth hormone deficiency is suspected to compromise U11/U12 snRNA bridging and/or recruitment of ZMAT5.","predictedComplex":false,"interactors":[{"ac":"EBI-1046261","identifier":"Q9Y3B4","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y3B4/entry","name":"SF3B6","description":"Splicing factor 3B subunit 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-11124401","identifier":"Q8TBF4","identifierLink":"https://www.uniprot.org/uniprotkb/Q8TBF4/entry","name":"ZCRB1","description":"Zinc finger CCHC-type and RNA-binding motif-containing protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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-2","xrefs":[]},{"ac":"EBI-624585","identifier":"P62308","identifierLink":"https://www.uniprot.org/uniprotkb/P62308/entry","name":"SNRPG","description":"Small nuclear ribonucleoprotein G","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-63974591","identifier":"URS000000A142_9606","identifierLink":"http://rnacentral.org/rna/URS000000A142_9606","name":"rna, u11 small nuclear (rnu11)","description":"Homo sapiens (human) RNA, U11 small nuclear (RNU11)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small nuclear rna","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-63983305","identifier":"URS00006ECA78_9606","identifierLink":"http://rnacentral.org/rna/URS00006ECA78_9606","name":"rna, u12 small nuclear (rnu12)","description":"Homo sapiens (human) RNA, U12 small nuclear (RNU12)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small nuclear rna","organismName":"Homo sapiens; 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Acts to stabilize the presynaptic filament, a right-handed helical nucleoprotein strand generated  by RAD51 and DMC1 from single-stranded DNA derived from the nucleolytic processing of a primary lesion. The HOP2-MND1 complex synergizes with the filament to assemble the synaptic complex, and promotes DMC1-/RAD51-mediated strand exchange between the presynaptic filament and recombining double-stranded DNA to form a D-loop, acting with RAD54 (P32863), a nucleosome remodeler, to promote homologous pairing with the nucleosomal double-stranded DNA.","predictedComplex":false,"interactors":[{"ac":"EBI-63983486","identifier":"Q9HGK2","identifierLink":"https://www.uniprot.org/uniprotkb/Q9HGK2/entry","name":"meu13","description":"Homologous-pairing protein 2","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR15938","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-63983506","identifier":"Q09739","identifierLink":"https://www.uniprot.org/uniprotkb/Q09739/entry","name":"mcp7","description":"Meiotic coiled-coil protein 7","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR31398","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26491","complexName":"Glycogen synthase-glycogenin complex, GYG1-GYS1 variant","organismName":"Homo sapiens; 9606","description":"Glycogen synthase complex which extends the oligosaccharide chain formed by homodimeric glycogenin (GYG) glycosyltransferase. GYG initiates glucose polymerization by catalyzing the formation of a short alpha (1,4)-glucosyl chain which it covalently attaches via auto-glucosylation to form a glucose 1-O-tyrosyl linkage to Tyr-195  This primer glucose chain of 8-12 residues is then further elongated by the GYG-GYS complex, successively adding alpha-1,4-linked glucose residues to the nonreducing end of the polysaccharide chain, using UDP-glucose as the sugar donor with the release of UDP after which, GYG and GYS dissociate.","predictedComplex":false,"interactors":[{"ac":"EBI-740533","identifier":"P46976","identifierLink":"https://www.uniprot.org/uniprotkb/P46976/entry","name":"GYG1","description":"Glycogenin-1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11183","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-740553","identifier":"P13807","identifierLink":"https://www.uniprot.org/uniprotkb/P13807/entry","name":"GYS1","description":"Glycogen [starch] synthase, muscle","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10176","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26492","complexName":"Glycogen synthase-glycogenin complex, GYG1-GYS2 variant","organismName":"Homo sapiens; 9606","description":"Glycogen synthase complex which  extends the oligosaccharide chain formed by homodimeric glycogenin (GYG) glycosyltransferase. GYG initiates glucose polymerization by catalyzing the formation of a short alpha (1,4)-glucosyl chain which it covalently attaches via auto-glucosylation to form a glucose 1-O-tyrosyl linkage to Tyr-195  This primer glucose chain of 8-12 residues is then further elongated by the GYG-GYS complex, successively adding alpha-1,4-linked glucose residues to the nonreducing end of the polysaccharide chain, using UDP-glucose as the sugar donor with the release of UDP after which, GYG and GYS dissociate.","predictedComplex":false,"interactors":[{"ac":"EBI-2952729","identifier":"P54840","identifierLink":"https://www.uniprot.org/uniprotkb/P54840/entry","name":"GYS2","description":"Glycogen [starch] synthase, liver","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10176","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-740533","identifier":"P46976","identifierLink":"https://www.uniprot.org/uniprotkb/P46976/entry","name":"GYG1","description":"Glycogenin-1","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11183","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26493","complexName":"Glycogen synthase-glycogenin complex, GYG2-GYS1 variant","organismName":"Homo sapiens; 9606","description":"Glycogen synthase complex which extends the oligosaccharide chain formed by homodimeric glycogenin (GYG) glycosyltransferase. GYG initiates glucose polymerization by catalyzing the formation of a short alpha (1,4)-glucosyl chain which it covalently attaches via auto-glucosylation to form a glucose 1-O-tyrosyl linkage to Tyr-195  This primer glucose chain of 8-12 residues is then further elongated by the GYG-GYS complex, successively adding alpha-1,4-linked glucose residues to the nonreducing end of the polysaccharide chain, using UDP-glucose as the sugar donor with the release of UDP after which, GYG and GYS dissociate.","predictedComplex":false,"interactors":[{"ac":"EBI-740553","identifier":"P13807","identifierLink":"https://www.uniprot.org/uniprotkb/P13807/entry","name":"GYS1","description":"Glycogen [starch] synthase, muscle","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10176","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752192","identifier":"O15488","identifierLink":"https://www.uniprot.org/uniprotkb/O15488/entry","name":"GYG2","description":"Glycogenin-2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11183","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26494","complexName":"Glycogen synthase-glycogenin complex, GYG2-GYS2 variant","organismName":"Homo sapiens; 9606","description":"Glycogen synthase complex which extends the oligosaccharide chain formed by homodimeric glycogenin (GYG) glycosyltransferase. GYG initiates glucose polymerization by catalyzing the formation of a short alpha (1,4)-glucosyl chain which it covalently attaches via auto-glucosylation to form a glucose 1-O-tyrosyl linkage to Tyr-195  This primer glucose chain of 8-12 residues is then further elongated by the GYG-GYS complex, successively adding alpha-1,4-linked glucose residues to the nonreducing end of the polysaccharide chain, using UDP-glucose as the sugar donor with the release of UDP after which, GYG and GYS dissociate.","predictedComplex":false,"interactors":[{"ac":"EBI-2952729","identifier":"P54840","identifierLink":"https://www.uniprot.org/uniprotkb/P54840/entry","name":"GYS2","description":"Glycogen [starch] synthase, liver","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10176","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-752192","identifier":"O15488","identifierLink":"https://www.uniprot.org/uniprotkb/O15488/entry","name":"GYG2","description":"Glycogenin-2","stochiometry":"minValue: 4, maxValue: 4","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11183","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26495","complexName":"U4atac small nuclear ribonucleoprotein complex","organismName":"Homo sapiens; 9606","description":"Minor spliceosome building block. 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U12-type intron containing genes are mainly related to information processing functions, including DNA replication and repair, transcription, RNA processing, and translation, but can also be found in genes related to cytoskeletal organization, vesicular transport, and voltage-gated ion channel activity.","predictedComplex":false,"interactors":[{"ac":"EBI-16411676","identifier":"URS000075ADBA_9606","identifierLink":"http://rnacentral.org/rna/URS000075ADBA_9606","name":"rnu4atac","description":"U4atac small nuclear RNA (U12-dependent splicing)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small nuclear rna","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-297993","identifier":"P62316","identifierLink":"https://www.uniprot.org/uniprotkb/P62316/entry","name":"SNRPD2","description":"Small nuclear ribonucleoprotein Sm D2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12777","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348082","identifier":"P62304","identifierLink":"https://www.uniprot.org/uniprotkb/P62304/entry","name":"SNRPE","description":"Small nuclear ribonucleoprotein E","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 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The exocyst is localized to the emerging bud tip, where it mediates exocytosis for the asymmetric expansion of daughter cell surfaces during polarized cell growth. During cytokinesis, the exocyst is localized to the mother–daughter cell junction to mediate abscission. The targeting of secretory vesicles to the plasma membrane involves direct interactions of the exocyst with PI(4,5)P2. In addition, a number of small GTP-binding proteins interact with components of the exocyst and regulate the assembly, localization, and function of this complex.","predictedComplex":false,"interactors":[{"ac":"EBI-63985868","identifier":"O14226","identifierLink":"https://www.uniprot.org/uniprotkb/O14226/entry","name":"exo84","description":"Exocyst complex component exo84","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]},{"ac":"EBI-63985949","identifier":"Q10339","identifierLink":"https://www.uniprot.org/uniprotkb/Q10339/entry","name":"exo70","description":"Exocyst complex component exo70","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12542","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-63985968","identifier":"O13705","identifierLink":"https://www.uniprot.org/uniprotkb/O13705/entry","name":"sec10","description":"Exocyst complex component sec10","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12100","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-63985986","identifier":"O74562","identifierLink":"https://www.uniprot.org/uniprotkb/O74562/entry","name":"sec8","description":"Exocyst complex component sec8","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR14146","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-63986013","identifier":"O94598","identifierLink":"https://www.uniprot.org/uniprotkb/O94598/entry","name":"sec5","description":"Exocyst complex component sec5","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR13043","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-63986028","identifier":"O74846","identifierLink":"https://www.uniprot.org/uniprotkb/O74846/entry","name":"sec6","description":"Exocyst complex component sec6","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR21292","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-63986050","identifier":"O75006","identifierLink":"https://www.uniprot.org/uniprotkb/O75006/entry","name":"sec15","description":"Exocyst complex component sec15","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[{"identifier":"PTHR12702","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-63986067","identifier":"Q10324","identifierLink":"https://www.uniprot.org/uniprotkb/Q10324/entry","name":"yd6c","description":"Uncharacterized protein C17G8.12","stochiometry":null,"interactorType":"protein","organismName":"Schizosaccharomyces pombe (strain 972 / ATCC 24843); 284812","xrefs":[]}]},{"complexAC":"CPX-26497","complexName":"Nucleosome, variant H3.2-H4-H2A.1-H2B1.1","organismName":"Xenopus laevis; 8355","description":"Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability.","predictedComplex":false,"interactors":[{"ac":"EBI-1251194","identifier":"P06897","identifierLink":"https://www.uniprot.org/uniprotkb/P06897/entry","name":"h2a1","description":"Histone H2A type 1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Xenopus laevis; 8355","xrefs":[{"identifier":"PTHR23430","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1251201","identifier":"P02281","identifierLink":"https://www.uniprot.org/uniprotkb/P02281/entry","name":"h2b11","description":"Histone H2B 1.1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Xenopus laevis; 8355","xrefs":[{"identifier":"PTHR23428","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-302085","identifier":"P62799","identifierLink":"https://www.uniprot.org/uniprotkb/P62799/entry","name":"h4","description":"Histone H4","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Xenopus laevis; 8355","xrefs":[{"identifier":"PTHR10484","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-350041","identifier":"P84233","identifierLink":"https://www.uniprot.org/uniprotkb/P84233/entry","name":"h32","description":"Histone H3.2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Xenopus laevis; 8355","xrefs":[{"identifier":"PTHR11426","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-63986426","identifier":"CHEBI:234102","identifierLink":"http://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:234102","name":"xenopus laevis double-stranded dna","description":"Xenopus laevis double-stranded DNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small molecule","organismName":"chemical synthesis; -2","xrefs":[]}]},{"complexAC":"CPX-26499","complexName":"U6atac small nuclear ribonucleoprotein complex","organismName":"Homo sapiens; 9606","description":"Minor spliceosome building block. The minor spliceosome catalyses the removal of an atypical (U12) class of eukaryotic precursor-mRNA (pre-mRNA) introns and is thought to excise approximately 1 in 300 introns in human pre-mRNA. U12 introns constitute roughly 0.5% of all introns, and are recognizable by their non-consensus AT-AC termini as well as a high degree of conservation at the 5' splice site. U12-dependent introns are thought to be evolutionarily ancient but absent in many species including model organisms such as Caenorhabditis elegans and Saccharomyces cerevisiae. \r\n\r\nThe minor spliceosome contains several specific low-abundance snRNPs, including U11, U12, U4atac, U6atac (this complex) and the common U5 snRNP also present in the major spliceosome. U12-type intron containing genes are mainly related to information processing functions, including DNA replication and repair, transcription, RNA processing, and translation, but can also be found in genes related to cytoskeletal organization, vesicular transport, and voltage-gated ion channel activity.\r\n\r\nU6atac is part of the activated spliceosome and is involved in the first trans-estherification step of splicing. After splicing is complete, the spliceosome disassembles and free U6atac snRNP forms. It then reassociates with U4atac snRNA to form U4/U6atac snRNP.\r\n\r\nSART3 (Q15020), an snRNP recycling factor, thought to associate with U6 and U4/U6 snRNP during the recycling phase of the spliceosome cycle but dissociating during the formation of the U4/U6.U5 tri-complex is likely to play a similar role with U6atac snRNPs and U4/U6atac snRNPs.","predictedComplex":false,"interactors":[{"ac":"EBI-308619","identifier":"Q15020","identifierLink":"https://www.uniprot.org/uniprotkb/Q15020/entry","name":"SART3","description":"Spliceosome associated factor 3, U4/U6 recycling protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15481","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347416","identifier":"Q9Y333","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y333/entry","name":"LSM2","description":"U6 snRNA-associated Sm-like protein LSm2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347779","identifier":"O95777","identifierLink":"https://www.uniprot.org/uniprotkb/O95777/entry","name":"LSM8","description":"U6 snRNA-associated Sm-like protein LSm8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348239","identifier":"P62310","identifierLink":"https://www.uniprot.org/uniprotkb/P62310/entry","name":"LSM3","description":"U6 snRNA-associated Sm-like protein LSm3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13110","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348372","identifier":"Q9UK45","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK45/entry","name":"LSM7","description":"U6 snRNA-associated Sm-like protein LSm7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372521","identifier":"Q9Y4Z0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4Z0/entry","name":"LSM4","description":"U6 snRNA-associated Sm-like protein LSm4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373007","identifier":"Q9Y4Y9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4Y9/entry","name":"LSM5","description":"U6 snRNA-associated Sm-like protein LSm5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373310","identifier":"P62312","identifierLink":"https://www.uniprot.org/uniprotkb/P62312/entry","name":"LSM6","description":"U6 snRNA-associated Sm-like protein LSm6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64038885","identifier":"URS0000443498_9606","identifierLink":"http://rnacentral.org/rna/URS0000443498_9606","name":"rna, u6atac small nuclear (rnu6atac)","description":"Homo sapiens (human) RNA, U6atac small nuclear (RNU6ATAC)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"ribonucleic acid","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-26500","complexName":"U4atac/U6atac small nuclear ribonucleoprotein complex","organismName":"Homo sapiens; 9606","description":"Minor spliceosome pre-catalytic complex. The minor spliceosome catalyses the removal of an atypical (U12) class of eukaryotic precursor-mRNA (pre-mRNA) introns and is thought to excise approximately 1 in 300 introns in human pre-mRNA. U12 introns constitute roughly 0.5% of all introns, and are recognizable by their non-consensus AT-AC termini as well as a high degree of conservation at the 5' splice site. U12-dependent introns are thought to be evolutionarily ancient but absent in many species including model organisms such as Caenorhabditis elegans and Saccharomyces cerevisiae. \r\n\r\nThe minor spliceosome contains several specific low-abundance snRNPs, including U11, U12, U4atac, U6atac and the common U5 snRNP also present in the major spliceosome. U12-type intron containing genes are mainly related to information processing functions, including DNA replication and repair, transcription, RNA processing, and translation, but can also be found in genes related to cytoskeletal organization, vesicular transport, and voltage-gated ion channel activity.\r\n\r\nU4atac/U6atac snRNP (this complex) is the functional analogue of the major spliceosome's U4/U6 snRNP (CPX-26418). U4atac/U6atac di-snRNPs associate with U5 snRNPs (CPX-26421) to form a 25S U4atac/U6atac.U5 trimeric complex which associates with pre-mRNA and undergoes several structural rearrangements before forming a catalytically active spliceosome.","predictedComplex":false,"interactors":[{"ac":"EBI-1567797","identifier":"Q8WWY3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WWY3/entry","name":"PRPF31","description":"U4/U6 small nuclear ribonucleoprotein Prp31","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13904","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-63985846","identifier":"CPX-26495","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-26495","name":"U4atac small nuclear ribonucleoprotein complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-64038805","identifier":"CPX-26499","identifierLink":"http://www.ebi.ac.uk/complexportal/complex/CPX-26499","name":"U6atac small nuclear ribonucleoprotein complex","description":null,"stochiometry":"minValue: 1, maxValue: 1","interactorType":"stable complex","organismName":"Homo sapiens; 9606","xrefs":[]}]},{"complexAC":"CPX-26502","complexName":"U4atac/U6atac.U5 small nuclear ribonucleoprotein complex","organismName":"Homo sapiens; 9606","description":"Minor spliceosome pre-catalytic complex. The Minor spliceosome catalyses the removal of an atypical (U12) class of eukaryotic precursor-mRNA (pre-mRNA) introns and is thought to excise approximately 1 in 300 introns in human pre-mRNA. U12 introns constitute roughly 0.5% of all introns, and are recognizable by their non-consensus AT-AC termini as well as a high degree of conservation at the 5' splice site. U12-dependent introns are thought to be evolutionarily ancient but absent in many species including model organisms such as Caenorhabditis elegans and Saccharomyces cerevisiae. \r\n\r\nThe minor spliceosome contains several specific low-abundance snRNPs, including U11, U12, U4atac, U6atac and the common U5 snRNP also present in the major spliceosome. U12-type intron containing genes are mainly related to information processing functions, including DNA replication and repair, transcription, RNA processing, and translation, but can also be found in genes related to cytoskeletal organization, vesicular transport, and voltage-gated ion channel activity.\r\n\r\nThe tripartate U4atac/U6atac.U5 snRNP (this complex) is formed upon association with the minor A complex (CPX-26489), generating the fully assembled pre-B spliceosome complex which undergoes substantial remodelling to become the activated minor spliceosome.","predictedComplex":false,"interactors":[{"ac":"EBI-10309345","identifier":"Q9NX01","identifierLink":"https://www.uniprot.org/uniprotkb/Q9NX01/entry","name":"TXNL4B","description":"Thioredoxin-like protein 4B","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12052","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1044822","identifier":"Q53GS9","identifierLink":"https://www.uniprot.org/uniprotkb/Q53GS9/entry","name":"USP39","description":"Ubiquitin carboxyl-terminal hydrolase 39","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR21646","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1045395","identifier":"O75643","identifierLink":"https://www.uniprot.org/uniprotkb/O75643/entry","name":"SNRNP200","description":"U5 small nuclear ribonucleoprotein 200 kDa helicase","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR24075","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-11028020","identifier":"Q86UT8","identifierLink":"https://www.uniprot.org/uniprotkb/Q86UT8/entry","name":"CENATAC","description":"Centrosomal AT-AC splicing factor","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR31198","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-1567797","identifier":"Q8WWY3","identifierLink":"https://www.uniprot.org/uniprotkb/Q8WWY3/entry","name":"PRPF31","description":"U4/U6 small nuclear ribonucleoprotein Prp31","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13904","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-16411676","identifier":"URS000075ADBA_9606","identifierLink":"http://rnacentral.org/rna/URS000075ADBA_9606","name":"rnu4atac","description":"U4atac small nuclear RNA (U12-dependent splicing)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small nuclear rna","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-27124791","identifier":"URS0000631BD4_9606","identifierLink":"http://rnacentral.org/rna/URS0000631BD4_9606","name":"u5_human_snrna","description":"U5 spliceosomal RNA","stochiometry":"minValue: 1, maxValue: 1","interactorType":"small nuclear rna","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-297993","identifier":"P62316","identifierLink":"https://www.uniprot.org/uniprotkb/P62316/entry","name":"SNRPD2","description":"Small nuclear ribonucleoprotein Sm D2","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR12777","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347416","identifier":"Q9Y333","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y333/entry","name":"LSM2","description":"U6 snRNA-associated Sm-like protein LSm2","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13829","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-347779","identifier":"O95777","identifierLink":"https://www.uniprot.org/uniprotkb/O95777/entry","name":"LSM8","description":"U6 snRNA-associated Sm-like protein LSm8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR15588","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348082","identifier":"P62304","identifierLink":"https://www.uniprot.org/uniprotkb/P62304/entry","name":"SNRPE","description":"Small nuclear ribonucleoprotein E","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11193","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348239","identifier":"P62310","identifierLink":"https://www.uniprot.org/uniprotkb/P62310/entry","name":"LSM3","description":"U6 snRNA-associated Sm-like protein LSm3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR13110","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-348372","identifier":"Q9UK45","identifierLink":"https://www.uniprot.org/uniprotkb/Q9UK45/entry","name":"LSM7","description":"U6 snRNA-associated Sm-like protein LSm7","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-356900","identifier":"P62306","identifierLink":"https://www.uniprot.org/uniprotkb/P62306/entry","name":"SNRPF","description":"Small nuclear ribonucleoprotein F","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-357897","identifier":"Q15029","identifierLink":"https://www.uniprot.org/uniprotkb/Q15029/entry","name":"EFTUD2","description":"116 kDa U5 small nuclear ribonucleoprotein component","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR42908","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372177","identifier":"P62314","identifierLink":"https://www.uniprot.org/uniprotkb/P62314/entry","name":"SNRPD1","description":"Small nuclear ribonucleoprotein Sm D1","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372458","identifier":"P14678","identifierLink":"https://www.uniprot.org/uniprotkb/P14678/entry","name":"SNRPB","description":"Small nuclear ribonucleoprotein-associated proteins B and B'","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10701","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372521","identifier":"Q9Y4Z0","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4Z0/entry","name":"LSM4","description":"U6 snRNA-associated Sm-like protein LSm4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-372789","identifier":"P62318","identifierLink":"https://www.uniprot.org/uniprotkb/P62318/entry","name":"SNRPD3","description":"Small nuclear ribonucleoprotein Sm D3","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23338","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373007","identifier":"Q9Y4Y9","identifierLink":"https://www.uniprot.org/uniprotkb/Q9Y4Y9/entry","name":"LSM5","description":"U6 snRNA-associated Sm-like protein LSm5","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR20971","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-373310","identifier":"P62312","identifierLink":"https://www.uniprot.org/uniprotkb/P62312/entry","name":"LSM6","description":"U6 snRNA-associated Sm-like protein LSm6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11021","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-536755","identifier":"O94906","identifierLink":"https://www.uniprot.org/uniprotkb/O94906/entry","name":"PRPF6","description":"Pre-mRNA-processing factor 6","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11246","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-538479","identifier":"Q6P2Q9","identifierLink":"https://www.uniprot.org/uniprotkb/Q6P2Q9/entry","name":"PRPF8","description":"Pre-mRNA-processing-splicing factor 8","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR11140","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-538492","identifier":"Q96DI7","identifierLink":"https://www.uniprot.org/uniprotkb/Q96DI7/entry","name":"SNRNP40","description":"U5 small nuclear ribonucleoprotein 40 kDa protein","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR44006","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-540096","identifier":"Q9BUQ8","identifierLink":"https://www.uniprot.org/uniprotkb/Q9BUQ8/entry","name":"DDX23","description":"Probable ATP-dependent RNA helicase DDX23","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR47958","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-607761","identifier":"O43290","identifierLink":"https://www.uniprot.org/uniprotkb/O43290/entry","name":"SART1","description":"U4/U6.U5 tri-snRNP-associated protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14152","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-624585","identifier":"P62308","identifierLink":"https://www.uniprot.org/uniprotkb/P62308/entry","name":"SNRPG","description":"Small nuclear ribonucleoprotein G","stochiometry":"minValue: 2, maxValue: 2","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR10553","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-64038885","identifier":"URS0000443498_9606","identifierLink":"http://rnacentral.org/rna/URS0000443498_9606","name":"rna, u6atac small nuclear (rnu6atac)","description":"Homo sapiens (human) RNA, U6atac small nuclear (RNU6ATAC)","stochiometry":"minValue: 1, maxValue: 1","interactorType":"ribonucleic acid","organismName":"Homo sapiens; 9606","xrefs":[]},{"ac":"EBI-712228","identifier":"P55769","identifierLink":"https://www.uniprot.org/uniprotkb/P55769/entry","name":"SNU13","description":"NHP2-like protein 1","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR23105","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-718395","identifier":"O43172","identifierLink":"https://www.uniprot.org/uniprotkb/O43172/entry","name":"PRPF4","description":"U4/U6 small nuclear ribonucleoprotein Prp4","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR19846","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]},{"ac":"EBI-744322","identifier":"O43395","identifierLink":"https://www.uniprot.org/uniprotkb/O43395/entry","name":"PRPF3","description":"U4/U6 small nuclear ribonucleoprotein Prp3","stochiometry":"minValue: 1, maxValue: 1","interactorType":"protein","organismName":"Homo sapiens; 9606","xrefs":[{"identifier":"PTHR14212","identifierLink":null,"database":"panther","qualifier":"orthology-group"}]}]},{"complexAC":"CPX-26503","complexName":"Spastizin-spatacsin complex","organismName":"Homo sapiens; 9606","description":"Essential in the formation of lysosomal tubulation and autophagic lysosome reformation. 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